P-POD: Princeton Protein Orthology Database: GO3/Jaccard36

This family has 325 members: 48 Arabidopsis thaliana, 21 Caenorhabditis elegans, 37 Danio rerio, 24 Dictyostelium discoideum, 15 Drosophila melanogaster, 4 Escherichia coli, 32 Gallus gallus, 37 Homo sapiens, 37 Mus musculus, 40 Rattus norvegicus, 16 Saccharomyces cerevisiae, 14 Schizosaccharomyces pombe.

Interactive Java Applets: Notung Tree Analysis · Jalview Alignment

GO3/Jaccard36
325 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaNCBI:NP_195479.1 · TAIR:locus:2120096 (F19F18.130 · F19F18_130 · AT4G37640 · ACA2)CALCIUM ATPASE 2⌘
A. thalianaNCBI:NP_177414.1 · TAIR:locus:2030180 (F28P22_11 · AT1G72700 · F28P22.11)⌘
A. thalianaNCBI:NP_189850.1 · TAIR:locus:2096549 (AHA8 · AT3G42640 · T12K4.90)Arabidopsis H(+)-ATPase 8⌘
A. thalianaNCBI:NP_568146.1 · TAIR:locus:3355727 (ALA1 · AT5G04930)aminophospholipid ATPase1⌘
A. thalianaNCBI:NP_178762.1 · TAIR:locus:2053343 (AT2G07560 · F9A16_7 · AHA6 · F9A16.7)Arabidopsis H(+)-ATPase 6⌘
A. thalianaNCBI:NP_189189.1 · TAIR:locus:2102345 (T5M7.10 · AT3G25610)⌘
A. thalianaNCBI:NP_179501.1 · TAIR:locus:2059083 (T20K24.12 · T20K24_12 · AT2G19110 · HMA4)⌘
A. thalianaNCBI:NP_189425.1 · TAIR:locus:2086465 (K16N12.23 · AT3G27870)⌘
A. thalianaNCBI:NP_192910.1 · TAIR:locus:2139782 (T5C23_160 · AT4G11730 · T5C23.160)⌘
A. thalianaNCBI:NP_191897.1 · TAIR:locus:2087363 (MAA21.10 · AT3G63380)⌘
A. thalianaNCBI:NP_181687.1 · TAIR:locus:2062673 (T32G6.8 · ACA4 · T32G6_8 · AT2G41560)AUTO-INHIBITED CA(2+)-ATPASE, ISOFORM 4⌘
A. thalianaNCBI:NP_200113.3 · TAIR:locus:2168397 (AT5G53010 · MNB8.7 · MNB8_7)⌘
A. thalianaNCBI:NP_180028.1 · TAIR:locus:2046623 (F25P17_18 · F25P17.18 · AT2G24520 · AHA5)Arabidopsis H(+)-ATPase 5⌘
A. thalianaNCBI:NP_188931.1 · TAIR:locus:2084578 (AT3G22910 · F5N5.18)⌘
A. thalianaNCBI:NP_200545.1 · TAIR:locus:2165600 (MJB24_16 · ATAHA3 · MJB24.16 · AHA3 · AT5G57350)P-TYPE H(+)-ATPASE ISOFOM 3⌘
A. thalianaNCBI:NP_177038.1 · TAIR:locus:2026900 (F24J5.6 · F24J5_6 · AT1G68710)⌘
A. thalianaNCBI:NP_194748.1 · TAIR:locus:2128941 (F9N11.40 · AHA2 · AT4G30190 · F9N11_40 · PMA2)p-type h(+)-atpase isoform 2 · PLASMA MEMBRANE PROTON ATPASE 2⌘
A. thalianaNCBI:NP_172780.1 · TAIR:locus:2031860 (F3F19.24 · ACA.l · F3F19_24 · AT1G13210)autoinhibited Ca2+/ATPase II⌘
A. thalianaNCBI:NP_849716.1 · TAIR:locus:2029794 (ACA1 · CA2+-ATPASE · T22C5_23 · PEA1 · T22C5.23 · AT1G27770)PLASTID ENVELOPE ATPASE 1 · AUTO-INHIBITED CA2+-ATPASE 1⌘
A. thalianaNCBI:NP_191999.1 · TAIR:locus:2134623 (A_TM018A10.4 · T18A10_20 · T18A10.20 · ATECA2 · A_TM018A10_4 · AT4G00900 · ECA2)ER-TYPE CA2+-ATPASE 2 · ARABIDOPSIS THALIANA ER-TYPE CA2+-ATPASE 2⌘
A. thalianaNCBI:NP_188755.2 · TAIR:locus:2094726 (MXL8.3 · AT3G21180 · ACA9 · ATACA9)AUTOINHIBITED CA(2+)-ATPASE · AUTOINHIBITED CA(2+)-ATPASE 9⌘
A. thalianaNCBI:NP_201073.1 · TAIR:locus:2172244 (MRG21.9 · MRG21_9 · AT5G62670 · AHA11)Arabidopsis H(+)-ATPase 11⌘
A. thalianaNCBI:NP_190378.2 · TAIR:locus:2097895 (AHA4 · T17F15.180 · AT3G47950)⌘
A. thalianaNCBI:NP_178181.1 · TAIR:locus:2025727 (AT1G80660 · AHA9 · F23A5_1 · F23A5.1)⌘
A. thalianaNCBI:NP_173938.1 · TAIR:locus:2011420 (F28B23_19 · F28B23.19 · AT1G26130)⌘
A. thalianaNCBI:NP_194740.1 · TAIR:locus:2126490 (F6G3_140 · F6G3.140 · AT4G30110 · HMA2)⌘
A. thalianaNCBI:NP_563860.1 · TAIR:locus:2201916 (T27I1_16 · T27I1.16 · ATECA3 · AT1G10130 · ECA3)ENDOPLASMIC RETICULUM-TYPE CALCIUM-TRANSPORTING ATPASE 3 · ARABIDOPSIS THALIANA ER-TYPE CA2+-ATPASE 3⌘
A. thalianaNCBI:NP_175830.1 · TAIR:locus:2020038 (F20D21_10 · AT1G54280 · F20D21.10)⌘
A. thalianaNCBI:NP_194741.2 · TAIR:locus:2126500 (HMA3 · ATHMA3 · AT4G30120 · F6G3_150 · F6G3.150)HEAVY METAL ATPASE 3 · A. THALIANA HEAVY METAL ATPASE 3⌘
A. thalianaNCBI:NP_680181.2 · TAIR:locus:504956435 (PAA2 · HMA8 · AT5G21930)P-TYPE ATPASE OF ARABIDOPSIS 2⌘
A. thalianaNCBI:NP_188006.1 · TAIR:locus:2088217 (AT3G13900 · MDC16.2)⌘
A. thalianaNCBI:NP_195444.1 · TAIR:locus:2115020 (AP22.4 · AP22_4 · HMA1 · ATHMA1 · AT4G37270)HEAVY METAL ATPASE 1⌘
A. thalianaNCBI:NP_974675.1 · TAIR:locus:2119265 (F17M5_280 · HMA6 · PAA1 · F17M5.280 · AT4G33520)P-TYPE ATP-ASE 1 · HEAVY METAL ATPASE 6⌘
A. thalianaNCBI:NP_176191.1 · TAIR:locus:2025961 (AT1G59820 · ALA3 · F23H11.14 · F23H11_14)Aminophospholipid ATPase3⌘
A. thalianaNCBI:NP_172259.1 · TAIR:locus:2026580 (F24B9_9 · F24B9.9 · ATECA1 · ECA1 · ACA3 · AT1G07810)ER-TYPE CA2+-ATPASE · ARABIDOPSIS THALIANA ER-TYPE CA2+-ATPASE 1 · ER-TYPE CA2+-ATPASE 1⌘
A. thalianaNCBI:NP_173169.2 · TAIR:locus:2020372 (AT1G17260 · AHA10 · F20D23.4 · F20D23_4)Autoinhibited H(+)-ATPase isoform 10⌘
A. thalianaNCBI:NP_176533.1 · TAIR:locus:2031361 (F2K11.18 · AT1G63440 · F2K11_18 · HMA5)HEAVY METAL ATPASE 5⌘
A. thalianaNCBI:NP_179486.1 · TAIR:locus:2044450 (PMA · OST2 · AHA1 · AT2G18960 · F19F24_16 · F19F24.16)OPEN STOMATA 2 · PLASMA MEMBRANE PROTON ATPASE · ARABIDOPSIS H+ ATPASE 1⌘
A. thalianaNCBI:NP_194719.1 · TAIR:locus:2123924 (F27B13.140 · ATACA10 · F27B13_140 · ACA10 · CIF1 · AT4G29900)COMPACT INFLORESCENCE 1 · AUTOINHIBITED CA(2+)-ATPASE 10 · AUTOINHIBITED CA(2+)-ATPASE⌘
A. thalianaNCBI:NP_191592.2 · TAIR:locus:2081932 (AHA7 · AT3G60330 · T8B10.1)Arabidopsis H(+)-ATPase 7⌘
A. thalianaNCBI:NP_199292.1 · TAIR:locus:2156354 (K23L20.14 · RAN1 · AT5G44790 · K23L20_14 · HMA7)RESPONSIVE-TO-ANTAGONIST 1⌘
A. thalianaNCBI:NP_191292.1 · TAIR:locus:2082528 (AT3G57330 · ACA11 · F28O9.180)autoinhibited Ca2+-ATPase 11⌘
A. thalianaNCBI:NP_179879.1 · TAIR:locus:2059201 (AT2G22950 · T20K9_16 · T20K9.16)⌘
A. thalianaTAIR:locus:2171686 (MQM1_11 · AT5G23630 · MQM1.11) · NCBI:NP_197752.1⌘
A. thalianaNCBI:NP_568633.1 · TAIR:locus:2167603 (MLN1_17 · AT5G44240 · MLN1.17)⌘
A. thalianaNCBI:NP_173193.2 · TAIR:locus:2007858 (AT1G17500 · F1L3.21 · F1L3_21)⌘
A. thalianaNCBI:NP_172246.3 · TAIR:locus:2026555 (F24B9_24 · F24B9.24 · AT1G07670)⌘
A. thalianaNCBI:NP_851200.1 · TAIR:locus:2175579 (MUL3.5 · AT-ACA8 · ACA8 · MUL3_5 · AT5G57110)"AUTOINHIBITED CA2+ -ATPASE, ISOFORM 8" · AUTOINHIBITED CA2+ -ATPASE, ISOFORM 8⌘
C. elegansWB:WBGene00019493 (K07E3.7 · catp-5) · UniProtKB:Q21286⌘
C. elegansWB:WBGene00007514 (C10C6.6) · UniProtKB:P90747⌘
C. elegansWB:WBGene00012341 (W08D2.5 · catp-6) · UniProtKB:Q27533⌘
C. elegansWB:WBGene00015660 (C09H5.2 · catp-3) · UniProtKB:O16331⌘
C. elegansWB:WBGene00015338 (C02E7.1 · catp-2) · UniProtKB:O16436⌘
C. elegansWB:WBGene00000834 (Y76A2A.2 · cua-1) · UniProtKB:O17737⌘
C. elegansWB:WBGene00012360 (W09D10.2 · tat-3) · UniProtKB:O18182⌘
C. elegansWB:WBGene00007248 (catp-4 · C01G12.8) · UniProtKB:O45240⌘
C. elegansWB:WBGene00009498 (tat-5 · F36H2.1) · UniProtKB:O45878⌘
C. elegansWB:WBGene00001137 (B0365.3 · eat-6) · UniProtKB:P90735⌘
C. elegansWB:WBGene00017174 (tat-6 · F02C9.3) · UniProtKB:P91203⌘
C. elegansWB:WBGene00020784 (T24H7.5 · tat-4) · UniProtKB:Q10463⌘
C. elegansWB:WBGene00004063 (ZK256.1 · pmr-1) · UniProtKB:Q6LA80⌘
C. elegansWB:WBGene00003151 (W09C2.3 · mca-1) · UniProtKB:Q6T364⌘
C. elegansWB:WBGene00013672 (Y105E8A.12 · catp-1) · UniProtKB:Q8WQB1⌘
C. elegansWB:WBGene00003153 (mca-3 · Y67D8C.10) · UniProtKB:Q95XP5⌘
C. elegansWB:WBGene00022010 (catp-7 · Y59H11AR.2) · UniProtKB:Q9N323⌘
C. elegansWB:WBGene00019166 (tat-2 · H06H21.10) · UniProtKB:Q9TXV2⌘
C. elegansWB:WBGene00019875 (R05C11.3) · UniProtKB:Q9TYP9⌘
C. elegansWB:WBGene00013034 (Y49E10.11 · tat-1) · UniProtKB:Q9U280⌘
C. elegansWB:WBGene00004736 (K11D9.2 · sca-1) · UniProtKB:Q9XTG6⌘
D. rerioENSEMBL:ENSDARP00000063158
D. rerioENSEMBL:ENSDARP00000084907
D. rerioENSEMBL:ENSDARP00000070629
D. rerioENSEMBL:ENSDARP00000087158
D. rerioENSEMBL:ENSDARP00000087549
D. rerioENSEMBL:ENSDARP00000040283
D. rerioENSEMBL:ENSDARP00000046561
D. rerioENSEMBL:ENSDARP00000029666
D. rerioENSEMBL:ENSDARP00000080960
D. rerioUniProtKB:A0JMP4 · ZFIN:ZDB-GENE-041229-2 (atp2a1l)ATPase, Ca++ transporting, cardiac muscle, fast twitch 1 like⌘
D. rerioZFIN:ZDB-GENE-061215-126 (zgc:136762) · UniProtKB:A1A5E5⌘
D. rerioENSEMBL:ENSDARG00000020056 · UniProtKB:A1A5T0
D. rerioENSEMBL:ENSDARG00000062040 · UniProtKB:A2BGP2
D. rerioENSEMBL:ENSDARG00000060978 · UniProtKB:A2BIP1
D. rerioZFIN:ZDB-GENE-060929-36 (zgc:154074) · UniProtKB:Q08BV9⌘
D. rerioUniProtKB:Q1LVC6 · ZFIN:ZDB-GENE-060503-583 (atp9b)ATPase, class II, type 9B⌘
D. rerioENSEMBL:ENSDARG00000042285 · UniProtKB:Q1LY58
D. rerioENSEMBL:ENSDARG00000060197 · UniProtKB:Q1LYL7
D. rerioUniProtKB:Q4F8H5 · ZFIN:ZDB-GENE-060825-45 (atp7a)ATPase, Cu++ transporting, alpha polypeptide⌘
D. rerioENSEMBL:ENSDARG00000007788 · UniProtKB:Q4V9D7
D. rerioUniProtKB:Q5RGZ4 · ZFIN:ZDB-GENE-030925-29 (atp2b1a)ATPase, Ca++ transporting, plasma membrane 1a⌘
D. rerioUniProtKB:Q5U3A4 · ZFIN:ZDB-GENE-020905-1 (atp2a1)ATPase, Ca++ transporting, cardiac muscle, fast twitch 1⌘
D. rerioUniProtKB:Q6ZM60 · ZFIN:ZDB-GENE-030131-867 (atp2a2b)ATPase, Ca++ transporting, cardiac muscle, slow twitch 2b⌘
D. rerioUniProtKB:Q7SXR0 · ZFIN:ZDB-GENE-040426-2804 (atp13a)ATPase type 13A⌘
D. rerioZFIN:ZDB-GENE-030616-51 · UniProtKB:Q7ZZ91
D. rerioUniProtKB:Q8JIV1 · ZFIN:ZDB-GENE-020501-1 (atp1a1a.5)ATPase, Na+/K+ transporting, alpha 1a.5 polypeptide⌘
D. rerioUniProtKB:Q9DEU1 · ZFIN:ZDB-GENE-001212-5 (atp1a1b)ATPase, Na+/K+ transporting, alpha 1b polypeptide⌘
D. rerioUniProtKB:Q9DEU2 · ZFIN:ZDB-GENE-001212-8 (atp1a3b)ATPase, Na+/K+ transporting, alpha 3b polypeptide⌘
D. rerioUniProtKB:Q9DEY3 · ZFIN:ZDB-GENE-001212-3 (atp1a1a.3)ATPase, Na+/K+ transporting, alpha 1a.3 polypeptide⌘
D. rerioUniProtKB:Q9DGL5 · ZFIN:ZDB-GENE-001212-6 (atp1a2a)ATPase, Na+/K+ transporting, alpha 2a polypeptide⌘
D. rerioUniProtKB:A9C3Q4 · ZFIN:ZDB-GENE-040426-702 (atp2a2a)ATPase, Ca++ transporting, cardiac muscle, slow twitch 2a⌘
D. rerioUniProtKB:B0S5H3 · ZFIN:ZDB-GENE-040718-174 (atp2b3a)ATPase, Ca++ transporting, plasma membrane 3a⌘
D. rerioUniProtKB:B2CZC1 · ZFIN:ZDB-GENE-061027-60 (atp2b4)ATPase, Ca++ transporting, plasma membrane 4⌘
D. rerioUniProtKB:Q9DEU0 · ZFIN:ZDB-GENE-001212-4 (atp1a1a.4)ATPase, Na+/K+ transporting, alpha 1a.4 polypeptide⌘
D. rerioUniProtKB:Q9DEY2 · ZFIN:ZDB-GENE-001212-7 (atp1a3a)ATPase, Na+/K+ transporting, alpha 3a polypeptide⌘
D. rerioUniProtKB:Q9DGL4 · ZFIN:ZDB-GENE-001212-2 (atp1a1a.2)ATPase, Na+/K+ transporting, alpha 1a.2 polypeptide⌘
D. rerioUniProtKB:Q9DGL6 · ZFIN:ZDB-GENE-001212-1 (atp1a1)ATPase, Na+/K+ transporting, alpha 1 polypeptide⌘
D. discoideumNCBI:EAL69686.1 · dictyBase:DDB_G0275871 (DDB_G0275871)phospholipid-translocating P-type ATPase family protein, transmembrane protein⌘
D. discoideumNCBI:EAL65923.1 · dictyBase:DDB_G0282959 (DDB_G0282959)P-type ATPase, transmembrane protein⌘
D. discoideumNCBI:EAL72145.2 · dictyBase:DDB_G0269590 (DDB_G0269590)P-type ATPase, transmembrane protein⌘
D. discoideumNCBI:EAL69518.1 · dictyBase:DDB_G0275535 (DDB_G0275535)phospholipid-translocating P-type ATPase family protein, transmembrane protein⌘
D. discoideumNCBI:EAL69224.1 · dictyBase:DDB_G0276541 (DDB_G0276541)P-type ATPase, transmembrane protein⌘
D. discoideumNCBI:EAL73415.2 · dictyBase:DDB_G0267924 (DDB_G0267924)sodium/potassium-transporting ATPase alpha chain 2, Na+/K+ ATPase, P-type ATPase, transmembrane protein⌘
D. discoideumNCBI:EAL64941.1 · dictyBase:DDB_G0284955 (DDB_G0284955)P-type ATPase⌘
D. discoideumNCBI:EAL64003.1 · dictyBase:DDB_G0286891 (DDB_G0286891)P-type ATPase, transmembrane protein⌘
D. discoideumNCBI:EAL72994.1 · dictyBase:DDB_G0268810 (DDB_G0268810)magnesium-translocating P-type ATPase, transmembrane protein⌘
D. discoideumNCBI:EAL69268.1 · dictyBase:DDB_G0276375 (DDB_G0276375)phospholipid-translocating P-type ATPase family protein, transmembrane protein⌘
D. discoideumNCBI:EAL70528.1 · dictyBase:DDB_G0273675 (DDB_G0273675)P-type ATPase, transmembrane protein⌘
D. discoideumNCBI:EAL66682.1 · dictyBase:DDB_G0281401 (DDB_G0281401)P-type ATPase, transmembrane protein⌘
D. discoideumNCBI:EAL70835.1 · dictyBase:DDB_G0273235 (DDB_G0273235)P-type ATPase⌘
D. discoideumUniProtKB:P54678 · dictyBase:DDB_G0277861 (patA · PAT1)P-type ATPase, Ca2+-ATPase⌘
D. discoideumUniProtKB:P54679 · dictyBase:DDB_G0282817 (PAT2 · patB)P-type ATPase⌘
D. discoideumUniProtKB:Q54CD1 · dictyBase:DDB_G0293004 (ctaA)putative cation-transporting ATPase⌘
D. discoideumUniProtKB:Q54HG6 · dictyBase:DDB_G0289473 (DDB_G0289473)P-type ATPase, Ca2+-ATPase⌘
D. discoideumUniProtKB:Q54P22 · dictyBase:DDB_G0284849 (DDB_G0284849)P-type ATPase⌘
D. discoideumUniProtKB:Q54PE8 · dictyBase:DDB_G0284605 (DDB_G0284605)P-type ATPase, Ca2+-ATPase⌘
D. discoideumUniProtKB:Q54Q77 · dictyBase:DDB_G0284141 (atp7a)P-type ATPase, copper-transporting ATPase⌘
D. discoideumUniProtKB:Q54X63 · dictyBase:DDB_G0279183 (DDB_G0279183)P-type ATPase⌘
D. discoideumUniProtKB:Q55E09 · dictyBase:DDB_G0270870 (atp9b)ATPase, class II, type 9B⌘
D. discoideumUniProtKB:Q55E61 · dictyBase:DDB_G0269380 (DDB_G0269380)P-type ATPase⌘
D. discoideumUniProtKB:Q76P11 · dictyBase:DDB_G0277269 (ionA)P-type ATPase, ATPase, P-type cation exchange, alpha subunit, putative sodium/potassium-transporting ATPase⌘
D. melanogasterUniProtKB:P22700 · FB:FBgn0004551 (l(2)k09025 · Kumbhakarna · CG3725 · Ca-p · Ca[2+]ATPase · Ca-P60 · Ca-P60A · Kum · SERCA · CA-P60A · CaP60A · l(2)k08308ab · Ca-ATPase · dSERCA)sarco/endoplasmic reticulum-type Ca-2+-ATPase. · calcium ATPase · Ca[2+] ATPase · Calcium ATPase at 60A · organellar-type Ca-ATPase⌘
D. melanogasterUniProtKB:P13607 · FB:FBgn0002921 (ATPa · Na[+]K[+]ATPase · NaK · l(3)01453 · Na-p · dnATPase · Na[+]/K[+]ATPase · Na[+],K[+]-ATPase · ATPBagr · Da-47 · l(3)j3B7 · Na/K-ATPase · ATPalpha · CG5670 · l(3)j6A4 · Na+-K+-ATPase · l(3)ry136 · l(3)01164 · l(3)04492 · JY · Na,K-ATPase · l(3)rM454 · l(3)j3B2 · Atpalpha · Na[+]/K[+]-ATPase)Na[+],K[+]-ATPase alpha subunit · Na+,K+ ATPase alpha-subunit · alpha-subunit of ATPase · Na,K-ATPase alpha subunit · Na pump alpha subunit · Atp a · Na[+], K[+] -ATPase · Na/K-ATPase alpha-subunit · Na,K ATPase alpha subunit · (Na[+],K[+])ATPase alpha subunit · Na,K-ATPase alpha-subunit · Na[+],K[+] ATPase alpha subunit · Na[+],K[+]-ATPase alpha-subunit · sodium/potassium transporting ATPase alpha · (Na[+] + K[+])-ATPase alpha-subunit · ATPase alpha subunit · NaK ATPase · Na[+]-K[+] ATPase · Na,K ATPase · ATPase alpha · Na[+]/K[+] ATPase · Na+/K+ ATPase alpha subunit · Na[+]-K[+]-ATPase alpha[[5]]-subunit⌘
D. melanogasterFB:FBgn0033837 · UniProtKB:Q0E990
D. melanogasterFB:FBgn0052000 (BcDNA:SD17880 · BcDNA:LD05303 · BcDNA:LD19039 · CG32000) · UniProtKB:Q7KQN3⌘
D. melanogasterFB:FBgn0032120 (CG18419 · CG13112 · CG33298) · UniProtKB:Q7KTG6⌘
D. melanogasterUniProtKB:Q7KTU2 · FB:FBgn0052451 (SPoCK · CG32451 · anon-WO0118547.249 · CG7651 · SPoCk · CG14449)Secretory Pathway Calcium atpase⌘
D. melanogasterFB:FBgn0040037 (JYalpha · JYAlpha · CG17923) · UniProtKB:Q9U458⌘
D. melanogasterFB:FBgn0025704 · UniProtKB:Q9V4C7
D. melanogasterFB:FBgn0037989 (CG14741) · UniProtKB:Q9VGD4⌘
D. melanogasterFB:FBgn0051729 (CG6263 · CG16823 · CG31729) · UniProtKB:Q9VK06⌘
D. melanogasterFB:FBgn0030747 (CG4301) · UniProtKB:Q9VXG6⌘
D. melanogasterFB:FBgn0030746 (CG9981) · UniProtKB:Q9VXG7⌘
D. melanogasterFB:FBgn0030343 (CG1886 · dmATP7 · ATP7 · DmATP7) · UniProtKB:Q9VYT4⌘
D. melanogasterFB:FBgn0034732 (CG3701) · UniProtKB:Q9W248⌘
D. melanogasterFB:FBgn0027582 (dCOD1 · CG6230 · BcDNA:GH06032) · UniProtKB:Q9Y139⌘
E. coliUniProtKB:P03960 · ECOLI:KDPB-MONOMER (kac · ECK0685 · kdpB · KdpB · b0697)⌘
E. coliUniProtKB:P0ABB8 · ECOLI:MGTA-MONOMER (corB · b4242 · mtg · ECK4237 · mgtA · mgt · atmA · MgtA)magnesium transporter⌘
E. coliUniProtKB:P37617 · ECOLI:YHHO-MONOMER (zinc · b3469 · yhhO · B3469 · zntA · ZntA · ECK3453 · YhhO)cobalt and lead efflux system · zinc, cobalt and lead efflux system⌘
E. coliUniProtKB:Q59385 · ECOLI:G6260-MONOMER (b0484 · ECK0478 · B0484 · YbaR · CopA · ybaR · copA)YbaR Cu+-exporting ATPase · copper transporter · Cu+-exporting ATPase⌘
G. gallusNCBI:XP_423767 · ENTREZ:426090
G. gallusNCBI:XP_422713 · ENTREZ:424902
G. gallusNCBI:XP_429208 · ENTREZ:431656
G. gallusNCBI:XP_426010 · ENTREZ:428450
G. gallusNCBI:XP_422773 · ENTREZ:424964
G. gallusNCBI:XP_416948 · ENTREZ:418749
G. gallusNCBI:XP_420307 · ENTREZ:422333
G. gallusNCBI:XP_001231642 · ENTREZ:415958
G. gallusNCBI:XP_420240 · ENTREZ:422254
G. gallusNCBI:XP_416881 · ENTREZ:418685
G. gallusNCBI:XP_420729 · ENTREZ:422776
G. gallusNCBI:XP_414491 · ENTREZ:416159
G. gallusNCBI:XP_418055 · ENTREZ:419934
G. gallusNCBI:XP_422709 · ENTREZ:424898
G. gallusNCBI:XP_420722 · ENTREZ:422768
G. gallusNCBI:XP_425888 · ENTREZ:428328
G. gallusNCBI:XP_417073 · ENTREZ:418879
G. gallusNCBI:XP_001233350 · ENTREZ:770035
G. gallusNCBI:XP_416133 · ENTREZ:374244
G. gallusNCBI:XP_415130 · ENTREZ:396446
G. gallusNCBI:XP_422947 · ENTREZ:425155
G. gallusNCBI:XP_417130 · ENTREZ:418936
G. gallusNCBI:XP_417508 · ENTREZ:419345
G. gallusENTREZ:424901 · UniProtKB:Q5ZKB7 (RCJMB04_11o9 · Q5ZKB7 · AT134_CHICK · IPI00587863 · ATP13A4)Probable cation-transporting ATPase 13A4⌘
G. gallusENTREZ:396530 · UniProtKB:P09572 (P09572 · IPI00819216 · ATP1A1 · AT1A1_CHICK)Sodium/potassium-transporting ATPase subunit alpha-1⌘
G. gallusENTREZ:396468 · UniProtKB:P24797 (ATP1A2 · AT1A2_CHICK · IPI00583240 · P24797)Sodium/potassium-transporting ATPase subunit alpha-2⌘
G. gallusENTREZ:396467 · UniProtKB:P24798 (P24798 · AT1A3_CHICK · IPI00587236 · ATP1A3)Sodium/potassium-transporting ATPase subunit alpha-3⌘
G. gallusENTREZ:396528 · UniProtKB:P13585 (IPI00578635 · ATP2A1 · AT2A1_CHICK · P13585)Sarcoplasmic/endoplasmic reticulum calcium ATPase 1⌘
G. gallusENTREZ:395707 · UniProtKB:Q9YGL9 (IPI00599579 · ATP2A3 · Q9YGL9 · IPI00582754 · AT2A3_CHICK)Sarcoplasmic/endoplasmic reticulum calcium ATPase 3⌘
G. gallusUniProtKB:Q5F3F1 (RCJMB04_19b13 · IPI00594621 · Q5F3F1) · ENTREZ:419466⌘
G. gallusUniProtKB:Q5ZIK7 (RCJMB04_25f22 · IPI00594501 · Q5ZIK7) · ENTREZ:419743⌘
G. gallusUniProtKB:Q5ZKC0 (IPI00577670 · RCJMB04_11n22 · Q5ZKC0) · ENTREZ:420817⌘
H. sapiensENSEMBL:ENSG00000206190 · UniProtKB:O60312 (ATPVC · AT10A_HUMAN · IPI00783442 · O60312 · KIAA0566 · ATP10A · ATP10C)Probable phospholipid-transporting ATPase VA⌘
H. sapiensENSEMBL:ENSG00000118322 · UniProtKB:O94823 (ATPVB · O94823 · IPI00852619 · ATP10B · IPI00186385 · IPI00293928 · KIAA0715 · AT10B_HUMAN)Probable phospholipid-transporting ATPase VB⌘
H. sapiensENSEMBL:ENSG00000145246 · UniProtKB:Q9P241 (AT10D_HUMAN · IPI00216521 · IPI00001723 · ATP10D · Q9P241 · KIAA1487)Probable phospholipid-transporting ATPase VD⌘
H. sapiensENSEMBL:ENSG00000068650 · UniProtKB:P98196 (AT11A_HUMAN · ATP11A · ATPIS · KIAA1021 · ATPIH · P98196 · IPI00255653)Probable phospholipid-transporting ATPase IH⌘
H. sapiensENSEMBL:ENSG00000058063 · UniProtKB:Q9Y2G3 (ATPIF · IPI00240793 · ATP11B · AT11B_HUMAN · Q9Y2G3 · KIAA0956 · ATPIR)Probable phospholipid-transporting ATPase IF⌘
H. sapiensENSEMBL:ENSG00000101974 · UniProtKB:Q8NB49 (Q8NB49 · AT11C_HUMAN · IPI00396234 · ATP11C · IPI00555989 · IPI00237446 · IPI00552319 · ATPIG · ATPIQ)Probable phospholipid-transporting ATPase IG⌘
H. sapiensENSEMBL:ENSG00000075673 · UniProtKB:P54707 (P54707 · AT12A_HUMAN · ATP12A · IPI00008161 · ATP1AL1 · IPI00872242)Potassium-transporting ATPase alpha chain 2⌘
H. sapiensENSEMBL:ENSG00000105726 · UniProtKB:Q9HD20 (IPI00034277 · ATP13A1 · IPI00218354 · KIAA1825 · IPI00218353 · AT131_HUMAN · CGI-152 · Q9HD20 · ATP13A)Probable cation-transporting ATPase 13A1⌘
H. sapiensENSEMBL:ENSG00000159363 · UniProtKB:Q9NQ11 (AT132_HUMAN · IPI00015154 · Q9NQ11 · IPI00177535 · PARK9 · ATP13A2)Probable cation-transporting ATPase 13A2⌘
H. sapiensENSEMBL:ENSG00000133657 · UniProtKB:Q9H7F0 (Q9H7F0 · ATP13A3 · IPI00847139 · AT133_HUMAN · AFURS1 · IPI00177661)Probable cation-transporting ATPase 13A3⌘
H. sapiensENSEMBL:ENSG00000127249 · UniProtKB:Q4VNC1 (IPI00791950 · AT134_HUMAN · IPI00795895 · Q4VNC1 · IPI00166229 · IPI00746808 · UNQ3052/PRO9871 · ATP13A4)Probable cation-transporting ATPase 13A4⌘
H. sapiensENSEMBL:ENSG00000187527 · UniProtKB:Q4VNC0 (IPI00607633 · AT135_HUMAN · ATP13A5 · UNQ488/PRO1004 · Q4VNC0)Probable cation-transporting ATPase 13A5⌘
H. sapiensENSEMBL:ENSG00000163399 · UniProtKB:P05023 (IPI00414005 · AT1A1_HUMAN · IPI00006482 · ATP1A1 · P05023)Sodium/potassium-transporting ATPase subunit alpha-1⌘
H. sapiensENSEMBL:ENSG00000018625 · UniProtKB:P50993 (ATP1A2 · AT1A2_HUMAN · IPI00003021 · KIAA0778 · P50993)Sodium/potassium-transporting ATPase subunit alpha-2⌘
H. sapiensENSEMBL:ENSG00000105409 · UniProtKB:P13637 (IPI00302840 · AT1A3_HUMAN · P13637 · ATP1A3)Sodium/potassium-transporting ATPase subunit alpha-3⌘
H. sapiensENSEMBL:ENSG00000132681 · UniProtKB:Q13733 (AT1A4_HUMAN · ATP1A4 · Q13733 · IPI00375339 · IPI00252122 · ATP1AL2)Sodium/potassium-transporting ATPase subunit alpha-4⌘
H. sapiensENSEMBL:ENSG00000196296 · UniProtKB:O14983 (O14983 · AT2A1_HUMAN · IPI00024804 · ATP2A1 · IPI00396118)Sarcoplasmic/endoplasmic reticulum calcium ATPase 1⌘
H. sapiensENSEMBL:ENSG00000174437 · UniProtKB:P16615 (ATP2A2 · IPI00219078 · P16615 · IPI00177817 · ATP2B · AT2A2_HUMAN)Sarcoplasmic/endoplasmic reticulum calcium ATPase 2⌘
H. sapiensENSEMBL:ENSG00000074370 · UniProtKB:Q93084 (AT2A3_HUMAN · IPI00004092 · ATP2A3 · IPI00218442 · IPI00218440 · IPI00303760 · Q93084 · IPI00748794 · IPI00478023)Sarcoplasmic/endoplasmic reticulum calcium ATPase 3⌘
H. sapiensENSEMBL:ENSG00000070961 · UniProtKB:P20020 (IPI00216529 · IPI00216526 · ATP2B1 · IPI00021695 · IPI00216528 · PMCA1 · IPI00216530 · AT2B1_HUMAN · P20020 · IPI00216527)Plasma membrane calcium-transporting ATPase 1⌘
H. sapiensENSEMBL:ENSG00000157087 · UniProtKB:Q01814 (IPI00219295 · IPI00009791 · IPI00219294 · ATP2B2 · IPI00219293 · Q01814 · AT2B2_HUMAN · IPI00219297 · IPI00219296 · PMCA2)Plasma membrane calcium-transporting ATPase 2⌘
H. sapiensENSEMBL:ENSG00000067842 · UniProtKB:Q16720 (AT2B3_HUMAN · IPI00219258 · Q16720 · IPI00219262 · IPI00219257 · IPI00219260 · IPI00003831 · IPI00219256 · IPI00219259 · IPI00219261 · ATP2B3)Plasma membrane calcium-transporting ATPase 3⌘
H. sapiensENSEMBL:ENSG00000058668 · UniProtKB:P23634 (IPI00217168 · IPI00217169 · IPI00217166 · IPI00217171 · IPI00217164 · AT2B4_HUMAN · ATP2B2 · MXRA1 · ATP2B4 · IPI00012490 · IPI00217165 · P23634 · IPI00217170)Plasma membrane calcium-transporting ATPase 4⌘
H. sapiensENSEMBL:ENSG00000017260 · UniProtKB:P98194 (ATP2C1 · HUSSY-28 · IPI00413116 · IPI00220473 · IPI00745171 · IPI00607568 · IPI00607812 · IPI00419957 · KIAA1347 · PMR1L · P98194 · AT2C1_HUMAN)Calcium-transporting ATPase type 2C member 1⌘
H. sapiensENSEMBL:ENSG00000064270 · UniProtKB:O75185 (AT2C2_HUMAN · KIAA0703 · ATP2C2 · O75185 · IPI00915432 · IPI00006653 · SPCA2)Calcium-transporting ATPase type 2C member 2⌘
H. sapiensENSEMBL:ENSG00000124406 · UniProtKB:Q9Y2Q0 (ATP8A1 · IPI00221038 · ATPIA · Q9Y2Q0 · AT8A1_HUMAN · IPI00032402)Probable phospholipid-transporting ATPase IA⌘
H. sapiensENSEMBL:ENSG00000132932 · UniProtKB:Q9NTI2 (AT8A2_HUMAN · IPI00465166 · Q9NTI2 · ATP8A2 · ATPIB · IPI00337792)Probable phospholipid-transporting ATPase IB⌘
H. sapiensENSEMBL:ENSG00000081923 · UniProtKB:O43520 (PFIC · AT8B1_HUMAN · IPI00012851 · ATPIC · ATP8B1 · FIC1 · O43520)Probable phospholipid-transporting ATPase IC⌘
H. sapiensENSEMBL:ENSG00000143515 · UniProtKB:P98198 (AT8B2_HUMAN · IPI00396074 · KIAA1137 · P98198 · ATPID · ATP8B2 · IPI00258027)Probable phospholipid-transporting ATPase ID⌘
H. sapiensENSEMBL:ENSG00000130270 · UniProtKB:O60423 (AT8B3_HUMAN · IPI00237913 · ATP1K · IPI00216974 · FOS37502_2 · ATP8B3 · O60423)Probable phospholipid-transporting ATPase IK⌘
H. sapiensENSEMBL:ENSG00000104043 · UniProtKB:Q8TF62 (ATP8B4 · Q8TF62 · AT8B4_HUMAN · IPI00152868 · KIAA1939)Probable phospholipid-transporting ATPase IM⌘
H. sapiensENSEMBL:ENSG00000179766 · UniProtKB:Q4G129 (Q4G129 · IPI00644725 · AT8B5_HUMAN · FETA)Putative FetA-like protein⌘
H. sapiensENSEMBL:ENSG00000105675 · UniProtKB:P20648 (IPI00218919 · P20648 · ATP4A · ATP4A_HUMAN)Potassium-transporting ATPase alpha chain 1⌘
H. sapiensENSEMBL:ENSG00000165240 · UniProtKB:Q04656 (IPI00215614 · IPI00215617 · ATP7A_HUMAN · IPI00028610 · IPI00215619 · MC1 · Q04656 · IPI00215616 · ATP7A · MNK · IPI00215615)Copper-transporting ATPase 1⌘
H. sapiensENSEMBL:ENSG00000123191 · UniProtKB:P35670 (ATP7B_HUMAN · IPI00216296 · WC1 · IPI00658175 · PWD · IPI00515019 · P35670 · ATP7B · WND · IPI00020058)Copper-transporting ATPase 2⌘
H. sapiensENSEMBL:ENSG00000054793 · UniProtKB:O75110 (ATPIIA · ATP9A · O75110 · IPI00024368 · KIAA0611 · ATP9A_HUMAN · IPI00220239)Probable phospholipid-transporting ATPase IIA⌘
H. sapiensENSEMBL:ENSG00000166377 · UniProtKB:O43861 (IPI00396022 · ATP9B_HUMAN · O43861 · ATP9B · ATPIIB · NEO1L · HUSSY-20 · IPI00479667)Probable phospholipid-transporting ATPase IIB⌘
M. musculusNCBI:NP_998781 · MGI:MGI:88111 (Atp2b4 · PMCA4)ATPase, Ca++ transporting, plasma membrane 4⌘
M. musculusNCBI:NP_796210 · MGI:MGI:1347353 (Pmca3 · Atp2b3)ATPase, Ca++ transporting, plasma membrane 3⌘
M. musculusNCBI:NP_795973 · MGI:MGI:2442688
M. musculusNCBI:NP_083846 · MGI:MGI:1923545
M. musculusNCBI:NP_080758 · MGI:MGI:104653 (Atp2b1 · PMCA1)ATPase, Ca++ transporting, plasma membrane 1⌘
M. musculusNCBI:NP_001074413 · MGI:MGI:1859664 (Im · Atp8b4)ATPase, class I, type 8B, member 4⌘
M. musculusNCBI:NP_080370 · MGI:MGI:1914581 (SAPLT · Atp8b3)ATPase, class I, type 8B, member 3⌘
M. musculusNCBI:NP_001001488 · MGI:MGI:1859665 (Ic · FIC1 · Atp8b1)ATPase, class I, type 8B, member 1⌘
M. musculusUniProtKB:O54827 · MGI:MGI:1330809 (Atp10a · Atp10c · pfatp)ATPase, class V, type 10A⌘
M. musculusUniProtKB:Q8K2X1 · MGI:MGI:2450125 (IMAGE:1069176 · D5Buc24e · Atp10d)ATPase, class V, type 10D⌘
M. musculusUniProtKB:P98197 · MGI:MGI:1354735 (Atp11a · Ih)ATPase, class VI, type 11A⌘
M. musculusUniProtKB:Q9QZW0 · MGI:MGI:1859661 (Atp11c · Ig)ATPase, class VI, type 11C⌘
M. musculusUniProtKB:Q9Z1W8 · MGI:MGI:1926943 (Atp1al1 · Atp12a · HKalpha2 · cHKA)ATPase H+K+-transporting, alpha 2 · ATPase, H+/K+ transporting, nongastric, alpha polypeptide⌘
M. musculusUniProtKB:Q9EPE9 · MGI:MGI:2180801 (Atp13a · Cgi152 · Atp13a1 · catp)ATPase type 13A1⌘
M. musculusUniProtKB:Q9CTG6 · MGI:MGI:1922022 (Atp13a2)ATPase type 13A2⌘
M. musculusUniProtKB:Q5XF90 · MGI:MGI:1924456 (Atp13a4)ATPase type 13A4⌘
M. musculusUniProtKB:Q3TYU2 · MGI:MGI:2444068 (Atp13a5)ATPase type 13A5⌘
M. musculusUniProtKB:Q8VDN2 · MGI:MGI:88105 (Atpa-1 · Atp1a1)ATPase, Na+/K+ transporting, alpha 1 polypeptide⌘
M. musculusUniProtKB:Q6PIE5 · MGI:MGI:88106 (Atp1a2 · Atpa-3)ATPase, Na+/K+ transporting, alpha 2 polypeptide⌘
M. musculusUniProtKB:Q6PIC6 · MGI:MGI:88107 (Atp1a3 · Atpa-2)ATPase, Na+/K+ transporting, alpha 3 polypeptide⌘
M. musculusUniProtKB:Q9WV27 · MGI:MGI:1351335 (Atp1a4)ATPase, Na+/K+ transporting, alpha 4 polypeptide⌘
M. musculusUniProtKB:Q8R429 · MGI:MGI:105058 (SERCA1 · Atp2a1)ATPase, Ca++ transporting, cardiac muscle, fast twitch 1⌘
M. musculusUniProtKB:O55143 · MGI:MGI:88110 (D5Wsu150e · Atp2a2 · SERCA2)sarco/endoplasmic reticulum Ca2+-ATPase 2 · ATPase, Ca++ transporting, cardiac muscle, slow twitch 2⌘
M. musculusUniProtKB:Q64518 · MGI:MGI:1194503 (Serca3 · Atp2a3)ATPase, Ca++ transporting, ubiquitous⌘
M. musculusUniProtKB:Q9R0K7 · MGI:MGI:105368 (D6Abb2e · Atp2b2 · jog · PMCA2 · wms)ATPase, Ca++ transporting, plasma membrane 2⌘
M. musculusUniProtKB:Q80XR2 · MGI:MGI:1889008 (SPCA · PMR1 · Atp2c1 · ATP2C1A)ATPase, Ca++-sequestering⌘
M. musculusUniProtKB:A7L9Z8 · MGI:MGI:1916297 (Atp2c2)ATPase, Ca++ transporting, type 2C, member 2⌘
M. musculusUniProtKB:P70704 · MGI:MGI:1330848 (Atp3a2 · Atp8a1)ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1⌘
M. musculusUniProtKB:P98200 · MGI:MGI:1354710 (Atp8a2 · Ib)ATPase, aminophospholipid transporter-like, class I, type 8A, member 2⌘
M. musculusUniProtKB:P98199 · MGI:MGI:1859660 (Atp8b2 · Id)ATPase, class I, type 8B, member 2⌘
M. musculusUniProtKB:A3FIN4 · MGI:MGI:2444287 (4930417M19Rik)RIKEN cDNA 4930417M19 gene⌘
M. musculusUniProtKB:Q64436 · MGI:MGI:88113 (Atp4a)ATPase, H+/K+ exchanging, gastric, alpha polypeptide · H+K+-transporting alpha 1⌘
M. musculusUniProtKB:Q64430 · MGI:MGI:99400 (br · MNK · Atp7a)Menkes protein · ATPase, Cu++ transporting, alpha polypeptide⌘
M. musculusUniProtKB:Q64446 · MGI:MGI:103297 (WND · Atp7a · Atp7b)Wilson protein · ATPase, Cu++ transporting, beta polypeptide⌘
M. musculusUniProtKB:O70228 · MGI:MGI:1330826 (Atp9a · IIa)Class II · ATPase, class II, type 9A⌘
M. musculusUniProtKB:P98195 · MGI:MGI:1354757 (IIb · Atp9b)ATPase, class II, type 9B⌘
M. musculusNCBI:NP_001121568 · MGI:MGI:2685387 (LOC385637 · LOC224088 · LOC224087 · Atp13a3)ATPase type 13A3⌘
R. norvegicusNCBI:XP_001052983 · RGD:1596980 (LOC678704)hypothetical protein LOC678704⌘
R. norvegicusNCBI:XP_001053941 · RGD:1306792 (Atp13a5)ATPase type 13A5⌘
R. norvegicusNCBI:XP_214310 · RGD:1306033 (Atp13a1)ATPase type 13A1⌘
R. norvegicusNCBI:XP_224270 · RGD:1561428
R. norvegicusNCBI:XP_001072145 · RGD:1307977 (Atp13a2)ATPase type 13A2⌘
R. norvegicusNCBI:XP_001069520 · RGD:1592709 (LOC684238)similar to Probable phospholipid-transporting ATPase ID (ATPase class I type 8B member 2)⌘
R. norvegicusNCBI:XP_001053119 · RGD:1590881
R. norvegicusNCBI:XP_001076905 · RGD:1587460 (LOC691125)similar to Probable phospholipid-transporting ATPase ID (ATPase class I type 8B member 2)⌘
R. norvegicusNCBI:XP_221355 · RGD:1306927 (Atp13a4)ATPase type 13A4⌘
R. norvegicusNCBI:XP_341210 · RGD:1588541 (Atp10d)ATPase, class V, type 10D⌘
R. norvegicusNCBI:XP_223394 · RGD:1565036
R. norvegicusNCBI:XP_001070245 · RGD:1309619 (Atp8a1)ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1⌘
R. norvegicusNCBI:XP_001064261 · RGD:1308488 (Atp8b1)ATPase, Class I, type 8B, member 1⌘
R. norvegicusNCBI:XP_001062555 · RGD:1597731 (LOC685152)similar to Probable phospholipid-transporting ATPase ID (ATPase class I type 8B member 2)⌘
R. norvegicusNCBI:XP_001075555 · RGD:1308688 (Atp11a)ATPase, class VI, type 11A⌘
R. norvegicusRGD:620569 (Atp12a) · UniProtKB:P54708 (Atp1al1 · AT12A_RAT · Atp12a · P54708 · IPI00188119 · IPI00231462)ATPase, H+/K+ transporting, nongastric, alpha polypeptide · Potassium-transporting ATPase alpha chain 2⌘⌘
R. norvegicusRGD:2167 (Atp1a1) · UniProtKB:P06685 (IPI00326305 · AT1A1_RAT · Atp1a1 · P06685)ATPase, Na+/K+ transporting, alpha 1 polypeptide · Sodium/potassium-transporting ATPase subunit alpha-1⌘⌘
R. norvegicusUniProtKB:P06686 · RGD:2168 (Atp1a2)ATPase, Na+/K+ transporting, alpha 2 polypeptide⌘
R. norvegicusUniProtKB:P06687 · RGD:2169 (Atp1a3)ATPase, Na+/K+ transporting, alpha 3 polypeptide⌘
R. norvegicusUniProtKB:Q64541 · RGD:61952 (Atp1a4)ATPase, Na+/K+ transporting, alpha 4 polypeptide⌘
R. norvegicusUniProtKB:Q64578 · RGD:621293 (Atp2a1)ATPase, Ca++ transporting, cardiac muscle, fast twitch 1⌘
R. norvegicusRGD:2174 (Atp2a2) · UniProtKB:P11507 (P11507 · IPI00190020 · IPI00231369 · AT2A2_RAT · Atp2a2)ATPase, Ca++ transporting, cardiac muscle, slow twitch 2 · Sarcoplasmic/endoplasmic reticulum calcium ATPase 2⌘⌘
R. norvegicusRGD:2175 (Atp2a3) · UniProtKB:P18596 (P18596 · IPI00192914 · Atp2a3 · AT2A3_RAT)ATPase, Ca++ transporting, ubiquitous · Sarcoplasmic/endoplasmic reticulum calcium ATPase 3⌘⌘
R. norvegicusRGD:621303 (Atp2b1) · UniProtKB:P11505 (AT2B1_RAT · IPI00231267 · IPI00231271 · IPI00194873 · IPI00231268 · IPI00231269 · P11505 · Atp2b1 · IPI00231270)ATPase, Ca++ transporting, plasma membrane 1 · Plasma membrane calcium-transporting ATPase 1⌘⌘
R. norvegicusRGD:2176 (Atp2b2) · UniProtKB:P11506 (AT2B2_RAT · IPI00231310 · Atp2b2 · IPI00231315 · IPI00339139 · IPI00231316 · IPI00231309 · IPI00231313 · IPI00194875 · P11506 · IPI00231312 · IPI00339140 · IPI00231311 · IPI00231314 · IPI00339141)ATPase, Ca++ transporting, plasma membrane 2 · Plasma membrane calcium-transporting ATPase 2⌘⌘
R. norvegicusRGD:621304 (Atp2b3) · UniProtKB:Q64568 (IPI00567465 · IPI00231665 · IPI00231522 · IPI00231525 · IPI00213586 · Pmca3 · IPI00231524 · IPI00231523 · IPI00231666 · IPI00231519 · IPI00231520 · Q64568 · AT2B3_RAT · Atp2b3 · IPI00231521 · IPI00231526)ATPase, Ca++ transporting, plasma membrane 3 · Plasma membrane calcium-transporting ATPase 3⌘⌘
R. norvegicusRGD:621305 (Atp2b4) · UniProtKB:Q64542 (IPI00230911 · IPI00230910 · Q64542 · AT2B4_RAT · IPI00213557 · Atp2b4 · IPI00230912)ATPase, Ca++ transporting, plasma membrane 4 · Plasma membrane calcium-transporting ATPase 4⌘⌘
R. norvegicusRGD:621311 (Atp2c1) · UniProtKB:Q64566 (IPI00231405 · AT2C1_RAT · Q64566 · IPI00213585 · Atp2c1)ATPase, Ca++ transporting, type 2C, member 1 · Calcium-transporting ATPase type 2C member 1⌘⌘
R. norvegicusUniProtKB:Q8R4C1 · RGD:620647 (Atp2c2)ATPase, Ca++ transporting, type 2C, member 2⌘
R. norvegicusRGD:2177 (Atp4a) · UniProtKB:P09626 (Hka · ATP4A_RAT · Atp4a · IPI00365705 · P09626)ATPase, H+/K+ exchanging, alpha polypeptide · Potassium-transporting ATPase alpha chain 1⌘⌘
R. norvegicusUniProtKB:P70705 · RGD:2179 (Atp7a)ATPase, Cu++ transporting, alpha polypeptide⌘
R. norvegicusRGD:2180 (Atp7b) · UniProtKB:Q64535 (ATP7B_RAT · Pina · IPI00760123 · IPI00324094 · IPI00230869 · Q64535 · Atp7b · Wnd)ATPase, Cu++ transporting, beta polypeptide · Copper-transporting ATPase 2⌘⌘
R. norvegicusUniProtKB:O70128 · RGD:621421 (Atp9a)ATPase, class II, type 9A⌘
R. norvegicusUniProtKB:Q32Q02 · RGD:1306150 (Atp10a)ATPase, class V, type 10A⌘
R. norvegicusUniProtKB:Q4KLY5 · RGD:1306712 (Atp8b4)ATPase, class I, type 8B, member 4⌘
R. norvegicusUniProtKB:Q5RJS7 · RGD:1561719 (Atp11b)ATPase, class VI, type 11B⌘
R. norvegicusUniProtKB:Q5XFX3 · RGD:1563006 (Atp9b)ATPase, class II, type 9B⌘
R. norvegicusUniProtKB:Q6TQG0 (Q6TQG0 · IPI00765545 · LOC292449) · RGD:1359441 (LOC292449)similar to hypothetical protein⌘⌘
R. norvegicusNCBI:XP_234937 · RGD:1307622 (Atp8b3)ATPase, Class I, type 8B, member 3⌘
R. norvegicusNCBI:XP_220314 · RGD:1565126 (Atp10b)ATPase, class V, type 10B⌘
S. cerevisiaeUniProtKB:P13586 · SGD:S000003135 (YGL167C · LDB1 · BSD1 · PMR1 · SSC1)High affinity Ca2+/Mn2+ P-type ATPase required for Ca2+ and Mn2+ transport into Golgi⌘
S. cerevisiaeUniProtKB:P38929 · SGD:S000002974 (PMC1 · YGL006W)Vacuolar Ca2+ ATPase involved in depleting cytosol of Ca2+ ions⌘
S. cerevisiaeUniProtKB:P39524 · SGD:S000000024 (FUN38 · DRS2 · SWA3 · YAL026C)Aminophospholipid translocase (flippase) that maintains membrane lipid asymmetry in post-Golgi secretory vesicles⌘
S. cerevisiaeUniProtKB:Q12675 · SGD:S000002500 (YDR093W · DNF2)Aminophospholipid translocase (flippase) that localizes primarily to the plasma membrane⌘
S. cerevisiaeUniProtKB:P32660 · SGD:S000000968 (DNF1 · YER166W)Aminophospholipid translocase (flippase) that localizes primarily to the plasma membrane⌘
S. cerevisiaeUniProtKB:P39986 · SGD:S000000757 (COD1 · YEL031W · PIO1 · SPF1 · PER9)P-type ATPase, ion transporter of the ER membrane involved in ER function and Ca2+ homeostasis⌘
S. cerevisiaeUniProtKB:P40527 · SGD:S000001310 (YIL048W · NEO1)Putative aminophospholipid translocase (flippase) involved in endocytosis and vacuolar biogenesis⌘
S. cerevisiaeUniProtKB:Q12674 · SGD:S000004772 (DNF3 · YMR162C)Aminophospholipid translocase (flippase) that maintains membrane lipid asymmetry in post-Golgi secretory vesicles⌘
S. cerevisiaeUniProtKB:Q12697 · SGD:S000005817 (YOR291W · YPK9)Vacuolar protein with a possible role in sequestering heavy metals⌘
S. cerevisiaeUniProtKB:P13587 · SGD:S000002447 (HOR6 · PMR2 · YDR040C · ENA1)P-type ATPase sodium pump, involved in Na+ and Li+ efflux to allow salt tolerance⌘
S. cerevisiaeUniProtKB:Q01896 · SGD:S000002446 (YDR039C · ENA2)P-type ATPase sodium pump, involved in Na+ efflux to allow salt tolerance⌘
S. cerevisiaeUniProtKB:Q12691 · SGD:S000002445 (YDR038C · ENA5)Protein with similarity to P-type ATPase sodium pumps, member of the Na+ efflux ATPase family⌘
S. cerevisiaeUniProtKB:P38360 · SGD:S000000499 (YBR295W · PAY2 · CAD2 · PCA1)Cadmium transporting P-type ATPase⌘
S. cerevisiaeUniProtKB:P38995 · SGD:S000002678 (CCC2 · YDR270W)Cu(+2)-transporting P-type ATPase, required for export of copper from the cytosol into an extracytosolic compartment⌘
S. cerevisiaeUniProtKB:P05030 · SGD:S000002976 (PMA1 · YGL008C · KTI10)Plasma membrane H+-ATPase, pumps protons out of the cell⌘
S. cerevisiaeUniProtKB:P19657 · SGD:S000005957 (YPL036W · PMA2)Plasma membrane H+-ATPase, isoform of Pma1p, involved in pumping protons out of the cell⌘
S. pombeUniProtKB:O59868 · GeneDB_Spombe:SPBC31E1.02c (SPBC31E1.02c · pmr1)P-type ATPase, calcium transporting Pmr1⌘
S. pombeUniProtKB:P22189 · GeneDB_Spombe:SPBC839.06 (SPBC839.06 · cta3)P-type ATPase, calcium transporting Cta3⌘
S. pombeUniProtKB:O14072 · GeneDB_Spombe:SPACUNK4.07c (sev4 · SPAPYUK71.01 · cta4 · SPACUNK4.07c)P-type ATPase, calcium transporting Cta4⌘
S. pombeUniProtKB:O74431 · GeneDB_Spombe:SPCC1672.11c (SPCC1672.11c)P-type ATPase⌘
S. pombeUniProtKB:Q09891 · GeneDB_Spombe:SPAC24B11.12c (SPAC24B11.12c)P-type ATPase⌘
S. pombeUniProtKB:O14022 · GeneDB_Spombe:SPAC29A4.19c (cta5 · SPAC29A4.19c)Ca2+/Mn2+ transporting P-type ATPase Cta5⌘
S. pombeUniProtKB:O36028 · GeneDB_Spombe:SPAC4F10.16c (SPAC4F10.16c)P-type ATPase⌘
S. pombeUniProtKB:O59666 · GeneDB_Spombe:SPBC29A3.01 (SPBC29A3.01 · ccc2)copper transporting ATPase Ccc2⌘
S. pombeUniProtKB:P09627 · GeneDB_Spombe:SPAC1071.10c (SPAC1071.10c · pma1)P-type proton ATPase Pma1⌘
S. pombeUniProtKB:P28876 · GeneDB_Spombe:SPCC1020.01c (pma2 · SPCC1020.01c · SPCC1393.01)P-type proton ATPase Pma2⌘
S. pombeUniProtKB:Q10309 · GeneDB_Spombe:SPAC6C3.06c (SPAC6C3.06c)P-type ATPase, calcium transporting⌘
S. pombeUniProtKB:Q9UT43 · GeneDB_Spombe:SPAC821.13c (SPAC821.13c · SPAC955.01c)P-type ATPase⌘
S. pombeUniProtKB:O94296 · GeneDB_Spombe:SPBC887.12 (SPBC887.12)P-type ATPase⌘
S. pombeUniProtKB:Q9HDW7 · GeneDB_Spombe:SPAPB2B4.04c (pmc1 · SPAPB2B4.04c)P-type ATPase, calcium transporting Pmc1⌘
ProteinPublicationCurator Notes
UniProtKB:P13586 · SGD:S000003135PMID:16088881 Soriani FM, et al. A PMR1-like calcium ATPase of Aspergillus fumigatus: cloning, identification and functional expression in S. cerevisiae. Yeast. 2005 Jul 30;22(10):813-24.The A. fumigatus protein Afpmr1 complements a homologous mutation in S. cerevisiae. This paper shows that A. fumigatus Afpmr1 complements a yeast pmr1 pmc1 cnb1 triple mutant, indicating that it encodes a Ca(2+) ATPase. A. fumigatus Afpmr1 contains all the conserved subdomains found in P-type ATPases such as yeast Pmr1p, and therefore it appears to be a PMR1-like calcium ATPase.
UniProtKB:P13586 · SGD:S000003135PMID:9238019 Liang F, et al. ECA1 complements yeast mutants defective in Ca2+ pumps and encodes an endoplasmic reticulum-type Ca2+-ATPase in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8579-84.The A. thaliana protein AT1G07810.1 complements a homologous mutation in S. cerevisiae. This paper shows that A. thaliana AT1G07810.1 complements a yeast pmr1 mutant, indicating that it functions as a Ca(2+) pump, and also suppresses a triple mutant (pmr1 pmc1 cnb 1) deficient in Golgi and vacuolar Ca(2+) pumps and calcineurin B.
UniProtKB:P13586 · SGD:S000003135PMID:9808725 Liang F, et al. A high-affinity Ca2+ pump, ECA1, from the endoplasmic reticulum is inhibited by cyclopiazonic acid but not by thapsigargin. Plant Physiol. 1998 Nov;118(3):817-25.The A. thaliana protein AT1G07810.1 complements a homologous mutation in S. cerevisiae. This paper shows A. thaliana ECA1 (AT1G07810.1) is a Ca2+-ATPase homolog that complements a yeast pmc1 pmr1 cnb1 triple mutant, deficient in Ca(2+) pumps, indicating that ECA1 encodes a functional Ca2+-ATPase. The triple mutant includes cnb1 which encodes the protein phosphatase calcineurin B, but the triple mutant was used to test for Ca2+-pump activity, not protein phosphatase activity.
UniProtKB:P13586 · SGD:S000003135PMID:11115896 Geisler M, et al. The ACA4 gene of Arabidopsis encodes a vacuolar membrane calcium pump that improves salt tolerance in yeast. Plant Physiol. 2000 Dec;124(4):1814-27.The A. thaliana protein AT2G41560.1 complements a homologous mutation in S. cerevisiae. This paper shows that AT2G41560.1 (ACA4) functions as a Ca2+ Pump, but only an N-terminally modified form of ACA4 rescues a yeast pmr1 pmc1 cnb1 triple mutant. The truncation of the N-terminal region seems to transfer ACA4 into an activated state.
UniProtKB:P13586 · SGD:S000003135PMID:15197266 Schiøtt M, et al. A plant plasma membrane Ca2+ pump is required for normal pollen tube growth and fertilization. Proc Natl Acad Sci U S A. 2004 Jun 22;101(25):9502-7.The A. thaliana protein AT3G21180.1 complements a homologous mutation in S. cerevisiae. An N-terminally modified form of AT3G21180.1 (ACA9) complements a yeast mutant devoid of Ca2+-ATPases (i.e. pmr1 pmc1 cnb1), demonstrating the Ca2+-ATPase activity of AT3G21180.1.
UniProtKB:P13586 · SGD:S000003135PMID:15623514 Ramos-Castañeda J, et al. Deficiency of ATP2C1, a Golgi ion pump, induces secretory pathway defects in endoplasmic reticulum (ER)-associated degradation and sensitivity to ER stress. J Biol Chem. 2005 Mar 11;280(10):9467-73.The R. norvegicus protein ATP2C1 complements a homologous mutation in S. cerevisiae. The authors only used a yeast pmr1 mutant.
UniProtKB:P13586 · SGD:S000003135PMID:11741891 Ton VK, et al. Functional expression in yeast of the human secretory pathway Ca(2+), Mn(2+)-ATPase defective in Hailey-Hailey disease. J Biol Chem. 2002 Feb 22;277(8):6422-7.The H. sapiens protein P98194 complements a homologous mutation in S. cerevisiae. Human ATP2C1/hSPCA1 complements the yeast triple mutant (pmr1 pmc1 cnb1) deficient in the Golgi and vacuolar Ca(2+) pumps. In this study, ATP2C1/hSPCA1 also transports Ca2+ and Mn2+ with a high affinity similar to yeast PMR1 which was also re-introduced into the triple mutant in a separate complementation experiment. Human ATP2C1/hSPCA1 appears to be the functional homolog of yeast PMR1.
UniProtKB:P13586 · SGD:S000003135PMID:15610533 Ton VK, et al. Expression of Hailey-Hailey disease mutations in yeast. J Invest Dermatol. 2004 Dec;123(6):1192-4.The H. sapiens protein P98194 complements a homologous mutation in S. cerevisiae. This paper shows that human ATP2C1 complements a yeast pmr1 pmc1 cnb1 triple mutant lacking endogenouse calcium pumps, however, human ATP2C1 shows greater homology to yeast PMR1.
UniProtKB:P13586 · SGD:S000003135PMID:15811312 Kellermayer R. Hailey-Hailey disease as an orthodisease of PMR1 deficiency in Saccharomyces cerevisiae. FEBS Lett. 2005 Apr 11;579(10):2021-5.The H. sapiens protein P98194 complements a homologous mutation in S. cerevisiae. Human ATP2C1 complements a yeast pmr1 mutant.
UniProtKB:P13586 · SGD:S000003135PMID:10948258 Chung WS, et al. Identification of a calmodulin-regulated soybean Ca(2+)-ATPase (SCA1) that is located in the plasma membrane. Plant Cell. 2000 Aug;12(8):1393-407.The G. max protein SCA1 complements a homologous mutation in S. cerevisiae. This papers shows that soybean SCA1 (Q9FVE8_SOYBN) encodes a Ca(2+)-ATPase and complements complements a yeast pmc1 pmr1 cnb1 triple mutant, deficient in Ca(2+) pumps, indicating that ECA1 encodes a functional Ca2+-ATPase. The triple mutant includes cnb1 which encodes the protein phosphatase calcineurin B, but the triple mutant was used to test for Ca2+-pump activity, not protein phosphatase activity.
UniProtKB:P13586 · SGD:S000003135PMID:10027971 Degand I, et al. Rabbit sarcoplasmic reticulum Ca(2+)-ATPase replaces yeast PMC1 and PMR1 Ca(2+)-ATPases for cell viability and calcineurin-dependent regulation of calcium tolerance. Mol Microbiol. 1999 Jan;31(2):545-56.The O. cuniculus protein SERCA1a complements a homologous mutation in S. cerevisiae. This paper shows that the rabbit SERCA1a Ca(2+)-ATPase complements yeast pmr1 pmc1 cnb1 and pmr1 pmc1 vcx1 triple mutants.
UniProtKB:P13586 · SGD:S000003135PMID:11382780 Furuya T, et al. TcSCA complements yeast mutants defective in Ca2+ pumps and encodes a Ca2+-ATPase that localizes to the endoplasmic reticulum of Trypanosoma cruzi. J Biol Chem. 2001 Aug 31;276(35):32437-45.The T. cruzi protein TcSCA complements a homologous mutation in S. cerevisiae. This paper shows that T. cruzi TcSCA contains several sequence motifs found in Ca2+-ATPases and that it complements a yeast triple mutant (pmr1 pmc1 cnb 1) deficient in the Ca(2+) pumps, indicating that TsSCA encodes a functional Ca2+-ATPase.
UniProtKB:P38929 · SGD:S000002974PMID:9238019 Liang F, et al. ECA1 complements yeast mutants defective in Ca2+ pumps and encodes an endoplasmic reticulum-type Ca2+-ATPase in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8579-84.The A. thaliana protein AT1G07810.1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows that A. thaliana AT1G07810.1 suppresses the phenotype associated with the yeast triple mutant (pmr1 pmc1 cnb1) which is deficient in golgi and vacuolar Ca(2+) pumps and calcineurin B.
UniProtKB:P38929 · SGD:S000002974PMID:9808725 Liang F, et al. A high-affinity Ca2+ pump, ECA1, from the endoplasmic reticulum is inhibited by cyclopiazonic acid but not by thapsigargin. Plant Physiol. 1998 Nov;118(3):817-25.The A. thaliana protein AT1G07810.1 complements a homologous mutation in S. cerevisiae. This paper shows A. thaliana ECA1 (AT1G07810.1) is a Ca2+-ATPase homolog that complements a yeast pmc1 pmr1 cnb1 triple mutant, deficient in Ca(2+) pumps, indicating that ECA1 encodes a functional Ca2+-ATPase. The triple mutant includes cnb1 which encodes the protein phosphatase calcineurin B, but the triple mutant was used to test for Ca2+-pump activity, not protein phosphatase activity.
UniProtKB:P38929 · SGD:S000002974PMID:16244156 Park S, et al. Increased calcium levels and prolonged shelf life in tomatoes expressing Arabidopsis H+/Ca2+ transporters. Plant Physiol. 2005 Nov;139(3):1194-206.The A. thaliana protein AT2G38170.3 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows that a modified form of CAX1 (AT2G38170.3) suppresses a yeast pmc1 cnb vcx1 triple mutant deficient in vacuolar Ca2+ transporters and lacking functional calcineurin.
UniProtKB:P38929 · SGD:S000002974PMID:11115896 Geisler M, et al. The ACA4 gene of Arabidopsis encodes a vacuolar membrane calcium pump that improves salt tolerance in yeast. Plant Physiol. 2000 Dec;124(4):1814-27.The A. thaliana protein AT2G41560.1 complements a homologous mutation in S. cerevisiae. This paper shows that AT2G41560.1 (ACA4) functions as a Ca2+ Pump, but only an N-terminally modified form of ACA4 rescues a yeast pmr1 pmc1 cnb1 triple mutant. The truncation of the N-terminal region seems to transfer ACA4 into an activated state.
UniProtKB:P38929 · SGD:S000002974PMID:15197266 Schiøtt M, et al. A plant plasma membrane Ca2+ pump is required for normal pollen tube growth and fertilization. Proc Natl Acad Sci U S A. 2004 Jun 22;101(25):9502-7.The A. thaliana protein AT3G21180.1 complements a homologous mutation in S. cerevisiae. An N-terminally modified form of AT3G21180.1 (ACA9) complements a yeast mutant devoid of Ca2+-ATPases (i.e. pmr1 pmc1 cnb1), demonstrating the Ca2+-ATPase activity of AT3G21180.1.
UniProtKB:P38929 · SGD:S000002974PMID:10948258 Chung WS, et al. Identification of a calmodulin-regulated soybean Ca(2+)-ATPase (SCA1) that is located in the plasma membrane. Plant Cell. 2000 Aug;12(8):1393-407.The G. max protein SCA1 complements a homologous mutation in S. cerevisiae. This papers shows that soybean SCA1 (Q9FVE8_SOYBN) encodes a Ca(2+)-ATPase and complements complements a yeast pmc1 pmr1 cnb1 triple mutant, deficient in Ca(2+) pumps, indicating that ECA1 encodes a functional Ca2+-ATPase. The triple mutant includes cnb1 which encodes the protein phosphatase calcineurin B, but the triple mutant was used to test for Ca2+-pump activity, not protein phosphatase activity.
UniProtKB:P38929 · SGD:S000002974PMID:10027971 Degand I, et al. Rabbit sarcoplasmic reticulum Ca(2+)-ATPase replaces yeast PMC1 and PMR1 Ca(2+)-ATPases for cell viability and calcineurin-dependent regulation of calcium tolerance. Mol Microbiol. 1999 Jan;31(2):545-56.The O. cuniculus protein SERCA1a complements a homologous mutation in S. cerevisiae. This paper shows that the rabbit SERCA1a Ca(2+)-ATPase complements yeast pmr1 pmc1 cnb1 and pmr1 pmc1 vcx1 triple mutants.
UniProtKB:P38929 · SGD:S000002974PMID:14724285 Luo S, et al. Trypanosoma brucei plasma membrane-type Ca(2+)-ATPase 1 (TbPMC1) and 2 (TbPMC2) genes encode functional Ca(2+)-ATPases localized to the acidocalcisomes and plasma membrane, and essential for Ca(2+) homeostasis and growth. J Biol Chem. 2004 Apr 2;279(14):14427-39.The T. brucei protein TbPMC1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows that complementing the yeast double mutant vcx1 pmc1 with T. brucei TbPMC1 results in essentially the same phenotype as a vcx1 yeast mutant with endogenous PMC1, indicating that TbPMC1 functions as a calcium ATPase.
UniProtKB:P38929 · SGD:S000002974PMID:14724285 Luo S, et al. Trypanosoma brucei plasma membrane-type Ca(2+)-ATPase 1 (TbPMC1) and 2 (TbPMC2) genes encode functional Ca(2+)-ATPases localized to the acidocalcisomes and plasma membrane, and essential for Ca(2+) homeostasis and growth. J Biol Chem. 2004 Apr 2;279(14):14427-39.The T. brucei protein TbPMC2 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows that T. brucei TbPMC2 partially suppresses a yeast vcx1 pmc1 double mutant indicating that TbPMC2 functions as a calcium ATPase.
UniProtKB:P38929 · SGD:S000002974PMID:9528801 Lu HG, et al. Ca2+ content and expression of an acidocalcisomal calcium pump are elevated in intracellular forms of Trypanosoma cruzi. Mol Cell Biol. 1998 Apr;18(4):2309-23.The T. cruzi protein tca1 complements a homologous mutation in S. cerevisiae. T. cruzi tca1 complements a yeast pmc1 vcx1 mutant and exhibits the same phenotype as a yeast vcx1 mutant alone with wildtype PMC1, suggesting that tca1 functionally complements pmc1.
UniProtKB:P38929 · SGD:S000002974PMID:11382780 Furuya T, et al. TcSCA complements yeast mutants defective in Ca2+ pumps and encodes a Ca2+-ATPase that localizes to the endoplasmic reticulum of Trypanosoma cruzi. J Biol Chem. 2001 Aug 31;276(35):32437-45.The T. cruzi protein TcSCA complements a homologous mutation in S. cerevisiae. This paper shows that T. cruzi TcSCA contains several sequence motifs found in Ca2+-ATPases and that it complements a yeast triple mutant (pmr1 pmc1 cnb 1) deficient in the Ca(2+) pumps, indicating that TsSCA encodes a functional Ca2+-ATPase.
UniProtKB:P38929 · SGD:S000002974PMID:15610533 Ton VK, et al. Expression of Hailey-Hailey disease mutations in yeast. J Invest Dermatol. 2004 Dec;123(6):1192-4.The H. sapiens protein P98194 complements a homologous mutation in S. cerevisiae. This paper shows that human ATP2C1 complements a yeast pmr1 pmc1 cnb1 triple mutant lacking endogenouse calcium pumps, however, human ATP2C1 shows greater homology to yeast PMR1.
UniProtKB:P38929 · SGD:S000002974PMID:16244156 Park S, et al. Increased calcium levels and prolonged shelf life in tomatoes expressing Arabidopsis H+/Ca2+ transporters. Plant Physiol. 2005 Nov;139(3):1194-206.The A. thaliana protein AT5G01490.1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows that a modified form of CAX4 (AT5G01490.1) suppresses a yeast pmc1 cnb vcx1 triple mutant deficient in vacuolar Ca2+ transporters and lacking functional calcineurin.
UniProtKB:P39524 · SGD:S000000024PMID:11148289 Gomès E, et al. Chilling tolerance in Arabidopsis involves ALA1, a member of a new family of putative aminophospholipid translocases. Plant Cell. 2000 Dec;12(12):2441-2454.The A. thaliana protein AT5G67260.1 complements a homologous mutation in S. cerevisiae. A. thaliana CYCD3 (AT5G67260.1) is able to complement a yeast cln1 cln2 cln3 triple mutant.
UniProtKB:P39986 · SGD:S000000757PMID:12058017 Cronin SR, et al. Cod1p/Spf1p is a P-type ATPase involved in ER function and Ca2+ homeostasis. J Cell Biol. 2002 Jun 10;157(6):1017-28.The D. melanogaster protein CG6230-PA complements a homologous mutation in S. cerevisiae.
UniProtKB:P13587 · SGD:S000002447PMID:9430707 Bañuelos MA, et al. P-type ATPases mediate sodium and potassium effluxes in Schwanniomyces occidentalis. J Biol Chem. 1998 Jan 16;273(3):1640-6.The S. occidentalis protein ENA1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P13587 · SGD:S000002447PMID:14991656 Nakayama H, et al. Yeast plasma membrane Ena1p ATPase alters alkali-cation homeostasis and confers increased salt tolerance in tobacco cultured cells. Biotechnol Bioeng. 2004 Mar 30;85(7):776-89.The S. cerevisiae protein ENA1 was expressed in N. tabacum, but complementation was not directly tested. This paper describes functional expression of yeast ENA1 in tobacco.
UniProtKB:P13587 · SGD:S000002447PMID:15702539 Kinclová-Zimmermannová O, et al. Rice Na+/H+-antiporter Nhx1 partially complements the alkali-metal-cation sensitivity of yeast strains lacking three sodium transporters. Folia Microbiol (Praha). 2004;49(5):519-25.The O. sativa protein NHX1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows that rice NHX1 partially restores growth to a yeast ena1 ena2 nha1 nhx1 mutant grown in high salt.
UniProtKB:P13587 · SGD:S000002447PMID:15907686 Brini F, et al. Cloning and characterization of a wheat vacuolar cation/proton antiporter and pyrophosphatase proton pump. Plant Physiol Biochem. 2005 Apr;43(4):347-54.The T. aestivum protein TVP1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P13587 · SGD:S000002447PMID:16232587 Watanabe Y, et al. Characterization of the Na+-ATPase gene (ZENA1) from the salt-tolerant yeast Zygosaccharomyces rouxii. J Biosci Bioeng. 1999;88(2):136-42.The Z. rouxii protein ZENA1 complements a homologous mutation in S. cerevisiae. This paper shows that ZENA1 can restore growth to a yeast ena1 ena2 mutant grown in high salt.
UniProtKB:P13587 · SGD:S000002447PMID:16303259 Velkova K, et al. The Debaryomyces hansenii NHA1 gene encodes a plasma membrane alkali-metal-cation antiporter with broad substrate specificity. Gene. 2006 Mar 15;369:27-34.The D. hansenii protein DhNHA1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows functional expression of D. hansenii DhNHA1 in an S. cerevisiae ena1 nha1 double mutant.
UniProtKB:P13587 · SGD:S000002447PMID:17311588 Montiel V, et al. Intracellular Na and K distribution in Debaryomyces hansenii. Cloning and expression in Saccharomyces cerevisiae of DhNHX1. FEMS Yeast Res. 2007 Jan;7(1):102-9.The D. hansenii protein DhNHX1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows functional expression of DhNHX1 in a yeast ena1-4 nhx1 nha1 mutant.
UniProtKB:P13587 · SGD:S000002447PMID:9238019 Liang F, et al. ECA1 complements yeast mutants defective in Ca2+ pumps and encodes an endoplasmic reticulum-type Ca2+-ATPase in Arabidopsis thaliana. Proc Natl Acad Sci U S A. 1997 Aug 5;94(16):8579-84.The A. thaliana protein AT1G07810.1 does not complement a homologous mutation in S. cerevisiae. This paper shows that A. thaliana AT1G07810.1 does not complement a yeast ena1 (alias pmr2) null mutant and does not function as a Na+ and Li+ efflux pump.
UniProtKB:Q01896 · SGD:S000002446PMID:15702539 Kinclová-Zimmermannová O, et al. Rice Na+/H+-antiporter Nhx1 partially complements the alkali-metal-cation sensitivity of yeast strains lacking three sodium transporters. Folia Microbiol (Praha). 2004;49(5):519-25.The O. sativa protein NHX1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows that rice NHX1 partially restores growth to a yeast ena1 ena2 nha1 nhx1 mutant grown in high salt.
UniProtKB:Q01896 · SGD:S000002446PMID:16232587 Watanabe Y, et al. Characterization of the Na+-ATPase gene (ZENA1) from the salt-tolerant yeast Zygosaccharomyces rouxii. J Biosci Bioeng. 1999;88(2):136-42.The Z. rouxii protein ZENA1 complements a homologous mutation in S. cerevisiae. This paper shows that ZENA1 can restore growth to a yeast ena1 ena2 mutant grown in high salt.
UniProtKB:P38360 · SGD:S000000499PMID:11035780 Rogers EE, et al. Altered selectivity in an Arabidopsis metal transporter. Proc Natl Acad Sci U S A. 2000 Oct 24;97(22):12356-60.The A. thaliana proteins AT4G19690.1 and AT4G19690.2 complement a homologous mutation in S. cerevisiae. A. thaliana IRT1 confers cadmium sensitivity to yeast strain DY1457; many lab strains lack a functional form of the cadmium transporter Pca1p. IRT1 is also shown to transport iron, manganese, and zinc.
UniProtKB:P38995 · SGD:S000002678PMID:11373292 Voskoboinik I, et al. The regulation of catalytic activity of the menkes copper-translocating P-type ATPase. Role of high affinity copper-binding sites. J Biol Chem. 2001 Jul 27;276(30):28620-7.The H. sapiens protein Q04656 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38995 · SGD:S000002678PMID:16826513 Paulsen M, et al. Evidence that translation reinitiation leads to a partially functional Menkes protein containing two copper-binding sites. Am J Hum Genet. 2006 Aug;79(2):214-29.The H. sapiens protein Q04656 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38995 · SGD:S000002678PMID:15147898 Southron JL, et al. Complementation of Saccharomyces cerevisiae ccc2 mutant by a putative P1B-ATPase from Brassica napus supports a copper-transporting function. FEBS Lett. 2004 May 21;566(1-3):218-22.The B. napus protein BRRAN1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38995 · SGD:S000002678PMID:9261163 Hung IH, et al. Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae. J Biol Chem. 1997 Aug 22;272(34):21461-6.The H. sapiens protein P35670 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38995 · SGD:S000002678PMID:10942420 Forbes JR, et al. Copper-dependent trafficking of Wilson disease mutant ATP7B proteins. Hum Mol Genet. 2000 Aug 12;9(13):1927-35.The H. sapiens protein P35670 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows the localization of human variant ATP7B proteins in yeast.
UniProtKB:P38995 · SGD:S000002678PMID:14962673 Hsi G, et al. Functional assessment of the carboxy-terminus of the Wilson disease copper-transporting ATPase, ATP7B. Genomics. 2004 Mar;83(3):473-81.The H. sapiens protein P35670 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38995 · SGD:S000002678PMID:15963506 Portmann R, et al. Purification and functional reconstitution of the human Wilson copper ATPase, ATP7B. FEBS Lett. 2005 Jul 4;579(17):3589-95.The H. sapiens protein P35670 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38995 · SGD:S000002678PMID:9452509 Payne AS, et al. Functional expression of the menkes disease protein reveals common biochemical mechanisms among the copper-transporting P-type ATPases. J Biol Chem. 1998 Feb 6;273(6):3765-70.The H. sapiens protein Q04656 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38995 · SGD:S000002678PMID:12572677 Mercer JF, et al. Copper-induced trafficking of the cU-ATPases: a key mechanism for copper homeostasis. Biometals. 2003 Mar;16(1):175-84.The H. sapiens protein Q04656 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38995 · SGD:S000002678PMID:9354393 Sambongi Y, et al. Caenorhabditis elegans cDNA for a Menkes/Wilson disease gene homologue and its function in a yeast CCC2 gene deletion mutant. J Biochem. 1997 Jun;121(6):1169-75.The C. elegans protein Y76A2A.2 complements a homologous mutation in S. cerevisiae.
UniProtKB:P05030 · SGD:S000002976PMID:7580256 Regenberg B, et al. C-terminal deletion analysis of plant plasma membrane H(+)-ATPase: yeast as a model system for solute transport across the plant plasma membrane. Plant Cell. 1995 Oct;7(10):1655-66.The A. thaliana protein AT4G30190.1 complements a homologous mutation in S. cerevisiae. This paper shows that wild-type AHA2 does not complement a pma1 mutant, but certain deletion mutants of AHA2 do complement.
UniProtKB:P05030 · SGD:S000002976PMID:8425607 Palmgren MG, et al. Complementation in situ of the yeast plasma membrane H(+)-ATPase gene pma1 by an H(+)-ATPase gene from a heterologous species. FEBS Lett. 1993 Feb 15;317(3):216-22.The A. thaliana protein AT4G30190.1 complements a homologous mutation in S. cerevisiae. This paper shows that a truncated form of A. thaliana AHA2 complements a yeast pma1 mutant.
UniProtKB:P05030 · SGD:S000002976PMID:10353834 Axelsen KB, et al. Molecular dissection of the C-terminal regulatory domain of the plant plasma membrane H+-ATPase AHA2: mapping of residues that when altered give rise to an activated enzyme. Biochemistry. 1999 Jun 1;38(22):7227-34.The A. thaliana protein AT4G30190.1 complements a homologous mutation in S. cerevisiae. This paper shows that wild-type AHA2 does not complement a pma1 mutant, but mutants of AHA2 lacking the C-terminal domain or with key residues mutated do complement.
UniProtKB:P05030 · SGD:S000002976PMID:11744700 Jahn TP, et al. Post-translational modification of plant plasma membrane H(+)-ATPase as a requirement for functional complementation of a yeast transport mutant. J Biol Chem. 2002 Feb 22;277(8):6353-8.The A. thaliana protein AT4G30190.1 complements a homologous mutation in S. cerevisiae. This paper shows that wild-type AHA2 does not complement a pma1 mutant, but mutants of AHA2 lacking the C-terminal domain or with key residues mutated do complement.
UniProtKB:P05030 · SGD:S000002976PMID:15829483 Fraysse AS, et al. A systematic mutagenesis study of Ile-282 in transmembrane segment M4 of the plasma membrane H+-ATPase. J Biol Chem. 2005 Jun 10;280(23):21785-90.The A. thaliana protein AT4G30190.1 complements a homologous mutation in S. cerevisiae. This paper shows that wild-type AHA2 does not complement a pma1 mutant, but mutants of AHA2 with key residues mutated do complement.
UniProtKB:P05030 · SGD:S000002976PMID:2900469 Perona R, et al. Increased pH and tumorigenicity of fibroblasts expressing a yeast proton pump. Nature. 1988 Aug 4;334(6181):438-40.The S. cerevisiae protein PMA1 was expressed in H. sapiens, but complementation was not directly tested. This paper shows expression of yeast PMA1 in human fibroblasts, but not a complementation experiment.
UniProtKB:P05030 · SGD:S000002976PMID:8852338 Monk BC, et al. Targeting the fungal plasma membrane proton pump. Acta Biochim Pol. 1995;42(4):481-96.The C. albicans/S. cerevisiae protein PMA1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper describes a domain-swapping experiment used to analyze the function of C. albicans PMA1.
UniProtKB:P05030 · SGD:S000002976PMID:9282738 de Kerchove d'Exaerde A, et al. Functional analysis of chimerical plasma membrane H+-ATPases from Saccharomyces cerevisiae and Schizosaccharomyces pombe. Mol Microbiol. 1997 Jul;25(2):261-73.The S. pombe/S. cerevisiae protein PMA1 complements a homologous mutation in S. cerevisiae. A chimeric S. pombe/S. cerevisiae PMA1 restores partial function to an S. cerevisiae pma1 pma2 strain.
UniProtKB:P05030 · SGD:S000002976PMID:2891694 Ghislain M, et al. Mutation of a conserved glycine residue modifies the vanadate sensitivity of the plasma membrane H+-ATPase from Schizosaccharomyces pombe. J Biol Chem. 1987 Dec 25;262(36):17549-55.The S. pombe protein pma1+ complements a homologous mutation in S. cerevisiae.
UniProtKB:P05030 · SGD:S000002976PMID:7559560 de Kerchove d'Exaerde A, et al. Functional complementation of a null mutation of the yeast Saccharomyces cerevisiae plasma membrane H(+)-ATPase by a plant H(+)-ATPase gene. J Biol Chem. 1995 Oct 6;270(40):23828-37.The N. plumbaginifolia protein PMA2 complements a homologous mutation in S. cerevisiae. This paper shows that N. plumbaginifolia PMA2 allows growth of a yeast pma1 pma2 mutant.
UniProtKB:P05030 · SGD:S000002976PMID:9952459 Luo H, et al. The two major types of plant plasma membrane H+-ATPases show different enzymatic properties and confer differential pH sensitivity of yeast growth. Plant Physiol. 1999 Feb;119(2):627-34.The N. plumbaginifolia protein PMA4 complements a homologous mutation in S. cerevisiae. This paper shows that NICOTIANA_PLUMBAGINIFOLIA PMA4 restores function to a yeast pma1 pma2 strain.
UniProtKB:P05030 · SGD:S000002976PMID:16677337 Grigore D, et al. Functional complementation of the yeast P-type H-ATPase, PMA1, by the Pneumocystis carinii P-type H-ATPase, PCA1. J Eukaryot Microbiol. 2006 May-Jun;53(3):157-64.The P. carinii protein PCA1 complements a homologous mutation in S. cerevisiae. This paper shows that P. carinii PCA1 complements a yeast pma1 mutant.
UniProtKB:P05030 · SGD:S000002976PMID:16730200 Shan W, et al. Phytophthora nicotianae PnPMA1 encodes an atypical plasma membrane H+ -ATPase that is functional in yeast and developmentally regulated. Fungal Genet Biol. 2006 Aug;43(8):583-92.The P. nicotianae protein PnPMA1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P05030 · SGD:S000002976PMID:16757482 Luo S, et al. Molecular characterization of Trypanosoma brucei P-type H+-ATPases. J Biol Chem. 2006 Aug 4;281(31):21963-73.The T. brucei protein TbHA1 complements a homologous mutation in S. cerevisiae. This paper shows that T. brucei TbHA1 complements a yeast pma1 mutant.
UniProtKB:P05030 · SGD:S000002976PMID:12221074 Luo S, et al. Trypanosoma cruzi H+-ATPase 1 (TcHA1) and 2 (TcHA2) genes complement yeast mutants defective in H+ pumps and encode plasma membrane P-type H+-ATPases with different enzymatic properties. J Biol Chem. 2002 Nov 15;277(46):44497-506.The T. cruzi protein TcHA1 complements a homologous mutation in S. cerevisiae. This paper shows that T. cruzi TcHA1 complements a yeast pma1 mutant.
UniProtKB:P05030 · SGD:S000002976PMID:16757482 Luo S, et al. Molecular characterization of Trypanosoma brucei P-type H+-ATPases. J Biol Chem. 2006 Aug 4;281(31):21963-73.The T. brucei protein TbHA2 complements a homologous mutation in S. cerevisiae. This paper shows that T. brucei TbHA2 complements a yeast pma1 mutant.
UniProtKB:P05030 · SGD:S000002976PMID:16757482 Luo S, et al. Molecular characterization of Trypanosoma brucei P-type H+-ATPases. J Biol Chem. 2006 Aug 4;281(31):21963-73.The T. brucei protein TbHA3 complements a homologous mutation in S. cerevisiae. This paper shows that T. brucei TbHA3 complements a yeast pma1 mutant.
UniProtKB:P05030 · SGD:S000002976PMID:16757482 Luo S, et al. Molecular characterization of Trypanosoma brucei P-type H+-ATPases. J Biol Chem. 2006 Aug 4;281(31):21963-73.The T. cruzi protein TcHA1 complements a homologous mutation in S. cerevisiae. This paper shows that T. cruzi TcHA1 complements a yeast pma1 mutant.
UniProtKB:P05030 · SGD:S000002976PMID:12221074 Luo S, et al. Trypanosoma cruzi H+-ATPase 1 (TcHA1) and 2 (TcHA2) genes complement yeast mutants defective in H+ pumps and encode plasma membrane P-type H+-ATPases with different enzymatic properties. J Biol Chem. 2002 Nov 15;277(46):44497-506.The T. cruzi protein TcHA2 complements a homologous mutation in S. cerevisiae. This paper shows that an N-terminal truncated version of T. cruzi TcHA2 complements a yeast pma1 mutant.
UniProtKB:P19657 · SGD:S000005957PMID:9282738 de Kerchove d'Exaerde A, et al. Functional analysis of chimerical plasma membrane H+-ATPases from Saccharomyces cerevisiae and Schizosaccharomyces pombe. Mol Microbiol. 1997 Jul;25(2):261-73.The S. pombe/S. cerevisiae protein PMA1 complements a homologous mutation in S. cerevisiae. A chimeric S. pombe/S. cerevisiae PMA1 restores partial function to an S. cerevisiae pma1 pma2 strain.
UniProtKB:P19657 · SGD:S000005957PMID:7559560 de Kerchove d'Exaerde A, et al. Functional complementation of a null mutation of the yeast Saccharomyces cerevisiae plasma membrane H(+)-ATPase by a plant H(+)-ATPase gene. J Biol Chem. 1995 Oct 6;270(40):23828-37.The N. plumbaginifolia protein PMA2 complements a homologous mutation in S. cerevisiae. This paper shows that N. plumbaginifolia PMA2 allows growth of a yeast pma1 pma2 mutant.
UniProtKB:P19657 · SGD:S000005957PMID:9952459 Luo H, et al. The two major types of plant plasma membrane H+-ATPases show different enzymatic properties and confer differential pH sensitivity of yeast growth. Plant Physiol. 1999 Feb;119(2):627-34.The N. plumbaginifolia protein PMA4 complements a homologous mutation in S. cerevisiae. This paper shows that NICOTIANA_PLUMBAGINIFOLIA PMA4 restores function to a yeast pma1 pma2 strain.
DescriptionSuffix
Sequences in this family.fasta
mafft aligned Fasta file.afasta
phyml newick file.newick
Notung rooted & rearranged newick file.newick.rooting.0.rearrange.0
Notung Homolog Table.newick.rooting.0.rearrange.0.homologs.csv
OMIM (15)
ENSEMBL:ENSG00000159363 · UniProtKB:Q9NQ11#105830 ANGELMAN SYNDROME; AS;;HAPPY PUPPET SYNDROME, FORMERLYANGELMAN SYNDROME CHROMOSOME REGION, INCLUDED; ANCR, INCLUDED
ENSEMBL:ENSG00000018625 · UniProtKB:P50993#606693 KUFOR-RAKEB SYNDROME; KRS;;PARKINSON DISEASE 9; PARK9;;PALLIDOPYRAMIDAL DEGENERATION WITH SUPRANUCLEAR UPGAZE PARESIS ANDDEMENTIA; KRPPD
ENSEMBL:ENSG00000105409 · UniProtKB:P13637#602481 MIGRAINE, FAMILIAL HEMIPLEGIC, 2; FHM2;;MHP2MIGRAINE, FAMILIAL BASILAR, INCLUDED
#104290 ALTERNATING HEMIPLEGIA OF CHILDHOOD
ENSEMBL:ENSG00000196296 · UniProtKB:O14983#128235 DYSTONIA 12; DYT12;;DYSTONIA-PARKINSONISM, RAPID-ONSET; RDP
ENSEMBL:ENSG00000174437 · UniProtKB:P16615#601003 BRODY MYOPATHY
ENSEMBL:ENSG00000017260 · UniProtKB:P98194#124200 DARIER-WHITE DISEASE; DAR;;KERATOSIS FOLLICULARIS;;DARIER DISEASE; DDDARIER DISEASE, ACRAL HEMORRHAGIC TYPE, INCLUDED;;DARIER DISEASE, SEGMENTAL, INCLUDED
#101900 ACROKERATOSIS VERRUCIFORMIS; AKV;;HOPF DISEASE
ENSEMBL:ENSG00000081923 · UniProtKB:O43520#169600 BENIGN CHRONIC PEMPHIGUS; BCPM;;PEMPHIGUS, BENIGN FAMILIAL;;HAILEY-HAILEY DISEASE; HHD
ENSEMBL:ENSG00000165240 · UniProtKB:Q04656#243300 CHOLESTASIS, BENIGN RECURRENT INTRAHEPATIC, 1; BRIC1;;SUMMERSKILL SYNDROME
#211600 CHOLESTASIS, PROGRESSIVE FAMILIAL INTRAHEPATIC, 1; PFIC1;;BYLER DISEASE;;CHOLESTASIS, FATAL INTRAHEPATIC
#147480 CHOLESTASIS, INTRAHEPATIC, OF PREGNANCY; ICP;;RECURRENT INTRAHEPATIC CHOLESTASIS OF PREGNANCY; RICP;;CHOLESTASIS, PREGNANCY-RELATED
ENSEMBL:ENSG00000123191 · UniProtKB:P35670#309400 MENKES DISEASE;;MK; MNK;;MENKEA SYNDROME;;KINKY HAIR DISEASE;;STEELY HAIR DISEASE;;COPPER TRANSPORT DISEASE
#304150 CUTIS LAXA, X-LINKED;;OCCIPITAL HORN SYNDROME; OHS;;EHLERS-DANLOS SYNDROME, OCCIPITAL HORN TYPE, FORMERLY;;EDS IX, FORMERLY;;EDS9, FORMERLY
UniProtKB:P13586 · SGD:S000003135#277900 WILSON DISEASE;;WND; WD;;HEPATOLENTICULAR DEGENERATION
SGD Disease Papers (31)
UniProtKB:P39524 · SGD:S000000024PMID:15811312 Kellermayer R (2005) Hailey-Hailey disease as an orthodisease of PMR1 deficiency in Saccharomyces cerevisiae. FEBS Lett 579(10):2021-5
PMID:15623514 Ramos-Castaneda J, et al. (2005) Deficiency of ATP2C1, a Golgi ion pump, induces secretory pathway defects in endoplasmic reticulum (ER)-associated degradation and sensitivity to ER stress. J Biol Chem 280(10):9467-73
PMID:15610534 Szigeti R and Kellermayer R (2004) Hailey-Hailey disease and calcium: lessons from yeast. J Invest Dermatol 123(6):1195-6
PMID:15610533 Ton VK and Rao R (2004) Expression of Hailey-Hailey disease mutations in yeast. J Invest Dermatol 123(6):1192-4
PMID:11741891 Ton VK, et al. (2002) Functional expression in yeast of the human secretory pathway Ca(2+), Mn(2+)-ATPase defective in Hailey-Hailey disease. J Biol Chem 277(8):6422-7
PMID:10767338 Sudbrak R, et al. (2000) Hailey-Hailey disease is caused by mutations in ATP2C1 encoding a novel Ca(2+) pump. Hum Mol Genet 9(7):1131-40
PMID:10615129 Hu Z, et al. (2000) Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease. Nat Genet 24(1):61-5
UniProtKB:Q12697 · SGD:S000005817PMID:9500542 Bull LN, et al. (1998) A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis. Nat Genet 18(3):219-24
UniProtKB:P38995 · SGD:S000002678PMID:19345671 Schmidt K, et al. (2009) Cd2+, Mn2+, Ni2+ and Se2+ toxicity to Saccharomyces cerevisiae lacking YPK9p the orthologue of human ATP13A2. Biochem Biophys Res Commun 383(2):198-202
PMID:19182805 Gitler AD, et al. (2009) Alpha-synuclein is part of a diverse and highly conserved interaction network that includes PARK9 and manganese toxicity. Nat Genet 41(3):308-15
UniProtKB:P05030 · SGD:S000002976PMID:9920665 Borjigin J, et al. (1999) A novel pineal night-specific ATPase encoded by the Wilson disease gene. J Neurosci 19(3):1018-26
PMID:9837819 Forbes JR and Cox DW (1998) Functional characterization of missense mutations in ATP7B: Wilson disease mutation or normal variant? Am J Hum Genet 63(6):1663-74
PMID:9654149 Iida M, et al. (1998) Analysis of functional domains of Wilson disease protein (ATP7B) in Saccharomyces cerevisiae. FEBS Lett 428(3):281-5
PMID:9546033 Dancis A (1998) Genetic analysis of iron uptake in the yeast Saccharomyces cerevisiae. J Pediatr 132(3 Pt 2):S24-9
PMID:9520490 Gaxiola RA, et al. (1998) The yeast CLC chloride channel functions in cation homeostasis. Proc Natl Acad Sci U S A 95(7):4046-50
PMID:9452509 Payne AS and Gitlin JD (1998) Functional expression of the menkes disease protein reveals common biochemical mechanisms among the copper-transporting P-type ATPases. J Biol Chem 273(6):3765-70
PMID:9325307 Yuan DS, et al. (1997) Restriction of copper export in Saccharomyces cerevisiae to a late Golgi or post-Golgi compartment in the secretory pathway. J Biol Chem 272(41):25787-93
PMID:9261163 Hung IH, et al. (1997) Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae. J Biol Chem 272(34):21461-6
PMID:8628392 Bassett DE Jr, et al. (1996) Yeast genes and human disease. Nature 379(6566):589-90
PMID:7785328 Fu D, et al. (1995) Sequence, mapping and disruption of CCC2, a gene that cross-complements the Ca(2+)-sensitive phenotype of csg1 mutants and encodes a P-type ATPase belonging to the Cu(2+)-ATPase subfamily. Yeast 11(3):283-92
PMID:7708696 Yuan DS, et al. (1995) The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake. Proc Natl Acad Sci U S A 92(7):2632-6
PMID:18752978 Tang J, et al. (2008) Clinical outcomes in Menkes disease patients with a copper-responsive ATP7A mutation, G727R. Mol Genet Metab 95(3):174-81
PMID:18291109 Valverde RH, et al. (2008) Cyclic AMP-dependent protein kinase controls energy interconversion during the catalytic cycle of the yeast copper-ATPase. FEBS Lett 582(6):891-5
PMID:17496194 Donsante A, et al. (2007) Differences in ATP7A gene expression underlie intrafamilial variability in Menkes disease/occipital horn syndrome. J Med Genet 44(8):492-7
PMID:15963506 Portmann R and Solioz M (2005) Purification and functional reconstitution of the human Wilson copper ATPase, ATP7B. FEBS Lett 579(17):3589-95
PMID:14962673 Hsi G, et al. (2004) Functional assessment of the carboxy-terminus of the Wilson disease copper-transporting ATPase, ATP7B. Genomics 83(3):473-81
PMID:12395188 Parisot D, et al. (2002) clap1, a gene encoding a copper-transporting ATPase involved in the process of infection by the phytopathogenic fungus Colletotrichum lindemuthianum. Mol Genet Genomics 268(2):139-51
PMID:12134146 Steinmetz LM, et al. (2002) Systematic screen for human disease genes in yeast. Nat Genet 31(4):400-4
PMID:11373292 Voskoboinik I, et al. (2001) The regulation of catalytic activity of the menkes copper-translocating P-type ATPase. Role of high affinity copper-binding sites. J Biol Chem 276(30):28620-7
PMID:10942420 Forbes JR and Cox DW (2000) Copper-dependent trafficking of Wilson disease mutant ATP7B proteins. Hum Mol Genet 9(13):1927-35
UniProtKB:P05030 · SGD:S000002976PMID:7802957 Monk BC and Perlin DS (1994) Fungal plasma membrane proton pumps as promising new antifungal targets. Crit Rev Microbiol 20(3):209-23
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