P-POD: Princeton Protein Orthology Database: GO3/Jaccard45

This family has 269 members: 45 Arabidopsis thaliana, 25 Caenorhabditis elegans, 29 Danio rerio, 25 Dictyostelium discoideum, 25 Drosophila melanogaster, 9 Escherichia coli, 22 Gallus gallus, 26 Homo sapiens, 25 Mus musculus, 25 Rattus norvegicus, 8 Saccharomyces cerevisiae, 5 Schizosaccharomyces pombe.

Interactive Java Applets: Notung Tree Analysis · Jalview Alignment

GO3/Jaccard45
269 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaNCBI:NP_176686.1 · TAIR:locus:2015003 (F16G16.6 · 4CL3 · F16G16_6 · AT1G65060)4-COUMARATE:COA LIGASE⌘
A. thalianaNCBI:NP_179356.1 · TAIR:locus:2057249
A. thalianaNCBI:NP_175929.3 · TAIR:locus:2035721 (AAE18 · F7A10_14 · F7A10.14 · AT1G55320)ACYL-ACTIVATING ENZYME 18⌘
A. thalianaNCBI:NP_197141.1 · TAIR:locus:2171402
A. thalianaNCBI:NP_176622.1 · TAIR:locus:2014265 (F15H21.7 · F15H21_7 · AT1G64400)⌘
A. thalianaNCBI:NP_175579.1 · TAIR:locus:2017602 (AT1G51680 · 4CL.1 · F19C24_11 · F19C24.11 · 4CL1 · AT4CL1)4-COUMARATE:COA LIGASE 1 · ARABIDOPSIS THALIANA 4-COUMARATE:COA LIGASE 1 · 4-COUMARATE:COA LIGASE⌘
A. thalianaNCBI:NP_188761.1 · TAIR:locus:2094716 (AT3G21240 · AT4CL2 · MXL8.10 · 4CL2)4-COUMARATE:COA LIGASE 2 · 4-COUMARATE:COA LIGASE⌘
A. thalianaNCBI:NP_177756.1 · TAIR:locus:2014599
A. thalianaNCBI:NP_198112.2 · TAIR:locus:2143661 (F15A18.60 · F15A18_60 · LACS7 · AT5G27600)LONG-CHAIN ACYL-COA SYNTHETASE 7⌘
A. thalianaNCBI:NP_177848.1 · TAIR:locus:2195950
A. thalianaNCBI:NP_566265.1 · TAIR:locus:2083013 (F2O10_7 · AT3G05970 · LACS6 · F2O10.7)long-chain acyl-CoA synthetase 6⌘
A. thalianaNCBI:NP_173573.1 · TAIR:locus:2027032
A. thalianaNCBI:NP_194116.1 · TAIR:locus:2138141 (T32A16.20 · AT4G23850 · T32A16_20)⌘
A. thalianaNCBI:NP_564115.1 · TAIR:locus:2034392 (F5M15_17 · AT1G20510 · F5M15.17 · OPCL1)OPC-8:0 COA LIGASE1⌘
A. thalianaNCBI:NP_175368.2 · TAIR:locus:2010177 (F13F21_14 · LACS2 · LRD2 · F13F21.14 · AT1G49430)LONG-CHAIN ACYL-COA SYNTHETASE 2 · LATERAL ROOT DEVELOPMENT 2⌘
A. thalianaNCBI:NP_177882.1 · TAIR:locus:2204765 (LACS9 · T5M16.18 · T5M16_18 · AT1G77590)LONG CHAIN ACYL-COA SYNTHETASE 9⌘
A. thalianaNCBI:NP_190468.1 · TAIR:locus:2101368 (T2J13.170 · AT3G48990)⌘
A. thalianaNCBI:NP_176763.1 · TAIR:locus:2009774 (F12P19_5 · BZO1 · F12P19.5 · AT1G65880)BENZOYLOXYGLUCOSINOLATE 1⌘
A. thalianaNCBI:NP_178516.1 · TAIR:locus:2058384 (T23O15_3 · T23O15.3 · AT2G04350)⌘
A. thalianaNCBI:NP_182246.1 · TAIR:locus:2065195 (AT2G47240 · T8I13.8)⌘
A. thalianaNCBI:NP_192841.1 · TAIR:locus:2136148 (T22B4.10 · T22B4_10 · AT4G11030)⌘
A. thalianaNCBI:NP_188760.3 · TAIR:locus:2094771 (MXL8.9 · AT3G21230 · 4CL5)4-coumarate:CoA ligase 5⌘
A. thalianaNCBI:NP_001031974.2 · TAIR:locus:2149104 (AT5G36880 · F5H8_15 · F5H8.15)⌘
A. thalianaNCBI:NP_193636.1 · TAIR:locus:2117209 (AT4G19010 · F13C5_180 · F13C5.180)⌘
A. thalianaNCBI:NP_197138.1 · TAIR:locus:2171357
A. thalianaNCBI:NP_174340.2 · TAIR:locus:2028165 (F26G16.14 · AT1G30520 · F26G16_14 · AAE14)Acyl-Activating Enzyme 14⌘
A. thalianaNCBI:NP_173473.2 · TAIR:locus:2034413 (F5M15_28 · F5M15.28 · AT1G20490)⌘
A. thalianaNCBI:NP_173474.2 · TAIR:locus:2034403 (F5M15.18 · AT1G20500 · F5M15_18)⌘
A. thalianaNCBI:NP_189021.2 · TAIR:locus:2095173
A. thalianaNCBI:NP_176482.1 · TAIR:locus:2015499 (F16P17.9 · AT1G62940 · ACOS5 · F16P17_9)ACYL-COA SYNTHETASE 5⌘
A. thalianaTAIR:locus:2093432 (MSL1.21 · AT3G16170) · NCBI:NP_566537.1⌘
A. thalianaNCBI:NP_176994.1 · TAIR:locus:2199267
A. thalianaNCBI:NP_173472.1 · TAIR:locus:2034423 (AT1G20480 · F5M15_29 · F5M15.29)⌘
A. thalianaNCBI:NP_001077573.1 · TAIR:locus:2027012
A. thalianaNCBI:NP_193143.2 · TAIR:locus:2129371 (AAE15 · AT4G14070 · FCAALL.81 · DL3075C)acyl-activating enzyme 15⌘
A. thalianaNCBI:NP_188316.1 · TAIR:locus:2086122 (K14A17.23 · AT3G16910 · ACN1 · AAE7)ACYL-ACTIVATING ENZYME 7 · AC NON-UTILIZING 1⌘
A. thalianaNCBI:NP_198442.2 · TAIR:locus:2142908 (F14A1.10 · F14A1_10 · AT5G35930)⌘
A. thalianaNCBI:NP_201143.1 · TAIR:locus:2158559 (K9H21.11 · AT5G63380 · K9H21_11)⌘
A. thalianaNCBI:NP_564116.1 · TAIR:locus:2030407 (AT1G20560 · F5M15.12 · F5M15_12 · AAE1)ACYL ACTIVATING ENZYME 1⌘
A. thalianaNCBI:NP_177724.1 · TAIR:locus:2204360
A. thalianaNCBI:NP_198628.2 · TAIR:locus:2176662 (MXA21_2 · AT5G38120 · MXA21.2)⌘
A. thalianaNCBI:NP_176786.1 · TAIR:locus:2013860
A. thalianaNCBI:NP_176764.1 · TAIR:locus:2009714
A. thalianaNCBI:NP_192425.1 · TAIR:locus:2115673 (C17L7.80 · AT4G05160 · C17L7_80)⌘
A. thalianaNCBI:NP_197696.2 · TAIR:locus:2178277 (AAE17 · MYJ24_4 · MYJ24.4 · AT5G23050)ACYL-ACTIVATING ENZYME 17⌘
C. elegansWB:WBGene00006351 (K03A1.5 · sur-5) · UniProtKB:Q21166⌘
C. elegansWB:WBGene00020634 · UniProtKB:O02171
C. elegansWB:WBGene00007082 · UniProtKB:O02200
C. elegansWB:WBGene00016849 · UniProtKB:O16481
C. elegansWB:WBGene00019920 · UniProtKB:O16775
C. elegansWB:WBGene00009221 · UniProtKB:O18693
C. elegansWB:WBGene00020343 (acs-3 · T08B1.6) · UniProtKB:O44560⌘
C. elegansWB:WBGene00003179 (mec-18) · UniProtKB:O45873⌘
C. elegansWB:WBGene00016324 · UniProtKB:P91123
C. elegansWB:WBGene00007228 · UniProtKB:Q17577
C. elegansWB:WBGene00007969 (C36A4.9 · acs-19) · UniProtKB:Q18496⌘
C. elegansWB:WBGene00016716 (C46F4.2 · acs-17) · UniProtKB:Q18660⌘
C. elegansWB:WBGene00017012 · UniProtKB:Q18916
C. elegansWB:WBGene00008669 · UniProtKB:Q19339
C. elegansWB:WBGene00009218 · UniProtKB:Q19878
C. elegansWB:WBGene00018152 (F37C12.7 · acs-4) · UniProtKB:Q20121⌘
C. elegansWB:WBGene00018269 · UniProtKB:Q20264
C. elegansWB:WBGene00011173 · UniProtKB:Q21872
C. elegansWB:WBGene00011174 · UniProtKB:Q21873
C. elegansWB:WBGene00022849 · UniProtKB:Q23404
C. elegansWB:WBGene00022037 · UniProtKB:Q9N302
C. elegansWB:WBGene00018579 · UniProtKB:Q9TZI7
C. elegansWB:WBGene00018488 (F46E10.1 · acs-1) · UniProtKB:Q9UAV8⌘
C. elegansWB:WBGene00009106 · UniProtKB:Q9XV68
C. elegansWB:WBGene00013575 · UniProtKB:Q9XWD1
D. rerioENSEMBL:ENSDARP00000090875
D. rerioENSEMBL:ENSDARP00000083765
D. rerioENSEMBL:ENSDARP00000067708
D. rerioENSEMBL:ENSDARP00000079273
D. rerioENSEMBL:ENSDARP00000089198
D. rerioENSEMBL:ENSDARP00000041805
D. rerioENSEMBL:ENSDARP00000046412
D. rerioENSEMBL:ENSDARP00000088650
D. rerioENSEMBL:ENSDARP00000077215
D. rerioENSEMBL:ENSDARP00000088720
D. rerioUniProtKB:A3QK15 · ZFIN:ZDB-GENE-040426-903 (aacs)acetoacetyl-CoA synthetase⌘
D. rerioUniProtKB:Q0P4F7 · ZFIN:ZDB-GENE-060825-7 (acsf2)acyl-CoA synthetase family member 2⌘
D. rerioZFIN:ZDB-GENE-061013-672 (zgc:153860) · UniProtKB:Q08BF2⌘
D. rerioUniProtKB:Q0P3V6 · ZFIN:ZDB-GENE-060825-27 (slc27a6)solute carrier family 27 (fatty acid transporter), member 6⌘
D. rerioENSEMBL:ENSDARG00000067924 · UniProtKB:Q0VG88
D. rerioENSEMBL:ENSDARG00000013177 · UniProtKB:Q1ECW0
D. rerioZFIN:ZDB-GENE-050420-181 (si:dkeyp-109h9.2) · UniProtKB:Q1LVA8⌘
D. rerioUniProtKB:Q1LWR6 · ZFIN:ZDB-GENE-060503-816 (acss3)acyl-CoA synthetase short-chain family member 3⌘
D. rerioUniProtKB:Q499A9 · ZFIN:ZDB-GENE-050809-115 (acsl1)acyl-CoA synthetase long-chain family member 1⌘
D. rerioZFIN:ZDB-GENE-050417-248 (zgc:112138) · UniProtKB:Q567D7⌘
D. rerioUniProtKB:Q58EE3 · ZFIN:ZDB-GENE-030131-6493 (acsl4l)acyl-CoA synthetase long-chain family member 4, like⌘
D. rerioUniProtKB:Q5BL26 · ZFIN:ZDB-GENE-050320-112 (slc27a1)solute carrier family 27 (fatty acid transporter), member 1⌘
D. rerioZFIN:ZDB-GENE-041212-67 (zgc:101540) · UniProtKB:Q5PRD9⌘
D. rerioZFIN:ZDB-GENE-040801-88 (zgc:101071) · UniProtKB:Q6DEJ3⌘
D. rerioUniProtKB:Q6DHN4 · ZFIN:ZDB-GENE-040718-388 (acss2)acyl-CoA synthetase short-chain family member 2⌘
D. rerioUniProtKB:Q6PFP1 · ZFIN:ZDB-GENE-040426-1565 (acsl4a)acyl-CoA synthetase long-chain family member 4a⌘
D. rerioZFIN:ZDB-GENE-070209-32 (zgc:158482) · UniProtKB:A2VCY4⌘
D. rerioUniProtKB:B0JZJ9 · ZFIN:ZDB-GENE-050320-139 (acss1)acyl-CoA synthetase short-chain family member 1⌘
D. rerioUniProtKB:B0S7E7 · ZFIN:ZDB-GENE-030131-7099 (acsbg2)acyl-CoA synthetase bubblegum family member 2⌘
D. discoideumNCBI:EAL73206.1 · dictyBase:DDB_G0267506 (aslH)putative acetyl-CoA synthetase⌘
D. discoideumNCBI:EAL70825.1 · dictyBase:DDB_G0273215
D. discoideumNCBI:EAL70900.1 · dictyBase:DDB_G0273365
D. discoideumNCBI:EAL70824.1 · dictyBase:DDB_G0273213 (aslA-1 · aslA)putative acetyl-CoA synthetase⌘
D. discoideumNCBI:EAL73225.1 · dictyBase:DDB_G0267544 (aslM)AMP-dependent synthetase and ligase domain-containing protein, putative acetyl-CoA synthetase⌘
D. discoideumNCBI:EAL70870.1 · dictyBase:DDB_G0273305
D. discoideumNCBI:EAL70832.1 · dictyBase:DDB_G0273229
D. discoideumNCBI:EAL70831.1 · dictyBase:DDB_G0273227
D. discoideumNCBI:EAL70823.1 · dictyBase:DDB_G0273211
D. discoideumNCBI:EAL73589.2 · dictyBase:DDB_G0268272 (aslN)AMP-dependent synthetase and ligase domain-containing protein, putative acetyl-CoA synthetase⌘
D. discoideumNCBI:EAL70829.1 · dictyBase:DDB_G0273223
D. discoideumNCBI:EAL70830.1 · dictyBase:DDB_G0273225
D. discoideumUniProtKB:Q54P77 · dictyBase:DDB_G0284831 (4cl · 4cl1)4-coumarate-CoA ligase⌘
D. discoideumUniProtKB:Q54P78 · dictyBase:DDB_G0284745 (4cl · 4cl2)4-coumarate-CoA ligase⌘
D. discoideumUniProtKB:Q54Z60 · dictyBase:DDB_G0277815 (ACS · acsA)acetyl-CoA synthetase, acetyl-CoA ligase⌘
D. discoideumUniProtKB:Q554Z5 · dictyBase:DDB_G0274939 (aslB)putative acyl-CoA synthetase⌘
D. discoideumUniProtKB:Q55DR6 · dictyBase:DDB_G0269242 (fcsA)LC-FACS 1 · fatty acyl-CoA synthetase, long-chain-fatty-acid-CoA ligase⌘
D. discoideumUniProtKB:Q1ZXQ4 · dictyBase:DDB_G0269474 (fcsB)fatty acyl-CoA synthetase, long-chain-fatty-acid-CoA ligase⌘
D. discoideumUniProtKB:Q54HD3 · dictyBase:DDB_G0289539 (DDB_G0289539)Glr1122 protein.⌘
D. discoideumdictyBase:DDB_G0288001 (DDB_G0288001) · UniProtKB:Q54JK0⌘
D. discoideumUniProtKB:Q54WL7 · dictyBase:DDB_G0279561 (DDB_G0279561)AMP-dependent synthetase and ligase domain-containing protein⌘
D. discoideumUniProtKB:Q551W4 · dictyBase:DDB_G0276321 (DDB_G0276321)putative acetoacetyl-CoA synthetase, AMP-dependent synthetase and ligase domain-containing protein, putative acetyl-CoA synthetase⌘
D. discoideumUniProtKB:Q55CD5 · dictyBase:DDB_G0270106 (DDB_G0270106)Bll7928 protein.⌘
D. discoideumUniProtKB:Q75JX7 · dictyBase:DDB_G0272216 (aslF)putative acetyl-CoA synthetase⌘
D. discoideumUniProtKB:Q8SSN6 · dictyBase:DDB_G0276337 (DDB_G0276337)AMP-dependent synthetase and ligase domain-containing protein⌘
D. melanogasterUniProtKB:Q9VP61 · FB:FBgn0012034 (BEST:GH28401 · AcCoAS · CG9390 · ACS)acetyl CoA synthase · Acetyl CoA synthetase · acetyl-coenzyme A synthase · Acetyl CoA synthase · Acetyl-CoA sythase · acetate-coenzyme A ligase · acetyl-CoA synthetase · Acetyl Coenzyme A synthase · Acetyl-CoA synthase⌘
D. melanogasterFB:FBgn0028519 (2a9 · anon-EST:CL2a9 · I · BG:DS05899.1 · CG4500) · UniProtKB:Q9V3U0⌘
D. melanogasterFB:FBgn0027348 (BG:DS01514.2 · bubblegum · BG:DS0514.2 · CG4501 · 2a9hom · bgm) · UniProtKB:Q9V3S9⌘
D. melanogasterFB:FBgn0033733 (CG8834) · UniProtKB:A1Z8Z9⌘
D. melanogasterFB:FBgn0050194 (CG13536 · CG30194 · CG3037) · UniProtKB:Q7KVJ6⌘
D. melanogasterFB:FBgn0038734 (CG11453) · UniProtKB:Q86P31⌘
D. melanogasterFB:FBgn0034999 (CG3394) · UniProtKB:Q8SXR7⌘
D. melanogasterUniProtKB:Q8T3L1 · FB:FBgn0010609 (anon-WO0172774.173 · l(2)7447 · l(2)05847 · CG8732 · l(2)k05304 · 7447 · l(2)44DEa)Fatty acyl-CoA synthetase · lethal (2) 44DEa · Fatty acyl CoA synthetase⌘
D. melanogasterFB:FBgn0039184 (CG6432) · UniProtKB:Q9VC92⌘
D. melanogasterFB:FBgn0039156 (CG6178) · UniProtKB:Q9VCC6⌘
D. melanogasterFB:FBgn0000527 (e · CG3331 · ebony · Ebony) · UniProtKB:Q9VDC6⌘
D. melanogasterFB:FBgn0038733 (CG11407) · UniProtKB:Q9VDU1⌘
D. melanogasterFB:FBgn0038732 (CG11391) · UniProtKB:Q9VDU2⌘
D. melanogasterFB:FBgn0038731 (CG11659) · UniProtKB:Q9VDU3⌘
D. melanogasterFB:FBgn0038730 (CG6300) · UniProtKB:Q9VDU4⌘
D. melanogasterFB:FBgn0037996 (CG4830) · UniProtKB:Q9VGC5⌘
D. melanogasterUniProtKB:Q9VKU1 · FB:FBgn0021953 (l(2)k10307 · Fatp · Dromel_CG7400_FBtr0080133_fatp_mORF · Dromel_CG7400_FBtr0080133_fatp_uORF · CG7400 · anon-WO0121795.74)Fatty acid (long chain) transport protein⌘
D. melanogasterUniProtKB:Q9VMR6 · FB:FBgn0031703 (CG12512)⌘
D. melanogasterFB:FBgn0035641 (CG5568) · UniProtKB:Q9VRQ4⌘
D. melanogasterFB:FBgn0035642 (CG18586) · UniProtKB:Q9VRQ5⌘
D. melanogasterFB:FBgn0036821 (CG3961) · UniProtKB:Q9VVT8⌘
D. melanogasterUniProtKB:Q9VXZ8 · FB:FBgn0027601 (CG9009 · BcDNA:GH02901)long chain fatty acid CoA ligase⌘
D. melanogasterFB:FBgn0035006 (CG4563) · UniProtKB:Q9W171⌘
D. melanogasterFB:FBgn0034553 (CG9993) · UniProtKB:Q9W2R1⌘
D. melanogasterFB:FBgn0034552 (CG17999) · UniProtKB:Q9W2R2⌘
E. coliUniProtKB:P31119 · ECOLI:AAS-MONOMER (b2836 · ECK2832 · aas · Aas)2-acylglycerophosphoethanolamine acyltransferase / acyl-ACP synthetase⌘
E. coliUniProtKB:P27550 · ECOLI:ACS-MONOMER (Acs · ECK4062 · acs · b4069 · yfaC · acsA)acetyl-CoA synthetase (AMP-forming)⌘
E. coliUniProtKB:P31552 · ECOLI:CAIC-MONOMER (b0037 · ECK0038 · caiC · CaiC · yaaM)carnitine-CoA ligase⌘
E. coliUniProtKB:P10378 · ECOLI:ENTE-MONOMER (ECK0587 · EntE · entE · b0594)⌘
E. coliUniProtKB:P11454 · ECOLI:ENTF-PANT
E. coliUniProtKB:P38135 · ECOLI:EG12357-MONOMER (fadK · FadK · ECK1699 · ydiD · b1701)short chain acyl-CoA synthetase monomer⌘
E. coliUniProtKB:P69451 · ECOLI:ACYLCOASYN-MONOMER (b1805 · oldD · fadD · ECK1803 · FadD)⌘
E. coliUniProtKB:P37353 · ECOLI:O-SUCCINYLBENZOATE-COA-LIG-MONOMER (b2260 · ECK2254 · menE · MenE)⌘
E. coliUniProtKB:P77495 · ECOLI:G6200-MONOMER (prpE · ECK0332 · PrpE · b0335 · yahU)putative propionyl-CoA synthetase⌘
G. gallusNCBI:XP_424596 · ENTREZ:426992
G. gallusNCBI:XP_416118 · ENTREZ:417875
G. gallusNCBI:XP_422625 · ENTREZ:424810
G. gallusNCBI:XP_001234991 · ENTREZ:423347
G. gallusNCBI:XP_424010 · ENTREZ:426354
G. gallusNCBI:XP_417342 · ENTREZ:419158
G. gallusNCBI:XP_414641 · ENTREZ:416324
G. gallusNCBI:XP_425134 · ENTREZ:427561
G. gallusNCBI:XP_001233248 · ENTREZ:769933
G. gallusNCBI:XP_415504 · ENTREZ:417220
G. gallusNCBI:XP_001235649 · ENTREZ:776093
G. gallusNCBI:XP_413747 · ENTREZ:415361
G. gallusNCBI:XP_415011 · ENTREZ:416714
G. gallusNCBI:XP_420317 · ENTREZ:422345
G. gallusNCBI:XP_424595 · ENTREZ:426991
G. gallusNCBI:XP_424601 · ENTREZ:426999
G. gallusNCBI:XP_420105 · ENTREZ:422102
G. gallusENTREZ:416811 · UniProtKB:Q5ZLG0 (Q5ZLG0 · AACS · RCJMB04_6g9 · IPI00822553 · AACS_CHICK)Acetoacetyl-CoA synthetase⌘
G. gallusENTREZ:420090 · UniProtKB:Q5ZKR7 (IPI00592307 · ACBG2_CHICK · ACSBG2 · Q5ZKR7 · RCJMB04_9i11)Long-chain-fatty-acid--CoA ligase ACSBG2⌘
G. gallusUniProtKB:Q2L7E6 (Q2L7E6 · IPI00592413) · ENTREZ:426008⌘
G. gallusUniProtKB:Q5F420 (Q5F420 · RCJMB04_3m22 · IPI00574629) · ENTREZ:422547⌘
G. gallusUniProtKB:Q5ZIG7 (RCJMB04_26g6 · IPI00651137 · Q5ZIG7) · ENTREZ:423896⌘
H. sapiensENSEMBL:ENSG00000081760 · UniProtKB:Q86V21 (AACS · IPI00646775 · Q86V21 · AACS_HUMAN · IPI00789348 · IPI00217272 · ACSF1)Acetoacetyl-CoA synthetase⌘
H. sapiensENSEMBL:ENSG00000103740 · UniProtKB:Q96GR2 (IPI00550128 · ACSBG1 · Q96GR2 · LPD · ACBG1_HUMAN · KIAA0631 · BGM)Long-chain-fatty-acid--CoA ligase ACSBG1⌘
H. sapiensENSEMBL:ENSG00000130377 · UniProtKB:Q5FVE4 (BGR · ACBG2_HUMAN · UNQ2443/PRO5005 · IPI00107719 · Q5FVE4 · ACSBG2 · IPI00879473 · IPI00642502 · IPI00879891)Long-chain-fatty-acid--CoA ligase ACSBG2⌘
H. sapiensENSEMBL:ENSG00000066813 · UniProtKB:Q08AH3 (ACS2A_HUMAN · Q08AH3 · MACS2 · IPI00644771 · ACSM2 · ACSM2A)Acyl-coenzyme A synthetase ACSM2A, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000183747 · UniProtKB:Q68CK6 (HYST1046 · Q68CK6 · ACSM2B · ACS2B_HUMAN · IPI00329444 · ACSM2)Acyl-coenzyme A synthetase ACSM2B, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000154930 · UniProtKB:Q9NUB1 (ACAS2L · IPI00216932 · Q9NUB1 · ACSS1 · IPI00248961 · KIAA1846 · ACS2L_HUMAN)Acetyl-coenzyme A synthetase 2-like, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000131069 · UniProtKB:Q9NR19 (Q9NR19 · ACSS2 · ACSA_HUMAN · ACAS2 · IPI00413730)Acetyl-coenzyme A synthetase, cytoplasmic⌘
H. sapiensENSEMBL:ENSG00000167107 · UniProtKB:Q96CM8 (ACSF2_HUMAN · IPI00304071 · UNQ493/PRO1009 · ACSF2 · Q96CM8)Acyl-CoA synthetase family member 2, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000176715 · UniProtKB:Q4G176 (ACSF3_HUMAN · IPI00450347 · Q4G176 · IPI00166395 · PSEC0197 · ACSF3)Acyl-CoA synthetase family member 3, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000151726 · UniProtKB:P33121 (FACL2 · IPI00012728 · FACL1 · ACSL1 · ACSL1_HUMAN · LACS2 · P33121 · LACS · LACS1 · IPI00401448)Long-chain-fatty-acid--CoA ligase 1⌘
H. sapiensENSEMBL:ENSG00000123983 · UniProtKB:O95573 (ACSL3_HUMAN · ACSL3 · ACS3 · LACS3 · FACL3 · IPI00031397 · O95573)Long-chain-fatty-acid--CoA ligase 3⌘
H. sapiensENSEMBL:ENSG00000068366 · UniProtKB:O60488 (IPI00029737 · ACSL4_HUMAN · FACL4 · O60488 · ACSL4 · IPI00219897 · ACS4 · LACS4)Long-chain-fatty-acid--CoA ligase 4⌘
H. sapiensENSEMBL:ENSG00000197142 · UniProtKB:Q9ULC5 (ACSL5 · FACL5 · Q9ULC5 · IPI00008037 · IPI00411387 · ACS5 · UNQ633/PRO1250 · ACSL5_HUMAN)Long-chain-fatty-acid--CoA ligase 5⌘
H. sapiensENSEMBL:ENSG00000164398 · UniProtKB:Q9UKU0 (FACL6 · ACSL6 · Q9UKU0 · IPI00296333 · LACS5 · ACS2 · IPI00657883 · IPI00657816 · KIAA0837 · ACSL6_HUMAN)Long-chain-fatty-acid--CoA ligase 6⌘
H. sapiensENSEMBL:ENSG00000166743 · UniProtKB:Q08AH1 (ACSM1_HUMAN · Q08AH1 · MACS1 · IPI00059184 · BUCS1 · ACSM1 · LAE · IPI00867642)Acyl-coenzyme A synthetase ACSM1, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000005187 · UniProtKB:Q53FZ2 (IPI00297635 · IPI00402513 · ACSM3_HUMAN · ACSM3 · SAH · Q53FZ2)Acyl-coenzyme A synthetase ACSM3, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000215009 · UniProtKB:P0C7M7 (IPI00243302 · ACSM4 · ACSM4_HUMAN · P0C7M7)Acyl-coenzyme A synthetase ACSM4, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000183549 · UniProtKB:Q6NUN0 (ACSM5_HUMAN · IPI00477605 · ACSM5 · Q6NUN0 · IPI00639980 · MACS3)Acyl-coenzyme A synthetase ACSM5, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000173124 · UniProtKB:Q6P461 (C10orf129 · IPI00893318 · ACSM6 · ACSM6_HUMAN · Q6P461 · IPI00884359 · IPI00789910)Acyl-coenzyme A synthetase ACSM6, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000111058 · UniProtKB:Q9H6R3 (IPI00795694 · ACSS3 · ACSS3_HUMAN · Q9H6R3 · IPI00002245)Acyl-CoA synthetase short-chain family member 3, mitochondrial⌘
H. sapiensENSEMBL:ENSG00000130304 · UniProtKB:Q6PCB7 (S27A1_HUMAN · SLC27A1 · IPI00442344 · Q6PCB7 · FATP1 · ACSVL5)Long-chain fatty acid transport protein 1⌘
H. sapiensENSEMBL:ENSG00000140284 · UniProtKB:O14975 (VLACS · FATP2 · S27A2_HUMAN · FACVL1 · O14975 · SLC27A2 · ACSVL1 · IPI00024787)Very long-chain acyl-CoA synthetase⌘
H. sapiensENSEMBL:ENSG00000143554 · UniProtKB:Q5K4L6 (IPI00013623 · ACSVL3 · Q5K4L6 · PSEC0067 · IPI00645636 · UNQ367/PRO703 · SLC27A3 · S27A3_HUMAN · FATP3)Long-chain fatty acid transport protein 3⌘
H. sapiensENSEMBL:ENSG00000167114 · UniProtKB:Q6P1M0 (S27A4_HUMAN · IPI00412147 · SLC27A4 · FATP4 · ACSVL4 · Q6P1M0)Long-chain fatty acid transport protein 4⌘
H. sapiensENSEMBL:ENSG00000083807 · UniProtKB:Q9Y2P5 (S27A5_HUMAN · Q9Y2P5 · ACSVL6 · SLC27A5 · FACVL3 · FATP5 · ACSB · IPI00016827)Bile acyl-CoA synthetase⌘
H. sapiensENSEMBL:ENSG00000113396 · UniProtKB:Q9Y2P4 (Q9Y2P4 · S27A6_HUMAN · ACSVL2 · FATP1 · SLC27A6 · IPI00470637 · FACVL2)Long-chain fatty acid transport protein 6⌘
M. musculusNCBI:NP_001074541 · MGI:MGI:3036230 (Slc27a6 · FATP6)solute carrier family 27 (fatty acid transporter), member 6⌘
M. musculusNCBI:NP_084417 · MGI:MGI:1925875
M. musculusUniProtKB:Q9D2R0 · MGI:MGI:1926144 (Aacs)acetoacetyl-CoA synthetase⌘
M. musculusUniProtKB:Q99PU5 · MGI:MGI:2385656 (Bgm · BG1 · Acsbg1 · Lpd)acyl-CoA synthetase bubblegum family member 1⌘
M. musculusUniProtKB:Q2XU92 · MGI:MGI:3587728 (Acsbg2 · Bgr)acyl-CoA synthetase bubblegum family member 2⌘
M. musculusUniProtKB:Q99NB1 · MGI:MGI:1915988 (Acas2l · Acas2 · Acss1 · AceCS2)acyl-CoA synthetase short-chain family member 1⌘
M. musculusUniProtKB:Q9QXG4 · MGI:MGI:1890410 (ACAS · Acss2 · Acas2 · Acs1 · AceCS1 · Acas1)acyl-CoA synthetase short-chain family member 2 · acetyl-CoA synthetase 1⌘
M. musculusUniProtKB:Q8VCW8 · MGI:MGI:2388287 (Acsf2)acyl-CoA synthetase family member 2⌘
M. musculusUniProtKB:Q3URE1 · MGI:MGI:2182591 (Acsf3)acyl-CoA synthetase family member 3⌘
M. musculusUniProtKB:P41216 · MGI:MGI:102797 (Acsl1 · Facl2 · Acas1)acyl-CoA synthetase long-chain family member 1⌘
M. musculusUniProtKB:Q9CZW4 · MGI:MGI:1921455 (Facl3 · C85929 · Acsl3)acyl-CoA synthetase long-chain family member 3⌘
M. musculusUniProtKB:Q9QUJ7 · MGI:MGI:1354713 (Acsl4 · Lacs4 · Facl4 · ACS4)acyl-CoA synthetase long-chain family member 4⌘
M. musculusUniProtKB:Q8JZR0 · MGI:MGI:1919129 (Facl5 · Acsl5)acyl-CoA synthetase long-chain family member 5⌘
M. musculusUniProtKB:Q91WC3 · MGI:MGI:894291 (Acsl6 · Lacsl · Facl6)acyl-CoA synthetase long-chain family member 6⌘
M. musculusUniProtKB:Q91VA0 · MGI:MGI:2152200 (Macs · Bucs1 · Acsm1)acyl-CoA synthetase medium-chain family member 1⌘
M. musculusUniProtKB:Q8K0L3 · MGI:MGI:2385289 (Acsm2)acyl-CoA synthetase medium-chain family member 2⌘
M. musculusUniProtKB:Q3UNX5 · MGI:MGI:99538 (Sah · Acsm3 · Sa)acyl-CoA synthetase medium-chain family member 3⌘
M. musculusUniProtKB:Q80W40 · MGI:MGI:2681844 (O-MACS · OMACS · Acsm4)acyl-CoA synthetase medium-chain family member 4⌘
M. musculusUniProtKB:Q8BGA8 · MGI:MGI:2444086 (Acsm5)acyl-CoA synthetase medium-chain family member 5⌘
M. musculusUniProtKB:Q14DH7 · MGI:MGI:2685720 (LOC380660 · Acss3)acyl-CoA synthetase short-chain family member 3⌘
M. musculusUniProtKB:Q60714 · MGI:MGI:1347098 (Fatp · FATP1 · Slc27a1)solute carrier family 27 (fatty acid transporter), member 1⌘
M. musculusUniProtKB:O35488 · MGI:MGI:1347099 (Vlacs · VLCS · FATP2 · Vlac · Slc27a2 · ACSVL1)solute carrier family 27 (fatty acid transporter), member 2⌘
M. musculusUniProtKB:O88561 · MGI:MGI:1347358 (Acsvl3 · Slc27a3 · FATP3)fatty acid transport protein 3 · solute carrier family 27 (fatty acid transporter), member 3⌘
M. musculusUniProtKB:Q91VE0 · MGI:MGI:1347347 (Slc27a4 · FATP4)solute carrier family 27 (fatty acid transporter), member 4 · fatty acid transport protein 4⌘
M. musculusUniProtKB:Q4LDG0 · MGI:MGI:1347100 (FATP5 · FACVL3 · Slc27a5 · VLCS-H2 · VLCSH2)solute carrier family 27 (fatty acid transporter), member 5⌘
R. norvegicusNCBI:XP_001079043 · RGD:1306813 (Bucs1)butyryl Coenzyme A synthetase 1⌘
R. norvegicusNCBI:XP_001080753 · RGD:1307051
R. norvegicusNCBI:XP_001079424 · RGD:1586037 (Acsf3)acyl-CoA synthetase family member 3⌘
R. norvegicusNCBI:XP_215897 · RGD:1306246 (Acss1)acyl-CoA synthetase short-chain family member 1⌘
R. norvegicusNCBI:XP_001060439 · RGD:1311977
R. norvegicusNCBI:XP_001075158 · RGD:1310605 (Slc27a3)solute carrier family 27 (fatty acid transporter), member 3⌘
R. norvegicusNCBI:XP_001059993 · RGD:1595856 (LOC316124)similar to gonadotropin-regulated long chain acyl-CoA synthetase⌘
R. norvegicusNCBI:XP_001064684 · RGD:1305489 (Acss2)acyl-CoA synthetase short-chain family member 2⌘
R. norvegicusUniProtKB:Q9JMI1 · RGD:708522 (Aacs)acetoacetyl-CoA synthetase⌘
R. norvegicusUniProtKB:Q924N5 · RGD:708557 (Acsbg1)acyl-CoA synthetase bubblegum family member 1⌘
R. norvegicusUniProtKB:A1L1K7 · RGD:1588580 (Acsbg2)acyl-CoA synthetase bubblegum family member 2⌘
R. norvegicusUniProtKB:Q499N5 · RGD:1562656 (Acsf2)acyl-CoA synthetase family member 2⌘
R. norvegicusUniProtKB:P18163 · RGD:2015 (Acsl1)acyl-CoA synthetase long-chain family member 1⌘
R. norvegicusRGD:70552 (Acsl3) · UniProtKB:Q63151 (ACSL3_RAT · IPI00760128 · Acs3 · Facl3 · Acsl3 · IPI00205908 · Q63151)acyl-CoA synthetase long-chain family member 3 · Long-chain-fatty-acid--CoA ligase 3⌘⌘
R. norvegicusUniProtKB:O35547 · RGD:69401 (Acsl4)acyl-CoA synthetase long-chain family member 4⌘
R. norvegicusUniProtKB:O88813 · RGD:69402 (Acsl5)acyl-CoA synthetase long-chain family member 5⌘
R. norvegicusRGD:69403 (Acsl6) · UniProtKB:P33124 (Acsl6 · Acs2 · ACSL6_RAT · IPI00324041 · Facl6 · P33124)acyl-CoA synthetase long-chain family member 6 · Long-chain-fatty-acid--CoA ligase 6⌘⌘
R. norvegicusUniProtKB:O70490 · RGD:708383 (Acsm2)acyl-CoA synthetase medium-chain family member 2⌘
R. norvegicusUniProtKB:Q6SKG1 · RGD:62086 (Acsm3)acyl-CoA synthetase medium-chain family member 3⌘
R. norvegicusUniProtKB:Q7TN78 · RGD:727928 (Acsm4)acyl-CoA synthetase medium-chain family member 4⌘
R. norvegicusRGD:1309578 (Acsm5) · UniProtKB:Q6AYT9 (Macs3 · Q6AYT9 · ACSM5_RAT · IPI00464802 · Acsm5)acyl-CoA synthetase medium-chain family member 5 · Acyl-coenzyme A synthetase ACSM5, mitochondrial⌘⌘
R. norvegicusRGD:620927 (Slc27a1) · UniProtKB:P97849 (Fatp · P97849 · Fatp1 · S27A1_RAT · Slc27a1 · IPI00567084)solute carrier family 27 (fatty acid transporter), member 1 · Long-chain fatty acid transport protein 1⌘⌘
R. norvegicusUniProtKB:P97524 · RGD:71103 (Slc27a2)solute carrier family 27 (fatty acid transporter), member 2⌘
R. norvegicusUniProtKB:Q9ES38 · RGD:708535 (Slc27a5)solute carrier family 27 (fatty acid transporter), member 5⌘
R. norvegicusUniProtKB:Q5BJL7 · RGD:1307383 (Slc27a4)solute carrier family 27 (fatty acid transporter), member 4⌘
S. cerevisiaeUniProtKB:Q01574 · SGD:S000000050 (YAL054C · FUN44 · ACS1)Acetyl-coA synthetase isoform which, along with Acs2p, is the nuclear source of acetyl-coA for histone acetlyation⌘
S. cerevisiaeUniProtKB:P52910 · SGD:S000004143 (YLR153C · ACS2)Acetyl-coA synthetase isoform which, along with Acs1p, is the nuclear source of acetyl-coA for histone acetylation⌘
S. cerevisiaeUniProtKB:P38225 · SGD:S000000245 (YBR041W · FAT1)Fatty acid transporter and very long-chain fatty acyl-CoA synthetase, may form a complex with Faa1p or Faa4p that imports and activates exogenous fatty acids⌘
S. cerevisiaeUniProtKB:P38137 · SGD:S000000426 (PCS60 · YBR222C · FAT2)Peroxisomal AMP-binding protein, localizes to both the peroxisomal peripheral membrane and matrix, expression is highly inducible by oleic acid, similar to E. coli long chain acyl-CoA synthetase⌘
S. cerevisiaeUniProtKB:P30624 · SGD:S000005844 (YOR317W · FAA1)Long chain fatty acyl-CoA synthetase with a preference for C12:0-C16:0 fatty acids⌘
S. cerevisiaeUniProtKB:P39518 · SGD:S000000817 (FAA2 · FAM1 · YER015W)Long chain fatty acyl-CoA synthetase⌘
S. cerevisiaeUniProtKB:P39002 · SGD:S000001271 (YIL009W · FAA3)Long chain fatty acyl-CoA synthetase, has a preference for C16 and C18 fatty acids⌘
S. cerevisiaeUniProtKB:P47912 · SGD:S000004860 (YMR246W · FAA4)Long chain fatty acyl-CoA synthetase, regulates protein modification during growth in the presence of ethanol, functions to incorporate palmitic acid into phospholipids and neutral lipids⌘
S. pombeUniProtKB:P78773 · GeneDB_Spombe:SPCC191.02c (SPCC191.02c · SPCC417.14c)acetyl-CoA ligase⌘
S. pombeUniProtKB:O74976 · GeneDB_Spombe:SPCC1827.03c (SPCC1827.03c)acetyl-CoA ligase⌘
S. pombeUniProtKB:O60135 · GeneDB_Spombe:SPBC18H10.02 (lcf1 · SPBC18H10.02)long-chain-fatty-acid-CoA ligase Lcf1⌘
S. pombeUniProtKB:Q9P7D7 · GeneDB_Spombe:SPBP4H10.11c (SPBP4H10.11c · lcf2)long-chain-fatty-acid-CoA ligase⌘
S. pombeUniProtKB:Q9P7T1 · GeneDB_Spombe:SPAC23G3.02c (sib1 · SPAC23G3.02c)ferrichrome synthetase Sib1⌘
ProteinPublicationCurator Notes
UniProtKB:P47912 · SGD:S000004860PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL1 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL1 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G20560.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G20560.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P38225 · SGD:S000000245PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein O35488 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein O35488 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P38225 · SGD:S000000245PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein O88561 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein O88561 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P38225 · SGD:S000000245PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q14C50 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q14C50 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P38225 · SGD:S000000245PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q4LDG0 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q4LDG0 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P38225 · SGD:S000000245PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q60714 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q60714 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P38225 · SGD:S000000245PMID:10880966 Dirusso CC, et al. Murine FATP alleviates growth and biochemical deficiencies of yeast fat1Delta strains. Eur J Biochem. 2000 Jul;267(14):4422-33.The M. musculus protein Q60714 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38225 · SGD:S000000245PMID:10880966 Dirusso CC, et al. Murine FATP alleviates growth and biochemical deficiencies of yeast fat1Delta strains. Eur J Biochem. 2000 Jul;267(14):4422-33.The M. musculus protein Q60714 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38225 · SGD:S000000245PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q60714 complements a homologous mutation in S. cerevisiae. This paper shows that mouse FATP1 (Q60714) complements a yeast faa1 fat1 double mutant.
UniProtKB:P38225 · SGD:S000000245PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q91VE0 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q91VE0 was expressed in S. cerevisiae, but complementation was not directly tested. In this paper, six isoforms of the M. musculus fatty acid transport proteins (FATP) were expressed in a yeast faa1 fat1 double mutant in order to carry out comparative biochemical studies.
UniProtKB:P47912 · SGD:S000004860PMID:7738025 Knoll LJ, et al. Complementation of Saccharomyces cerevisiae strains containing fatty acid activation gene (FAA) deletions with a mammalian acyl-CoA synthetase. J Biol Chem. 1995 May 5;270(18):10861-7.The R. norvegicus protein RLACS complements a homologous mutation in S. cerevisiae. The authors note that the sensitivity of Faa4p and rat liver acyl-CoA synthetase (RLACS), but not Faa1p, to inhibition by triacsin C suggests that RLACS is functionally more similar to Faa4p than to Faa1p.
UniProtKB:P30624 · SGD:S000005844PMID:7738025 Knoll LJ, et al. Complementation of Saccharomyces cerevisiae strains containing fatty acid activation gene (FAA) deletions with a mammalian acyl-CoA synthetase. J Biol Chem. 1995 May 5;270(18):10861-7.The R. norvegicus protein RLACS complements a homologous mutation in S. cerevisiae. The authors note that the sensitivity of Faa4p and rat liver acyl-CoA synthetase (RLACS), but not Faa1p, to inhibition by triacsin C suggests that RLACS is functionally more similar to Faa4p than to Faa1p.
UniProtKB:P52910 · SGD:S000004143PMID:15042592 Rodrigues F, et al. Isolation of an acetyl-CoA synthetase gene (ZbACS2) from Zygosaccharomyces bailii. Yeast. 2004 Mar;21(4):325-31.The Z. bailii protein ZbACS2 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q60714 complements a homologous mutation in S. cerevisiae. This paper shows that mouse FATP1 (Q60714) complements a yeast faa1 fat1 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL4 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL4 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL5 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL5 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL6 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:16466685 Tong F, et al. Fatty acid transport by vectorial acylation in mammals: roles played by different isoforms of rat long-chain acyl-CoA synthetases. Arch Biochem Biophys. 2006 Mar 1;447(1):46-52.The R. norvegicus protein ACSL6 complements a homologous mutation in S. cerevisiae. All four rat acyl-CoA synthetases (ACS) were able to restore ACS activity in a yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G21530.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G21530.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G21540.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G21540.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G75960.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G75960.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G77240.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT1G77240.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT2G17650.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT2G17650.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT3G16910.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT3G16910.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT5G16340.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT5G16340.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT5G16370.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:12805634 Shockey JM, et al. Arabidopsis contains a large superfamily of acyl-activating enzymes. Phylogenetic and biochemical analysis reveals a new class of acyl-coenzyme a synthetases. Plant Physiol. 2003 Jun;132(2):1065-76.The A. thaliana protein AT5G16370.1 does not complement a homologous mutation in S. cerevisiae. The authors note that none of the A. thaliana clade VI acyl-activating enzyme (AAE) constructs were able to complement the yeast faa1 faa4 double mutant.
UniProtKB:P38225 · SGD:S000000245PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein O35488 complements a homologous mutation in S. cerevisiae. This paper shows that mouse FATP2 (O35488) complements a yeast faa1 fat1 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein O35488 complements a homologous mutation in S. cerevisiae. This paper shows that mouse FATP2 (O35488) complements a yeast faa1 fat1 double mutant.
UniProtKB:P38225 · SGD:S000000245PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein O88561 does not complement a homologous mutation in S. cerevisiae. This paper shows that mouse FATP3 (O88561) does not complement a yeast faa1 fat1 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein O88561 does not complement a homologous mutation in S. cerevisiae. This paper shows that mouse FATP3 (O88561) does not complement a yeast faa1 fat1 double mutant.
UniProtKB:P38225 · SGD:S000000245PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q14C50 does not complement a homologous mutation in S. cerevisiae. This paper shows that mouse FATP6 (Q14C50) does not complement a yeast faa1 fat1 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q14C50 does not complement a homologous mutation in S. cerevisiae. This paper shows that mouse FATP6 (Q14C50) does not complement a yeast faa1 fat1 double mutant.
UniProtKB:P38225 · SGD:S000000245PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q4LDG0 does not complement a homologous mutation in S. cerevisiae. This paper shows that mouse FATP5 (Q4LDG0) does not complement a yeast faa1 fat1 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q4LDG0 does not complement a homologous mutation in S. cerevisiae. This paper shows that mouse FATP5 (Q4LDG0) does not complement a yeast faa1 fat1 double mutant.
UniProtKB:P38225 · SGD:S000000245PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q91VE0 complements a homologous mutation in S. cerevisiae. This paper shows that mouse FATP4 (Q91VE0) complements a yeast faa1 fat1 double mutant.
UniProtKB:P30624 · SGD:S000005844PMID:15699031 DiRusso CC, et al. Comparative biochemical studies of the murine fatty acid transport proteins (FATP) expressed in yeast. J Biol Chem. 2005 Apr 29;280(17):16829-37.The M. musculus protein Q91VE0 complements a homologous mutation in S. cerevisiae. This paper shows that mouse FATP4 (Q91VE0) complements a yeast faa1 fat1 double mutant.
UniProtKB:P47912 · SGD:S000004860PMID:22633490 Nakahara K, et al. The Sjögren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway. Mol Cell. 2012 May 25;46(4):461-71.The H. sapiens protein ACSL1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:22633490 Nakahara K, et al. The Sjögren-Larsson syndrome gene encodes a hexadecenal dehydrogenase of the sphingosine 1-phosphate degradation pathway. Mol Cell. 2012 May 25;46(4):461-71.The H. sapiens protein ACSL1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL3 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL3 complements a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL4 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL4 complements a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens proteins SLC27A4 and ACSVL4 complement a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens proteins SLC27A4 and ACSVL4 complement a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens proteins SLC27A2 and ACSLV1 complement a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens proteins SLC27A2 and ACSLV1 complement a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSBG1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSBG1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL6 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL6 complements a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL5 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:24269233 Ohkuni A, et al. Identification of acyl-CoA synthetases involved in the mammalian sphingosine 1-phosphate metabolic pathway. Biochem Biophys Res Commun. 2013 Dec 13;442(3-4):195-201.The H. sapiens protein ACSL5 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38225 · SGD:S000000245PMID:18258213 DiRusso CC, et al. Functional domains of the fatty acid transport proteins: studies using protein chimeras. Biochim Biophys Acta. 2008 Mar;1781(3):135-43.The M. musculus protein Slc27a1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38225 · SGD:S000000245PMID:18258213 DiRusso CC, et al. Functional domains of the fatty acid transport proteins: studies using protein chimeras. Biochim Biophys Acta. 2008 Mar;1781(3):135-43.The M. musculus protein Slc27a4 complements a homologous mutation in S. cerevisiae.
UniProtKB:P38225 · SGD:S000000245PMID:10880966 Dirusso CC, et al. Murine FATP alleviates growth and biochemical deficiencies of yeast fat1Delta strains. Eur J Biochem. 2000 Jul;267(14):4422-33.The M. musculus protein Slc27a1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P47912 · SGD:S000004860PMID:7738025 Knoll LJ, et al. Complementation of Saccharomyces cerevisiae strains containing fatty acid activation gene (FAA) deletions with a mammalian acyl-CoA synthetase. J Biol Chem. 1995 May 5;270(18):10861-7.The R. norvegicus protein Acsl1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P30624 · SGD:S000005844PMID:7738025 Knoll LJ, et al. Complementation of Saccharomyces cerevisiae strains containing fatty acid activation gene (FAA) deletions with a mammalian acyl-CoA synthetase. J Biol Chem. 1995 May 5;270(18):10861-7.The R. norvegicus protein Acsl1 complements a homologous mutation in S. cerevisiae.
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 (2)
ENSEMBL:ENSG00000068366 · UniProtKB:O60488#300194 AMME COMPLEX;;ALPORT SYNDROME, MENTAL RETARDATION, MIDFACE HYPOPLASIA, AND ELLIPTOCYTOSIS;;ATS-MR
UniProtKB:P38225 · SGD:S000000245#300387 MENTAL RETARDATION, X-LINKED 63; MRX63;;MENTAL RETARDATION, X-LINKED 68; MRX68
SGD Disease Papers (16)
UniProtKB:P39518 · SGD:S000000817PMID:9660783 Watkins PA, et al. (1998) Disruption of the Saccharomyces cerevisiae FAT1 gene decreases very long-chain fatty acyl-CoA synthetase activity and elevates intracellular very long-chain fatty acid concentrations. J Biol Chem 273(29):18210-9
PMID:12719378 Heinzer AK, et al. (2003) A very long-chain acyl-CoA synthetase-deficient mouse and its relevance to X-linked adrenoleukodystrophy. Hum Mol Genet 12(10):1145-54
PMID:11330068 Watkins PA, et al. (2000) Disruption of a yeast very-long-chain acyl-CoA synthetase gene simulates the cellular phenotype of X-linked adrenoleukodystrophy. Cell Biochem Biophys 32 Spring:333-7
UniProtKB:P39518 · SGD:S000000817PMID:8441467 Mosser J, et al. (1993) Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters. Nature 361(6414):726-30
PMID:8209376 Bojes HK and Thurman RG (1994) Peroxisomal proliferators inhibit acyl CoA synthetase and stimulate protein kinase C in vivo. Toxicol Appl Pharmacol 126(2):233-9
PMID:7818538 Kalish JE, et al. (1995) Peroxisomal activation of long- and very long-chain fatty acids in the yeast Pichia pastoris. Biochem Biophys Res Commun 206(1):335-40
PMID:6303275 Sasaki N, et al. (1982) Effect of hypertension on lipid metabolism and beta-oxidation in rat aorta and brain microvessels. Artery 11(2):108-18
PMID:6242313 Carroll JE, et al. (1984) Brominated vegetable oil myopathy: inhibition at multiple sites. Muscle Nerve 7(8):642-6
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