P-POD: Princeton Protein Orthology Database: GO3/Nens76

This family has 101 members: 26 Arabidopsis thaliana, 9 Caenorhabditis elegans, 10 Danio rerio, 6 Dictyostelium discoideum, 10 Drosophila melanogaster, 2 Escherichia coli, 7 Gallus gallus, 7 Homo sapiens, 7 Mus musculus, 8 Rattus norvegicus, 5 Saccharomyces cerevisiae, 4 Schizosaccharomyces pombe.

Interactive Java Applets: Notung Tree Analysis · Jalview Alignment

GO3/Nens76
101 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaNCBI:NP_188232.2 · TAIR:locus:2093447 (AT3G16110 · ATPDI4 · ATPDIL1-6 · PDI4 · MSL1.15)ARABIDOPSIS THALIANA PROTEIN DISULFIDE ISOMERASE 4 · PROTEIN DISULFIDE ISOMERASE 4 · PDI-LIKE 1-6⌘
A. thalianaNCBI:NP_173403.1 · TAIR:locus:2013169 (F14P1.32 · F14P1_32 · AT1G19730 · thioredoxin · ATH4 · ATTRX4)thioredoxin H-type 4⌘
A. thalianaNCBI:NP_191201.1 · TAIR:locus:2102579 (T5P19.70 · AT3G56420)⌘
A. thalianaNCBI:NP_181611.2 · TAIR:locus:2064854 (ATCXXS2 · T7D17_3 · AT2G40790 · T7D17.3)C-TERMINAL CYSTEINE RESIDUE IS CHANGED TO A SERINE 1⌘
A. thalianaNCBI:NP_190672.1 · TAIR:locus:2080963 (AT3G51030 · F24M12.70 · thioredoxin · ATTRX1)Attrx h1 · Arabidopsis thaliana thioredoxin H-type 1⌘
A. thalianaNCBI:NP_179159.1 · TAIR:locus:2053573 (ATHM3 · ATM3 · F9O13.12 · AT2G15570)Arabidopsis thioredoxin M-type 3⌘
A. thalianaNCBI:NP_177802.2 · TAIR:locus:2030051
A. thalianaNCBI:NP_175636.2 · TAIR:locus:2018134 (F19K6_17 · F19K6.17 · PDI3 · ATPDI3 · ATPDIL1-5 · AT1G52260)PROTEIN DISULFIDE ISOMERASE 3 · ARABIDOPSIS THALIANA PROTEIN DISULFIDE ISOMERASE 3 · PDI-LIKE 1-5⌘
A. thalianaNCBI:NP_849585.1 · TAIR:locus:2020813 (ATHM1 · ATM1 · TRX-M1 · AT1G03680)ARABIDOPSIS THIOREDOXIN M-TYPE 1 · THIOREDOXIN M-TYPE 1⌘
A. thalianaNCBI:NP_198811.1 · TAIR:locus:2178007 (ATTRX2 · MYH19_110 · ATTRXH2 · TRXH2 · MYH19.110 · ATH2 · AT5G39950 · THIOREDOXIN)THIOREDOXIN H2 · Arabidopsis thioredoxin h2 · THIOREDOXIN 2⌘
A. thalianaNCBI:NP_187483.1 · TAIR:locus:2077833 (ATH9 · AT3G08710 · F17O14.18)thioredoxin H-type 9⌘
A. thalianaNCBI:NP_177146.1 · TAIR:locus:2196784 (AT1G69880 · ATH8 · T17F3_9 · T17F3.9)thioredoxin H-type 8⌘
A. thalianaNCBI:NP_188155.1 · TAIR:locus:2090126 (MJK13.20 · ATHM4 · TRX-M4 · AT3G15360 · ATM4)ARABIDOPSIS THIOREDOXIN M-TYPE 4⌘
A. thalianaNCBI:NP_851234.1 · TAIR:locus:2175811 (MUP24.6 · AT5G60640 · PDI2 · ATPDIL1-4 · ATPDI2 · MUP24_6)PROTEIN DISULFIDE ISOMERASE 2 · PDI-LIKE 1-4 · ARABIDOPSIS THALIANA PROTEIN DISULFIDE ISOMERASE 2⌘
A. thalianaNCBI:NP_175128.1 · TAIR:locus:2825451 (F27F5.21 · LIV1 · ATH5 · ATTRX5 · AT1G45145 · F27F5_21 · thioredoxin)LOCUS OF INSENSITIVITY TO VICTORIN 1 · thioredoxin H-type 5⌘
A. thalianaNCBI:NP_175021.2 · TAIR:locus:2194661
A. thalianaNCBI:NP_172620.1 · TAIR:locus:2200141 (ATCXXS1 · AT1G11530 · T23J18_19 · T23J18.19)C-terminal cysteine residue is changed to a serine 1⌘
A. thalianaNCBI:NP_199680.2 · TAIR:locus:2156489 (K24G6.2 · K24G6_2 · AT5G48690)⌘
A. thalianaNCBI:NP_564566.1 · TAIR:locus:2011932 (F14I3_8 · F14I3.8 · ATX · ATHX · AT1G50320)thioredoxin x⌘
A. thalianaNCBI:NP_199112.1 · TAIR:locus:2159971 (ATH3 · AT5G42980 · MBD2.18 · ATTRX3 · TRXH3 · MBD2_18 · ATTRXH3 · THIOREDOXIN)THIOREDOXIN H3 · THIOREDOXIN 3 · thioredoxin H-type 3⌘
A. thalianaNCBI:NP_192261.1 · TAIR:locus:2128756 (F9H3_15 · F9H3.15 · ATHM2 · T5L23.1 · AT4G03520)⌘
A. thalianaNCBI:NP_563718.1 · TAIR:locus:2010637 (F13M7.16 · AT1G04850 · F13M7_16)⌘
A. thalianaNCBI:NP_177875.1 · TAIR:locus:2204670 (ATPDI6 · T5M16_10 · AT1G77510 · T5M16.10 · PDI6 · ATPDIL1-2)PROTEIN DISULFIDE ISOMERASE 6 · PDI-LIKE 1-2⌘
A. thalianaNCBI:NP_176182.1 · TAIR:locus:2025971 (F23H11_5 · F23H11.5 · AT1G59730 · ATH7)thioredoxin H-type 7⌘
A. thalianaNCBI:NP_191056.2 · TAIR:locus:2082712 (ATPDIL1-3 · ATPDI1 · AT3G54960 · PDI1 · T15C9.4)PDI-LIKE 1-3 · ARABIDOPSIS THALIANA PROTEIN DISULFIDE ISOMERASE 1 · PROTEIN DISULFIDE ISOMERASE 1⌘
A. thalianaNCBI:NP_173594.1 · TAIR:locus:2036906 (F8K7.19 · ATPDI5 · PDI5 · ATPDIL1-1 · F8K7_19 · AT1G21750)ARABIDOPSIS THALIANA PROTEIN DISULFIDE ISOMERASE 5 · PDI-LIKE 1-1 · PROTEIN DISULFIDE ISOMERASE 5⌘
C. elegansWB:WBGene00003962 (C14B1.1 · pdi-1) · UniProtKB:Q17967⌘
C. elegansWB:WBGene00003963 (C07A12.4 · pdi-2) · UniProtKB:Q17770⌘
C. elegansWB:WBGene00015752 (C14B9.2) · UniProtKB:P34329⌘
C. elegansWB:WBGene00015062 (trx-1 · B0228.5) · UniProtKB:Q09433⌘
C. elegansWB:WBGene00007099 (B0024.9 · trx-2) · UniProtKB:Q17424⌘
C. elegansWB:WBGene00003964 (H06O01.1 · pdi-3) · UniProtKB:O17908⌘
C. elegansWB:WBGene00021933 (Y55F3AR.2) · UniProtKB:Q9N357⌘
C. elegansWB:WBGene00017733 (ubxn-1 · F23C8.4) · UniProtKB:Q9TXH9 (ubxn-1 · F23C8.4)Ubx-containing protein in nematode protein 1⌘⌘
C. elegansWB:WBGene00021548 (Y44E3A.3) · UniProtKB:Q9TXY8⌘
D. rerioENSEMBL:ENSDARP00000068966
D. rerioUniProtKB:Q6NXA9 · ZFIN:ZDB-GENE-030131-792 (ubxn1)UBX domain protein 1⌘
D. rerioZFIN:ZDB-GENE-040801-20 (zgc:100906) · UniProtKB:Q6DEI4⌘
D. rerioZFIN:ZDB-GENE-060421-2552 (zgc:136472) · UniProtKB:Q6DG87⌘
D. rerioZFIN:ZDB-GENE-040718-162 (zgc:92903) · UniProtKB:Q6DGI6⌘
D. rerioZFIN:ZDB-GENE-040426-2238 (zgc:77086) · UniProtKB:Q6NXB9⌘
D. rerioZFIN:ZDB-GENE-040426-1795 (zgc:77127) · UniProtKB:Q6P131⌘
D. rerioZFIN:ZDB-GENE-030131-8581 (zgc:56493) · UniProtKB:Q7ZUI4⌘
D. rerioUniProtKB:Q7ZVH2 · ZFIN:ZDB-GENE-030131-5493 (pdia4)protein disulfide isomerase associated 4⌘
D. rerioUniProtKB:Q803D7 · ZFIN:ZDB-GENE-031002-9 (pdia3)protein disulfide isomerase family A, member 3⌘
D. discoideumNCBI:EAL64933.1 · dictyBase:DDB_G0284939 (DDB_G0284939)thioredoxin domain-containing protein⌘
D. discoideumUniProtKB:Q54EN4 · dictyBase:DDB_G0291434 (PDI · pdi2)protein disulfide isomerase⌘
D. discoideumdictyBase:DDB_G0294489 (trxC · thioredoxin · TRX3) · UniProtKB:P29447⌘
D. discoideumdictyBase:DDB_G0287849 (trxD · thioredoxin) · UniProtKB:Q1ZXE0⌘
D. discoideumdictyBase:DDB_G0287227 (trxE · thioredoxin) · UniProtKB:Q54KN7⌘
D. discoideumUniProtKB:Q75JM6 · dictyBase:DDB_G0276057 (DDB_G0276057)ZZ-type zinc finger-containing protein, thioredoxin domain-containing protein, UBX domain-containing protein, UBA domain-containing protein⌘
D. melanogasterUniProtKB:P54399 · FB:FBgn0014002 (dpdi · EP(3)1022 · Dpdi · CG6988 · Pdi · pdi · PDI)Protein disulfide isomerase · disulfide isomerase · protein disulfide isomerase · protein-disulfide isomerase⌘
D. melanogasterFB:FBgn0011761 (thioredoxin-like · CG4193 · deadhead · dhd · thioredoxin · DmTrx-1 · Trx-1) · UniProtKB:P47938⌘
D. melanogasterFB:FBgn0040070 (Trx-2 · DmTrx-2 · thioredoxin-2 · dmtrx-2 · CG31884 · thioredoxin · anon-WO0118547.188 · CG3864) · UniProtKB:Q9V429⌘
D. melanogasterUniProtKB:Q8IFW4 · FB:FBgn0029752 (CG3315 · thioredoxin · TrxT)Thioredoxin T⌘
D. melanogasterFB:FBgn0024986 (CG3719 · BcDNA:LD03613 · thioredoxin · EG:132E8.3) · UniProtKB:O76877⌘
D. melanogasterFB:FBgn0033663 (Erp60 · CG8983 · anon-fast-evolving-3D9 · D-ERp60 · ERp60 · anon-EST:fe3D9 · Ov6) · UniProtKB:Q3YMU0⌘
D. melanogasterFB:FBgn0034472 (mtr · CG8517 · thioredoxin) · UniProtKB:Q7K037⌘
D. melanogasterFB:FBgn0035830 (CG8209 · anon-WO0172774.138) · UniProtKB:Q9VSC5⌘
D. melanogasterFB:FBgn0036442 (CG13473) · UniProtKB:Q9VUG9⌘
D. melanogasterFB:FBgn0035334 (CG8993 · thioredoxin) · UniProtKB:Q9W022⌘
E. coliUniProtKB:P0AGG4 · ECOLI:OX-THIOREDOXIN2-MONOMER (trxC · yfiG · ECK2580 · b2582)oxidized thioredoxin 2⌘
E. coliUniProtKB:P0AA25 · ECOLI:OX-THIOREDOXIN-MONOMER
G. gallusNCBI:XP_420095 · ENTREZ:374091
G. gallusNCBI:XP_428969 · ENTREZ:431417
G. gallusENTREZ:396376 · UniProtKB:P12244 (GSBP_CHICK · P12244 · IPI00597613)Dolichyl-diphosphooligosaccharide--protein glycotransferase⌘
G. gallusENTREZ:373899 · UniProtKB:Q8JG64 (GRP58 · ERP57 · PDIA3_CHICK · IPI00575271 · PDIA3 · Q8JG64)Protein disulfide-isomerase A3⌘
G. gallusUniProtKB:P08629 (Thioredoxin · P08629 · TXN · THIO_CHICK · IPI00601777) · ENTREZ:396437⌘
G. gallusUniProtKB:Q5ZJY6 (Q5ZJY6 · IPI00589732 · RCJMB04_14g3) · ENTREZ:426978⌘
G. gallusUniProtKB:Q5ZK20 (Q5ZK20 · RCJMB04_13l7 · IPI00589958) · ENTREZ:420785⌘
H. sapiensENSEMBL:ENSG00000185624 · UniProtKB:P07237 (PDIA1 · PDIA1_HUMAN · P4HB · PDI · P07237 · ERBA2L · PO4DB · IPI00010796)Protein disulfide-isomerase⌘
H. sapiensENSEMBL:ENSG00000167004 · UniProtKB:P30101 (PDIA3_HUMAN · IPI00025252 · GRP58 · ERP60 · P30101 · ERP57 · PDIA3)Protein disulfide-isomerase A3⌘
H. sapiensENSEMBL:ENSG00000155660 · UniProtKB:P13667 (PDIA4 · PDIA4_HUMAN · ERP72 · P13667 · ERP70 · IPI00009904)Protein disulfide-isomerase A4⌘
H. sapiensENSEMBL:ENSG00000169340 · UniProtKB:Q8N807 (Q8N807 · PDILT_HUMAN · IPI00646007 · PDILT)Protein disulfide-isomerase-like protein of the testis⌘
H. sapiensENSEMBL:ENSG00000100348 · UniProtKB:Q99757 (THIOM_HUMAN · IPI00878215 · TRX2 · TXN2 · Q99757)Thioredoxin, mitochondrial⌘
H. sapiensUniProtKB:P10599 (TRX1 · Thioredoxin · P10599 · IPI00216298 · TXN · TRDX · TRX · THIO_HUMAN) · ENSEMBL:ENSG00000136810⌘
H. sapiensENSEMBL:ENSG00000162191 · UniProtKB:Q04323 (IPI00027378 · UBXN1_HUMAN · SAKS1 · IPI00396563 · UBXN1 · Q04323)UBX domain-containing protein 1⌘
M. musculusUniProtKB:P09103 · MGI:MGI:97464 (Thbp · ERp59 · P4hb)prolyl 4-hydroxylase, beta polypeptide · protein disulfide isomerase⌘
M. musculusUniProtKB:P27773 · MGI:MGI:95834 (Grp58 · ERp57 · Erp · Pdia3 · PDI · Plca · ERp60 · ERp61 · PDI-Q2)protein disulfide isomerase associated 3⌘
M. musculusUniProtKB:P08003 · MGI:MGI:104864 (ERp72 · Pdia4 · Cai)protein disulfide isomerase associated 4⌘
M. musculusUniProtKB:Q9DAN1 · MGI:MGI:1919080 (Pdilt · PDILT)protein disulfide isomerase-like, testis expressed⌘
M. musculusUniProtKB:P97493 · MGI:MGI:1929468 (Txn2)thioredoxin 2⌘
M. musculusUniProtKB:P10639 · MGI:MGI:98874 (Trx1 · Txn1)thioredoxin 1⌘
M. musculusUniProtKB:Q922Y1 · MGI:MGI:1289301 (Ubxn1 · D19Ertd721e · T25529)UBX domain protein 1⌘
R. norvegicusNCBI:XP_577822 · RGD:1559902 (RGD1559902)similar to thioredoxin⌘
R. norvegicusUniProtKB:P04785 · RGD:3244 (P4hb)prolyl 4-hydroxylase, beta polypeptide⌘
R. norvegicusUniProtKB:P11598 · RGD:68430 (Pdia3)protein disulfide isomerase family A, member 3⌘
R. norvegicusUniProtKB:P38659 · RGD:619835 (Pdia4)protein disulfide isomerase family A, member 4⌘
R. norvegicusUniProtKB:Q5XI02 · RGD:1307822 (Pdilt)protein disulfide isomerase-like protein of the testis⌘
R. norvegicusUniProtKB:P97615 · RGD:71040 (Txn2)thioredoxin 2⌘
R. norvegicusUniProtKB:P11232 · RGD:621157 (Txn1)thioredoxin 1⌘
R. norvegicusRGD:1309471 (Ubxn1) · UniProtKB:Q499N6 (Saks1 · UBXN1_RAT · IPI00371410 · Ubxn1 · IPI00785573 · Q499N6)UBX domain protein 1 · UBX domain-containing protein 1⌘⌘
S. cerevisiaeUniProtKB:P32474 · SGD:S000002926 (YDR518W · EUG1)Protein disulfide isomerase of the endoplasmic reticulum lumen, function overlaps with that of Pdi1p⌘
S. cerevisiaeUniProtKB:P17967 · SGD:S000000548 (MFP1 · YCL043C · PDI1 · TRG1)Protein disulfide isomerase, multifunctional protein resident in the endoplasmic reticulum lumen, essential for the formation of disulfide bonds in secretory and cell-surface proteins, unscrambles non-native disulfide bonds⌘
S. cerevisiaeUniProtKB:P22217 · SGD:S000004033 (TRX1 · YLR043C · LMA1)Cytoplasmic thioredoxin isoenzyme of the thioredoxin system which protects cells against oxidative and reductive stress, forms LMA1 complex with Pbi2p, acts as a cofactor for Tsa1p, required for ER-Golgi transport and vacuole inheritance⌘
S. cerevisiaeUniProtKB:P22803 · SGD:S000003441 (TRX2 · YGR209C · LMA1)Cytoplasmic thioredoxin isoenzyme of the thioredoxin system which protects cells against oxidative and reductive stress, forms LMA1 complex with Pbi2p, acts as a cofactor for Tsa1p, required for ER-Golgi transport and vacuole inheritance⌘
S. cerevisiaeUniProtKB:P25372 · SGD:S000000679 (YCR083W · TRX3)Mitochondrial thioredoxin, highly conserved oxidoreductase required to maintain the redox homeostasis of the cell, forms the mitochondrial thioredoxin system with Trr2p, redox state is maintained by both Trr2p and Glr1p⌘
S. pombeUniProtKB:Q10057 · GeneDB_Spombe:SPAC1F5.02 (SPAC1F5.02)protein disulfide isomerase⌘
S. pombeUniProtKB:O14463 · GeneDB_Spombe:SPAC7D4.07c (SPAC7D4.07c · trx1)cytosolic thioredoxin Trx1⌘
S. pombeUniProtKB:O94504 · GeneDB_Spombe:SPBC12D12.07c (SPBC12D12.07c · trx2)mitochondrial thioredoxin Trx2⌘
S. pombeUniProtKB:Q10483 · GeneDB_Spombe:SPAC17C9.11c (SPAC17C9.11c)zf-C2H2 type zinc finger protein/UBA domain protein⌘
ProteinPublicationCurator Notes
UniProtKB:P22803 · SGD:S000003441PMID:10906327 Bréheĺin C, et al. Characterization of determinants for the specificity of Arabidopsis thioredoxins h in yeast complementation. J Biol Chem. 2000 Oct 13;275(41):31641-7.The A. thaliana protein AT5G15410.1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows partial complementation of a yeast trx1 trx2 double mutant by A. thaliana AtTRX3 (AT5G15410.1). AtTRX3 induces methionine sulfoxide assimilation and restores a normal cell cycle.
UniProtKB:P22217 · SGD:S000004033PMID:10906327 Bréheĺin C, et al. Characterization of determinants for the specificity of Arabidopsis thioredoxins h in yeast complementation. J Biol Chem. 2000 Oct 13;275(41):31641-7.The A. thaliana protein AT5G39950.1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows partial complementation of a yeast trx1 trx2 double mutant by A. thaliana AtTRX2 (AT5G39950.1). AtTRX2 induces methionine sulfoxide assimilation and restores a normal cell cycle.
UniProtKB:P22217 · SGD:S000004033PMID:16299179 Lee MY, et al. Induction of thioredoxin is required for nodule development to reduce reactive oxygen species levels in soybean roots. Plant Physiol. 2005 Dec;139(4):1881-9.The G. max protein GmTRX complements a homologous mutation in S. cerevisiae. This paper shows that soybean GmTRX complements a yeast trx1 trx2 double mutant.
UniProtKB:P17967 · SGD:S000000548PMID:8385117 Günther R, et al. Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family. J Biol Chem. 1993 Apr 15;268(11):7728-32.The M. musculus protein P08003 complements a homologous mutation in S. cerevisiae. This paper shows that murine ERp72 (P08003) partially complements a yeast pdi1 null mutant.
UniProtKB:P17967 · SGD:S000000548PMID:7499282 Laboissiere MC, et al. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J Biol Chem. 1995 Nov 24;270(47):28006-9.The R. norvegicus protein PDI complements a homologous mutation in S. cerevisiae.
UniProtKB:P17967 · SGD:S000000548PMID:15377672 Xiao R, et al. The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum. J Biol Chem. 2004 Nov 26;279(48):49780-6.The R. norvegicus protein PDI complements a homologous mutation in S. cerevisiae. This paper shows that rat PDI partially complements a yeast pdi1 null mutant.
UniProtKB:P17967 · SGD:S000000548PMID:16889384 Zhang W, et al. Enhanced secretion of heterologous proteins in Pichia pastoris following overexpression of Saccharomyces cerevisiae chaperone proteins. Biotechnol Prog. 2006 Jul-Aug;22(4):1090-5.The S. cerevisiae protein PDI1 was expressed in P. pastoris, but complementation was not directly tested. This paper shows heterologous overexpression of S. cerevisiae PDI1 in P. pastoris.
UniProtKB:P22803 · SGD:S000003441PMID:17098852 Traverso JA, et al. PsTRXh1 and PsTRXh2 are both pea h-type thioredoxins with antagonistic behavior in redox imbalances. Plant Physiol. 2007 Jan;143(1):300-11.The P. sativum protein PsTRXh1 complements a homologous mutation in S. cerevisiae. P. sativum PsTRXh1 complements a yeast trx1 trx2 double mutant.
UniProtKB:P22217 · SGD:S000004033PMID:17098852 Traverso JA, et al. PsTRXh1 and PsTRXh2 are both pea h-type thioredoxins with antagonistic behavior in redox imbalances. Plant Physiol. 2007 Jan;143(1):300-11.The P. sativum protein PsTRXh2 complements a homologous mutation in S. cerevisiae. P. sativum PsTRXh2 complements a yeast trx1 trx2 double mutant.
UniProtKB:P22803 · SGD:S000003441PMID:16299179 Lee MY, et al. Induction of thioredoxin is required for nodule development to reduce reactive oxygen species levels in soybean roots. Plant Physiol. 2005 Dec;139(4):1881-9.The G. max protein GmTRX complements a homologous mutation in S. cerevisiae. This paper shows that soybean GmTRX complements a yeast trx1 trx2 double mutant.
UniProtKB:P22217 · SGD:S000004033PMID:10906327 Bréheĺin C, et al. Characterization of determinants for the specificity of Arabidopsis thioredoxins h in yeast complementation. J Biol Chem. 2000 Oct 13;275(41):31641-7.The A. thaliana protein AT5G15410.1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows partial complementation of a yeast trx1 trx2 double mutant by A. thaliana AtTRX3 (AT5G15410.1). AtTRX3 induces methionine sulfoxide assimilation and restores a normal cell cycle.
UniProtKB:P22803 · SGD:S000003441PMID:10906327 Bréheĺin C, et al. Characterization of determinants for the specificity of Arabidopsis thioredoxins h in yeast complementation. J Biol Chem. 2000 Oct 13;275(41):31641-7.The A. thaliana protein AT5G39950.1 was expressed in S. cerevisiae, but complementation was not directly tested. This paper shows partial complementation of a yeast trx1 trx2 double mutant by A. thaliana AtTRX2 (AT5G39950.1). AtTRX2 induces methionine sulfoxide assimilation and restores a normal cell cycle.
UniProtKB:P17967 · SGD:S000000548PMID:8385117 Günther R, et al. Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family. J Biol Chem. 1993 Apr 15;268(11):7728-32.The R. norvegicus protein ERp61 does not complement a homologous mutation in S. cerevisiae.
UniProtKB:P17967 · SGD:S000000548PMID:8385117 Günther R, et al. Functional replacement of the Saccharomyces cerevisiae Trg1/Pdi1 protein by members of the mammalian protein disulfide isomerase family. J Biol Chem. 1993 Apr 15;268(11):7728-32.The M. musculus protein P09103 complements a homologous mutation in S. cerevisiae. This paper shows that murine ERp59/PDI (P09103) partially complements a yeast pdi1 null mutant.
UniProtKB:P22803 · SGD:S000003441PMID:17098852 Traverso JA, et al. PsTRXh1 and PsTRXh2 are both pea h-type thioredoxins with antagonistic behavior in redox imbalances. Plant Physiol. 2007 Jan;143(1):300-11.The P. sativum protein PsTRXh1 complements a homologous mutation in S. cerevisiae. P. sativum PsTRXh1 complements a yeast trx1 trx2 double mutant.
UniProtKB:P22217 · SGD:S000004033PMID:17098852 Traverso JA, et al. PsTRXh1 and PsTRXh2 are both pea h-type thioredoxins with antagonistic behavior in redox imbalances. Plant Physiol. 2007 Jan;143(1):300-11.The P. sativum protein PsTRXh2 complements a homologous mutation in S. cerevisiae. P. sativum PsTRXh2 complements a yeast trx1 trx2 double mutant.
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
Send questions, suggestions, and comments to: yfgdb@genomics.princeton.edu