P-POD: Princeton Protein Orthology Database: GO3/Para1435

This family has 8 members: 1 Arabidopsis thaliana, 1 Caenorhabditis elegans, 1 Drosophila melanogaster, 1 Homo sapiens, 1 Mus musculus, 1 Rattus norvegicus, 1 Saccharomyces cerevisiae, 1 Schizosaccharomyces pombe.

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GO3/Para1435
8 members.
OrganismProtein (Synonyms)DescriptionAmiGO
A. thalianaNCBI:NP_179395.1 · TAIR:locus:2060922 (T27K22_9 · T27K22.9 · AT2G18040 · PIN1AT)PROLYL CIS/TRANS ISOMERASE · PEPTIDYLPROLYL CIS/TRANS ISOMERASE, NIMA-INTERACTING 1⌘
C. elegansWB:WBGene00022448 (Y110A2AL.13) · UniProtKB:Q9N492⌘
D. melanogasterUniProtKB:P54353 · FB:FBgn0015379 (CG17051 · dod · Pin1 · dodo)⌘
H. sapiensENSEMBL:ENSG00000127445 · UniProtKB:Q13526 (PIN1 · Q13526 · PIN1_HUMAN · IPI00013723)Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1⌘
M. musculusUniProtKB:Q9QUR7 · MGI:MGI:1346036 (Pin1 · D9Bwg1161e)protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1⌘
R. norvegicusNCBI:XP_216609 · RGD:1310299 (Pin1)peptidylprolyl cis/trans isomerase, NIMA-interacting 1⌘
S. cerevisiaeUniProtKB:P22696 · SGD:S000003778 (PTF1 · PIN1 · YJR017C · ESS1)Peptidylprolyl-cis/trans-isomerase (PPIase) specific for phosphorylated serine and threonine residues N-terminal to proline⌘
S. pombeUniProtKB:O74448 · GeneDB_Spombe:SPCC16C4.03 (SPCC16C4.03 · pin1)peptidyl-prolyl cis-trans isomerase Pin1⌘
ProteinPublicationCurator Notes
UniProtKB:P22696 · SGD:S000003778PMID:11118438 Yao JL, et al. Functional conservation of phosphorylation-specific prolyl isomerases in plants. J Biol Chem. 2001 Apr 27;276(17):13517-23.The A. thaliana protein AT2G18040.1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P22696 · SGD:S000003778PMID:11118437 Metzner M, et al. Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13. J Biol Chem. 2001 Apr 27;276(17):13524-9.The D. lanata protein DlPar13 complements a homologous mutation in S. cerevisiae.
UniProtKB:P22696 · SGD:S000003778PMID:15870468 Ren P, et al. The Ess1 prolyl isomerase is dispensable for growth but required for virulence in Cryptococcus neoformans. Microbiology. 2005 May;151(Pt 5):1593-605.The C. neoformans protein Ess1 complements a homologous mutation in S. cerevisiae. The C. neoformins Ess1 gene has the GenBank id AF533511. Three complementation tests indicated that C. neoformans ESS1 encodes a bona fide functional homologue of S. cerevisiae ESS1.
UniProtKB:P22696 · SGD:S000003778PMID:11707530 Huang HK, et al. Isolation and characterization of the Pin1/Ess1p homologue in Schizosaccharomyces pombe. J Cell Sci. 2001 Oct;114(Pt 20):3779-88.The S. pombe protein Pin1 complements a homologous mutation in S. cerevisiae.
UniProtKB:P22696 · SGD:S000003778PMID:11118438 Yao JL, et al. Functional conservation of phosphorylation-specific prolyl isomerases in plants. J Biol Chem. 2001 Apr 27;276(17):13517-23.The M. domestica protein MdPin1 complements a homologous mutation in S. cerevisiae. MdPin1 has the GenBank accession id AF209200.
UniProtKB:P22696 · SGD:S000003778PMID:11118437 Metzner M, et al. Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13. J Biol Chem. 2001 Apr 27;276(17):13524-9.The H. sapiens protein Q13526 complements a homologous mutation in S. cerevisiae.
UniProtKB:P22696 · SGD:S000003778PMID:11118437 Metzner M, et al. Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13. J Biol Chem. 2001 Apr 27;276(17):13524-9.The H. sapiens protein Q9Y237 does not complement a homologous mutation in S. cerevisiae. Human Par14/Pin4 (Q9Y237) was shown not to complement a yeast ess1 mutant, whereas human Pin1 (Q13526) did complement the yeast ess1 mutant indicating that it is likely the functional homolog of yeast Ess1p.
UniProtKB:P22696 · SGD:S000003778PMID:11118437 Metzner M, et al. Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13. J Biol Chem. 2001 Apr 27;276(17):13524-9.The H. sapiens protein PIN4 does not complement a homologous mutation in S. cerevisiae.
UniProtKB:P22696 · SGD:S000003778PMID:11118437 Metzner M, et al. Functional replacement of the essential ESS1 in yeast by the plant parvulin DlPar13. J Biol Chem. 2001 Apr 27;276(17):13524-9.The H. sapiens protein PIN1 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
SGD Disease Papers (1)
UniProtKB:P22696 · SGD:S000003778PMID:18844375 Bailey ML, et al. (2008) The dual histidine motif in the active site of Pin1 has a structural rather than catalytic role. Biochemistry 47(44):11481-9
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