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UniProtKB/Swiss-Prot entry Q9Y237


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PIN4_HUMAN
Primary accession number Q9Y237
Secondary accession number Q5HYW6
Integrated into Swiss-Prot on January 23, 2002
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 67)
Name and origin of the protein
Protein name Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4
Synonyms EC 5.2.1.8
Rotamase Pin4
PPIase Pin4
Parvulin 14
hPar14
Par14
Peptidyl-prolyl cis/trans isomerase EPVH
Gene name
Name: PIN4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1006/bbrc.1999.0828; PubMed=10364457 [NCBI, ExPASy, EBI, Israel, Japan]
Rulten S.L., Thorpe J.R., Kay J.E.;
"Identification of eukaryotic parvulin homologues: a new subfamily of peptidylprolyl cis-trans isomerases.";
Biochem. Biophys. Res. Commun. 259:557-562(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0014-5793(99)00239-2; PubMed=10100858 [NCBI, ExPASy, EBI, Israel, Japan]
Uchida T., Fujimori F., Tradler T., Fischer G., Rahfeld J.-U.;
"Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase.";
FEBS Lett. 446:278-282(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Urinary bladder;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
STRUCTURE BY NMR OF 36-131.
DOI=10.1006/jmbi.2000.4013; PubMed=10966801 [NCBI, ExPASy, EBI, Israel, Japan]
Sekerina E., Rahfeld J.-U., Mueller J., Fanghaenel J., Rascher C., Fischer G., Bayer P.;
"NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein.";
J. Mol. Biol. 301:1003-1017(2000).
[6]
STRUCTURE BY NMR OF 28-131.
DOI=10.1006/jmbi.2000.4293; PubMed=11162102 [NCBI, ExPASy, EBI, Israel, Japan]
Terada T., Shirouzu M., Fukumori Y., Fujimori F., Ito Y., Kigawa T., Yokoyama S., Uchida T.;
"Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14.";
J. Mol. Biol. 305:917-926(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF143096; AAD27893.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB009690; BAA82320.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX119917; CAI39856.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL135749; CAI39856.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005234; AAH05234.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_006214.2; -.
UniGene Hs.655623
3D structure databases
PDB
1EQ3; NMR; -; A=36-131.[ExPASy / RCSB / EBI]
1FJD; NMR; -; A=30-131.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EQ3; -.
1FJD; -.
ModBase Q9Y237.
Protein-protein interaction databases
IntAct Q9Y237; -.
PTM databases
PhosphoSite Q9Y237; -.
Organism-specific databases
H-InvDB HIX0012195; -.
HIX0016866; -.
HGNC HGNC:8992; PIN4.
GenAtlas PIN4.
MIM 300252; gene. [NCBI / EBI]
PharmGKB PA33324; -.
GeneCards Q9Y237.
Gene expression databases
ArrayExpress Q9Y237; -.
CleanEx HS_PIN4; -.
GermOnline ENSG00000102309; Homo sapiens.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (traceable author statement from ProtInc).
GO:0003755; Molecular function: peptidyl-prolyl cis-trans isomerase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006457; Biological process: protein folding (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000297; PPIase_PpiC.
Graphical view of domain structure.
Pfam PF00639; Rotamase; 1.
Pfam graphical view of domain structure.
PROSITE PS01096; PPIC_PPIASE_1; FALSE_NEG.
PS50198; PPIC_PPIASE_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9Y237.
Genome annotation databases
Ensembl ENSG00000102309; Homo sapiens. [Contig view]
GeneID 5303; -.
KEGG hsa:5303; -.
Phylogenomic databases
HOVERGEN Q9Y237; -.
Other
LinkHub Q9Y237; -.
NextBio 20496; -.
SOURCE PIN4; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Isomerase; Rotamase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   131  131     Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4. PRO_0000193438
DOMAIN   35   129  95     PpiC. 
STRAND   38    45  8      
HELIX   51    58  8      
TURN   59    62  4      
HELIX   64    71  8      
TURN   75    77  3      
STRAND   80    87  8      
STRAND   90    92  3      
HELIX   93   100  8      
TURN   108   110  3      
STRAND   116   118  3      
STRAND   121   129  9      
Sequence information
Length: 131 AA [This is the length of the unprocessed precursor] Molecular weight: 13810 Da [This is the MW of the unprocessed precursor] CRC64: 787C15BDB0701258 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPPKGKSGSG KAGKGGAASG SDSADKKAQG PKGGGNAVKV RHILCEKHGK IMEAMEKLKS 

        70         80         90        100        110        120 
GMRFNEVAAQ YSEDKARQGG DLGWMTRGSM VGPFQEAAFA LPVSGMDKPV FTDPPVKTKF 

       130 
GYHIIMVEGR K 

Q9Y237 in FASTA format

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