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Reviewed, UniProtKB/Swiss-Prot Q9Y237 (PIN4_HUMAN)

Last modified June 16, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4
    EC=5.2.1.8
Alternative name(s):
    Rotamase Pin4
    PPIase Pin4
    Parvulin 14
      Short name=hPar14
      Short name=Par14
    Peptidyl-prolyl cis/trans isomerase EPVH
Gene names
Name: PIN4
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length131 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Peptidylproline (omega=180) = peptidylproline (omega=0).

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the ppiC/parvulin rotamase family. PIN4 subfamily.

Contains 1 PpiC domain.

Ontologies

Keywords
   Molecular functionIsomerase
Rotamase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processprotein folding Ref.2

Traceable author statement. Source: ProtInc

   Cellular componentmitochondrial matrix Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionpeptidyl-prolyl cis-trans isomerase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 131131Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4
PRO_0000193438

Regions

Domain35 – 12995PpiC

Secondary structure

..................... 131
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y237-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 787C15BDB0701258

FASTA13113,810
        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 

« Hide

References

« Hide 'large scale' references
[1]"Identification of eukaryotic parvulin homologues: a new subfamily of peptidylprolyl cis-trans isomerases."
Rulten S.L., Thorpe J.R., Kay J.E.
Biochem. Biophys. Res. Commun. 259:557-562(1999) [PubMed: 10364457] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Identification and characterization of a 14 kDa human protein as a novel parvulin-like peptidyl prolyl cis/trans isomerase."
Uchida T., Fujimori F., Tradler T., Fischer G., Rahfeld J.-U.
FEBS Lett. 446:278-282(1999) [PubMed: 10100858] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The DNA sequence of the human X chromosome."
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. expand/collapse author list , 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.
Nature 434:325-337(2005) [PubMed: 15772651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Urinary bladder.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]"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."
Sekerina E., Rahfeld J.-U., Mueller J., Fanghaenel J., Rascher C., Fischer G., Bayer P.
J. Mol. Biol. 301:1003-1017(2000) [PubMed: 10966801] [Abstract]
Cited for: STRUCTURE BY NMR OF 36-131.
[7]"Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14."
Terada T., Shirouzu M., Fukumori Y., Fujimori F., Ito Y., Kigawa T., Yokoyama S., Uchida T.
J. Mol. Biol. 305:917-926(2001) [PubMed: 11162102] [Abstract]
Cited for: STRUCTURE BY NMR OF 28-131.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF143096 mRNA. Translation: AAD27893.1.
AB009690 mRNA. Translation: BAA82320.1.
BX119917, AL135749 Genomic DNA. Translation: CAI39856.1.
BC005234 mRNA. Translation: AAH05234.2. Different initiation.
IPIIPI00006658.
RefSeqNP_006214.2.
UniGeneHs.655623

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1EQ3NMR-A36-131[»]
1FJDNMR-A30-131[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Y237. 6 interactions.

PTM databases

PhosphoSiteQ9Y237.

Proteomic databases

PRIDEQ9Y237.

Genome annotation databases

EnsemblENSG00000102309. Homo sapiens. [Contig view]
GeneID5303.
KEGGhsa:5303.

Organism-specific databases

GeneCardsGC0XP071318.
H-InvDBHIX0012195.
HIX0016866.
HGNCHGNC:8992. PIN4.
MIM300252. gene.
PharmGKBPA33324.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9Y237.

Enzyme and pathway databases

BRENDA5.2.1.8. 247.

Gene expression databases

ArrayExpressQ9Y237.
BgeeQ9Y237.
CleanExHS_PIN4.
GermOnlineENSG00000102309. Homo sapiens.

Family and domain databases

InterProIPR000297. PPIase_PpiC.
[Graphical view]
PfamPF00639. Rotamase. 1 hit.
[Graphical view]
PROSITEPS01096. PPIC_PPIASE_1. False negative.
PS50198. PPIC_PPIASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio20496.
SOURCESearch...

Entry information

Entry namePIN4_HUMAN
AccessionPrimary (citable) accession number: Q9Y237
Secondary accession number(s): Q5HYW6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: November 1, 1999
Last modified: June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents