Reviewed, UniProtKB/Swiss-Prot Q9Y237 (PIN4_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	131 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 function	Isomerase Rotamase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	protein folding Ref.2 Traceable author statement. Source: ProtInc
Cellular component	mitochondrial matrix Ref.1 Traceable author statement. Source: ProtInc
Molecular function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 131

131

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4

PRO_0000193438

Regions

Domain

35 – 129

95

PpiC

Secondary structure

1

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131

Helix Strand Turn

Details...

Beta strand

38 – 45

8

Helix

51 – 58

8

Turn

59 – 62

4

Helix

64 – 71

8

Turn

75 – 77

3

Beta strand

80 – 87

8

Beta strand

90 – 92

3

Helix

93 – 100

8

Turn

108 – 110

3

Beta strand

116 – 118

3

Beta strand

121 – 129

9

Sequences

	Sequence		Length	Mass (Da)
	Q9Y237-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 787C15BDB0701258	FASTA	131	13,810
	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

References

	« Hide 'large scale' referencesShow '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. , 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

EMBLGenBankDDBJ

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

IPI

IPI00006658.

RefSeq

NP_006214.2.

UniGene

Hs.655623

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EQ3	NMR	-	A	36-131	[»]
1FJD	NMR	-	A	30-131	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y237. 6 interactions.

PTM databases

PhosphoSite

Q9Y237.

Proteomic databases

PRIDE

Q9Y237.

Genome annotation databases

Ensembl

ENSG00000102309. Homo sapiens. [Contig view]

GeneID

5303.

KEGG

hsa:5303.

Organism-specific databases

GeneCards

GC0XP071318.

H-InvDB

HIX0012195.
HIX0016866.

HGNC

HGNC:8992. PIN4.

MIM

300252. gene.

PharmGKB

PA33324.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9Y237.

Enzyme and pathway databases

BRENDA

5.2.1.8. 247.

Gene expression databases

ArrayExpress

Q9Y237.

Bgee

Q9Y237.

CleanEx

HS_PIN4.

GermOnline

ENSG00000102309. Homo sapiens.

Family and domain databases

InterPro

IPR000297. PPIase_PpiC.
[Graphical view]

Pfam

PF00639. Rotamase. 1 hit.
[Graphical view]

PROSITE

PS01096. PPIC_PPIASE_1. False negative.
PS50198. PPIC_PPIASE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

20496.

SOURCE

Search...

Entry information

Entry name

PIN4_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)