Q9QUR7 (PIN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
EC=5.2.1.8

Alternative name(s):
Peptidyl-prolyl cis-trans isomerase Pin1
Short name=PPIase Pin1

Gene names

Name:

Pin1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation By similarity. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation By similarity. Binds and targets PML for degradation in a phosphorylation-dependent manner By similarity.
Catalytic activity	Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit structure	Interacts with KIF20B By similarity. Interacts with NEK6 and BTK By similarity. Interacts with STIL. Interacts (via WW domain) with PRKX. Interacts (via PpiC domain) with DAPK1 By similarity. Interacts with the phosphorylated form of RAF1 By similarity. Interacts (via WW domain) with ATCAY; upon NGF stimulation By similarity. Interacts with PML By similarity. Ref.4 Ref.5
Subcellular location	Nucleus By similarity. Nucleus speckle By similarity. Cytoplasm By similarity. Note: Co-localizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-73 by DAPK1 results in inhibition of its nuclear localization By similarity.
Domain	The WW domain is required for the interaction with STIL and KIF20B.
Post-translational modification	Phosphorylation at Ser-73 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation By similarity.
Sequence similarities	Contains 1 PpiC domain. Contains 1 WW domain.

Ontologies

Keywords
Biological process	Cell cycle
Cellular component	Cytoplasm Nucleus
Molecular function	Isomerase Rotamase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of ERK1 and ERK2 cascade Inferred from electronic annotation. Source: Compara negative regulation of cell motility Inferred from electronic annotation. Source: Compara negative regulation of transforming growth factor beta receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of Rho GTPase activity Inferred from electronic annotation. Source: Compara positive regulation of protein phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara protein folding Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell proliferation Inferred from mutant phenotype PubMed 12810604. Source: MGI regulation of cytokinesis Inferred from mutant phenotype PubMed 19638580. Source: MGI regulation of pathway-restricted SMAD protein phosphorylation Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from electronic annotation. Source: Compara nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	peptidyl-prolyl cis-trans isomerase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Tp53	P02340	3	EBI-2432975,EBI-474016

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 165	165	Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1		PRO_0000193436
Regions
	Domain	5 – 39	35	WW
	Domain	54 – 165	112	PpiC
Amino acid modifications
	Modified residue	48	1	N6-acetyllysine By similarity
	Modified residue	73	1	Phosphoserine; by DAPK1 By similarity
	Modified residue	110	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9QUR7 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 188E95F009176B1F	FASTA	165	18,370
	10 20 30 40 50 60 MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGG STVGGSSKNG QGEPAKVRCS 70 80 90 100 110 120 HLLVKHSQSR RPSSWRQEKI TRSKEEALEL INGYIQKIKS GEEDFESLAS QFSDCSSAKA 130 140 150 160 RGDLGPFSRG QMQKPFEDAS FALRTGEMSG PVFTDSGIHI ILRTE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G0 arrest." Fujimori F., Takahashi K., Uchida C., Uchida T. Biochem. Biophys. Res. Commun. 265:658-663(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow, Embryo, Kidney and Oviduct.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Kidney.
[4]	"Sil phosphorylation in a Pin1 binding domain affects the duration of the spindle checkpoint." Campaner S., Kaldis P., Izraeli S., Kirsch I.R. Mol. Cell. Biol. 25:6660-6672(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH STIL.
[5]	"Protein kinase-X interacts with Pin-1 and Polycystin-1 during mouse kidney development." Li X., Hyink D.P., Radbill B., Sudol M., Zhang H., Zheleznova N.N., Wilson P.D. Kidney Int. 76:54-62(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PRKX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB009691 mRNA. Translation: BAA87037.1. AB009692 Genomic DNA. Translation: BAA87038.1. AK002665 mRNA. Translation: BAB22270.1. AK003369 mRNA. Translation: BAB22743.1. AK054045 mRNA. Translation: BAC35631.1. AK150652 mRNA. Translation: BAE29739.1. AK160228 mRNA. Translation: BAE35702.1. BC038254 mRNA. Translation: AAH38254.1.
IPI	IPI00132093.
PIR	JC7136.
RefSeq	NP_075860.1. NM_023371.3.
UniGene	Mm.7906.
3D structure databases
ProteinModelPortal	Q9QUR7.
SMR	Q9QUR7. Positions 1-165.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9QUR7. 3 interactions.
MINT	MINT-4107624.
PTM databases
PhosphoSite	Q9QUR7.
Proteomic databases
PaxDb	Q9QUR7.
PRIDE	Q9QUR7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034689; ENSMUSP00000034689; ENSMUSG00000032171.
GeneID	23988.
KEGG	mmu:23988.
UCSC	uc009ojd.1. mouse.
Organism-specific databases
CTD	5300.
MGI	MGI:1346036. Pin1.
Phylogenomic databases
eggNOG	COG0760.
GeneTree	ENSGT00640000091578.
HOGENOM	HOG000275331.
HOVERGEN	HBG002101.
InParanoid	Q9QUR7.
KO	K09578.
OMA	DCSSARK.
OrthoDB	EOG4VMFGM.
Enzyme and pathway databases
BRENDA	5.2.1.8. 3474.
Gene expression databases
Bgee	Q9QUR7.
Genevestigator	Q9QUR7.
GermOnline	ENSMUSG00000032171. Mus musculus.
Family and domain databases
InterPro	IPR000297. PPIase_PpiC. IPR023058. PPIase_PpiC_CS. IPR001202. WW_dom. [Graphical view]
Pfam	PF00639. Rotamase. 1 hit. PF00397. WW. 1 hit. [Graphical view]
SMART	SM00456. WW. 1 hit. [Graphical view]
SUPFAM	SSF51045. WW_Rsp5_WWP. 1 hit.
PROSITE	PS01096. PPIC_PPIASE_1. 1 hit. PS50198. PPIC_PPIASE_2. 1 hit. PS01159. WW_DOMAIN_1. 1 hit. PS50020. WW_DOMAIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	303885.
SOURCE	Search...

Entry information

Entry name

PIN1_MOUSE

Accession

Primary (citable) accession number: Q9QUR7
Secondary accession number(s): Q543B3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program