PIN1: Polycystic Ovarian Syndrome Database

Gene Information

Gene Symbol

PIN1

Aliases

DOD, UBL5

Entrez Gene ID

5300

Gene Name

Peptidylprolyl cis/trans isomerase, NIMA-interacting 1

Chromosomal Location

19p13.2

HGNC ID

HGNC:8988

Summary

Peptidyl-prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds. This gene encodes one of the PPIases, which specifically binds to phosphorylated ser/thr-pro motifs to catalytically regulate the post-phosphorylation conformation of its substrates. The conformational regulation catalyzed by this PPIase has a profound impact on key proteins involved in the regulation of cell growth, genotoxic and other stress responses, the immune response, induction and maintenance of pluripotency, germ cell development, neuronal differentiation, and survival. This enzyme also plays a key role in the pathogenesis of Alzheimer's disease and many cancers. Multiple alternatively spliced transcript variants have been found for this gene.[provided by RefSeq, Jun 2011]

RefSeq DNA

NG_029167.1

RefSeq mRNA

NR_038422.2, NR_038830.2, NM_006221.4, NM_006221.3

e!Ensembl

Gene	ENSG00000127445
Transcript	ENST00000587625, ENST00000247970, ENST00000588695, ENST00000586352, ENST00000591777
Protein	ENSP00000466656, ENSP00000247970, ENSP00000466962, ENSP00000467197, ENSP00000466780

Gene Ontology (GO)

Show/Hide all(48 )

GO ID	Ontology	Function	Evidence	Reference
GO:0000413	Biological process	Protein peptidyl-prolyl isomerization	TAS	11533658
GO:0001666	Biological process	Response to hypoxia	IDA	25576397
GO:0001932	Biological process	Regulation of protein phosphorylation	IDA	24964035
GO:0001934	Biological process	Positive regulation of protein phosphorylation	IGI	19638580
GO:0007088	Biological process	Regulation of mitotic nuclear division	TAS	10391244
GO:0010468	Biological process	Regulation of gene expression	IDA	24964035
GO:0030512	Biological process	Negative regulation of transforming growth factor beta receptor signaling pathway	IDA	19122240
GO:0031647	Biological process	Regulation of protein stability	IMP	25576397
GO:0032091	Biological process	Negative regulation of protein binding	IDA	11533658
GO:0032092	Biological process	Positive regulation of protein binding	IDA	24964035
GO:0032465	Biological process	Regulation of cytokinesis	IGI	19638580
GO:0032465	Biological process	Regulation of cytokinesis	IMP	19638580
GO:0035307	Biological process	Positive regulation of protein dephosphorylation	TAS	23362255
GO:0042177	Biological process	Negative regulation of protein catabolic process	IDA	11533658
GO:0043547	Biological process	Positive regulation of GTPase activity	IMP	20179103
GO:0045944	Biological process	Positive regulation of transcription by RNA polymerase II	IDA	11533658
GO:0046785	Biological process	Microtubule polymerization	IDA	26996940
GO:0050821	Biological process	Protein stabilization	IDA	11533658
GO:0051443	Biological process	Positive regulation of ubiquitin-protein transferase activity	IDA	19122240
GO:0060393	Biological process	Regulation of pathway-restricted SMAD protein phosphorylation	IDA	19122240
GO:0070373	Biological process	Negative regulation of ERK1 and ERK2 cascade	IDA	20179103
GO:0090263	Biological process	Positive regulation of canonical Wnt signaling pathway	IDA	11533658
GO:1900180	Biological process	Regulation of protein localization to nucleus	IDA	11533658
GO:1902430	Biological process	Negative regulation of amyloid-beta formation	IMP	25576397
GO:2000146	Biological process	Negative regulation of cell motility	IDA	20179103
GO:0005634	Cellular component	Nucleus	IBA	21873635
GO:0005634	Cellular component	Nucleus	IDA	16697218, 20179103, 25576397
GO:0005634	Cellular component	Nucleus	TAS	16697218
GO:0005737	Cellular component	Cytoplasm	IDA	16697218, 25576397
GO:0005829	Cellular component	Cytosol	IBA	21873635
GO:0030496	Cellular component	Midbody	IDA	19638580
GO:0098978	Cellular component	Glutamatergic synapse	IDA	28458925
GO:0099524	Cellular component	Postsynaptic cytosol	IDA	28458925
GO:0003755	Molecular function	Peptidyl-prolyl cis-trans isomerase activity	EXP	20956805
GO:0003755	Molecular function	Peptidyl-prolyl cis-trans isomerase activity	IBA	21873635
GO:0003755	Molecular function	Peptidyl-prolyl cis-trans isomerase activity	IDA	19122240
GO:0003755	Molecular function	Peptidyl-prolyl cis-trans isomerase activity	NAS	16697218
GO:0003755	Molecular function	Peptidyl-prolyl cis-trans isomerase activity	TAS	11533658, 24964035
GO:0005515	Molecular function	Protein binding	IPI	11470801, 16189514, 16476580, 16554819, 17906639, 18628984, 19122240, 19131971, 19151708, 19439498, 20179103, 20179161, 20622153, 21516116, 21741598, 21743479, 21847096, 21900206, 21988832, 22158035, 23911326, 24113655, 24265246, 24267382, 25416956, 26655473
GO:0008013	Molecular function	Beta-catenin binding	IPI	11533658
GO:0016859	Molecular function	Cis-trans isomerase activity	IMP	25576397
GO:0031434	Molecular function	Mitogen-activated protein kinase kinase binding	IPI	20179103
GO:0032794	Molecular function	GTPase activating protein binding	IPI	20179103
GO:0048156	Molecular function	Tau protein binding	NAS	28386764
GO:0050815	Molecular function	Phosphoserine residue binding	IDA	10037602, 11533658
GO:0050816	Molecular function	Phosphothreonine residue binding	IDA	10037602
GO:0050816	Molecular function	Phosphothreonine residue binding	IPI	10037602
GO:0051219	Molecular function	Phosphoprotein binding	ISS	23362255

Protein Information

Protein Name

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, PPIase Pin1, protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1, rotamase Pin1

Function

Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs. By inducing conformational changes in a subset of phosphorylated proteins, acts as a molecular switch in multiple cellular processes (PubMed:21497122, PubMed:22033920, Ref. 21). Displays a preference for acidic residues located N-terminally to the proline bond to be isomerized. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK (PubMed:16644721). Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation (PubMed:15664191). Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner (PubMed:17828269). Acts as a regulator of JNK cascade by binding to phosphorylated FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation: degradation of FBXW7 leads to subsequent stabilization of JUN (PubMed:22608923). May facilitate the ubiquitination and proteasomal degradation of RBBP8/CtIP through CUL3/KLHL15 E3 ubiquitin-protein ligase complex, hence favors DNA double-strand repair through error-prone non-homologous end joining (NHEJ) over error-free, RBBP8-mediated homologous recombination (HR) (PubMed:23623683, PubMed:27561354).

Refseq Proteins

, NP_006212.1

UniProt

Q13526

PDB

2N1O, 1F8A, 1I6C, 1I8G, 1I8H, 1NMV, 1NMW, 1PIN, 1ZCN, 2F21, 2ITK, 2KBU, 2KCF, 2LB3, 2M8I, 2M8J, 2M9E, 2M9F, 2M9I, 2M9J, 2Q5A, 2RUC, 2RUD, 2RUQ, 2RUR, 2XP3, 2XP4, 2XP5, 2XP6, 2XP7, 2XP8, 2XP9, 2XPA, 2XPB, 2ZQS, 2ZQT, 2ZQU, 2ZQV, 2ZR4, 2ZR5, 2ZR6, 3I6C, 3IK8, 3IKD, 3IKG, 3JYJ, 3KAB, 3KAC, 3KAD, 3KAF, 3KAG,

Pfam

Pfam Accession	Pfam ID
PF00639	Rotamase
PF00397	WW

PIN1

Proteomic biomarkers of endometrial cancer risk in women with polycystic ovary syndrome: a systematic review and biomarker database integration.