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Protein

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Gene

Pin1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Down-regulates kinase activity of BTK. 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 (By similarity). 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 (By similarity). 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) (By similarity).By similarity1 Publication

Catalytic activityi

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

GO - Molecular functioni

  • beta-catenin binding Source: ParkinsonsUK-UCL
  • GTPase activating protein binding Source: MGI
  • mitogen-activated protein kinase kinase binding Source: MGI
  • motor activity Source: ParkinsonsUK-UCL
  • peptidyl-prolyl cis-trans isomerase activity Source: MGI
  • phosphoprotein binding Source: ARUK-UCL
  • phosphoserine residue binding Source: MGI
  • phosphothreonine residue binding Source: MGI

GO - Biological processi

Keywordsi

Molecular functionIsomerase, Rotamase
Biological processCell cycle

Enzyme and pathway databases

BRENDAi5.2.1.8 3474
ReactomeiR-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-6811555 PI5P Regulates TP53 Acetylation
R-MMU-936440 Negative regulators of DDX58/IFIH1 signaling

Names & Taxonomyi

Protein namesi
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 namesi
Name:Pin1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1346036 Pin1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Animals display more and larger germinal centers.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001934361 – 165Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1Add BLAST165

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei48N6-acetyllysineBy similarity1
Modified residuei73Phosphoserine; by DAPK1By similarity1
Modified residuei110PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9QUR7
MaxQBiQ9QUR7
PaxDbiQ9QUR7
PRIDEiQ9QUR7

PTM databases

iPTMnetiQ9QUR7
PhosphoSitePlusiQ9QUR7

Expressioni

Gene expression databases

BgeeiENSMUSG00000032171
GenevisibleiQ9QUR7 MM

Interactioni

Subunit structurei

Interacts with STIL (PubMed:16024801). Interacts with KIF20B. Interacts with NEK6. Interacts (via WW domain) with PRKX (PubMed:19367327). Interacts with BTK. Interacts (via PpiC domain) with DAPK1. Interacts with the phosphorylated form of RAF1. Interacts (via WW domain) with ATCAY; upon NGF stimulation. Interacts with PML and BCL-6. Interacts with FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation (By similarity). Directly interacts with RBBP8/CtIP; this interaction depends upon RBBP8 phosphorylation (By similarity).By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204839, 10 interactors
DIPiDIP-44280N
ELMiQ9QUR7
IntActiQ9QUR7, 7 interactors
MINTiQ9QUR7
STRINGi10090.ENSMUSP00000034689

Structurei

3D structure databases

ProteinModelPortaliQ9QUR7
SMRiQ9QUR7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 39WWPROSITE-ProRule annotationAdd BLAST35
Domaini54 – 165PpiCPROSITE-ProRule annotationAdd BLAST112

Domaini

The WW domain is required for the interaction with STIL and KIF20B.

Phylogenomic databases

eggNOGiKOG3259 Eukaryota
COG0760 LUCA
GeneTreeiENSGT00640000091578
HOGENOMiHOG000275331
HOVERGENiHBG002101
InParanoidiQ9QUR7
KOiK09578
OMAiDEVQCLH
OrthoDBiEOG091G0RO7
PhylomeDBiQ9QUR7
TreeFamiTF101101

Family and domain databases

CDDicd00201 WW, 1 hit
InterProiView protein in InterPro
IPR000297 PPIase_PpiC
IPR023058 PPIase_PpiC_CS
IPR001202 WW_dom
IPR036020 WW_dom_sf
PfamiView protein in Pfam
PF00639 Rotamase, 1 hit
PF00397 WW, 1 hit
SMARTiView protein in SMART
SM00456 WW, 1 hit
SUPFAMiSSF51045 SSF51045, 1 hit
PROSITEiView protein in 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

Sequencei

Sequence statusi: Complete.

Q9QUR7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGG STVGGSSKNG
60 70 80 90 100
QGEPAKVRCS HLLVKHSQSR RPSSWRQEKI TRSKEEALEL INGYIQKIKS
110 120 130 140 150
GEEDFESLAS QFSDCSSAKA RGDLGPFSRG QMQKPFEDAS FALRTGEMSG
160
PVFTDSGIHI ILRTE
Length:165
Mass (Da):18,370
Last modified:May 1, 2000 - v1
Checksum:i188E95F009176B1F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS22882.1
PIRiJC7136
RefSeqiNP_075860.1, NM_023371.3
UniGeneiMm.7906

Genome annotation databases

EnsembliENSMUST00000034689; ENSMUSP00000034689; ENSMUSG00000032171
GeneIDi23988
KEGGimmu:23988
UCSCiuc009ojd.1 mouse

Similar proteinsi

Entry informationi

Entry nameiPIN1_MOUSE
AccessioniPrimary (citable) accession number: Q9QUR7
Secondary accession number(s): Q543B3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2000
Last modified: June 20, 2018
This is version 142 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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