Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Gene

PIN1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Peptidyl-prolyl cis/trans isomerase (PPIase) that binds to and isomerizes specific phosphorylated Ser/Thr-Pro (pSer/Thr-Pro) motifs in a subset of proteins, resulting in conformational changes in the proteins. 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. Binds and targets PML and BCL6 for degradation in a phosphorylation-dependent manner. 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

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

ReactomeiR-BTA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-BTA-936440. Negative regulators of RIG-I/MDA5 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
Rotamase Pin1
Gene namesi
Name:PIN1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 7

Subcellular locationi

  • Nucleus By similarity
  • Nucleus speckle By similarity
  • Cytoplasm By similarity

  • Note: Colocalizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 163163Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1PRO_0000236242Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461N6-acetyllysineBy similarity
Modified residuei71 – 711Phosphoserine; by DAPK1By similarity
Modified residuei108 – 1081PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Ser-71 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

PaxDbiQ5BIN5.
PRIDEiQ5BIN5.

Expressioni

Gene expression databases

BgeeiENSBTAG00000016988.

Interactioni

Subunit structurei

Interacts with STIL. Interacts with KIF20B. Interacts with NEK6. Interacts (via WW domain) with PRKX. 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 (By similarity). Interacts with FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022592.

Structurei

3D structure databases

ProteinModelPortaliQ5BIN5.
SMRiQ5BIN5. Positions 1-163.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 3935WWPROSITE-ProRule annotationAdd
BLAST
Domaini52 – 163112PpiCPROSITE-ProRule annotationAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 PpiC domain.PROSITE-ProRule annotation
Contains 1 WW domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3259. Eukaryota.
COG0760. LUCA.
GeneTreeiENSGT00640000091578.
HOGENOMiHOG000275331.
HOVERGENiHBG002101.
InParanoidiQ5BIN5.
KOiK09578.
OMAiDEVQCLH.
OrthoDBiEOG091G0RO7.
TreeFamiTF101101.

Family and domain databases

InterProiIPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00639. Rotamase. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS01096. 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]

Sequencei

Sequence statusi: Complete.

Q5BIN5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSGSGKNGQG
60 70 80 90 100
EPTRVRCSHL LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE
110 120 130 140 150
EDFESLASQF SDCSSAKARG DLGAFSRGQM QKPFEDASFA LRTGEMSGPV
160
FTDSGIHIIL RTE
Length:163
Mass (Da):18,273
Last modified:April 12, 2005 - v1
Checksum:i6CED0EF411C3AB0D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021189 mRNA. Translation: AAX31371.1.
BC112583 mRNA. Translation: AAI12584.1.
RefSeqiNP_001029804.1. NM_001034632.3.
UniGeneiBt.5583.

Genome annotation databases

EnsembliENSBTAT00000022592; ENSBTAP00000022592; ENSBTAG00000016988.
GeneIDi535470.
KEGGibta:535470.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021189 mRNA. Translation: AAX31371.1.
BC112583 mRNA. Translation: AAI12584.1.
RefSeqiNP_001029804.1. NM_001034632.3.
UniGeneiBt.5583.

3D structure databases

ProteinModelPortaliQ5BIN5.
SMRiQ5BIN5. Positions 1-163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000022592.

Proteomic databases

PaxDbiQ5BIN5.
PRIDEiQ5BIN5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000022592; ENSBTAP00000022592; ENSBTAG00000016988.
GeneIDi535470.
KEGGibta:535470.

Organism-specific databases

CTDi5300.

Phylogenomic databases

eggNOGiKOG3259. Eukaryota.
COG0760. LUCA.
GeneTreeiENSGT00640000091578.
HOGENOMiHOG000275331.
HOVERGENiHBG002101.
InParanoidiQ5BIN5.
KOiK09578.
OMAiDEVQCLH.
OrthoDBiEOG091G0RO7.
TreeFamiTF101101.

Enzyme and pathway databases

ReactomeiR-BTA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-BTA-936440. Negative regulators of RIG-I/MDA5 signaling.

Gene expression databases

BgeeiENSBTAG00000016988.

Family and domain databases

InterProiIPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00639. Rotamase. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTiSM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF51045. SSF51045. 1 hit.
PROSITEiPS01096. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPIN1_BOVIN
AccessioniPrimary (citable) accession number: Q5BIN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: April 12, 2005
Last modified: September 7, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.