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Protein

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Gene

PIN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 in a subset of proteins, resulting in conformational changes in the proteins (PubMed:21497122, PubMed:22033920). 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 (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).6 Publications

Catalytic activityi

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

GO - Molecular functioni

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

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • negative regulation of cell motility Source: BHF-UCL
  • negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • negative regulation of neuron apoptotic process Source: Ensembl
  • negative regulation of protein binding Source: ParkinsonsUK-UCL
  • negative regulation of protein catabolic process Source: ParkinsonsUK-UCL
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  • negative regulation of type I interferon production Source: Reactome
  • neuron differentiation Source: ParkinsonsUK-UCL
  • positive regulation of canonical Wnt signaling pathway Source: ParkinsonsUK-UCL
  • positive regulation of cell growth involved in cardiac muscle cell development Source: Ensembl
  • positive regulation of GTPase activity Source: BHF-UCL
  • positive regulation of neuron apoptotic process Source: Ensembl
  • positive regulation of protein dephosphorylation Source: Ensembl
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
  • positive regulation of ubiquitin-protein transferase activity Source: BHF-UCL
  • protein peptidyl-prolyl isomerization Source: ParkinsonsUK-UCL
  • protein stabilization Source: ParkinsonsUK-UCL
  • regulation of cytokinesis Source: MGI
  • regulation of mitotic nuclear division Source: ProtInc
  • regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
  • regulation of protein localization to nucleus Source: ParkinsonsUK-UCL
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • synapse organization Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

BioCyciZFISH:HS05098-MONOMER.
BRENDAi5.2.1.8. 2681.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6811555. PI5P Regulates TP53 Acetylation.
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.
SignaLinkiQ13526.
SIGNORiQ13526.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:8988. PIN1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: ParkinsonsUK-UCL
  • midbody Source: MGI
  • mitochondrion Source: Ensembl
  • neuron projection Source: Ensembl
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi23Y → A: Reduced affinity for KIF20B. 1 Publication1
Mutagenesisi34W → A: Loss of peptidyl-prolyl cis/trans isomerase activity. 1 Publication1
Mutagenesisi63K → A: Loss of peptidyl-prolyl cis/trans isomerase activity. 1 Publication1
Mutagenesisi71S → D or E: Loss of activity, nuclear localization and cellular function. 1 Publication1

Organism-specific databases

DisGeNETi5300.
OpenTargetsiENSG00000127445.
PharmGKBiPA33320.

Chemistry databases

ChEMBLiCHEMBL2288.

Polymorphism and mutation databases

BioMutaiPIN1.
DMDMi3024406.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001934351 – 163Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1Add BLAST163

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei43PhosphoserineCombined sources1
Modified residuei46N6-acetyllysineCombined sources1
Modified residuei71Phosphoserine; by DAPK11 Publication1
Modified residuei108PhosphoserineCombined sources1

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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ13526.
MaxQBiQ13526.
PaxDbiQ13526.
PeptideAtlasiQ13526.
PRIDEiQ13526.

PTM databases

iPTMnetiQ13526.
PhosphoSitePlusiQ13526.

Expressioni

Tissue specificityi

The phosphorylated form at Ser-71 is expressed in normal breast tissue cells but not in breast cancer cells.2 Publications

Gene expression databases

BgeeiENSG00000127445.
CleanExiHS_PIN1.
ExpressionAtlasiQ13526. baseline and differential.
GenevisibleiQ13526. HS.

Organism-specific databases

HPAiCAB004528.
CAB009326.

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 (isoform PML-4) and BCL-6. Interacts with FBXW7, disrupting FBXW7 dimerization and promoting FBXW7 autoubiquitination and degradation (PubMed:22608923).10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABI2Q9NYB93EBI-714158,EBI-743598
ADAMTSL4Q6UY14-33EBI-714158,EBI-10173507
ADARB1P7856312EBI-714158,EBI-2967304
AMOTQ4VCS5-23EBI-714158,EBI-3891843
ANKRD40Q6AI125EBI-714158,EBI-2838246
APPP05067-42EBI-714158,EBI-302641
ARHGAP8P85298-425EBI-714158,EBI-9523517
ARHGEF15D3DTR73EBI-714158,EBI-10176602
CBSP355203EBI-714158,EBI-740135
CCDC184Q52MB25EBI-714158,EBI-10179526
CDK10Q151315EBI-714158,EBI-1646959
CEP55D3DR373EBI-714158,EBI-10173536
CEP76Q8TAP65EBI-714158,EBI-742887
CNKSR1Q969H45EBI-714158,EBI-741671
DAB1O755533EBI-714158,EBI-7875264
FOXP2O154095EBI-714158,EBI-983612
GOLGA2Q083793EBI-714158,EBI-618309
Grm5P31424-23EBI-714158,EBI-8830305From a different organism.
Grm5Q3UVX52EBI-714158,EBI-8795045From a different organism.
HEXIM2Q96MH23EBI-714158,EBI-5460660
HOMEZQ8IX15-33EBI-714158,EBI-10172004
IKZF1Q134223EBI-714158,EBI-745305
IKZF3Q9UKT95EBI-714158,EBI-747204
IRAK1P5161710EBI-714158,EBI-358664
JAKMIP2Q96AA83EBI-714158,EBI-752007
KRT31Q153235EBI-714158,EBI-948001
KRT38O760155EBI-714158,EBI-1047263
KRT40Q6A1623EBI-714158,EBI-10171697
KRTAP10-7P604093EBI-714158,EBI-10172290
KRTAP10-9P604113EBI-714158,EBI-10172052
KRTAP4-2Q9BYR53EBI-714158,EBI-10172511
Map2k1P319384EBI-714158,EBI-298860From a different organism.
Map2k2Q6393212EBI-714158,EBI-397724From a different organism.
MAP3K8P412798EBI-714158,EBI-354900
MDFIQ997506EBI-714158,EBI-724076
MEOX2A4D1275EBI-714158,EBI-10172134
MTUS2Q5JR593EBI-714158,EBI-742948
NAB2Q157425EBI-714158,EBI-8641936
NEK6Q9HC983EBI-714158,EBI-740364
NONOQ152334EBI-714158,EBI-350527
NONOQ15233-23EBI-714158,EBI-10203843
NOTCH1P465319EBI-714158,EBI-636374
NUP62P371985EBI-714158,EBI-347978
PNMA1Q8ND903EBI-714158,EBI-302345
PRRC1Q96M273EBI-714158,EBI-2560879
RAI1Q7Z5J44EBI-714158,EBI-743815
RBBP8Q99708-23EBI-714158,EBI-10203615
RBPMSQ930624EBI-714158,EBI-740322
RUNX2Q139507EBI-714158,EBI-976402
SP140Q133424EBI-714158,EBI-2865100
SPERTQ8NA613EBI-714158,EBI-741724
SSBP3Q9BWW45EBI-714158,EBI-2902395
SSBP4Q9BWG43EBI-714158,EBI-744719
SULT4A1Q9BR014EBI-714158,EBI-6690555
SUPT5HO002673EBI-714158,EBI-710464
TAB3Q8N5C83EBI-714158,EBI-359964
TCF4P158843EBI-714158,EBI-533224
THAP7Q9BT493EBI-714158,EBI-741350
TNIP1Q150256EBI-714158,EBI-357849
TP53P0463712EBI-714158,EBI-366083
TRAF1Q130773EBI-714158,EBI-359224
TRAF2Q129336EBI-714158,EBI-355744
TRIP6Q156543EBI-714158,EBI-742327
TSC22D4Q9Y3Q84EBI-714158,EBI-739485
ZBTB14O438293EBI-714158,EBI-10176632
ZBTB22O152093EBI-714158,EBI-723574
ZBTB7BO151563EBI-714158,EBI-740434
ZBTB9Q96C005EBI-714158,EBI-395708
ZMIZ2Q8NF644EBI-714158,EBI-745786
ZMIZ2Q8NF64-23EBI-714158,EBI-10182121
ZNF446Q96AF53EBI-714158,EBI-740232

GO - Molecular functioni

  • beta-catenin binding Source: ParkinsonsUK-UCL
  • GTPase activating protein binding Source: BHF-UCL
  • mitogen-activated protein kinase kinase binding Source: BHF-UCL
  • phosphoserine binding Source: BHF-UCL
  • phosphothreonine binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi111317. 233 interactors.
DIPiDIP-29306N.
IntActiQ13526. 166 interactors.
MINTiMINT-86298.
STRINGi9606.ENSP00000247970.

Chemistry databases

BindingDBiQ13526.

Structurei

Secondary structure

1163
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 15Combined sources5
Turni17 – 19Combined sources3
Beta strandi22 – 26Combined sources5
Turni27 – 29Combined sources3
Beta strandi32 – 35Combined sources4
Beta strandi39 – 41Combined sources3
Beta strandi53 – 62Combined sources10
Beta strandi67 – 69Combined sources3
Beta strandi75 – 77Combined sources3
Helixi82 – 98Combined sources17
Beta strandi99 – 101Combined sources3
Helixi103 – 110Combined sources8
Helixi114 – 118Combined sources5
Beta strandi121 – 126Combined sources6
Helixi127 – 129Combined sources3
Helixi132 – 140Combined sources9
Beta strandi150 – 152Combined sources3
Beta strandi155 – 163Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F8AX-ray1.84B1-163[»]
1I6CNMR-A6-44[»]
1I8GNMR-B6-44[»]
1I8HNMR-B6-44[»]
1NMVNMR-A1-163[»]
1NMWNMR-A50-163[»]
1PINX-ray1.35A1-163[»]
1ZCNX-ray1.90A1-161[»]
2F21X-ray1.50A1-162[»]
2ITKX-ray1.45A1-163[»]
2KBUNMR-A6-39[»]
2KCFNMR-A6-39[»]
2LB3NMR-A6-41[»]
2M8INMR-A1-39[»]
2M8JNMR-A1-39[»]
2M9ENMR-A6-15[»]
A22-39[»]
2M9FNMR-A6-15[»]
A22-39[»]
2M9INMR-A6-39[»]
2M9JNMR-A6-39[»]
2N1ONMR-A7-39[»]
2Q5AX-ray1.50A1-163[»]
2RUCNMR-A51-163[»]
2RUDNMR-A51-163[»]
2RUQNMR-A51-163[»]
2RURNMR-A51-163[»]
2XP3X-ray2.00A1-163[»]
2XP4X-ray1.80A1-163[»]
2XP5X-ray1.90A1-163[»]
2XP6X-ray1.90A1-163[»]
2XP7X-ray2.00A1-163[»]
2XP8X-ray2.10A1-163[»]
2XP9X-ray1.90A1-163[»]
2XPAX-ray1.90A1-163[»]
2XPBX-ray2.00A1-163[»]
2ZQSX-ray1.90A1-163[»]
2ZQTX-ray1.46A1-163[»]
2ZQUX-ray2.50A1-163[»]
2ZQVX-ray2.50A1-163[»]
2ZR4X-ray2.00A1-163[»]
2ZR5X-ray2.60A1-163[»]
2ZR6X-ray3.20A1-163[»]
3I6CX-ray1.30A/B45-163[»]
3IK8X-ray1.85A/B45-163[»]
3IKDX-ray2.00A/B45-163[»]
3IKGX-ray1.86A/B45-163[»]
3JYJX-ray1.87A/B45-163[»]
3KABX-ray2.19A1-163[»]
3KACX-ray2.00A/B45-163[»]
3KADX-ray1.95A1-163[»]
3KAFX-ray2.30A1-163[»]
3KAGX-ray1.90A1-163[»]
3KAHX-ray2.30A1-163[»]
3KAIX-ray1.90A1-163[»]
3KCEX-ray1.90A1-163[»]
3NTPX-ray1.76A1-163[»]
3ODKX-ray2.30A1-163[»]
3OOBX-ray1.89A1-163[»]
3TC5X-ray1.40A1-163[»]
3TCZX-ray2.10A6-163[»]
3TDBX-ray2.27A6-163[»]
3WH0X-ray1.60A1-163[»]
4GWTX-ray2.25A6-39[»]
4GWVX-ray3.05A6-39[»]
4QIBX-ray1.86A7-163[»]
4TNSX-ray1.33A/B43-163[»]
4TYOX-ray1.75A/B45-163[»]
4U84X-ray1.78A1-163[»]
4U85X-ray1.70A1-163[»]
4U86X-ray1.60A1-163[»]
ProteinModelPortaliQ13526.
SMRiQ13526.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13526.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 39WWPROSITE-ProRule annotationAdd BLAST35
Domaini52 – 163PpiCPROSITE-ProRule annotationAdd BLAST112

Domaini

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

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.
InParanoidiQ13526.
KOiK09578.
OMAiDEVQCLH.
OrthoDBiEOG091G0RO7.
PhylomeDBiQ13526.
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.

Q13526-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEEKLPPG WEKRMSRSSG RVYYFNHITN ASQWERPSGN SSSGGKNGQG
60 70 80 90 100
EPARVRCSHL LVKHSQSRRP SSWRQEKITR TKEEALELIN GYIQKIKSGE
110 120 130 140 150
EDFESLASQF SDCSSAKARG DLGAFSRGQM QKPFEDASFA LRTGEMSGPV
160
FTDSGIHIIL RTE
Length:163
Mass (Da):18,243
Last modified:November 1, 1996 - v1
Checksum:i35391AF40B7D1E13
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49070 mRNA. Translation: AAC50492.1.
CR407654 mRNA. Translation: CAG28582.1.
BT019331 mRNA. Translation: AAV38138.1.
AK291074 mRNA. Translation: BAF83763.1.
CH471106 Genomic DNA. Translation: EAW84057.1.
BC002899 mRNA. Translation: AAH02899.1.
CCDSiCCDS12220.1.
PIRiS68520.
RefSeqiNP_006212.1. NM_006221.3.
UniGeneiHs.465849.

Genome annotation databases

EnsembliENST00000247970; ENSP00000247970; ENSG00000127445.
ENST00000588695; ENSP00000466962; ENSG00000127445.
GeneIDi5300.
KEGGihsa:5300.
UCSCiuc002mml.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U49070 mRNA. Translation: AAC50492.1.
CR407654 mRNA. Translation: CAG28582.1.
BT019331 mRNA. Translation: AAV38138.1.
AK291074 mRNA. Translation: BAF83763.1.
CH471106 Genomic DNA. Translation: EAW84057.1.
BC002899 mRNA. Translation: AAH02899.1.
CCDSiCCDS12220.1.
PIRiS68520.
RefSeqiNP_006212.1. NM_006221.3.
UniGeneiHs.465849.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1F8AX-ray1.84B1-163[»]
1I6CNMR-A6-44[»]
1I8GNMR-B6-44[»]
1I8HNMR-B6-44[»]
1NMVNMR-A1-163[»]
1NMWNMR-A50-163[»]
1PINX-ray1.35A1-163[»]
1ZCNX-ray1.90A1-161[»]
2F21X-ray1.50A1-162[»]
2ITKX-ray1.45A1-163[»]
2KBUNMR-A6-39[»]
2KCFNMR-A6-39[»]
2LB3NMR-A6-41[»]
2M8INMR-A1-39[»]
2M8JNMR-A1-39[»]
2M9ENMR-A6-15[»]
A22-39[»]
2M9FNMR-A6-15[»]
A22-39[»]
2M9INMR-A6-39[»]
2M9JNMR-A6-39[»]
2N1ONMR-A7-39[»]
2Q5AX-ray1.50A1-163[»]
2RUCNMR-A51-163[»]
2RUDNMR-A51-163[»]
2RUQNMR-A51-163[»]
2RURNMR-A51-163[»]
2XP3X-ray2.00A1-163[»]
2XP4X-ray1.80A1-163[»]
2XP5X-ray1.90A1-163[»]
2XP6X-ray1.90A1-163[»]
2XP7X-ray2.00A1-163[»]
2XP8X-ray2.10A1-163[»]
2XP9X-ray1.90A1-163[»]
2XPAX-ray1.90A1-163[»]
2XPBX-ray2.00A1-163[»]
2ZQSX-ray1.90A1-163[»]
2ZQTX-ray1.46A1-163[»]
2ZQUX-ray2.50A1-163[»]
2ZQVX-ray2.50A1-163[»]
2ZR4X-ray2.00A1-163[»]
2ZR5X-ray2.60A1-163[»]
2ZR6X-ray3.20A1-163[»]
3I6CX-ray1.30A/B45-163[»]
3IK8X-ray1.85A/B45-163[»]
3IKDX-ray2.00A/B45-163[»]
3IKGX-ray1.86A/B45-163[»]
3JYJX-ray1.87A/B45-163[»]
3KABX-ray2.19A1-163[»]
3KACX-ray2.00A/B45-163[»]
3KADX-ray1.95A1-163[»]
3KAFX-ray2.30A1-163[»]
3KAGX-ray1.90A1-163[»]
3KAHX-ray2.30A1-163[»]
3KAIX-ray1.90A1-163[»]
3KCEX-ray1.90A1-163[»]
3NTPX-ray1.76A1-163[»]
3ODKX-ray2.30A1-163[»]
3OOBX-ray1.89A1-163[»]
3TC5X-ray1.40A1-163[»]
3TCZX-ray2.10A6-163[»]
3TDBX-ray2.27A6-163[»]
3WH0X-ray1.60A1-163[»]
4GWTX-ray2.25A6-39[»]
4GWVX-ray3.05A6-39[»]
4QIBX-ray1.86A7-163[»]
4TNSX-ray1.33A/B43-163[»]
4TYOX-ray1.75A/B45-163[»]
4U84X-ray1.78A1-163[»]
4U85X-ray1.70A1-163[»]
4U86X-ray1.60A1-163[»]
ProteinModelPortaliQ13526.
SMRiQ13526.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111317. 233 interactors.
DIPiDIP-29306N.
IntActiQ13526. 166 interactors.
MINTiMINT-86298.
STRINGi9606.ENSP00000247970.

Chemistry databases

BindingDBiQ13526.
ChEMBLiCHEMBL2288.

PTM databases

iPTMnetiQ13526.
PhosphoSitePlusiQ13526.

Polymorphism and mutation databases

BioMutaiPIN1.
DMDMi3024406.

Proteomic databases

EPDiQ13526.
MaxQBiQ13526.
PaxDbiQ13526.
PeptideAtlasiQ13526.
PRIDEiQ13526.

Protocols and materials databases

DNASUi5300.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000247970; ENSP00000247970; ENSG00000127445.
ENST00000588695; ENSP00000466962; ENSG00000127445.
GeneIDi5300.
KEGGihsa:5300.
UCSCiuc002mml.3. human.

Organism-specific databases

CTDi5300.
DisGeNETi5300.
GeneCardsiPIN1.
HGNCiHGNC:8988. PIN1.
HPAiCAB004528.
CAB009326.
MIMi601052. gene.
neXtProtiNX_Q13526.
OpenTargetsiENSG00000127445.
PharmGKBiPA33320.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3259. Eukaryota.
COG0760. LUCA.
GeneTreeiENSGT00640000091578.
HOGENOMiHOG000275331.
HOVERGENiHBG002101.
InParanoidiQ13526.
KOiK09578.
OMAiDEVQCLH.
OrthoDBiEOG091G0RO7.
PhylomeDBiQ13526.
TreeFamiTF101101.

Enzyme and pathway databases

BioCyciZFISH:HS05098-MONOMER.
BRENDAi5.2.1.8. 2681.
ReactomeiR-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6811555. PI5P Regulates TP53 Acetylation.
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.
SignaLinkiQ13526.
SIGNORiQ13526.

Miscellaneous databases

ChiTaRSiPIN1. human.
EvolutionaryTraceiQ13526.
GeneWikiiPIN1.
GenomeRNAii5300.
PROiQ13526.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000127445.
CleanExiHS_PIN1.
ExpressionAtlasiQ13526. baseline and differential.
GenevisibleiQ13526. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q13526
Secondary accession number(s): A8K4V9, Q53X75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 172 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.