Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 194 (08 May 2019)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (PubMed:21497122, PubMed:22033920, PubMed:23623683). 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).8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIsomerase, Rotamase
Biological processCell cycle

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.2.1.8 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1169408 ISG15 antiviral mechanism
R-HSA-5668599 RHO GTPases Activate NADPH Oxidases
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-6811555 PI5P Regulates TP53 Acetylation
R-HSA-936440 Negative regulators of DDX58/IFIH1 signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q13526

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q13526

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PIN1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:8988 PIN1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
601052 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q13526

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi23Y → A: Reduced affinity for KIF20B. 1 Publication1
Mutagenesisi34W → A: Loss of binding to phosphorylated target proteins, including to phosphorylated RBBP8/CtIP; decrease in DNA repair of double-strand breaks by homologous recombination less efficient than that observed with wild-type protein. 2 Publications1
Mutagenesisi63K → A: Loss of peptidyl-prolyl cis/trans isomerase activity. 1 Publication1
Mutagenesisi71S → D or E: Loss of peptidyl-prolyl cis/trans isomerase activity, nuclear localization and cellular function. 1 Publication1
Mutagenesisi113C → A: Loss of peptidyl-prolyl cis/trans isomerase activity; decrease in DNA repair of double-strand breaks by homologous recombination slightly less efficient than that observed with wild-type protein. No effect on RBBP8/CtIP. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
5300

Open Targets

More...
OpenTargetsi
ENSG00000127445

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA33320

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2288

Drug and drug target database

More...
DrugBanki
DB01766 Beta-(2-Naphthyl)-Alanine

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PIN1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
3024406

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001934351 – 163Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1Add BLAST163

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei43PhosphoserineCombined sources1
Modified residuei46N6-acetyllysineCombined sources1
Modified residuei71Phosphoserine; by DAPK11 Publication1
Modified residuei108PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...
EPDi
Q13526

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q13526

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q13526

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q13526

PeptideAtlas

More...
PeptideAtlasi
Q13526

PRoteomics IDEntifications database

More...
PRIDEi
Q13526

ProteomicsDB human proteome resource

More...
ProteomicsDBi
59519

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q13526

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q13526

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000127445 Expressed in 221 organ(s), highest expression level in anterior cingulate cortex

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q13526 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q13526 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB004528
CAB009326
HPA068650

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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). Directly interacts with RBBP8/CtIP; this interaction depends upon RBBP8 phosphorylation (PubMed:23623683).11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>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
CCDC6Q162044EBI-714158,EBI-1045350
CDK10Q151315EBI-714158,EBI-1646959
CEP55Q53EZ43EBI-714158,EBI-747776
CEP76Q8TAP65EBI-714158,EBI-742887
CNKSR1Q969H45EBI-714158,EBI-741671
DAB1O755533EBI-714158,EBI-7875264
FOXP2O154095EBI-714158,EBI-983612
GOLGA2Q083795EBI-714158,EBI-618309
Grm5P31424-23EBI-714158,EBI-8830305From a different organism.
Grm5Q3UVX52EBI-714158,EBI-8795045From Mus musculus.
HEXIM2Q96MH27EBI-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
MAP2K1Q027505EBI-714158,EBI-492564
Map2k1P319384EBI-714158,EBI-298860From Mus musculus.
Map2k2Q6393212EBI-714158,EBI-397724From Mus musculus.
MAP3K8P412798EBI-714158,EBI-354900
MDFIQ997506EBI-714158,EBI-724076
MEOX2P502223EBI-714158,EBI-748397
MTUS2Q5JR593EBI-714158,EBI-742948
MYCP011065EBI-714158,EBI-447544
NAB2Q157425EBI-714158,EBI-8641936
NanogQ80Z64-12EBI-714158,EBI-15699014From a different organism.
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
RAF1P040492EBI-714158,EBI-365996
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
TSC22D4Q9Y3Q86EBI-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
ZNF446Q9NWS9-25EBI-714158,EBI-740232

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
111317, 248 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q13526

Database of interacting proteins

More...
DIPi
DIP-29306N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q13526

Protein interaction database and analysis system

More...
IntActi
Q13526, 201 interactors

Molecular INTeraction database

More...
MINTi
Q13526

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000247970

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q13526

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1163
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
5B3WX-ray2.40A/B5-15[»]
5B3XX-ray2.40A5-15[»]
5B3YX-ray1.90A5-23[»]
5B3ZX-ray2.30A/B/C/D5-39[»]
5BMYX-ray2.00A5-29[»]
5GPHNMR-A51-163[»]
5UY9X-ray1.85A1-163[»]
5VTIX-ray1.80A6-39[»]
5VTJX-ray1.50A6-39[»]
5VTKX-ray1.99A6-39[»]
6DUNX-ray1.59A/B46-163[»]

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q13526

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q13526

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini5 – 39WWPROSITE-ProRule annotationAdd BLAST35
Domaini52 – 163PpiCPROSITE-ProRule annotationAdd BLAST112

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3259 Eukaryota
COG0760 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00640000091578

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000275331

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q13526

KEGG Orthology (KO)

More...
KOi
K09578

Identification of Orthologs from Complete Genome Data

More...
OMAi
DEVQCLH

Database of Orthologous Groups

More...
OrthoDBi
1437969at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q13526

TreeFam database of animal gene trees

More...
TreeFami
TF101101

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00201 WW, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000297 PPIase_PpiC
IPR023058 PPIase_PpiC_CS
IPR001202 WW_dom
IPR036020 WW_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00639 Rotamase, 1 hit
PF00397 WW, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00456 WW, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51045 SSF51045, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i35391AF40B7D1E13
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
K7EMU7K7EMU7_HUMAN
Peptidyl-prolyl cis-trans isomerase
PIN1
145Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EN45K7EN45_HUMAN
Peptidyl-prolyl cis-trans isomerase
PIN1
90Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
K7EP26K7EP26_HUMAN
Peptidyl-prolyl cis-trans isomerase...
PIN1
50Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS12220.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S68520

NCBI Reference Sequences

More...
RefSeqi
NP_006212.1, NM_006221.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000247970; ENSP00000247970; ENSG00000127445
ENST00000588695; ENSP00000466962; ENSG00000127445

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5300

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5300

UCSC genome browser

More...
UCSCi
uc002mml.3 human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

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[»]
5B3WX-ray2.40A/B5-15[»]
5B3XX-ray2.40A5-15[»]
5B3YX-ray1.90A5-23[»]
5B3ZX-ray2.30A/B/C/D5-39[»]
5BMYX-ray2.00A5-29[»]
5GPHNMR-A51-163[»]
5UY9X-ray1.85A1-163[»]
5VTIX-ray1.80A6-39[»]
5VTJX-ray1.50A6-39[»]
5VTKX-ray1.99A6-39[»]
6DUNX-ray1.59A/B46-163[»]
SMRiQ13526
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111317, 248 interactors
CORUMiQ13526
DIPiDIP-29306N
ELMiQ13526
IntActiQ13526, 201 interactors
MINTiQ13526
STRINGi9606.ENSP00000247970

Chemistry databases

BindingDBiQ13526
ChEMBLiCHEMBL2288
DrugBankiDB01766 Beta-(2-Naphthyl)-Alanine

PTM databases

iPTMnetiQ13526
PhosphoSitePlusiQ13526

Polymorphism and mutation databases

BioMutaiPIN1
DMDMi3024406

Proteomic databases

EPDiQ13526
jPOSTiQ13526
MaxQBiQ13526
PaxDbiQ13526
PeptideAtlasiQ13526
PRIDEiQ13526
ProteomicsDBi59519

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5300
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5300
DisGeNETi5300

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PIN1
HGNCiHGNC:8988 PIN1
HPAiCAB004528
CAB009326
HPA068650
MIMi601052 gene
neXtProtiNX_Q13526
OpenTargetsiENSG00000127445
PharmGKBiPA33320

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3259 Eukaryota
COG0760 LUCA
GeneTreeiENSGT00640000091578
HOGENOMiHOG000275331
InParanoidiQ13526
KOiK09578
OMAiDEVQCLH
OrthoDBi1437969at2759
PhylomeDBiQ13526
TreeFamiTF101101

Enzyme and pathway databases

BRENDAi5.2.1.8 2681
ReactomeiR-HSA-1169408 ISG15 antiviral mechanism
R-HSA-5668599 RHO GTPases Activate NADPH Oxidases
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-6811555 PI5P Regulates TP53 Acetylation
R-HSA-936440 Negative regulators of DDX58/IFIH1 signaling
SignaLinkiQ13526
SIGNORiQ13526

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
PIN1 human
EvolutionaryTraceiQ13526

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PIN1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5300

Protein Ontology

More...
PROi
PR:Q13526

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000127445 Expressed in 221 organ(s), highest expression level in anterior cingulate cortex
ExpressionAtlasiQ13526 baseline and differential
GenevisibleiQ13526 HS

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPIN1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q13526
Secondary accession number(s): A8K4V9, Q53X75
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: May 8, 2019
This is version 194 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again