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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

  • GTPase activating protein binding Source: BHF-UCL
  • mitogen-activated protein kinase kinase binding Source: BHF-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
  • cytokine-mediated signaling pathway Source: Reactome
  • innate immune response Source: Reactome
  • negative regulation of cell motility Source: BHF-UCL
  • negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCL
  • negative regulation of type I interferon production Source: Reactome
  • positive regulation of GTPase activity Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of ubiquitin-protein transferase activity Source: BHF-UCL
  • protein peptidyl-prolyl isomerization Source: GOC
  • regulation of cytokinesis Source: MGI
  • regulation of mitotic nuclear division Source: ProtInc
  • regulation of pathway-restricted SMAD protein phosphorylation Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

BRENDAi5.2.1.8. 2681.
ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
SignaLinkiQ13526.

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
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:8988. PIN1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • midbody Source: MGI
  • 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231Y → A: Reduced affinity for KIF20B. 1 Publication
Mutagenesisi34 – 341W → A: Loss of peptidyl-prolyl cis/trans isomerase activity. 1 Publication
Mutagenesisi63 – 631K → A: Loss of peptidyl-prolyl cis/trans isomerase activity. 1 Publication
Mutagenesisi71 – 711S → D or E: Loss of activity, nuclear localization and cellular function. 1 Publication

Organism-specific databases

PharmGKBiPA33320.

Polymorphism and mutation databases

BioMutaiPIN1.
DMDMi3024406.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 163163Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1PRO_0000193435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461N6-acetyllysine1 Publication
Modified residuei71 – 711Phosphoserine; by DAPK11 Publication
Modified residuei108 – 1081Phosphoserine1 Publication

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

MaxQBiQ13526.
PaxDbiQ13526.
PeptideAtlasiQ13526.
PRIDEiQ13526.

PTM databases

PhosphoSiteiQ13526.

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

BgeeiQ13526.
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
ANKRD40Q6AI123EBI-714158,EBI-2838246
APPP05067-42EBI-714158,EBI-302641
ARHGAP8P85298-425EBI-714158,EBI-9523517
ARHGEF15D3DTR73EBI-714158,EBI-10176602
CBSP355203EBI-714158,EBI-740135
CCDC184Q52MB23EBI-714158,EBI-10179526
CDK10Q151315EBI-714158,EBI-1646959
CEP55D3DR373EBI-714158,EBI-10173536
CEP76Q8TAP63EBI-714158,EBI-742887
CNKSR1Q969H43EBI-714158,EBI-741671
DAB1O755533EBI-714158,EBI-7875264
FOXP2O154093EBI-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
IKZF3Q9UKT93EBI-714158,EBI-747204
IRAK1P5161710EBI-714158,EBI-358664
JAKMIP2Q96AA83EBI-714158,EBI-752007
KRT31Q153233EBI-714158,EBI-948001
KRT38O760153EBI-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
MDFIQ997504EBI-714158,EBI-724076
MEOX2A4D1273EBI-714158,EBI-10172134
MTUS2Q5JR593EBI-714158,EBI-742948
NAB2Q157423EBI-714158,EBI-8641936
NEK6Q9HC983EBI-714158,EBI-740364
NONOQ152334EBI-714158,EBI-350527
NONOQ15233-23EBI-714158,EBI-10203843
NOTCH1P465319EBI-714158,EBI-636374
NUP62P371983EBI-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
SSBP3Q9BWW43EBI-714158,EBI-2902395
SULT4A1Q9BR014EBI-714158,EBI-6690555
TAB3Q8N5C83EBI-714158,EBI-359964
TCF4P158843EBI-714158,EBI-533224
THAP7Q9BT493EBI-714158,EBI-741350
TNIP1Q150254EBI-714158,EBI-357849
TP53P0463712EBI-714158,EBI-366083
TRAF1Q130773EBI-714158,EBI-359224
TRAF2Q129334EBI-714158,EBI-355744
TRIP6Q156543EBI-714158,EBI-742327
TSC22D4Q9Y3Q84EBI-714158,EBI-739485
ZBTB14O438293EBI-714158,EBI-10176632
ZBTB22O152093EBI-714158,EBI-723574
ZBTB7BO151563EBI-714158,EBI-740434
ZBTB9Q96C003EBI-714158,EBI-395708
ZMIZ2Q8NF644EBI-714158,EBI-745786
ZMIZ2Q8NF64-23EBI-714158,EBI-10182121
ZNF446Q96AF53EBI-714158,EBI-740232

Protein-protein interaction databases

BioGridi111317. 202 interactions.
DIPiDIP-29306N.
IntActiQ13526. 127 interactions.
MINTiMINT-86298.
STRINGi9606.ENSP00000247970.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 155Combined sources
Turni17 – 193Combined sources
Beta strandi22 – 265Combined sources
Turni27 – 293Combined sources
Beta strandi32 – 354Combined sources
Beta strandi39 – 413Combined sources
Beta strandi53 – 6210Combined sources
Beta strandi67 – 693Combined sources
Beta strandi75 – 773Combined sources
Helixi82 – 9817Combined sources
Beta strandi99 – 1013Combined sources
Helixi103 – 1108Combined sources
Helixi114 – 1185Combined sources
Beta strandi121 – 1266Combined sources
Helixi127 – 1293Combined sources
Helixi132 – 1409Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi155 – 1639Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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-A22-39[»]
2M9FNMR-A6-39[»]
2M9INMR-A6-39[»]
2M9JNMR-A6-39[»]
2Q5AX-ray1.50A1-163[»]
2RUCNMR-A51-163[»]
2RUDNMR-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[»]
4TYOX-ray1.75A/B45-163[»]
ProteinModelPortaliQ13526.
SMRiQ13526. Positions 1-163.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13526.

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.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0760.
GeneTreeiENSGT00640000091578.
HOGENOMiHOG000275331.
HOVERGENiHBG002101.
InParanoidiQ13526.
KOiK09578.
OMAiFALKVGD.
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.
UCSCiuc002mmk.2. 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
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-A22-39[»]
2M9FNMR-A6-39[»]
2M9INMR-A6-39[»]
2M9JNMR-A6-39[»]
2Q5AX-ray1.50A1-163[»]
2RUCNMR-A51-163[»]
2RUDNMR-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[»]
4TYOX-ray1.75A/B45-163[»]
ProteinModelPortaliQ13526.
SMRiQ13526. Positions 1-163.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111317. 202 interactions.
DIPiDIP-29306N.
IntActiQ13526. 127 interactions.
MINTiMINT-86298.
STRINGi9606.ENSP00000247970.

Chemistry

BindingDBiQ13526.
ChEMBLiCHEMBL2288.

PTM databases

PhosphoSiteiQ13526.

Polymorphism and mutation databases

BioMutaiPIN1.
DMDMi3024406.

Proteomic databases

MaxQBiQ13526.
PaxDbiQ13526.
PeptideAtlasiQ13526.
PRIDEiQ13526.

Protocols and materials databases

DNASUi5300.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000247970; ENSP00000247970; ENSG00000127445.
ENST00000588695; ENSP00000466962; ENSG00000127445.
GeneIDi5300.
KEGGihsa:5300.
UCSCiuc002mmk.2. human.

Organism-specific databases

CTDi5300.
GeneCardsiGC19P009945.
HGNCiHGNC:8988. PIN1.
HPAiCAB004528.
CAB009326.
MIMi601052. gene.
neXtProtiNX_Q13526.
PharmGKBiPA33320.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0760.
GeneTreeiENSGT00640000091578.
HOGENOMiHOG000275331.
HOVERGENiHBG002101.
InParanoidiQ13526.
KOiK09578.
OMAiFALKVGD.
PhylomeDBiQ13526.
TreeFamiTF101101.

Enzyme and pathway databases

BRENDAi5.2.1.8. 2681.
ReactomeiREACT_115831. ISG15 antiviral mechanism.
REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
SignaLinkiQ13526.

Miscellaneous databases

ChiTaRSiPIN1. human.
EvolutionaryTraceiQ13526.
GeneWikiiPIN1.
GenomeRNAii5300.
NextBioi20486.
PROiQ13526.
SOURCEiSearch...

Gene expression databases

BgeeiQ13526.
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...

Publicationsi

« Hide 'large scale' publications
  1. "A human peptidyl-prolyl isomerase essential for regulation of mitosis."
    Lu K.P., Hanes S.D., Hunter T.
    Nature 380:544-547(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  7. "Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1."
    Kamimoto T., Zama T., Aoki R., Muro Y., Hagiwara M.
    J. Biol. Chem. 276:37520-37528(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIF20B, MUTAGENESIS OF TYR-23.
  8. Cited for: FUNCTION, INTERACTION WITH RAF1.
  9. "Interaction of Pin1 with Nek6 and characterization of their expression correlation in Chinese hepatocellular carcinoma patients."
    Chen J., Li L., Zhang Y., Yang H., Wei Y., Zhang L., Liu X., Yu L.
    Biochem. Biophys. Res. Commun. 341:1059-1065(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK6.
  10. "Regulation of Bruton tyrosine kinase by the peptidylprolyl isomerase Pin1."
    Yu L., Mohamed A.J., Vargas L., Berglof A., Finn G., Lu K.P., Smith C.I.
    J. Biol. Chem. 281:18201-18207(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BTK, FUNCTION.
  11. "Genotoxic stress regulates expression of the proto-oncogene Bcl6 in germinal center B cells."
    Phan R.T., Saito M., Kitagawa Y., Means A.R., Dalla-Favera R.
    Nat. Immunol. 8:1132-1139(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BCL6 STABILITY REGULATION, INTERACTION WITH BCL6, TISSUE SPECIFICITY.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. "Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons."
    Buschdorf J.P., Chew L.L., Soh U.J., Liou Y.C., Low B.C.
    PLoS ONE 3:E2686-E2686(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATCAY.
  14. "Protein kinase-X interacts with Pin-1 and Polycystin-1 during mouse kidney development."
    Li X., Hyink D.P., Radbill B., Sudol M., Zhang H., Zheleznova N.N., Wilson P.D.
    Kidney Int. 76:54-62(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKX.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Mitogen-activated protein kinase extracellular signal-regulated kinase 2 phosphorylates and promotes Pin1 protein-dependent promyelocytic leukemia protein turnover."
    Lim J.H., Liu Y., Reineke E., Kao H.Y.
    J. Biol. Chem. 286:44403-44411(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PML.
  18. "Death-associated protein kinase 1 phosphorylates Pin1 and inhibits its prolyl isomerase activity and cellular function."
    Lee T.H., Chen C.H., Suizu F., Huang P., Schiene-Fischer C., Daum S., Zhang Y.J., Goate A., Chen R.H., Zhou X.Z., Lu K.P.
    Mol. Cell 42:147-159(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-71, INTERACTION WITH DAPK1, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-71, TISSUE SPECIFICITY.
  19. "Negative regulation of the stability and tumor suppressor function of Fbw7 by the Pin1 prolyl isomerase."
    Min S.H., Lau A.W., Lee T.H., Inuzuka H., Wei S., Huang P., Shaik S., Lee D.Y., Finn G., Balastik M., Chen C.H., Luo M., Tron A.E., Decaprio J.A., Zhou X.Z., Wei W., Lu K.P.
    Mol. Cell 46:771-783(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FBXW7, MUTAGENESIS OF TRP-34 AND LYS-63.
  20. "Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent."
    Ranganathan R., Lu K.P., Hunter T., Noel J.P.
    Cell 89:875-886(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).

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: June 24, 2015
This is version 158 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

External Data

Dasty 3

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 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.