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Q9QUR7

- PIN1_MOUSE

UniProt

Q9QUR7 - PIN1_MOUSE

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Protein

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Gene

Pin1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Displays a preference for an acidic residue N-terminal to the isomerized proline bond. Catalyzes pSer/Thr-Pro cis/trans isomerizations. Down-regulates kinase activity of BTK. Can transactivate multiple oncogenes and induce centrosome amplification, chromosome instability and cell transformation (By similarity). Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation (By similarity). Binds and targets BCL6 and PML for degradation in a phosphorylation-dependent manner.By similarity1 Publication

Catalytic activityi

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

GO - Molecular functioni

  1. peptidyl-prolyl cis-trans isomerase activity Source: UniProtKB-KW

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. protein folding Source: UniProtKB-KW
  3. regulation of cell proliferation Source: MGI
  4. regulation of cytokinesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

BRENDAi5.2.1.8. 3474.
ReactomeiREACT_198532. 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
Gene namesi
Name:Pin1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:1346036. Pin1.

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-73 by DAPK1 results in inhibition of its nuclear localization (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Animals display more and larger germinal centers.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 165165Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1PRO_0000193436Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481N6-acetyllysineBy similarity
Modified residuei73 – 731Phosphoserine; by DAPK1By similarity
Modified residuei110 – 1101PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Ser-73 by DAPK1 results in inhibition of its catalytic activity, nuclear localization, and its ability to induce centrosome amplification, chromosome instability and cell transformation.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9QUR7.
PaxDbiQ9QUR7.
PRIDEiQ9QUR7.

PTM databases

PhosphoSiteiQ9QUR7.

Expressioni

Gene expression databases

BgeeiQ9QUR7.
GenevestigatoriQ9QUR7.

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-6.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GphnQ8BUV36EBI-2432975,EBI-771218
Tp53P023403EBI-2432975,EBI-474016

Protein-protein interaction databases

BioGridi204839. 9 interactions.
DIPiDIP-44280N.
IntActiQ9QUR7. 6 interactions.
MINTiMINT-4107624.

Structurei

3D structure databases

ProteinModelPortaliQ9QUR7.
SMRiQ9QUR7. Positions 1-165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 3935WWPROSITE-ProRule annotationAdd
BLAST
Domaini54 – 165112PpiCPROSITE-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.
InParanoidiQ9QUR7.
KOiK09578.
OMAiKLKHYMA.
OrthoDBiEOG7S4X82.
PhylomeDBiQ9QUR7.
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.

Q9QUR7-1 [UniParc]FASTAAdd to Basket

« Hide

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009691 mRNA. Translation: BAA87037.1.
AB009692 Genomic DNA. Translation: BAA87038.1.
AK002665 mRNA. Translation: BAB22270.1.
AK003369 mRNA. Translation: BAB22743.1.
AK054045 mRNA. Translation: BAC35631.1.
AK150652 mRNA. Translation: BAE29739.1.
AK160228 mRNA. Translation: BAE35702.1.
BC038254 mRNA. Translation: AAH38254.1.
CCDSiCCDS22882.1.
PIRiJC7136.
RefSeqiNP_075860.1. NM_023371.3.
UniGeneiMm.7906.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009691 mRNA. Translation: BAA87037.1 .
AB009692 Genomic DNA. Translation: BAA87038.1 .
AK002665 mRNA. Translation: BAB22270.1 .
AK003369 mRNA. Translation: BAB22743.1 .
AK054045 mRNA. Translation: BAC35631.1 .
AK150652 mRNA. Translation: BAE29739.1 .
AK160228 mRNA. Translation: BAE35702.1 .
BC038254 mRNA. Translation: AAH38254.1 .
CCDSi CCDS22882.1.
PIRi JC7136.
RefSeqi NP_075860.1. NM_023371.3.
UniGenei Mm.7906.

3D structure databases

ProteinModelPortali Q9QUR7.
SMRi Q9QUR7. Positions 1-165.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204839. 9 interactions.
DIPi DIP-44280N.
IntActi Q9QUR7. 6 interactions.
MINTi MINT-4107624.

PTM databases

PhosphoSitei Q9QUR7.

Proteomic databases

MaxQBi Q9QUR7.
PaxDbi Q9QUR7.
PRIDEi Q9QUR7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034689 ; ENSMUSP00000034689 ; ENSMUSG00000032171 .
GeneIDi 23988.
KEGGi mmu:23988.
UCSCi uc009ojd.1. mouse.

Organism-specific databases

CTDi 5300.
MGIi MGI:1346036. Pin1.

Phylogenomic databases

eggNOGi COG0760.
GeneTreei ENSGT00640000091578.
HOGENOMi HOG000275331.
HOVERGENi HBG002101.
InParanoidi Q9QUR7.
KOi K09578.
OMAi KLKHYMA.
OrthoDBi EOG7S4X82.
PhylomeDBi Q9QUR7.
TreeFami TF101101.

Enzyme and pathway databases

BRENDAi 5.2.1.8. 3474.
Reactomei REACT_198532. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

NextBioi 303885.
PROi Q9QUR7.
SOURCEi Search...

Gene expression databases

Bgeei Q9QUR7.
Genevestigatori Q9QUR7.

Family and domain databases

InterProi IPR000297. PPIase_PpiC.
IPR023058. PPIase_PpiC_CS.
IPR001202. WW_dom.
[Graphical view ]
Pfami PF00639. Rotamase. 1 hit.
PF00397. WW. 1 hit.
[Graphical view ]
SMARTi SM00456. WW. 1 hit.
[Graphical view ]
SUPFAMi SSF51045. SSF51045. 1 hit.
PROSITEi PS01096. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mice lacking Pin1 develop normally, but are defective in entering cell cycle from G0 arrest."
    Fujimori F., Takahashi K., Uchida C., Uchida T.
    Biochem. Biophys. Res. Commun. 265:658-663(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Embryo, Kidney and Oviduct.
  3. "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].
    Strain: FVB/N.
    Tissue: Kidney.
  4. "Sil phosphorylation in a Pin1 binding domain affects the duration of the spindle checkpoint."
    Campaner S., Kaldis P., Izraeli S., Kirsch I.R.
    Mol. Cell. Biol. 25:6660-6672(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STIL.
  5. "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, DISRUPTION PHENOTYPE.
  6. "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.

Entry informationi

Entry nameiPIN1_MOUSE
AccessioniPrimary (citable) accession number: Q9QUR7
Secondary accession number(s): Q543B3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 109 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3