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Protein

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1

Gene

Pin1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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. GTPase activating protein binding Source: MGI
  2. mitogen-activated protein kinase kinase binding Source: MGI
  3. peptidyl-prolyl cis-trans isomerase activity Source: MGI
  4. phosphoserine binding Source: MGI
  5. phosphothreonine binding Source: MGI

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. negative regulation of cell motility Source: MGI
  3. negative regulation of ERK1 and ERK2 cascade Source: MGI
  4. negative regulation of transforming growth factor beta receptor signaling pathway Source: MGI
  5. positive regulation of protein phosphorylation Source: MGI
  6. positive regulation of Rho GTPase activity Source: MGI
  7. positive regulation of ubiquitin-protein transferase activity Source: MGI
  8. protein peptidyl-prolyl isomerization Source: MGI
  9. regulation of cell proliferation Source: MGI
  10. regulation of cytokinesis Source: MGI
  11. regulation of pathway-restricted SMAD protein phosphorylation 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-SubCell
  2. midbody Source: MGI
  3. nuclear speck Source: UniProtKB-SubCell
  4. nucleus Source: MGI
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.
OMAiFALKVGD.
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.
CCDSiCCDS22882.1.
PIRiJC7136.
RefSeqiNP_075860.1. NM_023371.3.
UniGeneiMm.7906.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ9QUR7.

Proteomic databases

MaxQBiQ9QUR7.
PaxDbiQ9QUR7.
PRIDEiQ9QUR7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5300.
MGIiMGI:1346036. Pin1.

Phylogenomic databases

eggNOGiCOG0760.
GeneTreeiENSGT00640000091578.
HOGENOMiHOG000275331.
HOVERGENiHBG002101.
InParanoidiQ9QUR7.
KOiK09578.
OMAiFALKVGD.
OrthoDBiEOG7S4X82.
PhylomeDBiQ9QUR7.
TreeFamiTF101101.

Enzyme and pathway databases

BRENDAi5.2.1.8. 3474.
ReactomeiREACT_198532. Negative regulators of RIG-I/MDA5 signaling.

Miscellaneous databases

NextBioi303885.
PROiQ9QUR7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QUR7.
GenevestigatoriQ9QUR7.

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. "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: February 4, 2015
This is version 111 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

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.