UniProt Accession

 PIN1_HUMAN; Q13526; A8K4V9; Q53X75 

Genbank Protein ID

 U49070; CR407654; BT019331; AK291074; CH471106; BC002899 

Genbank Nucleotide ID

 AAC50492.1; CAG28582.1; AAV38138.1; BAF83763.1; EAW84057.1; AAH02899.1 

Protein Name

 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 

Protein Synonyms/Alias

 Peptidyl-prolyl cis-trans isomerase Pin1; PPIase Pin1; Rotamase Pin1 

Gene Name

 PIN1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MADEEKLPPGWEK	ubiquitination	[1]
13	KLPPGWEKRMSRSSG	ubiquitination	[1, 2, 3, 4, 5]
46	GNSSSGGKNGQGEPA	acetylation	[6]
82	QEKITRTKEEALELI	ubiquitination	[1, 3, 5]
95	LINGYIQKIKSGEED	ubiquitination	[1, 3, 4, 5]
97	NGYIQKIKSGEEDFE	ubiquitination	[1]
117	FSDCSSAKARGDLGA	ubiquitination	[1, 4]
132	FSRGQMQKPFEDASF	ubiquitination	[3, 5]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 

Functional Description

 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. Required for the efficient dephosphorylation and recycling of RAF1 after mitogen activation. Binds and targets PML for degradation in a phosphorylation-dependent manner. 

Sequence Annotation

 DOMAIN 5 39 WW.
 DOMAIN 52 163 PpiC.
 MOD_RES 46 46 N6-acetyllysine.
 MOD_RES 71 71 Phosphoserine; by DAPK1.
 MOD_RES 108 108 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Cell cycle; Complete proteome; Cytoplasm; Isomerase; Nucleus; Phosphoprotein; Reference proteome; Rotamase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 163 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0030496; C:midbody; IDA:MGI.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IDA:BHF-UCL.
 GO:0050815; F:phosphoserine binding; IDA:BHF-UCL.
 GO:0050816; F:phosphothreonine binding; IDA:BHF-UCL.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:2000146; P:negative regulation of cell motility; IDA:BHF-UCL.
 GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
 GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
 GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
 GO:0001934; P:positive regulation of protein phosphorylation; IGI:MGI.
 GO:0032321; P:positive regulation of Rho GTPase activity; IMP:BHF-UCL.
 GO:0051443; P:positive regulation of ubiquitin-protein ligase activity; IDA:BHF-UCL.
 GO:0006457; P:protein folding; IEA:UniProtKB-KW.
 GO:0042127; P:regulation of cell proliferation; IEA:Compara.
 GO:0032465; P:regulation of cytokinesis; IMP:MGI.
 GO:0007088; P:regulation of mitosis; TAS:ProtInc.
 GO:0060393; P:regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL. 

Interpro

 IPR000297; PPIase_PpiC.
 IPR023058; PPIase_PpiC_CS.
 IPR001202; WW_dom. 

Pfam

 PF00639; Rotamase
 PF00397; WW 

SMART

 SM00456; WW 

PROSITE

 PS01096; PPIC_PPIASE_1
 PS50198; PPIC_PPIASE_2
 PS01159; WW_DOMAIN_1
 PS50020; WW_DOMAIN_2 

PRINTS