Home

Pin1 (human)

Overview Pin1 a member of the parvulin family of peptidyl-prolyl isomerases (PPIase), has been implicated in the G2-M transition of the cell cycle. Has two distinct functional domains: an N-terminal WW domain and a C-terminal PPlase domain. Pin1 interacts with a series of mitotic phosphoproteins, including Plk1, cdc25C and cdc27, catalyzing pSer-Pro or pThr/Pro cis/trans isomerizations. Displays a preference for an acidic residue n-terminal to the isomerized proline bond. Note: This description may include information from UniProtKB. Protein type: Isomerase; EC 5.2.1.8; Nuclear receptor co-regulator Cellular Component: nucleoplasm; cytoplasm; nuclear speck; midbody; nucleus Molecular Function: identical protein binding; protein binding; peptidyl-prolyl cis-trans isomerase activity; mitogen-activated protein kinase kinase binding; phosphothreonine binding; GTPase activating protein binding; phosphoserine binding Biological Process: protein peptidyl-prolyl isomerization; protein folding; cytokine and chemokine mediated signaling pathway; cell cycle; regulation of cytokinesis; regulation of cell proliferation; positive regulation of ubiquitin-protein ligase activity; innate immune response; regulation of mitosis; positive regulation of protein amino acid phosphorylation; negative regulation of transforming growth factor beta receptor signaling pathway; negative regulation of interferon type I production; positive regulation of Rho GTPase activity Reference #:  Q13526 (UniProtKB) Alt. Names/Synonyms: DOD; Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl-prolyl cis-trans isomerase Pin1; peptidyl-prolyl cis/trans isomerase, NIMA-interacting; peptidylprolyl cis/trans isomerase, NIMA-interacting 1; PIN1; PPIase Pin1; prolyl isomerase; protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1; protein (peptidylprolyl cis/trans isomerase) NIMA-interacting 1; Rotamase Pin1; UBL5 Gene Symbols: PIN1 Molecular weight: 18,243 Da Basal Isoelectric point: 8.95  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below Pin1 1F8A - B=1-163 (human) 1I6C - A=6-44 (human) 1I8G - B=6-44 (human) 1I8H - B=6-44 (human) 1NMV - A=1-163 (human) 1NMW - A=50-163 (human) 1PIN - A=1-163 (human) 1ZCN - A=1-163 (human) 2F21 - A=1-163 (human) 2ITK - A=1-163 (human) 2KBU - A=6-39 (human) 2KCF - A=6-39 (human) 2LB3 - A=6-41 (human) 2Q5A - A=1-163 (human) 2XP3 - A=1-163 (human) 2XP4 - A=1-163 (human) 2XP5 - A=1-163 (human) 2XP6 - A=1-163 (human) 2XP7 - A=1-163 (human) 2XP8 - A=1-163 (human) 2XP9 - A=1-163 (human) 2XPA - A=1-163 (human) 2XPB - A=1-163 (human) 2ZQS - A=1-163 (human) 2ZQT - A=1-163 (human) 2ZQU - A=1-163 (human) 2ZQV - A=1-163 (human) 2ZR4 - A=1-163 (human) 2ZR5 - A=1-163 (human) 2ZR6 - A=1-163 (human) 3I6C - A/B=45-163 (human) 3IK8 - A/B=45-163 (human) 3IKD - A/B=45-163 (human) 3IKG - A/B=45-163 (human) 3JYJ - A/B=45-163 (human) 3KAB - A=1-163 (human) 3KAC - A/B=45-163 (human) 3KAD - A=1-163 (human) 3KAF - A=1-163 (human) 3KAG - A=1-163 (human) 3KAH - A=1-163 (human) 3KAI - A=1-163 (human) 3KCE - A=1-163 (human) 3NTP - A=1-163 (human) 3ODK - A=1-163 (human) 3OOB - A=1-163 (human) 3TC5 - A=1-163 (human) 3TCZ - A=6-163 (human) 3TDB - A=6-163 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1F8A 1I6C 1I8G 1I8H 1NMV 1NMW 1PIN 1ZCN 2F21 2ITK 2KBU 2KCF 2LB3 2Q5A 2XP3 2XP4 2XP5 2XP6 2XP7 2XP8 2XP9 2XPA 2XPB 2ZQS 2ZQT 2ZQU 2ZQV 2ZR4 2ZR5 2ZR6 3I6C 3IK8 3IKD 3IKG 3JYJ 3KAB 3KAC 3KAD 3KAF 3KAG 3KAH 3KAI 3KCE 3NTP 3ODK 3OOB 3TC5 3TCZ 3TDB  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  NURSA  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

	Sites Implicated In
cell cycle regulation: S16‑p, Y23‑p, S138‑p intracellular localization: S16‑p, S138‑p molecular association, regulation: Y23‑p protein degradation: S16‑p protein stabilization: S65‑p ubiquitination: S16‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	3		K13-u	KLPPGWEkRMsRSSG
8	0		S16-p	PGWEkRMsRSSGRVy
2	4		Y23-p	sRSSGRVyYFNHITN
0	1		Y24	RSSGRVyYFNHITNA
0	25		K46-a	GNSSSGGkNGQGEPA
0	3		K63-u	RCSHLLVkHsQSRRP
1	0		S65-p	SHLLVkHsQSRRPss
2	0		S71-p	HsQSRRPssWRQEKI
0	2		S72-p	sQSRRPssWRQEKIT
0	1		K82-a	QEKITRTkEEALELI
0	2		K82-u	QEKITRTkEEALELI
0	1		K97-u	NGYIQKIkSGEEDFE
0	9		S105-p	SGEEDFEsLAsQFSD
0	1		S108-p	EDFEsLAsQFSDCSS
0	3		K117-u	FSDCSSAkARGDLGA
0	1		K132-u	FSRGQMQkPFEDAsF
1	0		S138-p	QkPFEDAsFALRTGE

	mouse
K13-u	KLPPGWEkRMsRSSG
S16-p	PGWEkRMsRSSGRVY
Y23	sRSSGRVYyFNHITN
Y24-p	RSSGRVYyFNHITNA
K48	STVGGSSKNGQGEPA
K65	RCSHLLVKHSQSRRP
S67	SHLLVKHSQSRRPSS
S73	HSQSRRPSSWRQEKI
S74	SQSRRPSSWRQEKIT
K84	QEKITRSKEEALELI
K84	QEKITRSKEEALELI
K99	NGYIQKIKSGEEDFE
S107	SGEEDFESLASQFSD
S110	EDFESLASQFSDCSS
K119-u	FSDCSSAkARGDLGP
K134	FSRGQMQKPFEDASF
S140	QKPFEDASFALRTGE

	rat
K13	KLPSGWEKRMSRSSG
S16	SGWEKRMSRSSGRVY
Y23	SRSSGRVYYFNHITN
Y24	RSSGRVYYFNHITNA
K48	STVGGGSKNGQGEPA
K65-u	RCSHLLVkHSQSRRP
S67	SHLLVkHSQSRRPSS
S73	HSQSRRPSSWRQEKI
S74	SQSRRPSSWRQEKIT
K84	QEKITRSKEEALELI
K84	QEKITRSKEEALELI
K99	NGYIQKIKSGEEDFE
S107	SGEEDFESLASQFSD
S110	EDFESLASQFSDCSS
K119	FSDCSSAKARGDLGA
K134	FSRGQMQKPFEDASF
S140	QKPFEDASFALRTGE

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.