HUMAN:PIN1

From GONUTS

Jump to: navigation, search

Species (Taxon ID)	Homo sapiens (Human). (taxon:9606)
Gene Name(s)	PIN1
Protein Name(s)	Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 Peptidyl-prolyl cis-trans isomerase Pin1 PPIase Pin1 Rotamase Pin1
External Links
UniProt Identifier	PIN1_HUMAN
UniProt Accessions	Q13526, A8K4V9, Q53X75,
EMBL	U49070, CR407654, BT019331, AK291074, CH471106, BC002899,
PIR	S68520,
RefSeq	NP_006212.1,
PDB	1F8A, 1I6C, 1I8G, 1I8H, 1NMV, 1NMW, 1PIN, 1ZCN, 2F21, 2ITK, 2KBU, 2KCF, 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, 3ODK,
IntAct	Q13526,
Ensembl	ENST00000247970,
Pfam	PF00639, PF00397,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0005634	nucleus		TAS: Traceable Author Statement		C	Source: ProtInc
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity		IDA: Inferred from Direct Assay		F	Source: BHF-UCL
	GO:0050815	phosphoserine binding		IDA: Inferred from Direct Assay		F	Source: BHF-UCL
	GO:0050816	phosphothreonine binding		IDA: Inferred from Direct Assay		F	Source: BHF-UCL
	GO:0007049	cell cycle		IEA: Inferred from Electronic Annotation		P	Source: UniProtKB-KW
	GO:0030512	negative regulation of transforming growth ...		IDA: Inferred from Direct Assay		P	Source: BHF-UCL
	GO:0051443	positive regulation of ubiquitin-protein li...		IDA: Inferred from Direct Assay		P	Source: BHF-UCL
	GO:0006457	protein folding		IEA: Inferred from Electronic Annotation		P	Source: UniProtKB-KW
	GO:0007088	regulation of mitosis		TAS: Traceable Author Statement		P	Source: ProtInc
	GO:0005515	protein binding	PMID:20675384^[1]	IPI: Inferred from Physical Interaction	UniProtKB:Q53ET0	F	FIGURE 1. Pin1 associates with CRTC2.	complete
	GO:0060393	regulation of pathway-restricted SMAD prote...		IDA: Inferred from Direct Assay		P	Source: BHF-UCL
	GO:0033159	negative regulation of protein import into nucleus, translocation	PMID:20675384^[1]	IMP: Inferred from Mutant Phenotype		P	Figure 3 and Supplemental figure 4: Pin1 inhibits CRTC2 translocation into the nucleus.	complete
	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:5.2.1.8	P
	GO:0000413	protein peptidyl-prolyl isomerization	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0697	P
	GO:0000413	protein peptidyl-prolyl isomerization	PMID:19122240^[2]	IDA: Inferred from Direct Assay		P
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:5.2.1.8	F
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0697	F
	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:19122240^[2]	IDA: Inferred from Direct Assay		F
	GO:0005515	protein binding	PMID:11470801^[3]	IPI: Inferred from Physical Interaction	UniProtKB:Q96Q89	F
	GO:0005515	protein binding	PMID:16476580^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q9HC98	F
	GO:0005515	protein binding	PMID:16554819^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P05067-4	F
	GO:0005515	protein binding	PMID:16554819^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P12023	F
	GO:0005515	protein binding	PMID:17353931^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P40337	F
	GO:0005515	protein binding	PMID:20179103^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P04049	F
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C
	GO:0005634	nucleus	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0191	C
	GO:0005634	nucleus	PMID:20179103^[7]	IDA: Inferred from Direct Assay		C
	GO:0005634	nucleus	PMID:8606777^[8]	TAS: Traceable Author Statement		C
	GO:0005654	nucleoplasm	Reactome:REACT_24932	TAS: Traceable Author Statement		C
	GO:0005654	nucleoplasm	Reactome:REACT_25077	TAS: Traceable Author Statement		C
	GO:0006457	protein folding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0697	P
	GO:0007049	cell cycle	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0131	P
	GO:0007088	regulation of mitosis	PMID:10391244^[9]	TAS: Traceable Author Statement		P
	GO:0016853	isomerase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR000297	F
	GO:0016853	isomerase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0413	F
	GO:0030512	negative regulation of transforming growth factor beta receptor signaling pathway	PMID:19122240^[2]	IDA: Inferred from Direct Assay		P
	GO:0031434	mitogen-activated protein kinase kinase binding	PMID:20179103^[7]	IPI: Inferred from Physical Interaction	UniProtKB:Q63932	F
	GO:0032321	positive regulation of Rho GTPase activity	PMID:20179103^[7]	IMP: Inferred from Mutant Phenotype		P
	GO:0032480	negative regulation of type I interferon production	Reactome:REACT_25271	TAS: Traceable Author Statement		P
	GO:0032794	GTPase activating protein binding	PMID:20179103^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P85298	F
	GO:0045087	innate immune response	Reactome:REACT_6802	TAS: Traceable Author Statement		P
	GO:0050815	phosphoserine binding	PMID:10037602^[10]	IDA: Inferred from Direct Assay		F
	GO:0050816	phosphothreonine binding	PMID:10037602^[10]	IDA: Inferred from Direct Assay		F
	GO:0050816	phosphothreonine binding	PMID:10037602^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P30307	F
	GO:0051443	positive regulation of ubiquitin-protein ligase activity	PMID:19122240^[2]	IDA: Inferred from Direct Assay		P
	GO:0060393	regulation of pathway-restricted SMAD protein phosphorylation	PMID:19122240^[2]	IDA: Inferred from Direct Assay		P
	GO:0070373	negative regulation of ERK1 and ERK2 cascade	PMID:20179103^[7]	IDA: Inferred from Direct Assay		P
	GO:2000146	negative regulation of cell motility	PMID:20179103^[7]	IDA: Inferred from Direct Assay		P
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Nakatsu Y et al. (2010) Pin1 associates with and induces translocation of CRTC2 to the cytosol, thereby suppressing cAMP-responsive element transcriptional activity. J Biol Chem 285: 33018-27 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 Nakano A et al. (2009) Pin1 down-regulates transforming growth factor-beta (TGF-beta) signaling by inducing degradation of Smad proteins. J Biol Chem 284: 6109-15 PubMed GONUTS page
↑ Kamimoto T et al. (2001) Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1. J Biol Chem 276: 37520-8 PubMed GONUTS page
↑ Chen J et al. (2006) Interaction of Pin1 with Nek6 and characterization of their expression correlation in Chinese hepatocellular carcinoma patients. Biochem Biophys Res Commun 341: 1059-65 PubMed GONUTS page
↑ ^5.0 ^5.1 Pastorino L et al. (2006) The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production. Nature 440: 528-34 PubMed GONUTS page
↑ Ewing RM et al. (2007) Large-scale mapping of human protein-protein interactions by mass spectrometry. Mol Syst Biol 3: 89 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 Pan CQ et al. (2010) Active Mek2 as a regulatory scaffold that promotes Pin1 binding to BPGAP1 to suppress BPGAP1-induced acute Erk activation and cell migration. J Cell Sci 123: 903-16 PubMed GONUTS page
↑ Lu KP et al. (1996) A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380: 544-7 PubMed GONUTS page
↑ Lu PJ et al. (1999) The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature 399: 784-8 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Lu PJ et al. (1999) Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 283: 1325-8 PubMed GONUTS page

[PMID:20675384-0] 1.0 ^1.1 Nakatsu Y et al. (2010) Pin1 associates with and induces translocation of CRTC2 to the cytosol, thereby suppressing cAMP-responsive element transcriptional activity. J Biol Chem 285: 33018-27 PubMed GONUTS page

[PMID:19122240-1] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 Nakano A et al. (2009) Pin1 down-regulates transforming growth factor-beta (TGF-beta) signaling by inducing degradation of Smad proteins. J Biol Chem 284: 6109-15 PubMed GONUTS page

[PMID:11470801-2] Kamimoto T et al. (2001) Identification of a novel kinesin-related protein, KRMP1, as a target for mitotic peptidyl-prolyl isomerase Pin1. J Biol Chem 276: 37520-8 PubMed GONUTS page

[PMID:16476580-3] Chen J et al. (2006) Interaction of Pin1 with Nek6 and characterization of their expression correlation in Chinese hepatocellular carcinoma patients. Biochem Biophys Res Commun 341: 1059-65 PubMed GONUTS page

[PMID:16554819-4] 5.0 ^5.1 Pastorino L et al. (2006) The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production. Nature 440: 528-34 PubMed GONUTS page

[PMID:17353931-5] Ewing RM et al. (2007) Large-scale mapping of human protein-protein interactions by mass spectrometry. Mol Syst Biol 3: 89 PubMed GONUTS page

[PMID:20179103-6] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 Pan CQ et al. (2010) Active Mek2 as a regulatory scaffold that promotes Pin1 binding to BPGAP1 to suppress BPGAP1-induced acute Erk activation and cell migration. J Cell Sci 123: 903-16 PubMed GONUTS page

[PMID:8606777-7] Lu KP et al. (1996) A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380: 544-7 PubMed GONUTS page

[PMID:10391244-8] Lu PJ et al. (1999) The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein. Nature 399: 784-8 PubMed GONUTS page

[PMID:10037602-9] 10.0 ^10.1 ^10.2 Lu PJ et al. (1999) Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 283: 1325-8 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

HUMAN:PIN1

Contents

Annotations

Notes

References

c

e

g

h

i

i cont.

m

n

p

p cont.

r

s

v

Personal tools

Namespaces

Variants

Views

Actions

Search

Navigation

Cacao

Journal Clubs

page contributors

Toolbox