HUMAN:PIN1

Species (Taxon ID)	Homo sapiens (Human). (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	Q13526
EMBL	U49070 CR407654 BT019331 AK291074 CH471106 BC002899
CCDS	CCDS12220.1
PIR	S68520
RefSeq	NP_006212.1
UniGene	Hs.465849
PDB	1F8A 1I6C 1I8G 1I8H 1NMV 1NMW 1PIN 1ZCN 2F21 2ITK 2KBU 2KCF 2LB3 2M8I 2M8J 2M9E 2M9F 2M9I 2M9J 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 3WH0 4GWT 4GWV 4TYO
PDBsum	1F8A 1I6C 1I8G 1I8H 1NMV 1NMW 1PIN 1ZCN 2F21 2ITK 2KBU 2KCF 2LB3 2M8I 2M8J 2M9E 2M9F 2M9I 2M9J 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 3WH0 4GWT 4GWV 4TYO
ProteinModelPortal	Q13526
SMR	Q13526
BioGrid	111317
DIP	DIP-29306N
IntAct	Q13526
MINT	MINT-86298
STRING	9606.ENSP00000247970
BindingDB	Q13526
ChEMBL	CHEMBL2288
PhosphoSite	Q13526
DMDM	3024406
MaxQB	Q13526
PaxDb	Q13526
PeptideAtlas	Q13526
PRIDE	Q13526
DNASU	5300
Ensembl	ENST00000247970 ENST00000588695
GeneID	5300
KEGG	hsa:5300
UCSC	uc002mmk.2
CTD	5300
GeneCards	GC19P009945
HGNC	HGNC:8988
HPA	CAB004528 CAB009326
MIM	601052
neXtProt	NX_Q13526
PharmGKB	PA33320
eggNOG	COG0760
GeneTree	ENSGT00640000091578
HOGENOM	HOG000275331
HOVERGEN	HBG002101
InParanoid	Q13526
KO	K09578
OMA	FALKVGD
PhylomeDB	Q13526
TreeFam	TF101101
BRENDA	5.2.1.8
Reactome	REACT_115831 REACT_25271
SignaLink	Q13526
ChiTaRS	PIN1
EvolutionaryTrace	Q13526
GeneWiki	PIN1
GenomeRNAi	5300
NextBio	20486
PRO	PR:Q13526
Proteomes	UP000005640
Bgee	Q13526
CleanEx	HS_PIN1
ExpressionAtlas	Q13526
Genevestigator	Q13526
GO	GO:0005737 GO:0030496 GO:0016607 GO:0005654 GO:0005634 GO:0032794 GO:0031434 GO:0003755 GO:0050815 GO:0050816 GO:0007049 GO:0019221 GO:0045087 GO:2000146 GO:0070373 GO:0030512 GO:0032480 GO:0001934 GO:0032321 GO:0051443 GO:0000413 GO:0032465 GO:0007088 GO:0060393
InterPro	IPR000297 IPR023058 IPR001202
Pfam	PF00639 PF00397
SMART	SM00456
SUPFAM	SSF51045
PROSITE	PS01096 PS50198 PS01159 PS50020

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0005515	protein binding	PMID:20675384^[1]	ECO:0000021		UniProtKB:Q53ET0	F		FIGURE 1. Pin1 associates with CRTC2.	complete
	GO:0033159	negative regulation of protein import into nucleus, translocation	PMID:20675384^[1]	ECO:0000315			P		Figure 3 and Supplemental figure 4: Pin1 inhibits CRTC2 translocation into the nucleus.	complete
part_of	GO:0005634	nucleus	PMID:16697218^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16697218^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	part_of:(CL:0000540)	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:16697218^[2]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0051219	phosphoprotein binding	PMID:23362255^[3]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9QUR7	F	occurs_in:(UBERON:0000955) activated_by:(CHEBI:15422) happens_during:(GO:0006468) has_input:(UniProtKB:P10636)	Seeded From UniProt	complete
NOT\|involved_in	GO:0046785	microtubule polymerization	PMID:26996940^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0048156	tau protein binding	PMID:28386764^[5]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0032092	positive regulation of protein binding	PMID:24964035^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q15796) has_regulation_target:(UniProtKB:P10636)	Seeded From UniProt	complete
involved_in	GO:0001932	regulation of protein phosphorylation	PMID:24964035^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:Q15796)	Seeded From UniProt	complete
involved_in	GO:0010468	regulation of gene expression	PMID:24964035^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	regulates_expression_of:(ENSEMBL:ENSG00000175387)	Seeded From UniProt	complete
	GO:0045967	negative regulation of growth rate	PMID:24179535^[7]	ECO:0000314			P		Figure 3(A) shows the effect of PIN1 on the growth rate of siRNA-transfected RBE cells.	complete CACAO 9024
enables	GO:0008013	beta-catenin binding	PMID:11533658^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35222	F		Seeded From UniProt	complete
	GO:0006457	protein folding	PMID:24534472^[9]	ECO:0000314			P		Pin1 belongs to a family of enzymes called prolyl isomerases that catalyze the flip in orientation around the proline bond (Figure 1)	complete CACAO 9549
involved_in	GO:0042177	negative regulation of protein catabolic process	PMID:11533658^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P35222)	Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	PMID:11533658^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	stabilizes:(UniProtKB:P35222)	Seeded From UniProt	complete
enables	GO:0050815	phosphoserine residue binding	PMID:11533658^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P35222)	Seeded From UniProt	complete
involved_in	GO:0090263	positive regulation of canonical Wnt signaling pathway	PMID:11533658^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:11533658^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	regulates_transcription_of:(ENSEMBL:ENSG00000110092)\|regulates_transcription_of:(ENSEMBL:ENSG00000136997)\|regulates_transcription_of:(ENSEMBL:ENSG00000112033)\|regulates_transcription_of:(ENSEMBL:ENSG00000115414)	Seeded From UniProt	complete
involved_in	GO:0032091	negative regulation of protein binding	PMID:11533658^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P25054) has_regulation_target:(UniProtKB:P35222)	Seeded From UniProt	complete
involved_in	GO:1900180	regulation of protein localization to nucleus	PMID:11533658^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P35222)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9QUR7	C		Seeded From UniProt	complete
enables	GO:0008013	beta-catenin binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9QUR7	F	part_of:(GO:0030182)	Seeded From UniProt	complete
enables	GO:0003774	motor activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9QUR7	F		Seeded From UniProt	complete
involved_in	GO:0050821	protein stabilization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9QUR7	P	stabilizes:(UniProtKB:P35222) part_of:(GO:0030182)	Seeded From UniProt	complete
involved_in	GO:0050808	synapse organization	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9QUR7	P		Seeded From UniProt	complete
involved_in	GO:0030182	neuron differentiation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q9QUR7	P	occurs_in:(UBERON:0000956) happens_during:(GO:0009790)	Seeded From UniProt	complete
involved_in	GO:2000146	negative regulation of cell motility	PMID:20179103^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070373	negative regulation of ERK1 and ERK2 cascade	PMID:20179103^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0060393	regulation of pathway-restricted SMAD protein phosphorylation	PMID:19122240^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051443	positive regulation of ubiquitin-protein transferase activity	PMID:19122240^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0050816	phosphothreonine residue binding	PMID:10037602^[12]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P30307	F		Seeded From UniProt	complete
enables	GO:0050816	phosphothreonine residue binding	PMID:10037602^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0050815	phosphoserine residue binding	PMID:10037602^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0032794	GTPase activating protein binding	PMID:20179103^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P85298	F		Seeded From UniProt	complete
involved_in	GO:0043547	positive regulation of GTPase activity	PMID:20179103^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031434	mitogen-activated protein kinase kinase binding	PMID:20179103^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q63932	F		Seeded From UniProt	complete
involved_in	GO:0030512	negative regulation of transforming growth factor beta receptor signaling pathway	PMID:19122240^[11]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:20179103^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:19122240^[11]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0099524	postsynaptic cytosol	PMID:28458925^[13]	ECO:0006042	cell fractionation evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0000956)	Seeded From UniProt	complete
part_of	GO:0099524	postsynaptic cytosol	PMID:28458925^[13]	ECO:0005589	confocal microscopy evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0000956)	Seeded From UniProt	complete
part_of	GO:0099524	postsynaptic cytosol	PMID:28458925^[13]	ECO:0000279	western blot evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0000956)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:28458925^[13]	ECO:0006042	cell fractionation evidence used in manual assertion		C	part_of:(UBERON:0000061) part_of:(UBERON:0000956)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:28458925^[13]	ECO:0005589	confocal microscopy evidence used in manual assertion		C	part_of:(UBERON:0000061) part_of:(UBERON:0000956)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:28458925^[13]	ECO:0000279	western blot evidence used in manual assertion		C	part_of:(UBERON:0000061) part_of:(UBERON:0000956)	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1346036 PANTHER:PTN002579701 RGD:1310299 TAIR:locus:2060922	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0015379 MGI:MGI:1346036 PANTHER:PTN000069608 PomBase:SPCC16C4.03 RGD:1310299 UniProtKB:Q13526 dictyBase:DDB_G0268618	C		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1346036 MGI:MGI:3649546 PANTHER:PTN002579701 SGD:S000003778 TAIR:locus:2060922 UniProtKB:Q13526 dictyBase:DDB_G0268618	F		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:20956805^[15]	ECO:0000269	experimental evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0032465	regulation of cytokinesis	PMID:19638580^[16]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q53EZ4	P		Seeded From UniProt	complete
involved_in	GO:0032465	regulation of cytokinesis	PMID:19638580^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030496	midbody	PMID:19638580^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	PMID:19638580^[16]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P53350	P		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0061051	positive regulation of cell growth involved in cardiac muscle cell development	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B0BNL2 ensembl:ENSRNOP00000027819	P		Seeded From UniProt	complete
involved_in	GO:0043525	positive regulation of neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B0BNL2 ensembl:ENSRNOP00000027819	P		Seeded From UniProt	complete
involved_in	GO:0043524	negative regulation of neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B0BNL2 ensembl:ENSRNOP00000027819	P		Seeded From UniProt	complete
part_of	GO:0043005	neuron projection	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B0BNL2 ensembl:ENSRNOP00000027819	C		Seeded From UniProt	complete
involved_in	GO:0035307	positive regulation of protein dephosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B0BNL2 ensembl:ENSRNOP00000027819	P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B0BNL2 ensembl:ENSRNOP00000027819	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B0BNL2 ensembl:ENSRNOP00000027819	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B0BNL2 ensembl:ENSRNOP00000027819	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B0BNL2 ensembl:ENSRNOP00000027819	C		Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:B0BNL2 ensembl:ENSRNOP00000027819	P		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000297	F		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:5.2.1.8	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:16697218^[2] PMID:8606777^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0035307	positive regulation of protein dephosphorylation	PMID:23362255^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_regulation_target:(UniProtKB:P10636)	Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	PMID:24964035^[6] PMID:11533658^[8]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	causally_upstream_of:(GO:0006355)\|causally_upstream_of:(GO:0051726)\|causally_upstream_of:(GO:0023051)\|causally_upstream_of:(GO:0042176)\|causally_upstream_of:(GO:0042325)	Seeded From UniProt	complete
involved_in	GO:0000413	protein peptidyl-prolyl isomerization	PMID:11533658^[8]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007088	regulation of mitotic nuclear division	PMID:10391244^[18]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1901796	regulation of signal transduction by p53 class mediator	Reactome:R-HSA-5633007	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032480	negative regulation of type I interferon production	Reactome:R-HSA-936440	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-9626817 Reactome:R-HSA-9626816	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-936462 Reactome:R-HSA-936380 Reactome:R-HSA-8877692 Reactome:R-HSA-6799409 Reactome:R-HSA-3215251	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
enables	GO:0016853	isomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0413	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0003755	peptidyl-prolyl cis-trans isomerase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0697	F		Seeded From UniProt	complete
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P		Seeded From UniProt	complete
part_of	GO:0016607	nuclear speck	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0186	C		Seeded From UniProt	complete
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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 Hamdane, M et al. () Pin1 allows for differential Tau dephosphorylation in neuronal cells. Mol. Cell. Neurosci. 32 155-60 PubMed GONUTS page
↑ ^3.0 ^3.1 Kimura, T et al. (2013) Isomerase Pin1 stimulates dephosphorylation of tau protein at cyclin-dependent kinase (Cdk5)-dependent Alzheimer phosphorylation sites. J. Biol. Chem. 288 7968-77 PubMed GONUTS page
↑ Kutter, S et al. (2016) Regulation of Microtubule Assembly by Tau and not by Pin1. J. Mol. Biol. 428 1742-59 PubMed GONUTS page
↑ Guo, T et al. (2017) Roles of tau protein in health and disease. Acta Neuropathol. 133 665-704 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Ueberham, U et al. (2014) Pin1 promotes degradation of Smad proteins and their interaction with phosphorylated tau in Alzheimer's disease. Neuropathol. Appl. Neurobiol. 40 815-32 PubMed GONUTS page
↑ Jamiyandorj, U et al. (2013) Expression of peptidyl-prolyl isomerase PIN1 and its role in the pathogenesis of extrahepatic cholangiocarcinoma. Oncol Lett 6 1421-1426 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 ^8.6 ^8.7 ^8.8 ^8.9 Ryo, A et al. (2001) Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC. Nat. Cell Biol. 3 793-801 PubMed GONUTS page
↑ Driver, JA et al. (2014) Regulation of protein conformation by Pin1 offers novel disease mechanisms and therapeutic approaches in Alzheimer's disease. Discov Med 17 93-9 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 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
↑ ^11.0 ^11.1 ^11.2 ^11.3 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
↑ ^12.0 ^12.1 ^12.2 Lu, PJ et al. (1999) Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 283 1325-8 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 Xu, L et al. (2017) Pathological Role of Peptidyl-Prolyl Isomerase Pin1 in the Disruption of Synaptic Plasticity in Alzheimer's Disease. Neural Plast. 2017 3270725 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Boussetta, T et al. (2010) The prolyl isomerase Pin1 acts as a novel molecular switch for TNF-alpha-induced priming of the NADPH oxidase in human neutrophils. Blood 116 5795-802 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 van der Horst, A & Khanna, KK (2009) The peptidyl-prolyl isomerase Pin1 regulates cytokinesis through Cep55. Cancer Res. 69 6651-9 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

[PMID:20675384-1] 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:16697218-2] 2.0 ^2.1 ^2.2 ^2.3 Hamdane, M et al. () Pin1 allows for differential Tau dephosphorylation in neuronal cells. Mol. Cell. Neurosci. 32 155-60 PubMed GONUTS page

[PMID:23362255-3] 3.0 ^3.1 Kimura, T et al. (2013) Isomerase Pin1 stimulates dephosphorylation of tau protein at cyclin-dependent kinase (Cdk5)-dependent Alzheimer phosphorylation sites. J. Biol. Chem. 288 7968-77 PubMed GONUTS page

[PMID:26996940-4] Kutter, S et al. (2016) Regulation of Microtubule Assembly by Tau and not by Pin1. J. Mol. Biol. 428 1742-59 PubMed GONUTS page

[PMID:28386764-5] Guo, T et al. (2017) Roles of tau protein in health and disease. Acta Neuropathol. 133 665-704 PubMed GONUTS page

[PMID:24964035-6] 6.0 ^6.1 ^6.2 ^6.3 Ueberham, U et al. (2014) Pin1 promotes degradation of Smad proteins and their interaction with phosphorylated tau in Alzheimer's disease. Neuropathol. Appl. Neurobiol. 40 815-32 PubMed GONUTS page

[PMID:24179535-7] Jamiyandorj, U et al. (2013) Expression of peptidyl-prolyl isomerase PIN1 and its role in the pathogenesis of extrahepatic cholangiocarcinoma. Oncol Lett 6 1421-1426 PubMed GONUTS page

[PMID:11533658-8] 8.0 ^8.1 ^8.2 ^8.3 ^8.4 ^8.5 ^8.6 ^8.7 ^8.8 ^8.9 Ryo, A et al. (2001) Pin1 regulates turnover and subcellular localization of beta-catenin by inhibiting its interaction with APC. Nat. Cell Biol. 3 793-801 PubMed GONUTS page

[PMID:24534472-9] Driver, JA et al. (2014) Regulation of protein conformation by Pin1 offers novel disease mechanisms and therapeutic approaches in Alzheimer's disease. Discov Med 17 93-9 PubMed GONUTS page

[PMID:20179103-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 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:19122240-11] 11.0 ^11.1 ^11.2 ^11.3 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:10037602-12] 12.0 ^12.1 ^12.2 Lu, PJ et al. (1999) Function of WW domains as phosphoserine- or phosphothreonine-binding modules. Science 283 1325-8 PubMed GONUTS page

[PMID:28458925-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 ^13.5 Xu, L et al. (2017) Pathological Role of Peptidyl-Prolyl Isomerase Pin1 in the Disruption of Synaptic Plasticity in Alzheimer's Disease. Neural Plast. 2017 3270725 PubMed GONUTS page

[PMID:21873635-14] 14.0 ^14.1 ^14.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:20956805-15] Boussetta, T et al. (2010) The prolyl isomerase Pin1 acts as a novel molecular switch for TNF-alpha-induced priming of the NADPH oxidase in human neutrophils. Blood 116 5795-802 PubMed GONUTS page

[PMID:19638580-16] 16.0 ^16.1 ^16.2 ^16.3 van der Horst, A & Khanna, KK (2009) The peptidyl-prolyl isomerase Pin1 regulates cytokinesis through Cep55. Cancer Res. 69 6651-9 PubMed GONUTS page

[PMID:8606777-17] Lu, KP et al. (1996) A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380 544-7 PubMed GONUTS page

[PMID:10391244-18] 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

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