Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1  

UniProtKB / Swiss-Prot ID :  PIN1_HUMAN

Gene Name (Synonyms) : 
PIN1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Nucleus speckle. Cytoplasm. Note=Co-localizes with NEK6 in the nucleus. Mainly localized in the nucleus but phosphorylation at Ser-71 by DAPK1 results in inhibition of its nuclear localization. 

Protein Function :  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. 

Protein Sequence MADEEKLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSGGKNGQGEPARVRCSHLLVKHSQSRRP...
Predicted Secondary Structure CCCCCCCCCCCEEEEECCCCEEEEEECCCCEEEECCCCCCCCCCCCCCCCCCCCCCCCCCHHHCCHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
16PhosphoserineEKRMSRSSG
EEEEECCCC
32.80Phosphositeplus
Link
16Phosphoserine (PKA_group)EKRMSRSSG
EEEEECCCC
32.80PhosphoELM
Link
23PhosphotyrosineSGRVYYFNH
CCEEEEEEC
10.86Phosphositeplus
Link
38PhosphoserineWERPSGNSS
ECCCCCCCC
57.75Phosphositeplus
Link-
43PhosphoserineGNSSSGGKN
CCCCCCCCC
51.92HPRD
Link-
46N6-acetyllysineSSGGKNGQG
CCCCCCCCC
62.52HPRD
Link-
46N6-acetyllysineSSGGKNGQG
CCCCCCCCC
62.52Phosphositeplus
Link-
46N6-acetyllysine.SSGGKNGQG
CCCCCCCCC
62.52UniProtKB
Link-
65PhosphoserineLVKHSQSRR
HHHCCHHHH
24.92Phosphositeplus
Link
65Phosphoserine (PLK1)LVKHSQSRR
HHHCCHHHH
24.92PhosphoELM
Link
71PhosphoserineSRRPSSWRQ
HHHHHCCCC
40.50Phosphositeplus
Link
71Phosphoserine; by DAPK1.SRRPSSWRQ
HHHHHCCCC
40.50UniProtKB
Link
82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ITRTKEEAL
HCCCHHHHH
50.71Phosphositeplus
Link
108PhosphoserineESLASQFSD
HHHHHHHCC
36.73HPRD
Link
108PhosphoserineESLASQFSD
HHHHHHHCC
36.73PhosphoELM
Link
108PhosphoserineESLASQFSD
HHHHHHHCC
36.73Phosphositeplus
Link
108Phosphoserine.ESLASQFSD
HHHHHHHCC
36.73UniProtKB
Link
114PhosphoserineFSDCSSAKA
HCCCCCCCC
38.02HPRD
Link
132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GQMQKPFED
HCCCHHHHH
46.46Phosphositeplus
Link
138PhosphoserineFEDASFALR
HHHHHHHCC
24.31Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
P53_HUMANphysical interactionMINT-19915MINT12397361
P53_HUMANphysical interactionMINT-19916MINT12397361
HNRPC_HUMANphysical interactionMINT-67692MINT16189514
TOP2A_HUMANphysical interactionMINT-15316MINT11940573
CDC27_HUMANphysical interactionMINT-17047MINT10037602
MPIP3_HUMANphysical interactionMINT-15813MINT10037602
LEPR_HUMANphysical interactionMINT-63769MINT16169070
CSK21_HUMANphysical interactionMINT-15593MINT11940573
CSK21_HUMANphysical interactionMINT-15822MINT11940573
CSK21_HUMANphysical interactionMINT-15821MINT11940573
Q15559_HUMANphysical interactionMINT-68110MINT16189514
Q5T5T6_HUMANphysical interactionMINT-66184MINT16189514
CHSS2_HUMANphysical interactionMINT-64894MINT16169070
ZMIZ2_HUMANphysical interactionMINT-66724MINT16189514
MDFI_HUMANphysical interactionMINT-67038MINT16189514
GGA2_HUMANphysical interactionMINT-66490MINT16189514
T22D4_HUMANphysical interactionMINT-66285MINT16189514
ZMIZ2_HUMANphysical interactionEBI-754708
intact16189514
TRAF2_HUMANphysical interactionEBI-752986
intact16189514
RAI1_HUMANphysical interactionEBI-753652
intact16189514
GGA2_HUMANphysical interactionEBI-753949
intact16189514
T22D4_HUMANphysical interactionEBI-753286
intact16189514
RBPMS_HUMANphysical interactionEBI-758248
intact16189514
Q8NHQ3_HUMANphysical interactionEBI-758605
intact16189514
UBQL4_HUMANphysical interactionEBI-955078
intact16713569
CSK21_HUMANin vitro
in vivo
HPRD:03031HPRD11940573
CSK2B_HUMANin vitro
in vivo
HPRD:03031HPRD11940573
CSK22_HUMANin vitroHPRD:03031HPRD11940573
CTNB1_HUMANin vitro
in vivo
HPRD:03031HPRD11533658
CDC2_HUMANin vivoHPRD:03031HPRD11774038
CDC27_HUMANin vitroHPRD:03031HPRD9499405
10939594
10037602
TRAF2_HUMANyeast 2-hybridHPRD:03031HPRD16189514
RBBP8_HUMANyeast 2-hybridHPRD:03031HPRD16189514
SOCS3_HUMANyeast 2-hybridHPRD:03031HPRD16169070
MDFI_HUMANyeast 2-hybridHPRD:03031HPRD16189514
RAI1_HUMANyeast 2-hybridHPRD:03031HPRD16189514
GGA2_HUMANyeast 2-hybridHPRD:03031HPRD16189514
RBPMS_HUMANyeast 2-hybridHPRD:03031HPRD16189514
ZMIZ2_HUMANyeast 2-hybridHPRD:03031HPRD16189514
T22D4_HUMANyeast 2-hybridHPRD:03031HPRD16189514
CCNB1_HUMANin vitroHPRD:03031HPRD9499405
TOP2A_HUMANin vitroHPRD:03031HPRD11940573
BCL2_HUMANin vivoHPRD:03031HPRD11988841
JUN_HUMANin vitro
in vivo
HPRD:03031HPRD11432833
PTN1_HUMANin vitroHPRD:03031HPRD9499405
TAU_HUMANin vitro
in vivo
HPRD:03031HPRD10391244
MPIP3_HUMANin vitro
in vivo
HPRD:03031HPRD9499405
10037602
9482729
P53_HUMANin vitro
in vivo
HPRD:03031HPRD12397362
12388558
RAB4A_HUMANin vitroHPRD:03031HPRD10888662
NFAC2_HUMANin vitro
in vivo
HPRD:03031HPRD11356192
RAF1_HUMANin vitro
in vivo
HPRD:03031HPRD15664191
UBQL4_HUMANyeast 2-hybridHPRD:03031HPRD16713569
DDX24_HUMANyeast 2-hybridHPRD:03031HPRD16169070
MTFR1_HUMANyeast 2-hybridHPRD:03031HPRD16169070
KLH20_HUMANyeast 2-hybridHPRD:03031HPRD16169070
ZCH10_HUMANyeast 2-hybridHPRD:03031HPRD16169070
GPAA1_HUMANyeast 2-hybridHPRD:03031HPRD16169070
CDC27_HUMANENSP00000247970STRING
CDC27_HUMANENSP00000247970STRING
PP2AB_HUMANENSP00000247970STRING
PP2AB_HUMANENSP00000247970STRING
CCND1_HUMANENSP00000247970STRING
CCND1_HUMANENSP00000247970STRING
RAF1_HUMANENSP00000247970STRING
RAF1_HUMANENSP00000247970STRING
PMYT1_HUMANENSP00000247970STRING
PMYT1_HUMANENSP00000247970STRING
TAU_HUMANENSP00000247970STRING
TAU_HUMANENSP00000247970STRING
P53_HUMANENSP00000247970STRING
P53_HUMANENSP00000247970STRING
PLK1_HUMANENSP00000247970STRING
PLK1_HUMANENSP00000247970STRING
CDC2_HUMANENSP00000247970STRING
CDC2_HUMANENSP00000247970STRING
RPB1_HUMANENSP00000247970STRING
RPB1_HUMANENSP00000247970STRING
MPIP3_HUMANENSP00000247970STRING
MPIP3_HUMANENSP00000247970STRING
2AAA_HUMANENSP00000247970STRING
2AAA_HUMANENSP00000247970STRING
2ABA_HUMANENSP00000247970STRING
2ABA_HUMANENSP00000247970STRING
CTNB1_HUMANENSP00000247970STRING
CTNB1_HUMANENSP00000247970STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-46, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASSSPECTROMETRY.
"Death-associated protein kinase 1 phosphorylates Pin1 and inhibitsits prolyl isomerase activity and cellular function.";
Lee T.H., Chen C.H., Suizu F., Huang P., Schiene-Fischer C., Daum S.,Zhang Y.J., Goate A., Chen R.H., Zhou X.Z., Lu K.P.;
Mol. Cell 42:147-159(2011).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-71, INTERACTION WITH DAPK1,SUBCELLULAR LOCATION, MUTAGENESIS OF SER-71, AND TISSUE SPECIFICITY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures