Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Pinin  

UniProtKB / Swiss-Prot ID :  PININ_HUMAN

Gene Name (Synonyms) : 
PNN, DRS, MEMA  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus speckle. Cell junction, desmosome. Note=Cell-cell contact area, predominantly desmosome of intercellular adherens junction. Not a nucleocytoplasmic shuttling protein. 

Protein Function :  Transcriptional activator binding to the E-box 1 core sequence of the E-cadherin promoter gene; the core-binding sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated transcription repression. Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Participates in the regulation of alternative pre-mRNA splicing. Associates to spliced mRNA within 60 nt upstream of the 5'-splice sites. Involved in the establishment and maintenance of epithelia cell-cell adhesion. Potential tumor suppressor for renal cell carcinoma. 

Protein Sequence MAVAVRTLQEQLEKAKESLKNVDENIRKLTGRDPNDVRPIQARLLALSGPGGGRGRGSLLLRRGFSDSGG...
Predicted Secondary Structure CCHHHHHHHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCEEEEEEEEECCCCCCCCEEEEEEECCCCCCC...
Protein Variant
LocationDescription
441S -> T (in dbSNP:rs2180792). VAR_050540
671S -> G (in dbSNP:rs13021). VAR_023368
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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
Protein Variant
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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
2N-acetylalanine.---MAVAVR
---CCHHHH
9.66UniProtKB
Link-
30PhosphothreonineIRKLTGRDP
HHHHCCCCC
32.95HPRD
Link-
58PhosphoserineRGRGSLLLR
CCCEEEEEE
17.93Phosphositeplus
Link-
66PhosphoserineRRGFSDSGG
EECCCCCCC
33.42HPRD
Link-
66PhosphoserineRRGFSDSGG
EECCCCCCC
33.42PhosphoELM
Link-
66PhosphoserineRRGFSDSGG
EECCCCCCC
33.42Phosphositeplus
Link-
66PhosphoserineRRGFSDSGG
EECCCCCCC
33.42SysPTM
Link-
66Phosphoserine.RRGFSDSGG
EECCCCCCC
33.42UniProtKB
Link-
84PhosphoserineEGAVSRLGG
HHHHHHHCC
22.66HPRD
Link-
84PhosphoserineEGAVSRLGG
HHHHHHHCC
22.66Phosphositeplus
Link-
92PhosphothreonineGERRTRRES
CHHHHHHHH
40.06Phosphositeplus
Link-
96PhosphoserineTRRESRQES
HHHHHHHCC
37.14HPRD
Link-
96PhosphoserineTRRESRQES
HHHHHHHCC
37.14PhosphoELM
Link-
96PhosphoserineTRRESRQES
HHHHHHHCC
37.14Phosphositeplus
Link-
96Phosphoserine.TRRESRQES
HHHHHHHCC
37.14UniProtKB
Link-
100PhosphoserineSRQESDPED
HHHCCCCCH
50.56HPRD
Link-
100PhosphoserineSRQESDPED
HHHCCCCCH
50.56PhosphoELM
Link-
100PhosphoserineSRQESDPED
HHHCCCCCH
50.56Phosphositeplus
Link-
100PhosphoserineSRQESDPED
HHHCCCCCH
50.56SysPTM
Link-
100PhosphoserineSRQESDPED
HHHCCCCCH
50.56SysPTM
Link-
100Phosphoserine.SRQESDPED
HHHCCCCCH
50.56UniProtKB
Link-
114PhosphoserinePALQSSVVA
CHHHHHHHH
26.42HPRD
Link-
114PhosphoserinePALQSSVVA
CHHHHHHHH
26.42HPRD
Link-
114PhosphoserinePALQSSVVA
CHHHHHHHH
26.42PhosphoELM
Link-
114PhosphoserinePALQSSVVA
CHHHHHHHH
26.42Phosphositeplus
Link-
114PhosphoserinePALQSSVVA
CHHHHHHHH
26.42SysPTM
Link-
114Phosphoserine.PALQSSVVA
CHHHHHHHH
26.42UniProtKB
Link-
115PhosphoserineALQSSVVAT
HHHHHHHHC
13.98HPRD
Link-
115PhosphoserineALQSSVVAT
HHHHHHHHC
13.98Phosphositeplus
Link-
120PhosphoserineVVATSKERT
HHHCCHHHH
23.84HPRD
Link-
124PhosphothreonineSKERTRRDL
CHHHHHHHH
31.02HPRD
Link-
124PhosphothreonineSKERTRRDL
CHHHHHHHH
31.02Phosphositeplus
Link-
137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NMDEKGKQR
CCCCCCCCC
68.12Phosphositeplus
Link-
238N6-acetyllysineRTKTKPHLF
HHCCCCEEE
31.81HPRD
Link-
238N6-acetyllysineRTKTKPHLF
HHCCCCEEE
31.81Phosphositeplus
Link-
238N6-acetyllysine.RTKTKPHLF
HHCCCCEEE
31.81UniProtKB
Link-
304Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)NEEQKAEQE
CCCCCCCCC
58.11Phosphositeplus
Link-
347PhosphoserineAIVHSDAEK
CCCCCCCCC
27.85HPRD
Link-
347PhosphoserineAIVHSDAEK
CCCCCCCCC
27.85PhosphoELM
Link-
347PhosphoserineAIVHSDAEK
CCCCCCCCC
27.85Phosphositeplus
Link-
347PhosphoserineAIVHSDAEK
CCCCCCCCC
27.85SysPTM
Link-
347PhosphoserineAIVHSDAEK
CCCCCCCCC
27.85SysPTM
Link-
347Phosphoserine.AIVHSDAEK
CCCCCCCCC
27.85UniProtKB
Link-
375PhosphoserineEVRESEKQQ
CCCCCCCCC
39.26HPRD
Link-
375PhosphoserineEVRESEKQQ
CCCCCCCCC
39.26Phosphositeplus
Link-
381PhosphoserineKQQDSQPEE
CCCCCCCCC
43.21HPRD
Link-
381PhosphoserineKQQDSQPEE
CCCCCCCCC
43.21PhosphoELM
Link-
381PhosphoserineKQQDSQPEE
CCCCCCCCC
43.21Phosphositeplus
Link-
381PhosphoserineKQQDSQPEE
CCCCCCCCC
43.21SysPTM
Link-
381Phosphoserine.KQQDSQPEE
CCCCCCCCC
43.21UniProtKB
Link-
413PhosphoserineNRVESVEPS
CCCCCCCCC
28.99HPRD
Link-
413PhosphoserineNRVESVEPS
CCCCCCCCC
28.99PhosphoELM
Link-
413PhosphoserineNRVESVEPS
CCCCCCCCC
28.99Phosphositeplus
Link-
417PhosphoserineSVEPSENEA
CCCCCCCCC
39.28HPRD
Link-
417PhosphoserineSVEPSENEA
CCCCCCCCC
39.28Phosphositeplus
Link-
417PhosphoserineSVEPSENEA
CCCCCCCCC
39.28SysPTM
Link-
422PhosphoserineENEASKELE
CCCCCCCCC
22.08HPRD
Link-
422PhosphoserineENEASKELE
CCCCCCCCC
22.08Phosphositeplus
Link-
441PhosphoserineKECKSLSPG
CCCCCCCCC
45.82HPRD
Link-
441PhosphoserineKECKSLSPG
CCCCCCCCC
45.82Phosphositeplus
Link-
441PhosphoserineKECKSLSPG
CCCCCCCCC
45.82SysPTM
Link-
441Phosphoserine.KECKSLSPG
CCCCCCCCC
45.82UniProtKB
Link-
443PhosphoserineCKSLSPGKE
CCCCCCCCC
38.40HPRD
Link-
443PhosphoserineCKSLSPGKE
CCCCCCCCC
38.40PhosphoELM
Link-
443PhosphoserineCKSLSPGKE
CCCCCCCCC
38.40Phosphositeplus
Link-
443PhosphoserineCKSLSPGKE
CCCCCCCCC
38.40SysPTM
Link-
443PhosphoserineCKSLSPGKE
CCCCCCCCC
38.40SysPTM
Link-
443PhosphoserineCKSLSPGKE
CCCCCCCCC
38.40SysPTM
Link-
443Phosphoserine.CKSLSPGKE
CCCCCCCCC
38.40UniProtKB
Link-
450PhosphoserineKENVSALDM
CCCCCCCCC
34.39HPRD
Link-
450PhosphoserineKENVSALDM
CCCCCCCCC
34.39Phosphositeplus
Link-
450PhosphoserineKENVSALDM
CCCCCCCCC
34.39SysPTM
Link-
450Phosphoserine.KENVSALDM
CCCCCCCCC
34.39UniProtKB
Link-
458PhosphoserineMEKESEEKE
CCCCCCCCC
63.22HPRD
Link-
547PhosphothreonineEPVLTVHPE
CCCCCCCCC
19.59HPRD
Link-
552PhosphoserineVHPESKSKT
CCCCCCCCC
46.83HPRD
Link-
552PhosphoserineVHPESKSKT
CCCCCCCCC
46.83Phosphositeplus
Link-
552PhosphoserineVHPESKSKT
CCCCCCCCC
46.83SysPTM
Link-
552Phosphoserine.VHPESKSKT
CCCCCCCCC
46.83UniProtKB
Link-
649PhosphoserineKHRRSVDRK
HHHCCCCCC
28.46HPRD
Link-
649PhosphoserineKHRRSVDRK
HHHCCCCCC
28.46PhosphoELM
Link-
649PhosphoserineKHRRSVDRK
HHHCCCCCC
28.46Phosphositeplus
Link-
649PhosphoserineKHRRSVDRK
HHHCCCCCC
28.46SysPTM
Link-
649Phosphoserine.KHRRSVDRK
HHHCCCCCC
28.46UniProtKB
Link-
657PhosphothreonineKRRDTSGLE
CCCCCCCCC
23.92PhosphoELM
Link-
658PhosphoserineRRDTSGLER
CCCCCCCCC
45.74HPRD
Link-
658PhosphoserineRRDTSGLER
CCCCCCCCC
45.74PhosphoELM
Link-
658PhosphoserineRRDTSGLER
CCCCCCCCC
45.74Phosphositeplus
Link-
658PhosphoserineRRDTSGLER
CCCCCCCCC
45.74SysPTM
Link-
658Phosphoserine.RRDTSGLER
CCCCCCCCC
45.74UniProtKB
Link-
663PhosphoserineGLERSHKSS
CCCCCCCCC
26.37HPRD
Link-
663PhosphoserineGLERSHKSS
CCCCCCCCC
26.37PhosphoELM
Link-
663PhosphoserineGLERSHKSS
CCCCCCCCC
26.37Phosphositeplus
Link-
663Phosphoserine.GLERSHKSS
CCCCCCCCC
26.37UniProtKB
Link-
666PhosphoserineRSHKSSKGG
CCCCCCCCC
31.68HPRD
Link-
666PhosphoserineRSHKSSKGG
CCCCCCCCC
31.68PhosphoELM
Link-
666PhosphoserineRSHKSSKGG
CCCCCCCCC
31.68Phosphositeplus
Link-
666Phosphoserine.RSHKSSKGG
CCCCCCCCC
31.68UniProtKB
Link-
667PhosphoserineSHKSSKGGS
CCCCCCCCC
39.87HPRD
Link-
667PhosphoserineSHKSSKGGS
CCCCCCCCC
39.87PhosphoELM
Link-
667PhosphoserineSHKSSKGGS
CCCCCCCCC
39.87Phosphositeplus
Link-
667Phosphoserine.SHKSSKGGS
CCCCCCCCC
39.87UniProtKB
Link-
671PhosphoserineSKGGSSRDT
CCCCCCCCC
30.76HPRD
Link-
671PhosphoserineSKGGSSRDT
CCCCCCCCC
30.76PhosphoELM
Link-
671PhosphoserineSKGGSSRDT
CCCCCCCCC
30.76Phosphositeplus
Link-
671Phosphoserine.SKGGSSRDT
CCCCCCCCC
30.76UniProtKB
Link-
672PhosphoserineKGGSSRDTK
CCCCCCCCC
37.13HPRD
Link-
672PhosphoserineKGGSSRDTK
CCCCCCCCC
37.13PhosphoELM
Link-
672PhosphoserineKGGSSRDTK
CCCCCCCCC
37.13Phosphositeplus
Link-
672PhosphoserineKGGSSRDTK
CCCCCCCCC
37.13SysPTM
Link-
672Phosphoserine.KGGSSRDTK
CCCCCCCCC
37.13UniProtKB
Link-
690PhosphoserineDRKRSISES
CCCCCCCCH
33.24HPRD
Link-
690PhosphoserineDRKRSISES
CCCCCCCCH
33.24PhosphoELM
Link-
690PhosphoserineDRKRSISES
CCCCCCCCH
33.24Phosphositeplus
Link-
690PhosphoserineDRKRSISES
CCCCCCCCH
33.24SysPTM
Link-
690Phosphoserine.DRKRSISES
CCCCCCCCH
33.24UniProtKB
Link-
692PhosphoserineKRSISESSR
CCCCCCHHH
32.45HPRD
Link-
692PhosphoserineKRSISESSR
CCCCCCHHH
32.45HPRD
Link-
692PhosphoserineKRSISESSR
CCCCCCHHH
32.45PhosphoELM
Link-
692PhosphoserineKRSISESSR
CCCCCCHHH
32.45Phosphositeplus
Link-
692PhosphoserineKRSISESSR
CCCCCCHHH
32.45SysPTM
Link-
692PhosphoserineKRSISESSR
CCCCCCHHH
32.45SysPTM
Link-
692PhosphoserineKRSISESSR
CCCCCCHHH
32.45SysPTM
Link-
692Phosphoserine.KRSISESSR
CCCCCCHHH
32.45UniProtKB
Link-
695PhosphoserineISESSRSGK
CCCHHHHCC
26.81HPRD
Link-
695PhosphoserineISESSRSGK
CCCHHHHCC
26.81PhosphoELM
Link-
695PhosphoserineISESSRSGK
CCCHHHHCC
26.81Phosphositeplus
Link-
695PhosphoserineISESSRSGK
CCCHHHHCC
26.81SysPTM
Link-
695Phosphoserine.ISESSRSGK
CCCHHHHCC
26.81UniProtKB
Link-
697PhosphoserineESSRSGKRS
CHHHHCCCC
51.09HPRD
Link-
697PhosphoserineESSRSGKRS
CHHHHCCCC
51.09SysPTM
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SF3A2_HUMANphysical interactionMINT-5206259MINT17332742
TOE1_HUMANphysical interactionEBI-737651
intact16169070
VAMP8_HUMANphysical interactionEBI-737654
intact16169070
PDPK1_HUMANphysical interactionEBI-733277
intact16169070
K1C19_HUMANin vitro
yeast 2-hybrid
HPRD:04401HPRD10809736
K2C8_HUMANin vitro
yeast 2-hybrid
HPRD:04401HPRD10809736
K1C18_HUMANin vitro
yeast 2-hybrid
HPRD:04401HPRD10809736
CTBP1_HUMANin vitro
in vivo
HPRD:04401HPRD15542832
CTBP2_HUMANin vivoHPRD:04401HPRD15542832
PININ_HUMANyeast 2-hybridHPRD:04401HPRD16169070
TNF10_HUMANENSP00000216832STRING
CTBP1_HUMANENSP00000216832STRING
SRRM2_HUMANENSP00000216832STRING
CSKI1_HUMANENSP00000216832STRING
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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
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-66; SER-347; SER-381; SER-441; SER-443 ANDSER-450, AND MASS SPECTROMETRY.
"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-238, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100; SER-347;SER-381; SER-658 AND SER-692, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND SER-443, ANDMASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-100; SER-114;SER-443; SER-649; SER-663; SER-666; SER-667; SER-671; SER-672;SER-690; SER-692 AND SER-695, AND MASS SPECTROMETRY.
"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-381, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100; SER-347;SER-441 AND SER-443, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100; SER-381;SER-443; SER-450 AND SER-552, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-66; SER-347; SER-381; SER-441; SER-443 ANDSER-450, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-381; SER-443 ANDSER-450, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures