Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Myc box-dependent-interacting protein 1  

UniProtKB / Swiss-Prot ID :  BIN1_HUMAN

Gene Name (Synonyms) : 
BIN1, AMPHL  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Isoform BIN1: Nucleus. Isoform IIA: Cytoplasm. 

Protein Function :  May be involved in regulation of synaptic vesicle endocytosis. May act as a tumor suppressor and inhibits malignant cell transformation. 

Protein Sequence MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLA...
Predicted Secondary Structure CCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHCCCCCEECCCHHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
35K -> N (in CNM2; abolishes membranetubulation).
151D -> N (in CNM2; abolishes membranetubulation).
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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
56PhosphothreonineNKQLTEGTR
HHHHHHHHH
29.85HPRD
Link-
71PhosphoserineTYLASVKAM
HHHHHHHHH
22.89HPRD
Link-
296PhosphoserineKGNKSPSPP
CCCCCCCCC
34.31HPRD
Link-
296PhosphoserineKGNKSPSPP
CCCCCCCCC
34.31PhosphoELM
Link-
296PhosphoserineKGNKSPSPP
CCCCCCCCC
34.31Phosphositeplus
Link-
296PhosphoserineKGNKSPSPP
CCCCCCCCC
34.31SysPTM
Link-
296PhosphoserineKGNKSPSPP
CCCCCCCCC
34.31SysPTM
Link-
296PhosphoserineKGNKSPSPP
CCCCCCCCC
34.31SysPTM
Link-
296Phosphoserine.KGNKSPSPP
CCCCCCCCC
34.31UniProtKB
Link-
298PhosphoserineNKSPSPPDG
CCCCCCCCC
57.04HPRD
Link-
298PhosphoserineNKSPSPPDG
CCCCCCCCC
57.04PhosphoELM
Link-
298PhosphoserineNKSPSPPDG
CCCCCCCCC
57.04Phosphositeplus
Link-
298PhosphoserineNKSPSPPDG
CCCCCCCCC
57.04SysPTM
Link-
298PhosphoserineNKSPSPPDG
CCCCCCCCC
57.04SysPTM
Link-
298PhosphoserineNKSPSPPDG
CCCCCCCCC
57.04SysPTM
Link-
298Phosphoserine.NKSPSPPDG
CCCCCCCCC
57.04UniProtKB
Link-
303PhosphoserinePPDGSPAAT
CCCCCCCCC
20.81HPRD
Link-
303PhosphoserinePPDGSPAAT
CCCCCCCCC
20.81PhosphoELM
Link-
303PhosphoserinePPDGSPAAT
CCCCCCCCC
20.81Phosphositeplus
Link-
303PhosphoserinePPDGSPAAT
CCCCCCCCC
20.81SysPTM
Link-
303PhosphoserinePPDGSPAAT
CCCCCCCCC
20.81SysPTM
Link-
303PhosphoserinePPDGSPAAT
CCCCCCCCC
20.81SysPTM
Link-
303Phosphoserine.PPDGSPAAT
CCCCCCCCC
20.81UniProtKB
Link-
307PhosphothreonineSPAATPEIR
CCCCCCCCC
24.46HPRD
Link-
307PhosphothreonineSPAATPEIR
CCCCCCCCC
24.46HPRD
Link-
307PhosphothreonineSPAATPEIR
CCCCCCCCC
24.46HPRD
Link-
307PhosphothreonineSPAATPEIR
CCCCCCCCC
24.46PhosphoELM
Link-
307PhosphothreonineSPAATPEIR
CCCCCCCCC
24.46Phosphositeplus
Link-
307PhosphothreonineSPAATPEIR
CCCCCCCCC
24.46SysPTM
Link-
307PhosphothreonineSPAATPEIR
CCCCCCCCC
24.46SysPTM
Link-
307Phosphothreonine.SPAATPEIR
CCCCCCCCC
24.46UniProtKB
Link-
323PhosphothreonineAGGATPGAT
CCCCCCCCC
26.06HPRD
Link-
323PhosphothreonineAGGATPGAT
CCCCCCCCC
26.06HPRD
Link-
323PhosphothreonineAGGATPGAT
CCCCCCCCC
26.06PhosphoELM
Link-
323PhosphothreonineAGGATPGAT
CCCCCCCCC
26.06Phosphositeplus
Link-
323PhosphothreonineAGGATPGAT
CCCCCCCCC
26.06SysPTM
Link-
323Phosphothreonine.AGGATPGAT
CCCCCCCCC
26.06UniProtKB
Link-
327PhosphothreonineTPGATLPKS
CCCCCCCCC
49.89HPRD
Link-
327PhosphothreonineTPGATLPKS
CCCCCCCCC
49.89PhosphoELM
Link-
331PhosphoserineTLPKSPSQL
CCCCCCCCC
28.04HPRD
Link-
331PhosphoserineTLPKSPSQL
CCCCCCCCC
28.04PhosphoELM
Link-
331PhosphoserineTLPKSPSQL
CCCCCCCCC
28.04Phosphositeplus
Link-
331PhosphoserineTLPKSPSQL
CCCCCCCCC
28.04SysPTM
Link-
331Phosphoserine.TLPKSPSQL
CCCCCCCCC
28.04UniProtKB
Link-
333PhosphoserinePKSPSQLRK
CCCCCCCCC
49.27HPRD
Link-
333PhosphoserinePKSPSQLRK
CCCCCCCCC
49.27PhosphoELM
Link-
333PhosphoserinePKSPSQLRK
CCCCCCCCC
49.27Phosphositeplus
Link-
348PhosphothreoninePPKHTPSKE
CCCCCCCCC
35.07HPRD
Link-
488PhosphoserineEAASSSLPA
CCCCCCCCC
31.03PhosphoELM
Link-
489PhosphoserineAASSSLPAV
CCCCCCCCC
35.56PhosphoELM
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SNX4_HUMANphysical interactionMINT-58440MINT12668730
CUTL1_HUMANphysical interactionMINT-64663MINT16169070
RIN3_HUMANphysical interactionMINT-62883MINT12972505
RIN3_HUMANphysical interactionMINT-58365MINT12972505
ITA1_HUMANyeast 2-hybridHPRD:03150HPRD10094488
ABL1_HUMANin vitro
in vivo
HPRD:03150HPRD9356459
SYN1_HUMANin vitro
in vivo
HPRD:03150HPRD10899172
MYC_HUMANin vitro
in vivo
HPRD:03150HPRD11306501
AP2A1_HUMANin vitroHPRD:03150HPRD9280305
FAK1_HUMANin vitroHPRD:03150HPRD12558988
AMPH_HUMANin vitro
in vivo
HPRD:03150HPRD9348539
ITA6_HUMANyeast 2-hybridHPRD:03150HPRD10094488
BIN1_HUMANin vitroHPRD:03150HPRD10391921
DYN2_HUMANin vitroHPRD:03150HPRD15483625
DDEF2_HUMANin vitroHPRD:03150HPRD15483625
CUTL1_HUMANyeast 2-hybridHPRD:03150HPRD16169070
RIN3_HUMANENSP00000316779STRING
RIN2_HUMANENSP00000316779STRING
CLH1_HUMANENSP00000316779STRING
SYNJ1_HUMANENSP00000316779STRING
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Disease Reference
Kegg disease
OMIM disease
255200Myopathy, centronuclear, 2 (CNM2)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298 ANDSER-303, AND MASS SPECTROMETRY.
"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-296; SER-298; SER-303AND SER-331, AND MASS SPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, AND MASSSPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307, 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-296; SER-298; SER-303;THR-307; THR-323 AND SER-331, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298 ANDSER-303, 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