| Tag | Content |
|---|
| CPLM ID | CPLM-000150 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Myc box-dependent-interacting protein 1 |
Protein Synonyms/Alias | Amphiphysin II; Amphiphysin-like protein; Bridging integrator 1; SH3 domain-containing protein 9 |
Gene Name | Bin1 |
Gene Synonyms/Alias | Amphl; Sh3p9 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 35 | KVLQKLGKADETKDE | ubiquitination | [1] | | 53 | QCVQNFNKQLTEGTR | ubiquitination | [1] | | 73 | RTYLASVKAMHEASK | ubiquitination | [1] | | 146 | RIAKRGRKLVDYDSA | ubiquitination | [1] | | 211 | QAEEELIKAQKVFEE | ubiquitination | [1] | | 258 | NFHKEMSKLNQNLND | ubiquitination | [1] | | 272 | DVLVSLEKQHGSNTF | ubiquitination | [1] | | 282 | GSNTFTVKAQPSDNA | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | May be involved in regulation of synaptic vesicle endocytosis. May act as a tumor suppressor and inhibits malignant cell transformation. |
Sequence Annotation | DOMAIN 29 276 BAR.
DOMAIN 515 588 SH3.
REGION 1 122 Interaction with BIN2 (By similarity).
REGION 379 422 Clathrin-binding (By similarity).
MOD_RES 296 296 Phosphoserine.
MOD_RES 298 298 Phosphoserine.
MOD_RES 304 304 Phosphoserine.
MOD_RES 308 308 Phosphothreonine.
MOD_RES 324 324 Phosphoserine.
MOD_RES 332 332 Phosphoserine. |
Keyword | Alternative splicing; Coiled coil; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Endocytosis; Nucleus; Phosphoprotein; Reference proteome; SH3 domain; Tumor suppressor. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 588 AA |
Protein Sequence | MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR 60
LQKDLRTYLA SVKAMHEASK KLSECLQEVY EPEWPGRDEA NKIAENNDLL WMDYHQKLVD 120
QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKPVSLLEK 180
AAPQWCQGKL QAHLVAQTNL LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN 240
TFQSIAGLEE NFHKEMSKLN QNLNDVLVSL EKQHGSNTFT VKAQPSDNAP EKGNKSPSPP 300
PDGSPAATPE IRVNHEPEPA SGASPGATIP KSPSQLRKGP PVPPPPKHTP SKEMKQEQIL 360
SLFDDAFVPE ISVTTPSQFE APGPFSEQAS LLDLDFEPLP PVASPVKAPT PSGQSIPWDL 420
WEPTESQAGI LPSGEPSSAE GSFAVAWPSQ TAEPGPAQPA EASEVVGGAQ EPGETAASEA 480
TSSSLPAVVV ETFSATVNGA VEGSAGTGRL DLPPGFMFKV QAQHDYTATD TDELQLKAGD 540
VVLVIPFQNP EEQDEGWLMG VKESDWNQHK ELEKCRGVFP ENFTERVQ 588 |
Gene Ontology | GO:0043679; C:axon terminus; IEA:Compara. GO:0044300; C:cerebellar mossy fiber; IEA:Compara. GO:0005634; C:nucleus; IDA:MGI. GO:0008021; C:synaptic vesicle; IEA:Compara. GO:0043196; C:varicosity; IEA:Compara. GO:0006897; P:endocytosis; IEA:UniProtKB-KW. GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW. GO:0042692; P:muscle cell differentiation; IMP:MGI. GO:0045807; P:positive regulation of endocytosis; IEA:Compara. GO:0043547; P:positive regulation of GTPase activity; IEA:Compara. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |