CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024712
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Bridging integrator 2 
Protein Synonyms/Alias
  
Gene Name
 Bin2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
27KFSRAQEKVLQKLGKacetylation[1]
145RIAKRGRKLVDYDSAacetylation[2]
145RIAKRGRKLVDYDSAubiquitination[3]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] 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
 Promotes cell motility and migration, probably via its interaction with the cell membrane and with podosome proteins that mediate interaction with the cytoskeleton. Modulates membrane curvature and mediates membrane tubulation. Inhibits phagocytosis (By similarity). Plays a role in podosome formation. 
Sequence Annotation
 DOMAIN 28 244 BAR.
 MOD_RES 273 273 Phosphoserine (By similarity).
 MOD_RES 357 357 Phosphoserine (By similarity).
 MOD_RES 424 424 Phosphoserine (By similarity).
 MOD_RES 439 439 Phosphoserine (By similarity).  
Keyword
 Cell junction; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Membrane; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 489 AA 
Protein Sequence
MAEGKAGGAA GLFAKQMQKK FSRAQEKVLQ KLGKTVETKD ERFEQSASNF YQQQAEGHKL 60
YKDLKNFLSA VKVMHESSKR VSETLQEVYS SDWDGHEDLK AIVGNNDLLW EDYEEKLADQ 120
ALRTMENYVS QFSEIKERIA KRGRKLVDYD SARHHLEAVQ NAKKKDDAKM AKAEEDFSKA 180
QIVFEDLNQE LLEELPILYN SRIGCYVTVF QNISNLRDVF YREMSKLNHN LYEVMSKLEK 240
QHSNKVFVVK GLSSSSRRSL VISPPVQSCA ASSPVSPVSP VSPVTSPTSP SATSEPESVS 300
ATGEELTSEA GGEDSCESQE SLKDEEADEA QSETSSSLPA CNGPTPAPAS PAAEVGSQEE 360
ALSSSAQSPG RGQTGKDTPS PGDVVLRARA SSEGAEQSKR AASIQRTSAP PSRPPPPRAS 420
GSGSCNAPGS PEGSSQLCSP RASPDASSNP EPAETREKEG AGSSGPEEPR AVSTKSATQA 480
SGGLVGLFL 489 
Gene Ontology
 GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0042995; C:cell projection; IEA:UniProtKB-KW.
 GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
 GO:0002102; C:podosome; ISS:UniProtKB.
 GO:0005543; F:phospholipid binding; ISS:UniProtKB.
 GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
 GO:0097320; P:membrane tubulation; ISS:UniProtKB.
 GO:0071800; P:podosome assembly; ISS:UniProtKB. 
Interpro
 IPR027267; AH/BAR-dom.
 IPR003005; Amphiphysin.
 IPR004148; BAR_dom. 
Pfam
 PF03114; BAR 
SMART
 SM00721; BAR 
PROSITE
 PS51021; BAR 
PRINTS
 PR01251; AMPHIPHYSIN.