CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022378
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Abl interactor 2 
Protein Synonyms/Alias
 Abelson interactor 2; Abi-2; Abl-binding protein 3; AblBP3; Arg-binding protein 1; ArgBP1 
Gene Name
 ABI2 
Gene Synonyms/Alias
 ARGBPIA 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
43NYIQSADKQRALEETubiquitination[1]
139RPVRYIRKPIDYTILubiquitination[1]
167KVSTQNMKMGGLPRTubiquitination[1, 2, 3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
Functional Description
 May act in regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. Part of the WAVE complex that regulates lamellipodia formation. The WAVE complex regulates actin filament reorganization via its interaction with the Arp2/3 complex. Regulates ABL1/c-Abl-mediated phosphorylation of MENA. 
Sequence Annotation
 DOMAIN 45 107 t-SNARE coiled-coil homology.
 DOMAIN 451 510 SH3.
 MOD_RES 227 227 Phosphoserine.
 MOD_RES 368 368 Phosphoserine.
 MOD_RES 462 462 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; SH3 domain. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 513 AA 
Protein Sequence
MAELQMLLEE EIPGGRRALF DSYTNLERVA DYCENNYIQS ADKQRALEET KAYTTQSLAS 60
VAYLINTLAN NVLQMLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR 120
THKIIAPANL ERPVRYIRKP IDYTILDDIG HGVKWLLRFK VSTQNMKMGG LPRTTPPTQK 180
PPSPPMSGKG TLGRHSPYRT LEPVRPPVVP NDYVPSPTRN MAPSQQSPVR TASVNQRNRT 240
YSSSGSSGGS HPSSRSSSRE NSGSGSVGVP IAVPTPSPPS VFPAPAGSAG TPPLPATSAS 300
APAPLVPATV PSSTAPNAAA GGAPNLADGF TSPTPPVVSS TPPTGHPVQF YSMNRPASRH 360
TPPTIGGSLP YRRPPSITSQ TSLQNQMNGG PFYSQNPVSD TPPPPPPVEE PVFDESPPPP 420
PPPEDYEEEE AAVVEYSDPY AEEDPPWAPR SYLEKVVAIY DYTKDKEDEL SFQEGAIIYV 480
IKKNDDGWYE GVMNGVTGLF PGNYVESIMH YSE 513 
Gene Ontology
 GO:0005913; C:cell-cell adherens junction; IEA:Compara.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; IDA:BHF-UCL.
 GO:0030425; C:dendrite; IEA:Compara.
 GO:0030175; C:filopodium; IDA:UniProtKB.
 GO:0030027; C:lamellipodium; IDA:UniProtKB.
 GO:0008093; F:cytoskeletal adaptor activity; TAS:UniProtKB.
 GO:0003677; F:DNA binding; TAS:ProtInc.
 GO:0019900; F:kinase binding; NAS:UniProtKB.
 GO:0017124; F:SH3 domain binding; TAS:UniProtKB.
 GO:0008154; P:actin polymerization or depolymerization; NAS:UniProtKB.
 GO:0043010; P:camera-type eye development; IEA:Compara.
 GO:0016477; P:cell migration; TAS:UniProtKB.
 GO:0016358; P:dendrite development; IEA:Compara.
 GO:0007611; P:learning or memory; IEA:Compara.
 GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI. 
Interpro
 IPR012849; Abl-interactor_HHR_dom.
 IPR001452; SH3_domain.
 IPR000727; T_SNARE_dom. 
Pfam
 PF07815; Abi_HHR
 PF00018; SH3_1 
SMART
 SM00326; SH3 
PROSITE
 PS50002; SH3
 PS50192; T_SNARE 
PRINTS
 PR00452; SH3DOMAIN.