Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Abl interactor 1  

UniProtKB / Swiss-Prot ID :  ABI1_MOUSE

Gene Name (Synonyms) : 
Abi1, Ssh3bp1  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Cytoplasm (By similarity). Nucleus (By similarity). Cell projection, lamellipodium (By similarity). Cell projection, filopodium (By similarity). Cell projection, growth cone (By similarity). Cell junction, synapse, synaptosome (By similarity). Cytoplasm, 

Protein Function :  May act in negative regulation of cell growth and transformation by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2. In vitro, at least isoform 2 and isoform 4 suppress the transforming activity of Abelson murine leukemia virus (v-Abl) after overexpression in fibroblasts. May play a role in regulation EGF-induced Erk pathway activation. Involved in cytoskeletal reorganization and EGFR signaling. Together with EPS8 participates in transduction of signals from Ras to Rac. In vitro, a trimeric complex of ABI1, EPS8 and SOS1 exhibits Rac specific guanine nucleotide exchange factor (GEF) activity and ABI1 seems to act as an adapter in the complex. Regulates ABL1/c-Abl-mediated phosphorylation of ENAH (By similarity). Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. 

Protein Sequence MAELQMLLEEEIPSGKRALIESYQNLTRVADYCENNYIQATDKRKALEETKAYTTQSLASVAYQINALAN...
Predicted Secondary Structure CHHHHHHHHHHCCCHHHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant -
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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
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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
178PhosphothreonineTNPPTQKPP
CCCCCCCCC
50.94Phosphositeplus
Link-
183PhosphoserineQKPPSPPVS
CCCCCCCCC
50.81PhosphoELM
Link-
183PhosphoserineQKPPSPPVS
CCCCCCCCC
50.81Phosphositeplus
Link-
183PhosphoserineQKPPSPPVS
CCCCCCCCC
50.81SysPTM
Link-
183Phosphoserine.QKPPSPPVS
CCCCCCCCC
50.81UniProtKB
Link-
198PhosphotyrosineRNTPYKTLE
CCCCCCCCC
17.99Phosphositeplus
Link-
200PhosphothreonineTPYKTLEPV
CCCCCCCCC
30.43Phosphositeplus
Link-
213PhosphotyrosineVPNDYMTSP
CCCCCCCCC
14.66Phosphositeplus
Link-
213PhosphotyrosineVPNDYMTSP
CCCCCCCCC
14.66SysPTM
Link-
213Phosphotyrosine.VPNDYMTSP
CCCCCCCCC
14.66UniProtKB
Link-
215PhosphothreonineNDYMTSPAR
CCCCCCCCC
25.90Phosphositeplus
Link-
222PhosphoserineARLGSQHSP
CCCCCCCCC
29.34Phosphositeplus
Link-
222Phosphoserine.ARLGSQHSP
CCCCCCCCC
29.34UniProtKB
Link-
225PhosphoserineGSQHSPGRT
CCCCCCCCC
22.78Phosphositeplus
Link-
231PhosphoserineGRTASLNQR
CCCCCCCCC
27.52Phosphositeplus
Link-
231PhosphoserineGRTASLNQR
CCCCCCCCC
27.52SysPTM
Link-
240PhosphoserinePRTHSGSSG
CCCCCCCCC
39.49Phosphositeplus
Link-
243PhosphoserineHSGSSGGSG
CCCCCCCCC
51.18Phosphositeplus
Link-
296PhosphoserineSRHNSTTSS
CCCCCCCCC
27.26Phosphositeplus
Link-
428PhosphotyrosineVVAIYDYTK
EEEECCCCC
7.99Phosphositeplus
Link-
428PhosphotyrosineVVAIYDYTK
EEEECCCCC
7.99SysPTM
Link-
428Phosphotyrosine.VVAIYDYTK
EEEECCCCC
7.99UniProtKB
Link-
430PhosphotyrosineAIYDYTKDK
EECCCCCCC
9.94Phosphositeplus
Link-
430PhosphotyrosineAIYDYTKDK
EECCCCCCC
9.94SysPTM
Link-
431PhosphothreonineIYDYTKDKD
ECCCCCCCC
29.84Phosphositeplus
Link-
439PhosphoserineDDELSFKEG
CCCEEECCC
32.02Phosphositeplus
Link-
439PhosphoserineDDELSFKEG
CCCEEECCC
32.02SysPTM
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-428, AND MASSSPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASSSPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-222, ANDMASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-222, ANDMASS SPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND TYR-213, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures