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_HUMAN

Gene Name (Synonyms) : 
ABI1, SSH3BP1  

Species :  Homo sapiens (Human). 

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. May play a role in regulation of 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-mediated phosphorylation of ENAH. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level (By similarity). 

Protein Sequence MAELQMLLEEEIPSGKRALIESYQNLTRVADYCENNYIQATDKRKALEETKAYTTQSLASVAYQINALAN...
Predicted Secondary Structure CHHHHHHHHHHCCCHHHHHHHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
331G -> A (in dbSNP:rs2306236). VAR_048159
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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
2N-acetylalanine.---MAELQM
---CHHHHH
26.63UniProtKB
Link-
23PhosphotyrosineLIESYQNLT
HHHHHHHHH
6.66Phosphositeplus
Link-
174PhosphothreonineTLSRTNPPT
CCCCCCCCC
49.02Phosphositeplus
Link-
178PhosphothreonineTNPPTQKPP
CCCCCCCCC
50.94HPRD
Link-
178PhosphothreonineTNPPTQKPP
CCCCCCCCC
50.94Phosphositeplus
Link-
178PhosphothreonineTNPPTQKPP
CCCCCCCCC
50.94SysPTM
Link-
183PhosphoserineQKPPSPPMS
CCCCCCCCC
50.60HPRD
Link-
183PhosphoserineQKPPSPPMS
CCCCCCCCC
50.60Phosphositeplus
Link-
183PhosphoserineQKPPSPPMS
CCCCCCCCC
50.60SysPTM
Link-
183Phosphoserine.QKPPSPPMS
CCCCCCCCC
50.60UniProtKB
Link-
187PhosphoserineSPPMSGRGT
CCCCCCCCC
30.98Phosphositeplus
Link-
187PhosphoserineSPPMSGRGT
CCCCCCCCC
30.98SysPTM
Link-
191PhosphothreonineSGRGTLGRN
CCCCCCCCC
25.36Phosphositeplus
Link-
198PhosphotyrosineRNTPYKTLE
CCCCCCCCC
17.99HPRD
Link-
198PhosphotyrosineRNTPYKTLE
CCCCCCCCC
17.99PhosphoELM
Link-
198PhosphotyrosineRNTPYKTLE
CCCCCCCCC
17.99Phosphositeplus
Link-
200PhosphothreonineTPYKTLEPV
CCCCCCCCC
30.43HPRD
Link-
200PhosphothreonineTPYKTLEPV
CCCCCCCCC
30.43Phosphositeplus
Link-
208PhosphothreonineVKPPTVPND
CCCCCCCCC
58.06HPRD
Link-
208PhosphothreonineVKPPTVPND
CCCCCCCCC
58.06Phosphositeplus
Link-
213PhosphotyrosineVPNDYMTSP
CCCCCCCCC
14.66HPRD
Link-
213PhosphotyrosineVPNDYMTSP
CCCCCCCCC
14.66PhosphoELM
Link-
213PhosphotyrosineVPNDYMTSP
CCCCCCCCC
14.66Phosphositeplus
Link-
213PhosphotyrosineVPNDYMTSP
CCCCCCCCC
14.66SysPTM
Link-
213Phosphotyrosine; by ABL1.VPNDYMTSP
CCCCCCCCC
14.66UniProtKB
Link-
215PhosphothreonineNDYMTSPAR
CCCCCCCCC
25.90HPRD
Link-
215PhosphothreonineNDYMTSPAR
CCCCCCCCC
25.90Phosphositeplus
Link-
215PhosphothreonineNDYMTSPAR
CCCCCCCCC
25.90SysPTM
Link-
216PhosphoserineDYMTSPARL
CCCCCCCCC
10.47HPRD
Link-
216PhosphoserineDYMTSPARL
CCCCCCCCC
10.47Phosphositeplus
Link-
216PhosphoserineDYMTSPARL
CCCCCCCCC
10.47SysPTM
Link-
216Phosphoserine.DYMTSPARL
CCCCCCCCC
10.47UniProtKB
Link-
222PhosphoserineARLGSQHSP
CCCCCCCCC
29.34HPRD
Link-
222PhosphoserineARLGSQHSP
CCCCCCCCC
29.34Phosphositeplus
Link-
225PhosphoserineGSQHSPGRT
CCCCCCCCC
22.78HPRD
Link-
225PhosphoserineGSQHSPGRT
CCCCCCCCC
22.78PhosphoELM
Link-
225PhosphoserineGSQHSPGRT
CCCCCCCCC
22.78Phosphositeplus
Link-
225PhosphoserineGSQHSPGRT
CCCCCCCCC
22.78SysPTM
Link-
225Phosphoserine.GSQHSPGRT
CCCCCCCCC
22.78UniProtKB
Link-
229PhosphothreonineSPGRTASLN
CCCCCCCCC
26.89Phosphositeplus
Link-
231PhosphoserineGRTASLNQR
CCCCCCCCC
27.52Phosphositeplus
Link-
265PhosphothreonineIAVPTPSPP
CCCCCCCCC
29.78Phosphositeplus
Link-
267PhosphoserineVPTPSPPTI
CCCCCCCCC
46.09Phosphositeplus
Link-
319PhosphoserineTRQISRHNS
CCCCCCCCC
21.10Phosphositeplus
Link-
323PhosphoserineSRHNSTTSS
CCCCCCCCC
27.26HPRD
Link-
323PhosphoserineSRHNSTTSS
CCCCCCCCC
27.26Phosphositeplus
Link-
324PhosphothreonineRHNSTTSST
CCCCCCCCC
35.69Phosphositeplus
Link-
326PhosphoserineNSTTSSTSS
CCCCCCCCC
31.54Phosphositeplus
Link-
333PhosphotyrosineSSGGYRRTP
CCCCCCCCC
10.63PhosphoELM
Link-
333PhosphotyrosineSSGGYRRTP
CCCCCCCCC
10.63Phosphositeplus
Link-
333Phosphotyrosine.SSGGYRRTP
CCCCCCCCC
10.63UniProtKB
Link-
336PhosphothreonineGYRRTPSVT
CCCCCCCCC
15.77Phosphositeplus
Link-
338PhosphoserineRRTPSVTAQ
CCCCCCCCC
31.33Phosphositeplus
Link-
361PhosphoserineQNSISIAPP
CCCCCCCCC
16.72Phosphositeplus
Link-
392PhosphoserineNIADSPTPP
CCCCCCCCC
22.96Phosphositeplus
Link-
394PhosphothreonineADSPTPPPP
CCCCCCCCC
52.99Phosphositeplus
Link-
410PhosphoserineMFDDSPPPP
CCCCCCCCC
40.94Phosphositeplus
Link-
421PhosphotyrosinePPVDYEDEE
CCCCCCCCC
26.05Phosphositeplus
Link-
431PhosphotyrosineAVVQYNDPY
CCCCCCCCC
15.21Phosphositeplus
Link-
506PhosphotyrosineSIMHYTD
ECCCCCC
8.67Phosphositeplus
Link-
507PhosphothreonineIMHYTD
CCCCCC
22.13HPRD
Link-
507PhosphothreonineIMHYTD
CCCCCC
22.13Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
HSP7C_HUMANphysical interactionMINT-45995MINT15048123
SOS1_HUMANphysical interactionMINT-16552MINT10499589
SOS1_HUMANphysical interactionMINT-16551MINT10499589
EPS8_HUMANphysical interactionMINT-15665MINT9010225
EPS8_HUMANphysical interactionMINT-15663MINT9010225
EPS8_HUMANphysical interactionMINT-15664MINT9010225
CYFP1_HUMANphysical interactionMINT-45994MINT15048123
CYFP2_HUMANphysical interactionMINT-45988MINT15048123
NCKP1_HUMANphysical interaction
physical interaction
EBI-389864
EBI-389854
intact11418237
11418237
NCK1_HUMANphysical interactionEBI-389899
intact11418237
NCF1_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
physical interaction
EBI-395177
EBI-395069
EBI-494
intact12681507
12681507
12681507
12681507
12681507
NEBU_HUMANin vitroHPRD:04336HPRD15048123
SOS1_HUMANin vitro
in vivo
HPRD:04336HPRD10499589
SPTA2_HUMANin vitro
yeast 2-hybrid
HPRD:04336HPRD9593709
SPTA1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:04336HPRD9593709
NCK1_HUMANyeast 2-hybridHPRD:04336HPRD11418237
EPS8_HUMANin vitro
in vivo
HPRD:04336HPRD11099046
9010225
1049958
12127568
10499589
15289329
SOS2_HUMANin vivoHPRD:04336HPRD11003655
ABI1_HUMANin vitroHPRD:04336HPRD12672821
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry.";
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-333, AND MASSSPECTROMETRY.
"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-225, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213, AND MASSSPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213, 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-183, AND MASSSPECTROMETRY.
"Allosteric inhibition of the nonMyristoylated c-Abl tyrosine kinaseby phosphopeptides derived from Abi1/Hssh3bp1.";
Xiong X., Cui P., Hossain S., Xu R., Warner B., Guo X., An X.,Debnath A.K., Cowburn D., Kotula L.;
Biochim. Biophys. Acta 1783:737-747(2008).
Cited for: FUNCTION, AND PHOSPHORYLATION AT TYR-213.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, 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-183 AND SER-216, ANDMASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-213, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures