ABI1_MOUSE - dbPTM
ABI1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABI1_MOUSE
UniProt AC Q8CBW3
Protein Name Abl interactor 1
Gene Name Abi1 {ECO:0000312|MGI:MGI:104913}
Organism Mus musculus (Mouse).
Sequence Length 481
Subcellular Localization Cytoplasm. Nucleus. Cell projection, lamellipodium. Cell projection, filopodium. Cell projection, growth cone. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cytoplasm, cytoskeleton. Localized to protruding lamellipodia and
Protein Description 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. Recruits WASF1 to lamellipodia and there seems to regulate WASF1 protein level. In brain, seems to regulate the dendritic outgrowth and branching as well as to determine the shape and number of synaptic contacts of developing neurons..
Protein Sequence MAELQMLLEEEIPSGKRALIESYQNLTRVADYCENNYIQATDKRKALEETKAYTTQSLASVAYQINALANNVLQLLDIQASQLRRMESSINHISQTVDIHKEKVARREIGILTTNKNTSRTHKIIAPANMERPVRYIRKPIDYTVLDDVGHGVKWLKAKHGNNQPARTGTLSRTNPPTQKPPSPPVSGRGTLGRNTPYKTLEPVKPPTVPNDYMTSPARLGSQHSPGRTASLNQRPRTHSGSSGGSGSRENSGSSSIGIPIAVPTPSPPTAGPAAPGAAPGSQYGTMTRQISRHNSTTSSTSSGGYRRTPSVAAQFSAQPHVNGGPLYSQNSISVAPPPPPMPQLTPQIPLTGFVARVQENIADSPTPPPPPPPDDIPMFDDSPPPPPPPPVDYEDEEAAVVQYSDPYADGDPAWAPKNYIEKVVAIYDYTKDKDDELSFKEGAIIYVIKKNDDGWFEGVCNRVTGLFPGNYVESIMHYTD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAELQMLLE
------CHHHHHHHH		26.63-
23PhosphorylationKRALIESYQNLTRVA
HHHHHHHHHHHHHHH		6.6622817900
53PhosphorylationALEETKAYTTQSLAS
HHHHHHHHCHHHHHH		16.33-
88PhosphorylationSQLRRMESSINHISQ
HHHHHHHHHHHHHHH		27.4654231201
89PhosphorylationQLRRMESSINHISQT
HHHHHHHHHHHHHHH		17.6928059163
143 (in isoform 5)Phosphorylation-10.2429514104
143 (in isoform 4)Phosphorylation-10.2429514104
143PhosphorylationYIRKPIDYTVLDDVG
HCCCCCCEEEECCCC		10.2429514104
143 (in isoform 2)Phosphorylation-10.2429514104
143 (in isoform 3)Phosphorylation-10.2429514104
154UbiquitinationDDVGHGVKWLKAKHG
CCCCCHHHHHHHCCC		51.94-
154 (in isoform 2)Ubiquitination-51.94-
165 (in isoform 3)Phosphorylation-26.3229514104
165 (in isoform 2)Phosphorylation-26.3229514104
165 (in isoform 5)Phosphorylation-26.3229514104
165 (in isoform 4)Phosphorylation-26.3229514104
170PhosphorylationNQPARTGTLSRTNPP
CCCCCCCCCCCCCCC		22.4346157091
172PhosphorylationPARTGTLSRTNPPTQ
CCCCCCCCCCCCCCC		36.5867380211
174PhosphorylationRTGTLSRTNPPTQKP
CCCCCCCCCCCCCCC		49.0224925903
178PhosphorylationLSRTNPPTQKPPSPP
CCCCCCCCCCCCCCC		50.9424925903
178 (in isoform 4)Phosphorylation-50.9419144319
183PhosphorylationPPTQKPPSPPVSGRG
CCCCCCCCCCCCCCC		50.8124925903
187PhosphorylationKPPSPPVSGRGTLGR
CCCCCCCCCCCCCCC		28.6625521595
191PhosphorylationPPVSGRGTLGRNTPY
CCCCCCCCCCCCCCC		25.3625266776
196PhosphorylationRGTLGRNTPYKTLEP
CCCCCCCCCCCCCCC		27.0026824392
198PhosphorylationTLGRNTPYKTLEPVK
CCCCCCCCCCCCCCC		17.9920116462
199UbiquitinationLGRNTPYKTLEPVKP
CCCCCCCCCCCCCCC		48.08-
200PhosphorylationGRNTPYKTLEPVKPP
CCCCCCCCCCCCCCC		30.4323527152
205UbiquitinationYKTLEPVKPPTVPND
CCCCCCCCCCCCCCC		56.87-
208PhosphorylationLEPVKPPTVPNDYMT
CCCCCCCCCCCCCCC		58.0622499769
213PhosphorylationPPTVPNDYMTSPARL
CCCCCCCCCCCCHHC		14.6618515860
215PhosphorylationTVPNDYMTSPARLGS
CCCCCCCCCCHHCCC		25.9022942356
216PhosphorylationVPNDYMTSPARLGSQ
CCCCCCCCCHHCCCC		10.4723527152
217 (in isoform 4)Phosphorylation-16.5419144319
222PhosphorylationTSPARLGSQHSPGRT
CCCHHCCCCCCCCCC		29.3425521595
225PhosphorylationARLGSQHSPGRTASL
HHCCCCCCCCCCCCC		22.7827087446
229PhosphorylationSQHSPGRTASLNQRP
CCCCCCCCCCCCCCC		26.8928542873
231PhosphorylationHSPGRTASLNQRPRT
CCCCCCCCCCCCCCC		27.5226824392
233 (in isoform 4)Phosphorylation-33.0623984901
233 (in isoform 2)Phosphorylation-33.0623984901
235 (in isoform 2)Phosphorylation-22.9223984901
235 (in isoform 4)Phosphorylation-22.9223984901
237 (in isoform 4)Phosphorylation-47.4623984901
237 (in isoform 2)Phosphorylation-47.4623984901
238 (in isoform 4)Phosphorylation-24.0723984901
238 (in isoform 2)Phosphorylation-24.0723984901
240PhosphorylationNQRPRTHSGSSGGSG
CCCCCCCCCCCCCCC		39.4921183079
241 (in isoform 4)Phosphorylation-20.4423984901
241 (in isoform 2)Phosphorylation-20.4423984901
242PhosphorylationRPRTHSGSSGGSGSR
CCCCCCCCCCCCCCC		28.9121183079
243 (in isoform 4)Phosphorylation-51.1823984901
243PhosphorylationPRTHSGSSGGSGSRE
CCCCCCCCCCCCCCC		51.1819367708
243 (in isoform 2)Phosphorylation-51.1823984901
247 (in isoform 4)Phosphorylation-33.7223984901
247 (in isoform 2)Phosphorylation-33.7223984901
248PhosphorylationGSSGGSGSRENSGSS
CCCCCCCCCCCCCCC		37.8121183079
249 (in isoform 4)Phosphorylation-51.1223984901
249 (in isoform 2)Phosphorylation-51.1223984901
250 (in isoform 4)Phosphorylation-58.4023984901
250 (in isoform 2)Phosphorylation-58.4023984901
251 (in isoform 4)Phosphorylation-51.0323984901
251 (in isoform 2)Phosphorylation-51.0323984901
252PhosphorylationGSGSRENSGSSSIGI
CCCCCCCCCCCCCCC		34.9921183079
254PhosphorylationGSRENSGSSSIGIPI
CCCCCCCCCCCCCEE		22.2621183079
255PhosphorylationSRENSGSSSIGIPIA
CCCCCCCCCCCCEEE		29.5125777480
256PhosphorylationRENSGSSSIGIPIAV
CCCCCCCCCCCEEEE		26.9125777480
260 (in isoform 4)Phosphorylation-11.85-
260 (in isoform 2)Phosphorylation-11.85-
265PhosphorylationGIPIAVPTPSPPTAG
CCEEEECCCCCCCCC		29.7825777480
265 (in isoform 4)Phosphorylation-29.78-
265 (in isoform 2)Phosphorylation-29.78-
267PhosphorylationPIAVPTPSPPTAGPA
EEEECCCCCCCCCCC		46.0925777480
270PhosphorylationVPTPSPPTAGPAAPG
ECCCCCCCCCCCCCC		47.8625777480
282PhosphorylationAPGAAPGSQYGTMTR
CCCCCCCCCCCCCCE		21.1225777480
284PhosphorylationGAAPGSQYGTMTRQI
CCCCCCCCCCCCEEH		19.0925777480
286PhosphorylationAPGSQYGTMTRQISR
CCCCCCCCCCEEHCC		15.5025777480
288PhosphorylationGSQYGTMTRQISRHN
CCCCCCCCEEHCCCC		21.1825777480
292PhosphorylationGTMTRQISRHNSTTS
CCCCEEHCCCCCCCC		21.102497921
296PhosphorylationRQISRHNSTTSSTSS
EEHCCCCCCCCCCCC		27.2627087446
297PhosphorylationQISRHNSTTSSTSSG
EHCCCCCCCCCCCCC		35.6930387612
298PhosphorylationISRHNSTTSSTSSGG
HCCCCCCCCCCCCCC		22.0924899341
299PhosphorylationSRHNSTTSSTSSGGY
CCCCCCCCCCCCCCC		31.5427087446
300PhosphorylationRHNSTTSSTSSGGYR
CCCCCCCCCCCCCCC		30.1630814537
301PhosphorylationHNSTTSSTSSGGYRR
CCCCCCCCCCCCCCC		27.0323684622
302PhosphorylationNSTTSSTSSGGYRRT
CCCCCCCCCCCCCCC		29.0029899451
303PhosphorylationSTTSSTSSGGYRRTP
CCCCCCCCCCCCCCH		36.0023984901
306PhosphorylationSSTSSGGYRRTPSVA
CCCCCCCCCCCHHHH		10.6323684622
404PhosphorylationEEAAVVQYSDPYADG
CCEEEEEECCCCCCC		11.9312316903
428PhosphorylationIEKVVAIYDYTKDKD
HCEEEEEEEECCCCC		7.9925521595
430PhosphorylationKVVAIYDYTKDKDDE
EEEEEEEECCCCCCC		9.9422817900
431PhosphorylationVVAIYDYTKDKDDEL
EEEEEEECCCCCCCC		29.8422817900
439PhosphorylationKDKDDELSFKEGAII
CCCCCCCCCCCCEEE		32.0218779572
475PhosphorylationFPGNYVESIMHYTD-
CCCCHHHHHHCCCC-		18.3725619855
479PhosphorylationYVESIMHYTD-----
HHHHHHCCCC-----		8.6725619855
480PhosphorylationVESIMHYTD------
HHHHHCCCC------		22.1325619855
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
88SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
88SPhosphorylationKinaseCAMK2AP11275
PSP
213YPhosphorylationKinaseABL1P00519
GPS
428YPhosphorylationKinaseABL1P00519
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABI1_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of ABI1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRK1_MOUSEBrk1physical
20697350
WASF2_MOUSEWasf2physical
20697350
CYFP2_MOUSECyfip2physical
20697350
P85A_MOUSEPik3r1physical
12515821
RASH_MOUSEHrasgenetic
12515821
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABI1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.

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