ABI2_MOUSE - dbPTM
ABI2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABI2_MOUSE
UniProt AC P62484
Protein Name Abl interactor 2
Gene Name Abi2
Organism Mus musculus (Mouse).
Sequence Length 446
Subcellular Localization Cytoplasm . Cell projection, lamellipodium . Cell projection, filopodium . Cytoplasm, cytoskeleton . Localized to protruding lamellipodia and filopodia tips.
Protein 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. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes. [PubMed: 27605705]
Protein Sequence MAELQMLLEEEIPGGRRALFDSYTNLERVADYCENNYIQSPDKQRALEETKAYTTQSLASVAYLINTLANNVLQMLDIQASQLRRMESSINHISQTVDIHKEKVARREIGILTTNKNTSRTHKIIAPANLERPVRYIRKPIDYTILDDIGHGVKVSTQNMKMGGLPRTTPPTQKPPSPPMSGKGTLGRHSPYRTLEPVRPPVVPNDYVPSPTRNMAPSQQSPVRTASVNQRNRTYSSSGSSGGSHPSSRSSSRENSGSGSVGVPIAVPTPSPPSVFPGHPVQFYSMNRPASRHTPPTIGGSLPYRRPPSITSQTSLQNQMNGGPFYNQNPVSDTPPPPPPVEEPVFDESPPPPPPPEDYEEEEAAVVEYSDPYAEEDPPWAPRAYLEKVVAIYDYTKDKEDELSFQEGAIIYVIKKNDDGWYEGVMNGVTGLFPGNYVESIMHYSE
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
32PhosphorylationNLERVADYCENNYIQ
CHHHHHHHHHCCCCC		7.6020415495
37PhosphorylationADYCENNYIQSPDKQ
HHHHHCCCCCCHHHH		16.3620415495
40PhosphorylationCENNYIQSPDKQRAL
HHCCCCCCHHHHHHH		26.0525521595
88PhosphorylationSQLRRMESSINHISQ
HHHHHHHHHHHHHHH		27.4654231201
89PhosphorylationQLRRMESSINHISQT
HHHHHHHHHHHHHHH		17.6928059163
168PhosphorylationKMGGLPRTTPPTQKP
CCCCCCCCCCCCCCC		41.5427087446
169PhosphorylationMGGLPRTTPPTQKPP
CCCCCCCCCCCCCCC		28.6624925903
172PhosphorylationLPRTTPPTQKPPSPP
CCCCCCCCCCCCCCC		50.8924925903
177PhosphorylationPPTQKPPSPPMSGKG
CCCCCCCCCCCCCCC		50.6025521595
181PhosphorylationKPPSPPMSGKGTLGR
CCCCCCCCCCCCCCC		43.0324925903
185PhosphorylationPPMSGKGTLGRHSPY
CCCCCCCCCCCCCCC		29.5329514104
190PhosphorylationKGTLGRHSPYRTLEP
CCCCCCCCCCCCCCC		23.4315980943
192PhosphorylationTLGRHSPYRTLEPVR
CCCCCCCCCCCCCCC		21.1720116462
194PhosphorylationGRHSPYRTLEPVRPP
CCCCCCCCCCCCCCC		29.6323527152
207PhosphorylationPPVVPNDYVPSPTRN
CCCCCCCCCCCCCCC		22.3922499769
210PhosphorylationVPNDYVPSPTRNMAP
CCCCCCCCCCCCCCC		28.9422499769
212PhosphorylationNDYVPSPTRNMAPSQ
CCCCCCCCCCCCCCC		38.7322499769
218PhosphorylationPTRNMAPSQQSPVRT
CCCCCCCCCCCCCEE		31.1723527152
221PhosphorylationNMAPSQQSPVRTASV
CCCCCCCCCCEECCC		20.0925521595
225PhosphorylationSQQSPVRTASVNQRN
CCCCCCEECCCCCCC		24.4222324799
227PhosphorylationQSPVRTASVNQRNRT
CCCCEECCCCCCCCE		22.4622324799
234PhosphorylationSVNQRNRTYSSSGSS
CCCCCCCEECCCCCC		31.1629895711
235PhosphorylationVNQRNRTYSSSGSSG
CCCCCCEECCCCCCC		11.8821454597
236PhosphorylationNQRNRTYSSSGSSGG
CCCCCEECCCCCCCC		19.8812563567
237PhosphorylationQRNRTYSSSGSSGGS
CCCCEECCCCCCCCC		28.4523984901
238PhosphorylationRNRTYSSSGSSGGSH
CCCEECCCCCCCCCC		36.4321454597
240PhosphorylationRTYSSSGSSGGSHPS
CEECCCCCCCCCCCC		27.9723984901
241PhosphorylationTYSSSGSSGGSHPSS
EECCCCCCCCCCCCC		51.1823984901
269PhosphorylationGVPIAVPTPSPPSVF
CCEEEECCCCCCCCC		29.7826160508
271PhosphorylationPIAVPTPSPPSVFPG
EEEECCCCCCCCCCC		52.5026160508
274PhosphorylationVPTPSPPSVFPGHPV
ECCCCCCCCCCCCCC		39.5126160508
284PhosphorylationPGHPVQFYSMNRPAS
CCCCCEEEECCCCCC		7.0126160508
285PhosphorylationGHPVQFYSMNRPASR
CCCCEEEECCCCCCC		15.7426160508
291PhosphorylationYSMNRPASRHTPPTI
EECCCCCCCCCCCCC		27.5526160508
294PhosphorylationNRPASRHTPPTIGGS
CCCCCCCCCCCCCCC		29.8321082442
297O-linked_GlycosylationASRHTPPTIGGSLPY
CCCCCCCCCCCCCCC		33.2022645316
297PhosphorylationASRHTPPTIGGSLPY
CCCCCCCCCCCCCCC		33.2025521595
301PhosphorylationTPPTIGGSLPYRRPP
CCCCCCCCCCCCCCC		22.4325521595
304PhosphorylationTIGGSLPYRRPPSIT
CCCCCCCCCCCCCCC		25.2583435
309PhosphorylationLPYRRPPSITSQTSL
CCCCCCCCCCCCHHH		40.9851457463
311PhosphorylationYRRPPSITSQTSLQN
CCCCCCCCCCHHHCH		21.0851457483
326PhosphorylationQMNGGPFYNQNPVSD
HHCCCCCCCCCCCCC		20.97-
393PhosphorylationLEKVVAIYDYTKDKE
HHEEEEEEECCCCCC		7.9925521595
395PhosphorylationKVVAIYDYTKDKEDE
EEEEEEECCCCCCCC		9.9428066266
396PhosphorylationVVAIYDYTKDKEDEL
EEEEEECCCCCCCCC		29.8428066266
437PhosphorylationTGLFPGNYVESIMHY
CCCCCCCHHHHHHCC		16.1229899451
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
-KUbiquitinationE3 ubiquitin ligaseTrim32Q8CH72
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABI2_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 ABI2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ABI2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABI2_MOUSE

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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-395, AND MASSSPECTROMETRY.

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