ABI2_HUMAN - dbPTM
ABI2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ABI2_HUMAN
UniProt AC Q9NYB9
Protein Name Abl interactor 2
Gene Name ABI2
Organism Homo sapiens (Human).
Sequence Length 513
Subcellular Localization Cytoplasm.
Isoform 1: Cell projection, lamellipodium. Cell projection, filopodium. Cytoplasm, cytoskeleton. Isoform 1 but not isoform 3 is 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 (By similarity)..
Protein Sequence MAELQMLLEEEIPGGRRALFDSYTNLERVADYCENNYIQSADKQRALEETKAYTTQSLASVAYLINTLANNVLQMLDIQASQLRRMESSINHISQTVDIHKEKVARREIGILTTNKNTSRTHKIIAPANLERPVRYIRKPIDYTILDDIGHGVKWLLRFKVSTQNMKMGGLPRTTPPTQKPPSPPMSGKGTLGRHSPYRTLEPVRPPVVPNDYVPSPTRNMAPSQQSPVRTASVNQRNRTYSSSGSSGGSHPSSRSSSRENSGSGSVGVPIAVPTPSPPSVFPAPAGSAGTPPLPATSASAPAPLVPATVPSSTAPNAAAGGAPNLADGFTSPTPPVVSSTPPTGHPVQFYSMNRPASRHTPPTIGGSLPYRRPPSITSQTSLQNQMNGGPFYSQNPVSDTPPPPPPVEEPVFDESPPPPPPPEDYEEEEAAVVEYSDPYAEEDPPWAPRSYLEKVVAIYDYTKDKEDELSFQEGAIIYVIKKNDDGWYEGVMNGVTGLFPGNYVESIMHYSE
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
23PhosphorylationRRALFDSYTNLERVA
HHHHHHHCCCHHHHH		11.0722817900
32PhosphorylationNLERVADYCENNYIQ
CHHHHHHHHHHCCCC		7.6022817900
40PhosphorylationCENNYIQSADKQRAL
HHHCCCCHHHHHHHH		28.9530631047
43UbiquitinationNYIQSADKQRALEET
CCCCHHHHHHHHHHH		41.21-
88PhosphorylationSQLRRMESSINHISQ
HHHHHHHHHHHHHHH		27.4628348404
89PhosphorylationQLRRMESSINHISQT
HHHHHHHHHHHHHHH		17.6928348404
123UbiquitinationKNTSRTHKIIAPANL
CCCCCCEEEECCCCC		34.88-
139UbiquitinationRPVRYIRKPIDYTIL
CCHHHCCCCCCEEEE		36.45-
162PhosphorylationWLLRFKVSTQNMKMG
HHHEEEEECCCCCCC		25.5128122231
163PhosphorylationLLRFKVSTQNMKMGG
HHEEEEECCCCCCCC		27.2728122231
167UbiquitinationKVSTQNMKMGGLPRT
EEECCCCCCCCCCCC		41.78-
174PhosphorylationKMGGLPRTTPPTQKP
CCCCCCCCCCCCCCC		41.5423927012
175PhosphorylationMGGLPRTTPPTQKPP
CCCCCCCCCCCCCCC		28.6625159151
178PhosphorylationLPRTTPPTQKPPSPP
CCCCCCCCCCCCCCC		50.8930266825
183PhosphorylationPPTQKPPSPPMSGKG
CCCCCCCCCCCCCCC		50.6025159151
187PhosphorylationKPPSPPMSGKGTLGR
CCCCCCCCCCCCCCC		43.0330266825
191PhosphorylationPPMSGKGTLGRHSPY
CCCCCCCCCCCCCCC		29.5328176443
196PhosphorylationKGTLGRHSPYRTLEP
CCCCCCCCCCCCCCC		23.4328176443
198PhosphorylationTLGRHSPYRTLEPVR
CCCCCCCCCCCCCCC		21.1728176443
200PhosphorylationGRHSPYRTLEPVRPP
CCCCCCCCCCCCCCC		29.6327273156
205 (in isoform 3)Phosphorylation-40.2927251275
205MethylationYRTLEPVRPPVVPND
CCCCCCCCCCCCCCC		40.29-
206 (in isoform 3)Phosphorylation-26.6927251275
207 (in isoform 3)Phosphorylation-29.2227251275
211 (in isoform 3)Phosphorylation-41.4527251275
213 (in isoform 3)Phosphorylation-22.3927251275
213PhosphorylationPPVVPNDYVPSPTRN
CCCCCCCCCCCCCCC		22.3927273156
215 (in isoform 3)Phosphorylation-28.5027251275
216PhosphorylationVPNDYVPSPTRNMAP
CCCCCCCCCCCCCCC		28.9425159151
218PhosphorylationNDYVPSPTRNMAPSQ
CCCCCCCCCCCCCCC		38.7330183078
224 (in isoform 3)Phosphorylation-31.1729523821
224PhosphorylationPTRNMAPSQQSPVRT
CCCCCCCCCCCCCEE		31.1729255136
226 (in isoform 3)Phosphorylation-54.7825850435
227PhosphorylationNMAPSQQSPVRTASV
CCCCCCCCCCEECCC		20.0919664994
229 (in isoform 3)Phosphorylation-11.7025850435
230MethylationPSQQSPVRTASVNQR
CCCCCCCEECCCCCC		28.14-
231PhosphorylationSQQSPVRTASVNQRN
CCCCCCEECCCCCCC		24.4227422710
233PhosphorylationQSPVRTASVNQRNRT
CCCCEECCCCCCCCE		22.4618641825
239 (in isoform 3)Phosphorylation-36.9125850435
240PhosphorylationSVNQRNRTYSSSGSS
CCCCCCCEECCCCCC		31.1622360455
240 (in isoform 3)Phosphorylation-31.1625849741
241PhosphorylationVNQRNRTYSSSGSSG
CCCCCCEECCCCCCC		11.8824043423
242PhosphorylationNQRNRTYSSSGSSGG
CCCCCEECCCCCCCC		19.8823401153
243PhosphorylationQRNRTYSSSGSSGGS
CCCCEECCCCCCCCC		28.4521955146
244PhosphorylationRNRTYSSSGSSGGSH
CCCEECCCCCCCCCC		36.4327273156
246 (in isoform 3)Phosphorylation-27.9729523821
246PhosphorylationRTYSSSGSSGGSHPS
CEECCCCCCCCCCCC		27.9728152594
247PhosphorylationTYSSSGSSGGSHPSS
EECCCCCCCCCCCCC		51.1828152594
250 (in isoform 2)Phosphorylation-35.4327251275
250PhosphorylationSSGSSGGSHPSSRSS
CCCCCCCCCCCCCCC		35.4328450419
251 (in isoform 2)Phosphorylation-29.5427251275
252 (in isoform 2)Phosphorylation-35.3827251275
253PhosphorylationSSGGSHPSSRSSSRE
CCCCCCCCCCCCCCC		32.7228450419
254PhosphorylationSGGSHPSSRSSSREN
CCCCCCCCCCCCCCC		40.4028450419
256PhosphorylationGSHPSSRSSSRENSG
CCCCCCCCCCCCCCC		34.3123898821
256 (in isoform 2)Phosphorylation-34.3127251275
258 (in isoform 2)Phosphorylation-44.8827251275
260 (in isoform 2)Phosphorylation-58.6627251275
269 (in isoform 2)Phosphorylation-2.6529523821
271 (in isoform 2)Phosphorylation-5.8425850435
274 (in isoform 2)Phosphorylation-29.5725850435
284 (in isoform 2)Phosphorylation-8.6325850435
285 (in isoform 2)Phosphorylation-37.0725849741
291 (in isoform 2)Phosphorylation-22.8129523821
297PhosphorylationGTPPLPATSASAPAP
CCCCCCCCCCCCCCC		23.9220068231
309 (in isoform 2)Phosphorylation-27.2128348404
311 (in isoform 2)Phosphorylation-20.4328348404
312 (in isoform 2)Phosphorylation-35.6628348404
314 (in isoform 2)Phosphorylation-50.9328348404
315 (in isoform 2)Phosphorylation-9.4128348404
351PhosphorylationTGHPVQFYSMNRPAS
CCCCCEEEECCCCCC		7.01-
352PhosphorylationGHPVQFYSMNRPASR
CCCCEEEECCCCCCC		15.7420068231
361PhosphorylationNRPASRHTPPTIGGS
CCCCCCCCCCCCCCC		29.8329255136
364PhosphorylationASRHTPPTIGGSLPY
CCCCCCCCCCCCCCC		33.2030266825
368PhosphorylationTPPTIGGSLPYRRPP
CCCCCCCCCCCCCCC		22.4329255136
371PhosphorylationTIGGSLPYRRPPSIT
CCCCCCCCCCCCCCC		25.2523927012
376PhosphorylationLPYRRPPSITSQTSL
CCCCCCCCCCCCHHH		40.9851457467
460PhosphorylationLEKVVAIYDYTKDKE
HHHHHEEEECCCCCC		7.9925159151
462PhosphorylationKVVAIYDYTKDKEDE
HHHEEEECCCCCCCC		9.9428060719
463PhosphorylationVVAIYDYTKDKEDEL
HHEEEECCCCCCCCC		29.84-
466AcetylationIYDYTKDKEDELSFQ
EEECCCCCCCCCCCC		69.4919812139
482AcetylationGAIIYVIKKNDDGWY
CCEEEEEEECCCCHH		35.1619812153
504PhosphorylationTGLFPGNYVESIMHY
CCCCCCCHHHHHHCC		16.12-
507PhosphorylationFPGNYVESIMHYSE-
CCCCHHHHHHCCCC-		18.3727251275
512PhosphorylationVESIMHYSE------
HHHHHCCCC------		23.3522617229
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 ligaseTRIM32Q13049
PMID:18632609
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ABI2_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
K1C20_HUMANKRT20physical
16189514
WASC3_HUMANCCDC53physical
16189514
IFT20_HUMANIFT20physical
16189514
ABL1_HUMANABL1physical
7590236
TRI32_HUMANTRIM32physical
18632609
DP13B_HUMANAPPL2physical
22863883
ABI2_HUMANABI2physical
25416956
STAM2_HUMANSTAM2physical
25416956
EFS_HUMANEFSphysical
25416956
TRI32_HUMANTRIM32physical
25416956
NUP62_HUMANNUP62physical
25416956
TFP11_HUMANTFIP11physical
25416956
BL1S6_HUMANBLOC1S6physical
25416956
LARGN_HUMANPRR16physical
25416956
CCHCR_HUMANCCHCR1physical
25416956
SKT_HUMANKIAA1217physical
25416956
SYVM_HUMANVARS2physical
25416956
RM44_HUMANMRPL44physical
25416956
GCC1_HUMANGCC1physical
25416956
ARMC7_HUMANARMC7physical
25416956
C102B_HUMANCCDC102Bphysical
25416956
PRAM_HUMANPRAM1physical
25416956
IFT20_HUMANIFT20physical
25416956
EGLN3_HUMANEGLN3physical
25416956
MR1L1_HUMANMRFAP1L1physical
25416956
IHO1_HUMANCCDC36physical
25416956
ENAH_HUMANENAHphysical
17101133
WASF2_HUMANWASF2physical
17101133
WASL_HUMANWASLphysical
26344197
DTNB_HUMANDTNBphysical
21516116
IHO1_HUMANCCDC36physical
21516116
WASF3_HUMANWASF3physical
28514442
RAPH1_HUMANRAPH1physical
28514442
WASF1_HUMANWASF1physical
28514442
SAS6_HUMANSASS6physical
28514442
NHSL1_HUMANNHSL1physical
28514442
CSKI2_HUMANCASKIN2physical
28514442
NCKP1_HUMANNCKAP1physical
28514442
BRK1_HUMANBRK1physical
28514442
ABI1_HUMANABI1physical
28514442
WASF2_HUMANWASF2physical
28514442
TNIP1_HUMANTNIP1physical
28514442
K1522_HUMANKIAA1522physical
28514442
CEP44_HUMANCEP44physical
28514442
NCKPL_HUMANNCKAP1Lphysical
28514442
CYFP2_HUMANCYFIP2physical
28514442
TRI32_HUMANTRIM32physical
28514442
ABL2_HUMANABL2physical
28514442
CYFP1_HUMANCYFIP1physical
28514442
PIMT_HUMANPCMT1physical
28514442
UBR3_HUMANUBR3physical
28514442
RGPD5_HUMANRGPD5physical
28514442
OBSL1_HUMANOBSL1physical
28514442
EXOC7_HUMANEXOC7physical
28514442
GRN_HUMANGRNphysical
28514442
ABL1_HUMANABL1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ABI2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-227, AND MASSSPECTROMETRY.
"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.

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