BI2L1_HUMAN - dbPTM
BI2L1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BI2L1_HUMAN
UniProt AC Q9UHR4
Protein Name Brain-specific angiogenesis inhibitor 1-associated protein 2-like protein 1
Gene Name BAIAP2L1
Organism Homo sapiens (Human).
Sequence Length 511
Subcellular Localization Cytoplasm, cytoskeleton . Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites.
Protein Description May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection..
Protein Sequence MSRGPEEVNRLTESTYRNVMEQFNPGLRNLINLGKNYEKAVNAMILAGKAYYDGVAKIGEIATGSPVSTELGHVLIEISSTHKKLNESLDENFKKFHKEIIHELEKKIELDVKYMNATLKRYQTEHKNKLESLEKSQAELKKIRRKSQGSRNALKYEHKEIEYVETVTSRQSEIQKFIADGCKEALLEEKRRFCFLVDKHCGFANHIHYYHLQSAELLNSKLPRWQETCVDAIKVPEKIMNMIEEIKTPASTPVSGTPQASPMIERSNVVRKDYDTLSKCSPKMPPAPSGRAYTSPLIDMFNNPATAAPNSQRVNNSTGTSEDPSLQRSVSVATGLNMMKKQKVKTIFPHTAGSNKTLLSFAQGDVITLLIPEEKDGWLYGEHDVSKARGWFPSSYTKLLEENETEAVTVPTPSPTPVRSISTVNLSENSSVVIPPPDYLECLSMGAAADRRADSARTTSTFKAPASKPETAAPNDANGTAKPPFLSGENPFATVKLRPTVTNDRSAPIIR
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
2Phosphorylation------MSRGPEEVN
------CCCCHHHHH		46.0424719451
14PhosphorylationEVNRLTESTYRNVME
HHHHHCHHHHHHHHH		26.0428152594
15PhosphorylationVNRLTESTYRNVMEQ
HHHHCHHHHHHHHHH		21.9228152594
16PhosphorylationNRLTESTYRNVMEQF
HHHCHHHHHHHHHHH		14.9628152594
20SulfoxidationESTYRNVMEQFNPGL
HHHHHHHHHHHCHHH		3.7028183972
37PhosphorylationLINLGKNYEKAVNAM
HHHCCCCHHHHHHHH		23.4621840312
39UbiquitinationNLGKNYEKAVNAMIL
HCCCCHHHHHHHHHH		47.4729967540
51PhosphorylationMILAGKAYYDGVAKI
HHHCCCCCCCCCCHH		12.94-
63PhosphorylationAKIGEIATGSPVSTE
CHHHHHCCCCCCCHH		43.80-
84UbiquitinationEISSTHKKLNESLDE
EEHHHHHHHHHHHHH		49.2729901268
88PhosphorylationTHKKLNESLDENFKK
HHHHHHHHHHHHHHH		39.7921815630
94UbiquitinationESLDENFKKFHKEII
HHHHHHHHHHHHHHH		67.1429967540
94AcetylationESLDENFKKFHKEII
HHHHHHHHHHHHHHH		67.1426051181
942-HydroxyisobutyrylationESLDENFKKFHKEII
HHHHHHHHHHHHHHH		67.14-
95UbiquitinationSLDENFKKFHKEIIH
HHHHHHHHHHHHHHH		48.8729967540
98UbiquitinationENFKKFHKEIIHELE
HHHHHHHHHHHHHHH		54.4629967540
98AcetylationENFKKFHKEIIHELE
HHHHHHHHHHHHHHH		54.4626051181
106UbiquitinationEIIHELEKKIELDVK
HHHHHHHHHHHCCHH		72.2229901268
106AcetylationEIIHELEKKIELDVK
HHHHHHHHHHHCCHH		72.2223236377
114PhosphorylationKIELDVKYMNATLKR
HHHCCHHHHHHHHHH		8.7521840312
118PhosphorylationDVKYMNATLKRYQTE
CHHHHHHHHHHHHHH		28.0128387310
122PhosphorylationMNATLKRYQTEHKNK
HHHHHHHHHHHHHHH		20.4228152594
132PhosphorylationEHKNKLESLEKSQAE
HHHHHHHHHHHHHHH		52.8725159151
136PhosphorylationKLESLEKSQAELKKI
HHHHHHHHHHHHHHH		25.8319664994
146UbiquitinationELKKIRRKSQGSRNA
HHHHHHHHCHHCCCC		36.96-
147PhosphorylationLKKIRRKSQGSRNAL
HHHHHHHCHHCCCCH		37.6525849741
150PhosphorylationIRRKSQGSRNALKYE
HHHHCHHCCCCHHHH		18.0930576142
155UbiquitinationQGSRNALKYEHKEIE
HHCCCCHHHHHHHEE		46.3027667366
156PhosphorylationGSRNALKYEHKEIEY
HCCCCHHHHHHHEEE		24.9028152594
163PhosphorylationYEHKEIEYVETVTSR
HHHHHEEEEEEHHCC		14.8425159151
166PhosphorylationKEIEYVETVTSRQSE
HHEEEEEEHHCCHHH		21.0228152594
168PhosphorylationIEYVETVTSRQSEIQ
EEEEEEHHCCHHHHH		26.1328152594
169PhosphorylationEYVETVTSRQSEIQK
EEEEEHHCCHHHHHH		24.8028152594
172PhosphorylationETVTSRQSEIQKFIA
EEHHCCHHHHHHHHH		35.2428348404
183UbiquitinationKFIADGCKEALLEEK
HHHHHCHHHHHHHHH		52.1029967540
1832-HydroxyisobutyrylationKFIADGCKEALLEEK
HHHHHCHHHHHHHHH		52.10-
220PhosphorylationQSAELLNSKLPRWQE
HHHHHHHCCCCHHHH		35.2220068231
234AcetylationETCVDAIKVPEKIMN
HHHHHHHHCCHHHHH		54.1526051181
234UbiquitinationETCVDAIKVPEKIMN
HHHHHHHHCCHHHHH		54.1521963094
238UbiquitinationDAIKVPEKIMNMIEE
HHHHCCHHHHHHHHH		40.9821906983
247UbiquitinationMNMIEEIKTPASTPV
HHHHHHCCCCCCCCC		52.3023503661
248PhosphorylationNMIEEIKTPASTPVS
HHHHHCCCCCCCCCC		29.7330266825
251PhosphorylationEEIKTPASTPVSGTP
HHCCCCCCCCCCCCC		34.1530266825
252PhosphorylationEIKTPASTPVSGTPQ
HCCCCCCCCCCCCCC		29.8030266825
255PhosphorylationTPASTPVSGTPQASP
CCCCCCCCCCCCCCC		37.8529255136
257PhosphorylationASTPVSGTPQASPMI
CCCCCCCCCCCCCCC		12.5329255136
261PhosphorylationVSGTPQASPMIERSN
CCCCCCCCCCCCCCC		15.1119664994
267PhosphorylationASPMIERSNVVRKDY
CCCCCCCCCCCCCCH		22.6129978859
274PhosphorylationSNVVRKDYDTLSKCS
CCCCCCCHHHHHHCC		17.5423927012
276PhosphorylationVVRKDYDTLSKCSPK
CCCCCHHHHHHCCCC		27.0523927012
278PhosphorylationRKDYDTLSKCSPKMP
CCCHHHHHHCCCCCC		33.4423927012
279UbiquitinationKDYDTLSKCSPKMPP
CCHHHHHHCCCCCCC		41.6733845483
281PhosphorylationYDTLSKCSPKMPPAP
HHHHHHCCCCCCCCC		31.1523927012
293PhosphorylationPAPSGRAYTSPLIDM
CCCCCCCCCCCHHHC		13.3421712546
294PhosphorylationAPSGRAYTSPLIDMF
CCCCCCCCCCHHHCC		23.9225159151
295PhosphorylationPSGRAYTSPLIDMFN
CCCCCCCCCHHHCCC		12.6725159151
317PhosphorylationNSQRVNNSTGTSEDP
CCCCCCCCCCCCCCH		24.0225159151
318PhosphorylationSQRVNNSTGTSEDPS
CCCCCCCCCCCCCHH		46.7527251275
320PhosphorylationRVNNSTGTSEDPSLQ
CCCCCCCCCCCHHHH		29.0927251275
325PhosphorylationTGTSEDPSLQRSVSV
CCCCCCHHHHHHHHH		49.8329759185
329PhosphorylationEDPSLQRSVSVATGL
CCHHHHHHHHHHHCH		13.0430266825
331PhosphorylationPSLQRSVSVATGLNM
HHHHHHHHHHHCHHH		13.7923927012
334PhosphorylationQRSVSVATGLNMMKK
HHHHHHHHCHHHHHH		39.7930266825
351PhosphorylationVKTIFPHTAGSNKTL
CEEECCCCCCCCCHH		32.7123090842
354PhosphorylationIFPHTAGSNKTLLSF
ECCCCCCCCCHHHHC		32.4625159151
380PhosphorylationEEKDGWLYGEHDVSK
CCCCCEEECCCCHHH		17.6028152594
394PhosphorylationKARGWFPSSYTKLLE
HHCCCCCHHHHHHHH		26.8828152594
395PhosphorylationARGWFPSSYTKLLEE
HCCCCCHHHHHHHHC		36.7428152594
396PhosphorylationRGWFPSSYTKLLEEN
CCCCCHHHHHHHHCC		16.5428152594
397PhosphorylationGWFPSSYTKLLEENE
CCCCHHHHHHHHCCC		19.7028152594
405PhosphorylationKLLEENETEAVTVPT
HHHHCCCCCCEECCC		40.6030108239
409PhosphorylationENETEAVTVPTPSPT
CCCCCCEECCCCCCC		28.0228176443
412PhosphorylationTEAVTVPTPSPTPVR
CCCEECCCCCCCCCC		31.8729255136
414PhosphorylationAVTVPTPSPTPVRSI
CEECCCCCCCCCCEE		43.8319664994
416PhosphorylationTVPTPSPTPVRSIST
ECCCCCCCCCCEEEE		38.4630266825
420PhosphorylationPSPTPVRSISTVNLS
CCCCCCCEEEEEECC		22.5628176443
422PhosphorylationPTPVRSISTVNLSEN
CCCCCEEEEEECCCC		27.7826657352
423PhosphorylationTPVRSISTVNLSENS
CCCCEEEEEECCCCC		16.2526657352
427PhosphorylationSISTVNLSENSSVVI
EEEEEECCCCCCEEE		29.5426657352
439PhosphorylationVVIPPPDYLECLSMG
EEECCCCHHHHHHCC		15.3527259358
444PhosphorylationPDYLECLSMGAAADR
CCHHHHHHCCHHHHH		27.1628176443
494PhosphorylationSGENPFATVKLRPTV
CCCCCCCEEECCCCC		20.6726657352
496UbiquitinationENPFATVKLRPTVTN
CCCCCEEECCCCCCC		34.1322817900
500PhosphorylationATVKLRPTVTNDRSA
CEEECCCCCCCCCCC		33.2626437602
505MethylationRPTVTNDRSAPIIR-
CCCCCCCCCCCCCC-		36.47115480623
506PhosphorylationPTVTNDRSAPIIR--
CCCCCCCCCCCCC--		41.0627251275
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
37YPhosphorylationKinaseSRCP12931
PSP
156YPhosphorylationKinaseSRCP12931
PSP
163YPhosphorylationKinaseSRCP12931
PSP
274YPhosphorylationKinaseSRCP12931
PSP
293YPhosphorylationKinaseSRCP12931
PSP
331SPhosphorylationKinaseCHEK2O96017
GPS
439YPhosphorylationKinaseSRCP12931
PSP
-KUbiquitinationE3 ubiquitin ligaseMDM2Q00987
PMID:21887275
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BI2L1_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 BI2L1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
21887275
MDM2_HUMANMDM2physical
21887275
EPS8_HUMANEPS8physical
22921828
WASP_HUMANWASphysical
22921828
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 BI2L1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-261; THR-412;SER-414 AND THR-416, AND MASS SPECTROMETRY.
"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 THR-248; THR-257; SER-261;SER-281; SER-331; THR-412 AND SER-414, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, 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-261, 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 THR-257 AND SER-261, 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-274, AND MASSSPECTROMETRY.

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