DBNL_MOUSE - dbPTM
DBNL_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DBNL_MOUSE
UniProt AC Q62418
Protein Name Drebrin-like protein
Gene Name Dbnl {ECO:0000312|MGI:MGI:700006}
Organism Mus musculus (Mouse).
Sequence Length 436
Subcellular Localization Cytoplasm, cytoskeleton . Cell projection, lamellipodium . Cell projection, ruffle . Cytoplasm, cell cortex . Cytoplasm, cytosol . Cell junction, synapse . Cell projection . Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic vesicl
Protein Description Adapter protein that binds F-actin and DNM1, and thereby plays a role in receptor-mediated endocytosis. Plays a role in the reorganization of the actin cytoskeleton, formation of cell projections, such as neurites, in neuron morphogenesis and synapse formation via its interaction with WASL and COBL. Does not bind G-actin and promote actin polymerization by itself. Required for the formation of organized podosome rosettes. May act as a common effector of antigen receptor-signaling pathways in leukocytes. Acts as a key component of the immunological synapse that regulates T-cell activation by bridging TCRs and the actin cytoskeleton to gene activation and endocytic processes..
Protein Sequence MAVNLSRNGPALQEAYVRVVTEKSPTDWALFTYEGNSNDIRVAGTGEGGLEELVEELNSGKVMYAFCRVKDPNSGLPKFVLINWTGEGVNDVRKGACANHVSTMANFLKGAHVTINARAEEDVEPECIMEKVAKASGANYSFHKESTSFQDVGPQAPVGSVYQKTNAISEIKRVGKDNFWAKAEKEEENRRLEEKRRAEEERQRLEEERRERELQEAARREQRYQEQHRSAGAPSPSSRTGEPEQEAVSRTRQEWESAGQQAPHPREIFKQKERAMSTTSVTSSQPGKLRSPFLQKQLTQPETSYGREPTAPVSRPAAGVCEEPAPSTLSSAQTEEEPTYEVPPEQDTLYEEPPLVQQQGAGSEHIDNYMQSQGFSGQGLCARALYDYQAADDTEISFDPENLITGIEVIDEGWWRGYGPDGHFGMFPANYVELIE
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
21PhosphorylationEAYVRVVTEKSPTDW
EEEEEEEECCCCCCE		34.5324925903
23AcetylationYVRVVTEKSPTDWAL
EEEEEECCCCCCEEE		52.9823236377
24PhosphorylationVRVVTEKSPTDWALF
EEEEECCCCCCEEEE		27.1424925903
26PhosphorylationVVTEKSPTDWALFTY
EEECCCCCCEEEEEE		51.7925521595
97GlutathionylationNDVRKGACANHVSTM
HHHHHCHHHHHHHHH		5.4824333276
127S-nitrosocysteineEEDVEPECIMEKVAK
CCCCCHHHHHHHHHH		5.41-
127S-nitrosylationEEDVEPECIMEKVAK
CCCCCHHHHHHHHHH		5.4122178444
140PhosphorylationAKASGANYSFHKEST
HHHHCCCCEECCCCC		16.5125367039
141PhosphorylationKASGANYSFHKESTS
HHHCCCCEECCCCCC		22.2330352176
146PhosphorylationNYSFHKESTSFQDVG
CCEECCCCCCCCCCC		33.8725159016
147PhosphorylationYSFHKESTSFQDVGP
CEECCCCCCCCCCCC		34.3525367039
148PhosphorylationSFHKESTSFQDVGPQ
EECCCCCCCCCCCCC		30.1425521595
160PhosphorylationGPQAPVGSVYQKTNA
CCCCCCCCHHHHHCC		20.2025521595
162PhosphorylationQAPVGSVYQKTNAIS
CCCCCCHHHHHCCHH		13.1418779572
169PhosphorylationYQKTNAISEIKRVGK
HHHHCCHHHHHHHCC		30.7529176673
172MalonylationTNAISEIKRVGKDNF
HCCHHHHHHHCCCCC		36.6626320211
176AcetylationSEIKRVGKDNFWAKA
HHHHHHCCCCCHHHH		46.79-
224PhosphorylationAARREQRYQEQHRSA
HHHHHHHHHHHHHHC		18.9818779572
230 (in isoform 3)Phosphorylation-29.0025338131
230PhosphorylationRYQEQHRSAGAPSPS
HHHHHHHHCCCCCCC		29.0030635358
235PhosphorylationHRSAGAPSPSSRTGE
HHHCCCCCCCCCCCC		36.5627087446
237PhosphorylationSAGAPSPSSRTGEPE
HCCCCCCCCCCCCCH		36.4726160508
238PhosphorylationAGAPSPSSRTGEPEQ
CCCCCCCCCCCCCHH		36.9326160508
240PhosphorylationAPSPSSRTGEPEQEA
CCCCCCCCCCCHHHH		48.0926160508
277PhosphorylationKQKERAMSTTSVTSS
HHHHHHHCCCCCCCC		27.7827087446
278PhosphorylationQKERAMSTTSVTSSQ
HHHHHHCCCCCCCCC		15.2525521595
279O-linked_GlycosylationKERAMSTTSVTSSQP
HHHHHCCCCCCCCCC		17.5628528544
279PhosphorylationKERAMSTTSVTSSQP
HHHHHCCCCCCCCCC		17.5627087446
280PhosphorylationERAMSTTSVTSSQPG
HHHHCCCCCCCCCCC		24.4025521595
282PhosphorylationAMSTTSVTSSQPGKL
HHCCCCCCCCCCCCC		23.5628833060
283PhosphorylationMSTTSVTSSQPGKLR
HCCCCCCCCCCCCCC		25.4828833060
284PhosphorylationSTTSVTSSQPGKLRS
CCCCCCCCCCCCCCC		30.9128833060
288AcetylationVTSSQPGKLRSPFLQ
CCCCCCCCCCCHHHH		47.6223806337
291PhosphorylationSQPGKLRSPFLQKQL
CCCCCCCCHHHHHHH		30.3626824392
296AcetylationLRSPFLQKQLTQPET
CCCHHHHHHHCCCCC		49.80-
299PhosphorylationPFLQKQLTQPETSYG
HHHHHHHCCCCCCCC		39.3125521595
304PhosphorylationQLTQPETSYGREPTA
HHCCCCCCCCCCCCC		24.7527566939
340PhosphorylationQTEEEPTYEVPPEQD
CCCCCCCCCCCCCCC		26.1622303001
350PhosphorylationPPEQDTLYEEPPLVQ
CCCCCCCCCCCCCCC		21.9716141072
363PhosphorylationVQQQGAGSEHIDNYM
CCCCCCCCHHHHHHH		26.01-
369PhosphorylationGSEHIDNYMQSQGFS
CCHHHHHHHHHCCCC		7.87-
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
340YPhosphorylationKinaseBLKP51451
PSP
340YPhosphorylationKinaseFYNP06241
PSP
340YPhosphorylationKinaseSYKP43405
PSP
340YPhosphorylationKinaseLYNP07948
PSP
350YPhosphorylationKinaseBLKP51451
PSP
350YPhosphorylationKinaseFYNP06241
PSP
350YPhosphorylationKinaseSYKP43405
PSP
350YPhosphorylationKinaseLYNP07948
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND THR-278, 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 THR-299, AND MASSSPECTROMETRY.
"SH3P7 is a cytoskeleton adapter protein and is coupled to signaltransduction from lymphocyte antigen receptors.";
Larbolette O., Wollscheid B., Schweikert J., Nielsen P.J.,Wienands J.;
Mol. Cell. Biol. 19:1539-1546(1999).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 79-94 AND135-144, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OFTYR-340 AND TYR-350, AND PHOSPHORYLATION AT TYR-340 AND TYR-350.

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