BRK1_HUMAN - dbPTM
BRK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID BRK1_HUMAN
UniProt AC Q8WUW1
Protein Name Protein BRICK1
Gene Name BRK1
Organism Homo sapiens (Human).
Sequence Length 75
Subcellular Localization Cytoplasm, cytoskeleton.
Protein Description Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex. As component of the WAVE1 complex, required for BDNF-NTRK2 endocytic trafficking and signaling from early endosomes (By similarity)..
Protein Sequence MAGQEDPVQREIHQDWANREYIEIITSSIKKIADFLNSFDMSCRSRLATLNEKLTALERRIEYIEARVTKGETLT
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------MAGQEDPVQ
------CCCCCCHHH
28.5122814378
21PhosphorylationQDWANREYIEIITSS
HHHHHHHHHHHHHHH
10.7030243723
21 (in isoform 2)Phosphorylation-10.7027642862
26PhosphorylationREYIEIITSSIKKIA
HHHHHHHHHHHHHHH
23.2930243723
27PhosphorylationEYIEIITSSIKKIAD
HHHHHHHHHHHHHHH
21.4730243723
28PhosphorylationYIEIITSSIKKIADF
HHHHHHHHHHHHHHH
29.7630243723
30UbiquitinationEIITSSIKKIADFLN
HHHHHHHHHHHHHHH
39.8221890473
30 (in isoform 1)Ubiquitination-39.8221890473
30UbiquitinationEIITSSIKKIADFLN
HHHHHHHHHHHHHHH
39.8221890473
30 (in isoform 2)Ubiquitination-39.8221890473
31 (in isoform 2)Ubiquitination-41.26-
31UbiquitinationIITSSIKKIADFLNS
HHHHHHHHHHHHHHH
41.2623000965
41SulfoxidationDFLNSFDMSCRSRLA
HHHHHCCHHHHHHHH
3.7221406390
46MethylationFDMSCRSRLATLNEK
CCHHHHHHHHHHHHH
14.69-
53 (in isoform 2)Ubiquitination-50.4921890473
53UbiquitinationRLATLNEKLTALERR
HHHHHHHHHHHHHHH
50.4923000965
532-HydroxyisobutyrylationRLATLNEKLTALERR
HHHHHHHHHHHHHHH
50.49-
53UbiquitinationRLATLNEKLTALERR
HHHHHHHHHHHHHHH
50.4921890473
53 (in isoform 1)Ubiquitination-50.4921890473
63 (in isoform 2)Phosphorylation-11.1627642862
63PhosphorylationALERRIEYIEARVTK
HHHHHHHHHHHHHCC
11.1625884760
70UbiquitinationYIEARVTKGETLT--
HHHHHHCCCCCCC--
52.4733845483
70 (in isoform 2)Ubiquitination-52.47-
70 (in isoform 1)Ubiquitination-52.4721890473
75PhosphorylationVTKGETLT-------
HCCCCCCC-------
43.9425332170

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

Oops, there are no upstream regulatory protein records of BRK1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of BRK1_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 BRK1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DTBP1_HUMANDTNBP1physical
25416956

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 BRK1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-63, AND MASSSPECTROMETRY.

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