SGCB_HUMAN - dbPTM
SGCB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SGCB_HUMAN
UniProt AC Q16585
Protein Name Beta-sarcoglycan
Gene Name SGCB
Organism Homo sapiens (Human).
Sequence Length 318
Subcellular Localization Cell membrane, sarcolemma
Single-pass type II membrane protein. Cytoplasm, cytoskeleton.
Protein Description Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix..
Protein Sequence MAAAAAAAAEQQSSNGPVKKSMREKAVERRSVNKEHNSNFKAGYIPIDEDRLHKTGLRGRKGNLAICVIILLFILAVINLIITLVIWAVIRIGPNGCDSMEFHESGLLRFKQVSDMGVIHPLYKSTVGGRRNENLVITGNNQPIVFQQGTTKLSVENNKTSITSDIGMQFFDPRTQNILFSTDYETHEFHLPSGVKSLNVQKASTERITSNATSDLNIKVDGRAIVRGNEGVFIMGKTIEFHMGGNMELKAENSIILNGSVMVSTTRLPSSSSGDQLGSGDWVRYKLCMCADGTLFKVQVTSQNMGCQISDNPCGNTH
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
13PhosphorylationAAAAEQQSSNGPVKK
HHHHHHHHCCCCCCH
26.0128857561
21PhosphorylationSNGPVKKSMREKAVE
CCCCCCHHHHHHHHH
19.8424275569
31PhosphorylationEKAVERRSVNKEHNS
HHHHHHHCCCHHCCC
35.9429514088
34UbiquitinationVERRSVNKEHNSNFK
HHHHCCCHHCCCCCC
59.19-
41UbiquitinationKEHNSNFKAGYIPID
HHCCCCCCCEEEECC
45.1921906983
41MalonylationKEHNSNFKAGYIPID
HHCCCCCCCEEEECC
45.1926320211
41UbiquitinationKEHNSNFKAGYIPID
HHCCCCCCCEEEECC
45.19-
44PhosphorylationNSNFKAGYIPIDEDR
CCCCCCEEEECCHHH
14.3725884760
54UbiquitinationIDEDRLHKTGLRGRK
CCHHHHHHCCCCCCC
49.21-
82UbiquitinationLAVINLIITLVIWAV
HHHHHHHHHHHHHHH
2.48-
111UbiquitinationESGLLRFKQVSDMGV
HHCCEEEEEECCCCC
43.2721906983
123PhosphorylationMGVIHPLYKSTVGGR
CCCEEEEEECCCCCC
13.8229116813
124UbiquitinationGVIHPLYKSTVGGRR
CCEEEEEECCCCCCC
47.5421906983
126UbiquitinationIHPLYKSTVGGRRNE
EEEEEECCCCCCCCC
21.01-
132UbiquitinationSTVGGRRNENLVITG
CCCCCCCCCCEEEEC
40.94-
149UbiquitinationQPIVFQQGTTKLSVE
CCEEEECCCEEEEEE
25.27-
152UbiquitinationVFQQGTTKLSVENNK
EEECCCEEEEEECCC
38.3121906983
158N-linked_GlycosylationTKLSVENNKTSITSD
EEEEEECCCCEEEEE
35.1619159218
196UbiquitinationFHLPSGVKSLNVQKA
EECCCCCEEECCCCC
53.3921906983
202UbiquitinationVKSLNVQKASTERIT
CEEECCCCCCCCEEC
39.7721906983
211N-linked_GlycosylationSTERITSNATSDLNI
CCCEECCCCCCCCEE
38.2919159218
216UbiquitinationTSNATSDLNIKVDGR
CCCCCCCCEEEECCE
7.76-
219UbiquitinationATSDLNIKVDGRAIV
CCCCCEEEECCEEEE
32.9521906983
258N-linked_GlycosylationAENSIILNGSVMVST
EECEEEECCEEEEEE
30.22UniProtKB CARBOHYD
264PhosphorylationLNGSVMVSTTRLPSS
ECCEEEEEECCCCCC
13.1327732954
265PhosphorylationNGSVMVSTTRLPSSS
CCEEEEEECCCCCCC
12.4327732954
266PhosphorylationGSVMVSTTRLPSSSS
CEEEEEECCCCCCCC
23.7827732954
286UbiquitinationSGDWVRYKLCMCADG
CCCCEEEEEEEECCC
25.33-

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 SGCB_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SGCB_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 SGCB_HUMAN !!

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

Oops, there are no PPI records of SGCB_HUMAN !!

Drug and Disease Associations
Kegg Disease
H00565 Sarcoglycanopathies, including: Limb-girdle muscular dystrophy (LGMD) 2C; Limb-girdle muscular dystr
H00593 Limb-girdle muscular dystrophy (LGMD)
OMIM Disease
604286Limb-girdle muscular dystrophy 2E (LGMD2E)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SGCB_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-158 AND ASN-211, AND MASSSPECTROMETRY.

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