SGCD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SGCD_HUMAN
• UniProt AC: Q92629
• Protein Name: Delta-sarcoglycan
• Gene Name: SGCD
• Organism: Homo sapiens (Human).
• Sequence Length: 289
• 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: MPQEQYTHHRSTMPGSVGPQVYKVGIYGWRKRCLYFFVLLLMILILVNLAMTIWILKVMNFTIDGMGNLRITEKGLKLEGDSEFLQPLYAKEIQSRPGNALYFKSARNVTVNILNDQTKVLTQLITGPKAVEAYGKKFEVKTVSGKLLFSADNNEVVVGAERLRVLGAEGTVFPKSIETPNVRADPFKELRLESPTRSLVMEAPKGVEINAEAGNMEATCRTELRLESKDGEIKLDAAKIRLPRLPHGSYTPTGTRQKVFEICVCANGRLFLSQAGAGSTCQINTSVCL

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
11	Phosphorylation	EQYTHHRSTMPGSVG HHCCCCCCCCCCCCC	25.38	28857561
12	Phosphorylation	QYTHHRSTMPGSVGP HCCCCCCCCCCCCCC	27.60	28857561
16	Phosphorylation	HRSTMPGSVGPQVYK CCCCCCCCCCCCEEE	20.31	23312004
22	Phosphorylation	GSVGPQVYKVGIYGW CCCCCCEEEEEECHH	8.49	21214269
60	N-linked_Glycosylation	IWILKVMNFTIDGMG HHHHHHHCCEECCCC	33.62	UniProtKB CARBOHYD
108	N-linked_Glycosylation	LYFKSARNVTVNILN EEEEECCCEEEEEEC	33.26	UniProtKB CARBOHYD
110	Phosphorylation	FKSARNVTVNILNDQ EEECCCEEEEEECCH	16.04	28555341
118	Phosphorylation	VNILNDQTKVLTQLI EEEECCHHHHHHHHH	26.45	28555341
122	Phosphorylation	NDQTKVLTQLITGPK CCHHHHHHHHHHCHH	25.07	24719451
123	Phosphorylation	DQTKVLTQLITGPKA CHHHHHHHHHHCHHH	27.06	24719451
126	Phosphorylation	KVLTQLITGPKAVEA HHHHHHHHCHHHHHH	56.90	28555341
194	Phosphorylation	FKELRLESPTRSLVM CCCCCCCCCCCEEEE	35.84	18088087
195	Phosphorylation	KELRLESPTRSLVME CCCCCCCCCCEEEEE	23.58	18088087
196	Phosphorylation	ELRLESPTRSLVMEA CCCCCCCCCEEEEEC	42.01	18088087
197	Phosphorylation	LRLESPTRSLVMEAP CCCCCCCCEEEEECC	31.23	18088087
253	Phosphorylation	PHGSYTPTGTRQKVF CCCCCCCCCCCCEEE	43.30	22210691
255	Phosphorylation	GSYTPTGTRQKVFEI CCCCCCCCCCEEEEE	32.19	22210691
284	N-linked_Glycosylation	AGSTCQINTSVCL-- CCCCCEEECCEEC--	10.62	UniProtKB CARBOHYD

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SGCD_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SGCD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FLNC_HUMAN	FLNC	physical	14506720
SGCB_HUMAN	SGCB	physical	26186194
CD032_HUMAN	C4orf32	physical	26186194
DNJB9_HUMAN	DNAJB9	physical	26186194
CJ035_HUMAN	C10orf35	physical	26186194
CD032_HUMAN	C4orf32	physical	28514442
DNJB9_HUMAN	DNAJB9	physical	28514442
PPAL_HUMAN	ACP2	physical	28514442
CJ035_HUMAN	C10orf35	physical	28514442

Drug and Disease Associations

• Kegg Disease
• H00294: Dilated cardiomyopathy (DCM)
• H00565: Sarcoglycanopathies, including: Limb-girdle muscular dystrophy (LGMD) 2C; Limb-girdle muscular dystr
• H00593: Limb-girdle muscular dystrophy (LGMD)
• OMIM Disease
• 601287: Limb-girdle muscular dystrophy 2F (LGMD2F)
• 606685: Cardiomyopathy, dilated 1L (CMD1L)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND THR-196, ANDMASS SPECTROMETRY.
PubMed: 18088087