CO4A3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CO4A3_HUMAN
• UniProt AC: Q01955
• Protein Name: Collagen alpha-3(IV) chain
• Gene Name: COL4A3
• Organism: Homo sapiens (Human).
• Sequence Length: 1670
• Subcellular Localization: Secreted, extracellular space, extracellular matrix, basement membrane. Colocalizes with COL4A4 and COL4A5 in GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL)..
• Protein Description: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; Tumstatin, a cleavage fragment corresponding to the collagen alpha 3(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor cell activity; these two anti-tumor properties may be regulated via RGD-independent ITGB3-mediated mechanisms..
• Protein Sequence: MSARTAPRPQVLLLPLLLVLLAAAPAASKGCVCKDKGQCFCDGAKGEKGEKGFPGPPGSPGQKGFTGPEGLPGPQGPKGFPGLPGLTGSKGVRGISGLPGFSGSPGLPGTPGNTGPYGLVGVPGCSGSKGEQGFPGLPGTLGYPGIPGAAGLKGQKGAPAKEEDIELDAKGDPGLPGAPGPQGLPGPPGFPGPVGPPGPPGFFGFPGAMGPRGPKGHMGERVIGHKGERGVKGLTGPPGPPGTVIVTLTGPDNRTDLKGEKGDKGAMGEPGPPGPSGLPGESYGSEKGAPGDPGLQGKPGKDGVPGFPGSEGVKGNRGFPGLMGEDGIKGQKGDIGPPGFRGPTEYYDTYQEKGDEGTPGPPGPRGARGPQGPSGPPGVPGSPGSSRPGLRGAPGWPGLKGSKGERGRPGKDAMGTPGSPGCAGSPGLPGSPGPPGPPGDIVFRKGPPGDHGLPGYLGSPGIPGVDGPKGEPGLLCTQCPYIPGPPGLPGLPGLHGVKGIPGRQGAAGLKGSPGSPGNTGLPGFPGFPGAQGDPGLKGEKGETLQPEGQVGVPGDPGLRGQPGRKGLDGIPGTPGVKGLPGPKGELALSGEKGDQGPPGDPGSPGSPGPAGPAGPPGYGPQGEPGLQGTQGVPGAPGPPGEAGPRGELSVSTPVPGPPGPPGPPGHPGPQGPPGIPGSLGKCGDPGLPGPDGEPGIPGIGFPGPPGPKGDQGFPGTKGSLGCPGKMGEPGLPGKPGLPGAKGEPAVAMPGGPGTPGFPGERGNSGEHGEIGLPGLPGLPGTPGNEGLDGPRGDPGQPGPPGEQGPPGRCIEGPRGAQGLPGLNGLKGQQGRRGKTGPKGDPGIPGLDRSGFPGETGSPGIPGHQGEMGPLGQRGYPGNPGILGPPGEDGVIGMMGFPGAIGPPGPPGNPGTPGQRGSPGIPGVKGQRGTPGAKGEQGDKGNPGPSEISHVIGDKGEPGLKGFAGNPGEKGNRGVPGMPGLKGLKGLPGPAGPPGPRGDLGSTGNPGEPGLRGIPGSMGNMGMPGSKGKRGTLGFPGRAGRPGLPGIHGLQGDKGEPGYSEGTRPGPPGPTGDPGLPGDMGKKGEMGQPGPPGHLGPAGPEGAPGSPGSPGLPGKPGPHGDLGFKGIKGLLGPPGIRGPPGLPGFPGSPGPMGIRGDQGRDGIPGPAGEKGETGLLRAPPGPRGNPGAQGAKGDRGAPGFPGLPGRKGAMGDAGPRGPTGIEGFPGPPGLPGAIIPGQTGNRGPPGSRGSPGAPGPPGPPGSHVIGIKGDKGSMGHPGPKGPPGTAGDMGPPGRLGAPGTPGLPGPRGDPGFQGFPGVKGEKGNPGFLGSIGPPGPIGPKGPPGVRGDPGTLKIISLPGSPGPPGTPGEPGMQGEPGPPGPPGNLGPCGPRGKPGKDGKPGTPGPAGEKGNKGSKGEPGPAGSDGLPGLKGKRGDSGSPATWTTRGFVFTRHSQTTAIPSCPEGTVPLYSGFSFLFVQGNQRAHGQDLGTLGSCLQRFTTMPFLFCNVNDVCNFASRNDYSYWLSTPALMPMNMAPITGRALEPYISRCTVCEGPAIAIAVHSQTTDIPPCPHGWISLWKGFSFIMFTSAGSEGTGQALASPGSCLEEFRASPFLECHGRGTCNYYSNSYSFWLASLNPERMFRKPIPSTVKAGELEKIISRCQVCMKKRH

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
2	Phosphorylation	------MSARTAPRP ------CCCCCCCCH	37.45	22210691
5	Phosphorylation	---MSARTAPRPQVL ---CCCCCCCCHHHH	40.50	22210691
28	Phosphorylation	LAAAPAASKGCVCKD HHHCHHHHCCCEECC	31.52	22210691
235	Phosphorylation	ERGVKGLTGPPGPPG CCCCCCCCCCCCCCC	57.20	-
243	Phosphorylation	GPPGPPGTVIVTLTG CCCCCCCEEEEEEEC	16.91	-
249	Phosphorylation	GTVIVTLTGPDNRTD CEEEEEEECCCCCCC	36.98	-
253	N-linked_Glycosylation	VTLTGPDNRTDLKGE EEEECCCCCCCCCCC	52.46	UniProtKB CARBOHYD
382	Phosphorylation	GPPGVPGSPGSSRPG CCCCCCCCCCCCCCC	21.73	-
386	Phosphorylation	VPGSPGSSRPGLRGA CCCCCCCCCCCCCCC	48.70	24719451
835	Phosphorylation	QQGRRGKTGPKGDPG CCCCCCCCCCCCCCC	62.63	-
1001	Ubiquitination	GPRGDLGSTGNPGEP CCCCCCCCCCCCCCC	40.20	17370265
1059	Phosphorylation	DKGEPGYSEGTRPGP CCCCCCCCCCCCCCC	35.15	24719451
1206	Methylation	FPGLPGRKGAMGDAG CCCCCCCCCCCCCCC	57.86	-
1206	"N6,N6-dimethyllysine"	FPGLPGRKGAMGDAG CCCCCCCCCCCCCCC	57.86	-
1246	Phosphorylation	GNRGPPGSRGSPGAP CCCCCCCCCCCCCCC	38.96	-
1249	Phosphorylation	GPPGSRGSPGAPGPP CCCCCCCCCCCCCCC	21.03	-
1379	Ubiquitination	QGEPGPPGPPGNLGP CCCCCCCCCCCCCCC	44.14	17370265
1401	Phosphorylation	GKDGKPGTPGPAGEK CCCCCCCCCCCCCCC	33.33	22210691
1414	Ubiquitination	EKGNKGSKGEPGPAG CCCCCCCCCCCCCCC	75.79	17370265
1422	Phosphorylation	GEPGPAGSDGLPGLK CCCCCCCCCCCCCCC	30.52	28111955
1429	Acetylation	SDGLPGLKGKRGDSG CCCCCCCCCCCCCCC	69.19	23236377
1435	Phosphorylation	LKGKRGDSGSPATWT CCCCCCCCCCCCCEE	43.95	7768924
1443	Phosphorylation	GSPATWTTRGFVFTR CCCCCEEECEEEEEE	21.98	-
1452	Phosphorylation	GFVFTRHSQTTAIPS EEEEEECCCCCCCCC	26.40	7768924
1519	Phosphorylation	NFASRNDYSYWLSTP CCCCCCCCCEEECCC	13.75	24275569
1525	Phosphorylation	DYSYWLSTPALMPMN CCCEEECCCCCCCCC	15.48	24275569
1537	Phosphorylation	PMNMAPITGRALEPY CCCCCCCCCCCCCCC	21.40	24275569
1544	Phosphorylation	TGRALEPYISRCTVC CCCCCCCCHHHCEEE	11.36	24275569
1546	Phosphorylation	RALEPYISRCTVCEG CCCCCCHHHCEEECC	18.56	24275569
1612 (in isoform 2)	Phosphorylation	-	36.54	7758473
1648	Phosphorylation	MFRKPIPSTVKAGEL HHCCCCCCCCHHHHH	46.69	22199227
1649	Phosphorylation	FRKPIPSTVKAGELE HCCCCCCCCHHHHHH	22.22	22199227

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
1435	S	Phosphorylation	Kinase	COL4A3BP	Q9Y5P4	PSP
1435	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
1452	S	Phosphorylation	Kinase	PRKACA	P00517	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CO4A3_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 CO4A3_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of CO4A3_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• : Note=Autoantibodies against the NC1 domain of alpha 3(IV) are found in Goodpasture syndrome, an autoimmune disease of lung and kidney.
• 203780:
• 141200: Hematuria, benign familial (BFH)
• 104200: Alport syndrome, autosomal dominant (APSAD)
• 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

Ubiquitylation

"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1414, AND MASSSPECTROMETRY.
PubMed: 17370265