dbPTM

CO5A2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CO5A2_HUMAN
UniProt AC	P05997
Protein Name	Collagen alpha-2(V) chain
Gene Name	COL5A2
Organism	Homo sapiens (Human).
Sequence Length	1499
Subcellular Localization	Secreted, extracellular space, extracellular matrix .
Protein Description	Type V collagen is a member of group I collagen (fibrillar forming collagen). It is a minor connective tissue component of nearly ubiquitous distribution. Type V collagen binds to DNA, heparan sulfate, thrombospondin, heparin, and insulin. Type V collagen is a key determinant in the assembly of tissue-specific matrices (By similarity)..
Protein Sequence	MMANWAEARPLLILIVLLGQFVSIKAQEEDEDEGYGEEIACTQNGQMYLNRDIWKPAPCQICVCDNGAILCDKIECQDVLDCADPVTPPGECCPVCSQTPGGGNTNFGRGRKGQKGEPGLVPVVTGIRGRPGPAGPPGSQGPRGERGPKGRPGPRGPQGIDGEPGVPGQPGAPGPPGHPSHPGPDGLSRPFSAQMAGLDEKSGLGSQVGLMPGSVGPVGPRGPQGLQGQQGGAGPTGPPGEPGDPGPMGPIGSRGPEGPPGKPGEDGEPGRNGNPGEVGFAGSPGARGFPGAPGLPGLKGHRGHKGLEGPKGEVGAPGSKGEAGPTGPMGAMGPLGPRGMPGERGRLGPQGAPGQRGAHGMPGKPGPMGPLGIPGSSGFPGNPGMKGEAGPTGARGPEGPQGQRGETGPPGPVGSPGLPGAIGTDGTPGAKGPTGSPGTSGPPGSAGPPGSPGPQGSTGPQGIRGQPGDPGVPGFKGEAGPKGEPGPHGIQGPIGPPGEEGKRGPRGDPGTVGPPGPVGERGAPGNRGFPGSDGLPGPKGAQGERGPVGSSGPKGSQGDPGRPGEPGLPGARGLTGNPGVQGPEGKLGPLGAPGEDGRPGPPGSIGIRGQPGSMGLPGPKGSSGDPGKPGEAGNAGVPGQRGAPGKDGEVGPSGPVGPPGLAGERGEQGPPGPTGFQGLPGPPGPPGEGGKPGDQGVPGDPGAVGPLGPRGERGNPGERGEPGITGLPGEKGMAGGHGPDGPKGSPGPSGTPGDTGPPGLQGMPGERGIAGTPGPKGDRGGIGEKGAEGTAGNDGARGLPGPLGPPGPAGPTGEKGEPGPRGLVGPPGSRGNPGSRGENGPTGAVGFAGPQGPDGQPGVKGEPGEPGQKGDAGSPGPQGLAGSPGPHGPNGVPGLKGGRGTQGPPGATGFPGSAGRVGPPGPAGAPGPAGPLGEPGKEGPPGLRGDPGSHGRVGDRGPAGPPGGPGDKGDPGEDGQPGPDGPPGPAGTTGQRGIVGMPGQRGERGMPGLPGPAGTPGKVGPTGATGDKGPPGPVGPPGSNGPVGEPGPEGPAGNDGTPGRDGAVGERGDRGDPGPAGLPGSQGAPGTPGPVGAPGDAGQRGDPGSRGPIGPPGRAGKRGLPGPQGPRGDKGDHGDRGDRGQKGHRGFTGLQGLPGPPGPNGEQGSAGIPGPFGPRGPPGPVGPSGKEGNPGPLGPIGPPGVRGSVGEAGPEGPPGEPGPPGPPGPPGHLTAALGDIMGHYDESMPDPLPEFTEDQAAPDDKNKTDPGVHATLKSLSSQIETMRSPDGSKKHPARTCDDLKLCHSAKQSGEYWIDPNQGSVEDAIKVYCNMETGETCISANPSSVPRKTWWASKSPDNKPVWYGLDMNRGSQFAYGDHQSPNTAITQMTFLRLLSKEASQNITYICKNSVGYMDDQAKNLKKAVVLKGANDLDIKAEGNIRFRYIVLQDTCSKRNGNVGKTVFEYRTQNVARLPIIDLAPVDVGGTDQEFGVEIGPVCFV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
139	Phosphorylation	GPAGPPGSQGPRGER CCCCCCCCCCCCCCC	37.42	-
188	O-linked_Glycosylation	HPGPDGLSRPFSAQM CCCCCCCCCCCHHHH	43.36	OGP
236	Phosphorylation	QQGGAGPTGPPGEPG CCCCCCCCCCCCCCC	62.49	30242111
253	Phosphorylation	GPMGPIGSRGPEGPP CCCCCCCCCCCCCCC	34.48	30242111
283	Phosphorylation	GEVGFAGSPGARGFP CCCCCCCCCCCCCCC	19.41	24719451
290	Hydroxylation	SPGARGFPGAPGLPG CCCCCCCCCCCCCCC	40.64	8181482
293	Hydroxylation	ARGFPGAPGLPGLKG CCCCCCCCCCCCCCC	51.25	8181482
296	Hydroxylation	FPGAPGLPGLKGHRG CCCCCCCCCCCCCCC	52.57	8181482
319	Phosphorylation	GEVGAPGSKGEAGPT CCCCCCCCCCCCCCC	36.11	23879269
326	Phosphorylation	SKGEAGPTGPMGAMG CCCCCCCCCCCCCCC	53.66	-
376	Phosphorylation	GPLGIPGSSGFPGNP CCCCCCCCCCCCCCC	23.18	-
575	Phosphorylation	LPGARGLTGNPGVQG CCCCCCCCCCCCCCC	37.42	30576742
604	Phosphorylation	GRPGPPGSIGIRGQP CCCCCCCCCCCCCCC	24.34	22210691
611	Hydroxylation	SIGIRGQPGSMGLPG CCCCCCCCCCCCCCC	39.38	8181482
613	Phosphorylation	GIRGQPGSMGLPGPK CCCCCCCCCCCCCCC	19.16	22210691
617	Hydroxylation	QPGSMGLPGPKGSSG CCCCCCCCCCCCCCC	51.84	8181482
725	Phosphorylation	ERGEPGITGLPGEKG CCCCCCCCCCCCCCC	38.28	23403867
745	Phosphorylation	GPDGPKGSPGPSGTP CCCCCCCCCCCCCCC	32.58	23532336
749	Phosphorylation	PKGSPGPSGTPGDTG CCCCCCCCCCCCCCC	62.30	23532336
772	Phosphorylation	GERGIAGTPGPKGDR CCCCCCCCCCCCCCC	18.95	24670416
785	Ubiquitination	DRGGIGEKGAEGTAG CCCCCCCCCCCCCCC	59.20	-
790	Phosphorylation	GEKGAEGTAGNDGAR CCCCCCCCCCCCCCC	23.93	-
901	Phosphorylation	GLKGGRGTQGPPGAT CCCCCCCCCCCCCCC	29.05	-
908	Phosphorylation	TQGPPGATGFPGSAG CCCCCCCCCCCCCCC	45.32	-
913	Phosphorylation	GATGFPGSAGRVGPP CCCCCCCCCCCCCCC	27.99	-
919	Hydroxylation	GSAGRVGPPGPAGAP CCCCCCCCCCCCCCC	28.02	21757687
988	Phosphorylation	GPPGPAGTTGQRGIV CCCCCCCCCCCCCCC	29.84	-
989	Phosphorylation	PPGPAGTTGQRGIVG CCCCCCCCCCCCCCC	30.33	-
1015	O-linked_Glycosylation	GLPGPAGTPGKVGPT CCCCCCCCCCCCCCC	30.86	55826725
1148	Phosphorylation	QKGHRGFTGLQGLPG CCCCCCCCCCCCCCC	39.54	28634298
1156	Hydroxylation	GLQGLPGPPGPNGEQ CCCCCCCCCCCCCCC	28.83	21757687
1262	N-linked_Glycosylation	QAAPDDKNKTDPGVH CCCCCCCCCCCHHHH	60.50	UniProtKB CARBOHYD
1276	Phosphorylation	HATLKSLSSQIETMR HHHHHHHHHHHHHCC	27.56	-
1277	Phosphorylation	ATLKSLSSQIETMRS HHHHHHHHHHHHCCC	40.23	-
1281	Phosphorylation	SLSSQIETMRSPDGS HHHHHHHHCCCCCCC	21.36	-
1284	Phosphorylation	SQIETMRSPDGSKKH HHHHHCCCCCCCCCC	19.27	-
1398	Phosphorylation	RLLSKEASQNITYIC HHHCHHHHCCCEEEE	25.50	30377224
1400	N-linked_Glycosylation	LSKEASQNITYICKN HCHHHHCCCEEEECC	26.52	UniProtKB CARBOHYD
1402	Phosphorylation	KEASQNITYICKNSV HHHHCCCEEEECCCC	17.87	30377224
1403	Phosphorylation	EASQNITYICKNSVG HHHCCCEEEECCCCC	10.67	30377224

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 CO5A2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
919	P	Hydroxylation	21757687
Probably 3-hydroxylated on Pro-919 and Pro-1156 by LEPREL1.
1156	P	Hydroxylation	21757687
Probably 3-hydroxylated on Pro-919 and Pro-1156 by LEPREL1.

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 CO5A2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CO5A2_HUMAN !!

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
130000	Ehlers-Danlos syndrome, classic type (EDS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CO5A2_HUMAN

Related Literatures of Post-Translational Modification

Hydroxylation
Reference	PubMed
"A role for prolyl 3-hydroxylase 2 in post-translational modificationof fibril-forming collagens."; Fernandes R.J., Farnand A.W., Traeger G.R., Weis M.A., Eyre D.R.; J. Biol. Chem. 286:30662-30669(2011). Cited for: HYDROXYLATION AT PRO-919 AND PRO-1156, AND MASS SPECTROMETRY.	21757687 [Abstract]

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