COKA1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: COKA1_HUMAN
• UniProt AC: Q9P218
• Protein Name: Collagen alpha-1(XX) chain
• Gene Name: COL20A1
• Organism: Homo sapiens (Human).
• Sequence Length: 1284
• Subcellular Localization: Secreted, extracellular space .
• Protein Description: Probable collagen protein..
• Protein Sequence: MSSGDPAHLGLCLWLWLGATLGREQVQASGLLRLAVLPEDRLQMKWRESEGSGLGYLVQVKPMAGDSEQEVILTTKTPKATVGGLSPSKGYTLQIFELTGSGRFLLARREFVIEDLKSSSLDRSSQRPLGSGAPEPTPSHTGSPDPEQASEPQVAFTPSQDPRTPAGPQFRCLPPVPADMVFLVDGSWSIGHSHFQQVKDFLASVIAPFEIGPDKVQVGLTQYSGDAQTEWDLNSLSTKEQVLAAVRRLRYKGGNTFTGLALTHVLGQNLQPAAGLRPEAAKVVILVTDGKSQDDVHTAARVLKDLGVNVFAVGVKNADEAELRLLASPPRDITVHSVLDFLQLGALAGLLSRLICQRLQGGSPRQGPAAAPALDTLPAPTSLVLSQVTSSSIRLSWTPAPRHPLKYLIVWRASRGGTPREVVVEGPAASTELHNLASRTEYLVSVFPIYEGGVGEGLRGLVTTAPLPPPRALTLAAVTPRTVHLTWQPSAGATHYLVRCSPASPKGEEEEREVQVGRPEVLLDGLEPGRDYEVSVQSLRGPEGSEARGIRARTPTLAPPRHLGFSDVSHDAARVFWEGAPRPVRLVRVTYVSSEGGHSGQTEAPGNATSATLGPLSSSTTYTVRVTCLYPGGGSSTLTGRVTTKKAPSPSQLSMTELPGDAVQLAWVAAAPSGVLVYQITWTPLGEGKAHEISVPGNLGTAVLPGLGRHTEYDVTILAYYRDGARSDPVSLRYTPSTVSRSPPSNLALASETPDSLQVSWTPPLGRVLHYWLTYAPASGLGPEKSVSVPGARSHVTLPDLQAATKYRVLVSAIYAAGRSEAVSATGQTACPALRPDGSLPGFDLMVAFSLVEKAYASIRGVAMEPSAFGGTPTFTLFKDAQLTRRVSDVYPAPLPPEHTIVFLVRLLPETPREAFALWQMTAEDFQPLLGVLLDAGKKSLTYFHRDPRAALQEATFDPQEVRKIFFGSFHKVHVAVGRSKVRLYVDCRKVAERPLGEMGSPPAAGFVTLGRLAKARGPRSSSAAFQLQMLQIVCSDTWADEDRCCELPASRDGETCPAFVSACSCSSETPGPPGPQGPPGLPGRNGTPGEQGFPGPRGPPGVKGEKGDHGLPGLQGHPGHQGIPGRVGLQGPKGMRGLEGTAGLPGPPGPRGFQGMAGARGTSGERGPPGTVGPTGLPGPKGERGEKGEPQSLATLYQLVSQASHVSKFDSFHENTRPPMPILEQKLEPGTEPLGSPGTRSKALVPGEWGRGGRHLEGRGEPGAVGQMGSPGQQGASTQGLWE

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
52	Phosphorylation	KWRESEGSGLGYLVQ EEECCCCCCCCEEEE	27.13	-
56	Phosphorylation	SEGSGLGYLVQVKPM CCCCCCCEEEEEEEC	14.56	-
74	Phosphorylation	SEQEVILTTKTPKAT CCCEEEEEECCCCCC	18.34	-
86	Phosphorylation	KATVGGLSPSKGYTL CCCCCCCCCCCCCEE	30.33	24719451
117	Acetylation	EFVIEDLKSSSLDRS EEHHHHHHCCCCCCC	61.69	11794841
137 (in isoform 2)	Phosphorylation	-	35.44	22210691
139 (in isoform 2)	Phosphorylation	-	35.84	22210691
150 (in isoform 2)	Phosphorylation	-	49.88	22210691
328	Phosphorylation	AELRLLASPPRDITV HHHHHHCCCCCCCCH	35.09	26437602
376	Phosphorylation	AAAPALDTLPAPTSL CCCCCCCCCCCCCEE	35.18	24043423
381	Phosphorylation	LDTLPAPTSLVLSQV CCCCCCCCEEEEEEC	36.48	24043423
382	Phosphorylation	DTLPAPTSLVLSQVT CCCCCCCEEEEEECC	18.54	24043423
386	Phosphorylation	APTSLVLSQVTSSSI CCCEEEEEECCCCCE	18.35	24043423
389	Phosphorylation	SLVLSQVTSSSIRLS EEEEEECCCCCEEEE	18.43	24043423
390	Phosphorylation	LVLSQVTSSSIRLSW EEEEECCCCCEEEEE	24.19	24043423
391	Phosphorylation	VLSQVTSSSIRLSWT EEEECCCCCEEEEEC	22.03	24043423
392	Phosphorylation	LSQVTSSSIRLSWTP EEECCCCCEEEEECC	16.11	24043423
396	O-linked_Glycosylation	TSSSIRLSWTPAPRH CCCCEEEEECCCCCC	21.03	31637018
398	O-linked_Glycosylation	SSIRLSWTPAPRHPL CCEEEEECCCCCCCC	13.24	31637018
407	Phosphorylation	APRHPLKYLIVWRAS CCCCCCEEEEEEEEC	14.89	23532336
474	Phosphorylation	LPPPRALTLAAVTPR CCCCCEEEEEEECCC	17.23	32142685
479	Phosphorylation	ALTLAAVTPRTVHLT EEEEEEECCCEEEEE	11.43	24719451
545	Phosphorylation	SLRGPEGSEARGIRA ECCCCCCHHHCCCCC	26.82	-
554	Phosphorylation	ARGIRARTPTLAPPR HCCCCCCCCCCCCCC	21.46	-
556	Phosphorylation	GIRARTPTLAPPRHL CCCCCCCCCCCCCCC	34.63	-
594	Phosphorylation	VRVTYVSSEGGHSGQ EEEEEEECCCCCCCC	30.16	22817900
599	Phosphorylation	VSSEGGHSGQTEAPG EECCCCCCCCCCCCC	35.55	22817900
602	Phosphorylation	EGGHSGQTEAPGNAT CCCCCCCCCCCCCCC	37.33	22817900
607	N-linked_Glycosylation	GQTEAPGNATSATLG CCCCCCCCCCCCEEC	38.70	UniProtKB CARBOHYD
609	Phosphorylation	TEAPGNATSATLGPL CCCCCCCCCCEECCC	23.93	22817900
610	Phosphorylation	EAPGNATSATLGPLS CCCCCCCCCEECCCC	19.49	22817900
617	Phosphorylation	SATLGPLSSSTTYTV CCEECCCCCCCEEEE	25.94	22817900
618	Phosphorylation	ATLGPLSSSTTYTVR CEECCCCCCCEEEEE	39.11	22817900
619	Phosphorylation	TLGPLSSSTTYTVRV EECCCCCCCEEEEEE	22.76	22817900
639	Phosphorylation	GGGSSTLTGRVTTKK CCCCCEEEEEEECCC	24.03	-
643	Phosphorylation	STLTGRVTTKKAPSP CEEEEEEECCCCCCH	31.38	-
644	Phosphorylation	TLTGRVTTKKAPSPS EEEEEEECCCCCCHH	27.91	-
649	Phosphorylation	VTTKKAPSPSQLSMT EECCCCCCHHHCCCE	41.88	22210691
771	Phosphorylation	PLGRVLHYWLTYAPA CCHHHHHHHHHCCCC	9.65	26657352
779	Phosphorylation	WLTYAPASGLGPEKS HHHCCCCCCCCCCCC	33.23	26657352
856	Phosphorylation	FSLVEKAYASIRGVA HHHHHHHHHHHHCEE	16.37	25278378
858	Phosphorylation	LVEKAYASIRGVAME HHHHHHHHHHCEECC	10.51	25278378
888	Phosphorylation	AQLTRRVSDVYPAPL CCCEEEHHHCCCCCC	21.39	24719451
900	Phosphorylation	APLPPEHTIVFLVRL CCCCCHHEEEEEEEE	19.71	24719451
911	Phosphorylation	LVRLLPETPREAFAL EEEECCCCHHHHHHH	26.21	24719451
942	Phosphorylation	DAGKKSLTYFHRDPR HCCCCCEEEECCCHH	31.09	28509920
1088	Phosphorylation	GLPGRNGTPGEQGFP CCCCCCCCCCCCCCC	31.50	25002506
1142	Phosphorylation	GMRGLEGTAGLPGPP CCCCCCCCCCCCCCC	14.26	23612710
1172	Phosphorylation	GERGPPGTVGPTGLP CCCCCCCCCCCCCCC	28.23	-

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

Oops, there are no upstream regulatory protein records of COKA1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of COKA1_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 COKA1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FAM9B_HUMAN	FAM9B	physical	25416956
GGACT_HUMAN	GGACT	physical	28514442
TSC2_HUMAN	TSC2	physical	28514442
COEA1_HUMAN	COL14A1	physical	28514442
MEIS1_HUMAN	MEIS1	physical	28514442
CDN2C_HUMAN	CDKN2C	physical	28514442
PBX2_HUMAN	PBX2	physical	28514442

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.