dbPTM

C1QA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	C1QA_HUMAN
UniProt AC	P02745
Protein Name	Complement C1q subcomponent subunit A
Gene Name	C1QA
Organism	Homo sapiens (Human).
Sequence Length	245
Subcellular Localization	Secreted.
Protein Description	C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes..
Protein Sequence	MEGPRGWLVLCVLAISLASMVTEDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIRTGIQGLKGDQGEPGPSGNPGKVGYPGPSGPLGARGIPGIKGTKGSPGNIKDQPRPAFSAIRRNPPMGGNVVIFDTVITNQEEPYQNHSGRFVCTVPGYYYFTFQVLSQWEICLSIVSSSRGQVRRSLGFCDTTNKGLFQVVSGGMVLQLQQGDQVWVEKDPKKGHIYQGSEADSVFSGFLIFPSA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Hydroxylation	CRAPDGKKGEAGRPG HCCCCCCCCCCCCCC	68.46	486087
33	O-linked_Glycosylation	CRAPDGKKGEAGRPG HCCCCCCCCCCCCCC	68.46	486087
39	Hydroxylation	KKGEAGRPGRRGRPG CCCCCCCCCCCCCCC	39.46	486087
45	Hydroxylation	RPGRRGRPGLKGEQG CCCCCCCCCCCCCCC	56.12	486087
48	Hydroxylation	RRGRPGLKGEQGEPG CCCCCCCCCCCCCCC	67.33	486087
48	O-linked_Glycosylation	RRGRPGLKGEQGEPG CCCCCCCCCCCCCCC	67.33	486087
54	Hydroxylation	LKGEQGEPGAPGIRT CCCCCCCCCCCCHHH	51.58	486087
57	Hydroxylation	EQGEPGAPGIRTGIQ CCCCCCCCCHHHCCC	44.66	486087
67	Hydroxylation	RTGIQGLKGDQGEPG HHCCCCCCCCCCCCC	68.23	486087
67	O-linked_Glycosylation	RTGIQGLKGDQGEPG HHCCCCCCCCCCCCC	68.23	486087
73	Hydroxylation	LKGDQGEPGPSGNPG CCCCCCCCCCCCCCC	67.81	486087
79	Hydroxylation	EPGPSGNPGKVGYPG CCCCCCCCCCCCCCC	47.73	486087
85	Hydroxylation	NPGKVGYPGPSGPLG CCCCCCCCCCCCCCC	42.14	486087
100	Hydroxylation	ARGIPGIKGTKGSPG CCCCCCCCCCCCCCC	67.45	486087
100	O-linked_Glycosylation	ARGIPGIKGTKGSPG CCCCCCCCCCCCCCC	67.45	486087
103	Hydroxylation	IPGIKGTKGSPGNIK CCCCCCCCCCCCCCC	67.09	-
146	N-linked_Glycosylation	NQEEPYQNHSGRFVC CCCCCCCCCCCCEEE	26.00	17623646
146	N-linked_Glycosylation	NQEEPYQNHSGRFVC CCCCCCCCCCCCEEE	26.00	16335952
174	Phosphorylation	SQWEICLSIVSSSRG CCHHHHHHHHHCCCC	19.28	-

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 C1QA_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of C1QA_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 C1QA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PGS2_HUMAN	DCN	physical	1431141
C1S_HUMAN	C1S	physical	10878362
C1R_HUMAN	C1R	physical	10878362
FINC_HUMAN	FN1	physical	6981115
UBQL2_HUMAN	UBQLN2	physical	21988832
SGTA_HUMAN	SGTA	physical	21988832
PIAS2_HUMAN	PIAS2	physical	21988832
UBQL1_HUMAN	UBQLN1	physical	21988832
GNA1_HUMAN	GNPNAT1	physical	21988832
RAC1_HUMAN	RAC1	physical	25301945

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613652	Complement component C1q deficiency (C1QD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of C1QA_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-146, AND MASSSPECTROMETRY.	19159218 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-146, AND MASSSPECTROMETRY.	16335952 [Abstract]