dbPTM

C1QR1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	C1QR1_HUMAN
UniProt AC	Q9NPY3
Protein Name	Complement component C1q receptor
Gene Name	CD93
Organism	Homo sapiens (Human).
Sequence Length	652
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	Receptor (or element of a larger receptor complex) for C1q, mannose-binding lectin (MBL2) and pulmonary surfactant protein A (SPA). May mediate the enhancement of phagocytosis in monocytes and macrophages upon interaction with soluble defense collagens. May play a role in intercellular adhesion..
Protein Sequence	MATSMGLLLLLLLLLTQPGAGTGADTEAVVCVGTACYTAHSGKLSAAEAQNHCNQNGGNLATVKSKEEAQHVQRVLAQLLRREAALTARMSKFWIGLQREKGKCLDPSLPLKGFSWVGGGEDTPYSNWHKELRNSCISKRCVSLLLDLSQPLLPSRLPKWSEGPCGSPGSPGSNIEGFVCKFSFKGMCRPLALGGPGQVTYTTPFQTTSSSLEAVPFASAANVACGEGDKDETQSHYFLCKEKAPDVFDWGSSGPLCVSPKYGCNFNNGGCHQDCFEGGDGSFLCGCRPGFRLLDDLVTCASRNPCSSSPCRGGATCVLGPHGKNYTCRCPQGYQLDSSQLDCVDVDECQDSPCAQECVNTPGGFRCECWVGYEPGGPGEGACQDVDECALGRSPCAQGCTNTDGSFHCSCEEGYVLAGEDGTQCQDVDECVGPGGPLCDSLCFNTQGSFHCGCLPGWVLAPNGVSCTMGPVSLGPPSGPPDEEDKGEKEGSTVPRAATASPTRGPEGTPKATPTTSRPSLSSDAPITSAPLKMLAPSGSPGVWREPSIHHATAASGPQEPAGGDSSVATQNNDGTDGQKLLLFYILGTVVAILLLLALALGLLVYRKRRAKREEKKEKKPQNAADSYSWVPERAESRAMENQYSPTPGTDC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
87	Phosphorylation	LRREAALTARMSKFW HHHHHHHHHHHHHHH	13.90	23532336
91	Phosphorylation	AALTARMSKFWIGLQ HHHHHHHHHHHHCCC	21.10	-
143	Phosphorylation	CISKRCVSLLLDLSQ HHHHHHHHHHHHHCC	19.54	-
149	Phosphorylation	VSLLLDLSQPLLPSR HHHHHHHCCCCCCCC	29.44	-
155	Phosphorylation	LSQPLLPSRLPKWSE HCCCCCCCCCCCCCC	46.55	25278378
167	Phosphorylation	WSEGPCGSPGSPGSN CCCCCCCCCCCCCCC	32.57	-
170	Phosphorylation	GPCGSPGSPGSNIEG CCCCCCCCCCCCCCC	29.49	-
173	Phosphorylation	GSPGSPGSNIEGFVC CCCCCCCCCCCCEEE	37.71	-
183	Phosphorylation	EGFVCKFSFKGMCRP CCEEEEEEECCCCCE	16.14	29496963
325	N-linked_Glycosylation	VLGPHGKNYTCRCPQ EECCCCCCEECCCCC	41.77	UniProtKB CARBOHYD
473	O-linked_Glycosylation	SCTMGPVSLGPPSGP EEEECCCCCCCCCCC	30.64	OGP
492	Phosphorylation	DKGEKEGSTVPRAAT CCCCCCCCCCCCCCC	27.59	23532336
553	O-linked_Glycosylation	EPSIHHATAASGPQE CCCHHEECCCCCCCC	20.57	OGP
607	Methylation	ALGLLVYRKRRAKRE HHHHHHHHHHHHHHH	20.65	-
627	Phosphorylation	KPQNAADSYSWVPER CCCCHHHCCCCCHHH	19.15	28857561
628	Phosphorylation	PQNAADSYSWVPERA CCCHHHCCCCCHHHH	13.70	22817900
629	Phosphorylation	QNAADSYSWVPERAE CCHHHCCCCCHHHHH	26.08	-
637	Phosphorylation	WVPERAESRAMENQY CCHHHHHHHHHHHCC	25.10	28857561
644	Phosphorylation	SRAMENQYSPTPGTD HHHHHHCCCCCCCCC	28.35	22817900
645	Phosphorylation	RAMENQYSPTPGTDC HHHHHCCCCCCCCCC	16.72	28857561
647	Phosphorylation	MENQYSPTPGTDC-- HHHCCCCCCCCCC--	28.54	28857561

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
628	Y	Phosphorylation	Kinase	SRC	P12931	PSP
644	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of C1QR1_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 C1QR1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GIPC1_HUMAN	GIPC1	physical	15459234
RHG15_HUMAN	ARHGAP15	physical	15459234
SCYL1_HUMAN	SCYL1	physical	15459234
FA46A_HUMAN	FAM46A	physical	21988832
UBQL2_HUMAN	UBQLN2	physical	21988832
MYD88_HUMAN	MYD88	physical	21988832
CSN5_HUMAN	COPS5	physical	21988832
SYRC_HUMAN	RARS	physical	28514442
KCD17_HUMAN	KCTD17	physical	28514442
ASPH_HUMAN	ASPH	physical	28514442
RN114_HUMAN	RNF114	physical	28514442
MEMO1_HUMAN	MEMO1	physical	28514442
PPAL_HUMAN	ACP2	physical	28514442
ORC4_HUMAN	ORC4	physical	28514442
CNTP1_HUMAN	CNTNAP1	physical	28514442
CLDN1_HUMAN	CLDND1	physical	28514442
ECSIT_HUMAN	ECSIT	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.

Regulatory Network of C1QR1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-644, AND MASSSPECTROMETRY.	18083107 [Abstract]