dbPTM

C1R_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	C1R_HUMAN
UniProt AC	P00736
Protein Name	Complement C1r subcomponent
Gene Name	C1R
Organism	Homo sapiens (Human).
Sequence Length	705
Subcellular Localization	Secreted .
Protein Description	C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system..
Protein Sequence	MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVFQQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDFSNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGYELQEDTHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPFDIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKLRYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQDDGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSRESEQGVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVFTNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRVSVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVMEEKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAVRDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
84	Phosphorylation	KISADKKSLGRFCGQ EEECCHHHHHHHHHH	41.62	22210691
94	Phosphorylation	RFCGQLGSPLGNPPG HHHHHCCCCCCCCCC	26.08	22210691
118	Phosphorylation	KMLLTFHTDFSNEEN EEEEEEECCCCCCCC	34.25	-
125	N-linked_Glycosylation	TDFSNEENGTIMFYK CCCCCCCCCEEEEEE	46.89	16335952
127	Phosphorylation	FSNEENGTIMFYKGF CCCCCCCEEEEEEEH	22.35	-
167	Hydroxylation	QCQHLCHNYVGGYFC HHHHHHHHHCCCCCC	31.99	2820791
206	Phosphorylation	TEASGYISSLEYPRS HHHCCEEECCCCCCC	22.01	3030286
221	N-linked_Glycosylation	YPPDLRCNYSIRVER CCCCCCCCEEEEEEC	27.44	16335952
223	Phosphorylation	PDLRCNYSIRVERGL CCCCCCEEEEEECCE	7.02	24719451
270	Ubiquitination	NIGEFCGKQRPPDLD CHHHHCCCCCCCCCC	44.29	29967540
389	Phosphorylation	LPNGDFRYTTTMGVN CCCCCCEEEEEEECC	14.39	25907765
390	Phosphorylation	PNGDFRYTTTMGVNT CCCCCEEEEEEECCE	16.13	25907765
391	Phosphorylation	NGDFRYTTTMGVNTY CCCCEEEEEEECCEE	13.07	25907765
392	Phosphorylation	GDFRYTTTMGVNTYK CCCEEEEEEECCEEE	12.25	25907765
397	Phosphorylation	TTTMGVNTYKARIQY EEEEECCEEEEEEEE	24.80	25907765
398	Phosphorylation	TTMGVNTYKARIQYY EEEECCEEEEEEEEE	9.46	25907765
419	Phosphorylation	KMQTRAGSRESEQGV CCEECCCCCCCCCCE	31.71	24275569
422	Phosphorylation	TRAGSRESEQGVYTC ECCCCCCCCCCEEEE	33.82	24850871
469	Ubiquitination	QRIIGGQKAKMGNFP HHHHCCCCCCCCCCC	53.93	29967540
514	N-linked_Glycosylation	KEHEAQSNASLDVFL CCHHHHCCCCCEEEE	22.82	16335952
541	Phosphorylation	NHPIRRVSVHPDYRQ CCCCCEEEECCCCCC	16.94	23312004
546	Phosphorylation	RVSVHPDYRQDESYN EEEECCCCCCCCCCC	18.02	23312004
581	N-linked_Glycosylation	LPICLPDNDTFYDLG ECEECCCCCCCCCCH	48.56	UniProtKB CARBOHYD
671	Phosphorylation	NTDRWVATGIVSWGI CCCCEEEEEEEEECC	20.16	-
675	Phosphorylation	WVATGIVSWGIGCSR EEEEEEEEECCCCCC	20.05	-
681	Phosphorylation	VSWGIGCSRGYGFYT EEECCCCCCCCCHHH	24.43	-
684	Phosphorylation	GIGCSRGYGFYTKVL CCCCCCCCCHHHHHH	11.71	18083107
687	Phosphorylation	CSRGYGFYTKVLNYV CCCCCCHHHHHHHHH	10.99	18083107
693	Phosphorylation	FYTKVLNYVDWIKKE HHHHHHHHHHHHHHH	8.81	25690035

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
206	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
206	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
206	S	Phosphorylation	Kinase	CK2	-	Uniprot
206	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of C1R_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 C1R_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
C1S_HUMAN	C1S	physical	10878362
C1R_HUMAN	C1R	physical	11823416
IC1_HUMAN	SERPING1	physical	6282262
EP300_HUMAN	EP300	physical	21988832
PCKGC_HUMAN	PCK1	physical	21988832
C1RL_HUMAN	C1RL	physical	28514442
BIRC2_HUMAN	BIRC2	physical	28514442
LRC15_HUMAN	LRRC15	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 C1R_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-514, 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-125; ASN-221 AND ASN-514,AND MASS SPECTROMETRY.	16335952 [Abstract]
Phosphorylation
Reference	PubMed
"Identification of a cryptic protein kinase CK2 phosphorylation sitein human complement protease Clr, and its use to probe intramolecularinteraction."; Pelloux S., Thielens N.M., Hudry-Clergeon G., Petillot Y., Filhol O.,Arlaud G.J.; FEBS Lett. 386:15-20(1996). Cited for: PROTEIN SEQUENCE OF 133-137; 187-211 AND 609-613, AND PHOSPHORYLATIONAT SER-206 BY CK2.	8635594 [Abstract]