C163A_HUMAN - dbPTM
C163A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C163A_HUMAN
UniProt AC Q86VB7
Protein Name Scavenger receptor cysteine-rich type 1 protein M130
Gene Name CD163
Organism Homo sapiens (Human).
Sequence Length 1156
Subcellular Localization Soluble CD163: Secreted .
Cell membrane
Single-pass type I membrane protein . Isoform 1 and isoform 2 show a lower surface expression when expressed in cells.
Protein Description Acute phase-regulated receptor involved in clearance and endocytosis of hemoglobin/haptoglobin complexes by macrophages and may thereby protect tissues from free hemoglobin-mediated oxidative damage. May play a role in the uptake and recycling of iron, via endocytosis of hemoglobin/haptoglobin and subsequent breakdown of heme. Binds hemoglobin/haptoglobin complexes in a calcium-dependent and pH-dependent manner. Exhibits a higher affinity for complexes of hemoglobin and multimeric haptoglobin of HP*1F phenotype than for complexes of hemoglobin and dimeric haptoglobin of HP*1S phenotype. Induces a cascade of intracellular signals that involves tyrosine kinase-dependent calcium mobilization, inositol triphosphate production and secretion of IL6 and CSF1. Isoform 3 exhibits the higher capacity for ligand endocytosis and the more pronounced surface expression when expressed in cells.; After shedding, the soluble form (sCD163) may play an anti-inflammatory role, and may be a valuable diagnostic parameter for monitoring macrophage activation in inflammatory conditions..
Protein Sequence MSKLRMVLLEDSGSADFRRHFVNLSPFTITVVLLLSACFVTSSLGGTDKELRLVDGENKCSGRVEVKVQEEWGTVCNNGWSMEAVSVICNQLGCPTAIKAPGWANSSAGSGRIWMDHVSCRGNESALWDCKHDGWGKHSNCTHQQDAGVTCSDGSNLEMRLTRGGNMCSGRIEIKFQGRWGTVCDDNFNIDHASVICRQLECGSAVSFSGSSNFGEGSGPIWFDDLICNGNESALWNCKHQGWGKHNCDHAEDAGVICSKGADLSLRLVDGVTECSGRLEVRFQGEWGTICDDGWDSYDAAVACKQLGCPTAVTAIGRVNASKGFGHIWLDSVSCQGHEPAIWQCKHHEWGKHYCNHNEDAGVTCSDGSDLELRLRGGGSRCAGTVEVEIQRLLGKVCDRGWGLKEADVVCRQLGCGSALKTSYQVYSKIQATNTWLFLSSCNGNETSLWDCKNWQWGGLTCDHYEEAKITCSAHREPRLVGGDIPCSGRVEVKHGDTWGSICDSDFSLEAASVLCRELQCGTVVSILGGAHFGEGNGQIWAEEFQCEGHESHLSLCPVAPRPEGTCSHSRDVGVVCSRYTEIRLVNGKTPCEGRVELKTLGAWGSLCNSHWDIEDAHVLCQQLKCGVALSTPGGARFGKGNGQIWRHMFHCTGTEQHMGDCPVTALGASLCPSEQVASVICSGNQSQTLSSCNSSSLGPTRPTIPEESAVACIESGQLRLVNGGGRCAGRVEIYHEGSWGTICDDSWDLSDAHVVCRQLGCGEAINATGSAHFGEGTGPIWLDEMKCNGKESRIWQCHSHGWGQQNCRHKEDAGVICSEFMSLRLTSEASREACAGRLEVFYNGAWGTVGKSSMSETTVGVVCRQLGCADKGKINPASLDKAMSIPMWVDNVQCPKGPDTLWQCPSSPWEKRLASPSEETWITCDNKIRLQEGPTSCSGRVEIWHGGSWGTVCDDSWDLDDAQVVCQQLGCGPALKAFKEAEFGQGTGPIWLNEVKCKGNESSLWDCPARRWGHSECGHKEDAAVNCTDISVQKTPQKATTGRSSRQSSFIAVGILGVVLLAIFVALFFLTKKRRQRQRLAVSSRGENLVHQIQYREMNSCLNADDLDLMNSSENSHESADFSAAELISVSKFLPISGMEKEAILSHTEKENGNL
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 Orthologous
Protein Cluster
36PhosphorylationITVVLLLSACFVTSS
HHHHHHHHHHHHHHH		23.9823612710
43PhosphorylationSACFVTSSLGGTDKE
HHHHHHHHCCCCCCE		22.9723612710
47PhosphorylationVTSSLGGTDKELRLV
HHHHCCCCCCEEEEE		41.9423612710
105N-linked_GlycosylationIKAPGWANSSAGSGR
EECCCCCCCCCCCCC		29.9519139490
140N-linked_GlycosylationDGWGKHSNCTHQQDA
CCCCCCCCCCCCCCC		34.1319159218
260AcetylationDAGVICSKGADLSLR
HCCEEEECCCCEEEE		54.4218530583
265PhosphorylationCSKGADLSLRLVDGV
EECCCCEEEEEECCC		16.4024719451
473PhosphorylationEEAKITCSAHREPRL
HHCEEEEECCCCCCE		20.6125954137
701O-linked_GlycosylationNSSSLGPTRPTIPEE
CCCCCCCCCCCCCHH		47.70OGP
704O-linked_GlycosylationSLGPTRPTIPEESAV
CCCCCCCCCCHHHHE		45.96OGP
709O-linked_GlycosylationRPTIPEESAVACIES
CCCCCHHHHEEEEHH		26.78OGP
767N-linked_GlycosylationLGCGEAINATGSAHF
CCCCCHHCCCCCCCC		38.2019159218
823PhosphorylationVICSEFMSLRLTSEA
CCCHHHHHHHCCCHH		18.6924719451
828PhosphorylationFMSLRLTSEASREAC
HHHHHCCCHHHHHHH		35.4424719451
858PhosphorylationGKSSMSETTVGVVCR
CCCCCCCCCHHHHHH		21.3423090842
859PhosphorylationKSSMSETTVGVVCRQ
CCCCCCCCHHHHHHH		15.9423090842
1027N-linked_GlycosylationHKEDAAVNCTDISVQ
CCCCCCCCCEEEEEE		20.4619159218
1072PhosphorylationFVALFFLTKKRRQRQ
HHHHHHHHHHHHHHH		29.3911298324
1084PhosphorylationQRQRLAVSSRGENLV
HHHHHEECCCCCCHH		14.5420166139
1085PhosphorylationRQRLAVSSRGENLVH
HHHHEECCCCCCHHH		37.3926657352
1101PhosphorylationIQYREMNSCLNADDL
HHHHHHHHCCCHHHH		20.76-
1101 (in isoform 3)Phosphorylation-20.7627251275
1113 (in isoform 3)Phosphorylation-25.6827251275
1114 (in isoform 3)Phosphorylation-35.4727251275
1130PhosphorylationFSAAELISVSKFLPI
CCHHHHHHHHHCCCC		32.7224719451
1134 (in isoform 4)Phosphorylation-8.3727251275
1137 (in isoform 2)Phosphorylation-6.3823898821
1139 (in isoform 2)Phosphorylation-29.0523898821
1146 (in isoform 4)Phosphorylation-3.8527251275
1147 (in isoform 4)Phosphorylation-23.4227251275
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 C163A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of C163A_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 C163A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSK2B_HUMANCSNK2Bphysical
11298324
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 C163A_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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-105; ASN-140; ASN-767 ANDASN-1027, AND MASS SPECTROMETRY.
"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-105, AND MASSSPECTROMETRY.

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