Details for: C3

Gene ID: 718

Symbol: C3

Ensembl ID: ENSG00000125730

Description: complement C3

Associated with

Other Information

Genular Protein ID: 1215384334

Symbol: CO3_HUMAN

Name: Complement C3

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 2579379

Title: Human complement component C3: cDNA coding sequence and derived primary structure.

PubMed ID: 2579379

DOI: 10.1073/pnas.82.3.708

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8376604

Title: The adipsin-acylation stimulating protein system and regulation of intracellular triglyceride synthesis.

PubMed ID: 8376604

DOI: 10.1172/jci116733

PubMed ID: 1238393

Title: Human anaphylatoxin (C3a) from the third component of complement. Primary structure.

PubMed ID: 1238393

DOI: 10.1016/s0021-9258(19)40758-8

PubMed ID: 24367091

Title: Neisseria meningitidis NalP cleaves human complement C3, facilitating degradation of C3b and survival in human serum.

PubMed ID: 24367091

DOI: 10.1073/pnas.1321556111

PubMed ID: 7539791

Title: Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma.

PubMed ID: 7539791

DOI: 10.1074/jbc.270.23.13645

PubMed ID: 6175959

Title: Third component of human complement: localization of the internal thiolester bond.

PubMed ID: 6175959

DOI: 10.1073/pnas.79.4.1054

PubMed ID: 2972794

Title: Identification of distinct C3b and C4b recognition sites in the human C3b/C4b receptor (CR1, CD35) by deletion mutagenesis.

PubMed ID: 2972794

DOI: 10.1084/jem.168.5.1699

PubMed ID: 3279119

Title: A 34-amino acid peptide of the third component of complement mediates properdin binding.

PubMed ID: 3279119

PubMed ID: 2849025

Title: Complement component C3b binds directly to purified glycoprotein C of herpes simplex virus types 1 and 2.

PubMed ID: 2849025

DOI: 10.1016/0882-4010(87)90012-x

PubMed ID: 2909530

Title: Purification and characterization of acylation stimulating protein.

PubMed ID: 2909530

DOI: 10.1016/s0021-9258(17)31275-9

PubMed ID: 1577777

Title: Structural requirements for thioester bond formation in human complement component C3. Reassessment of the role of thioester bond integrity on the conformation of C3.

PubMed ID: 1577777

DOI: 10.1016/s0021-9258(19)50200-9

PubMed ID: 8416818

Title: Disulfide bridges in human complement component C3b.

PubMed ID: 8416818

DOI: 10.1016/0014-5793(93)81139-q

PubMed ID: 8175757

Title: Analysis of the functional domains of complement receptor type 1 (C3b/C4b receptor; CD35) by substitution mutagenesis.

PubMed ID: 8175757

DOI: 10.1016/s0021-9258(17)36829-1

PubMed ID: 9059512

Title: Acylation-stimulating protein (ASP) regulates glucose transport in the rat L6 muscle cell line.

PubMed ID: 9059512

DOI: 10.1016/s0005-2760(96)00144-0

PubMed ID: 9555951

Title: Coordinated release of acylation stimulating protein (ASP) and triacylglycerol clearance by human adipose tissue in vivo in the postprandial period.

PubMed ID: 9555951

PubMed ID: 10432298

Title: Acylation-stimulating protein (ASP): structure-function determinants of cell surface binding and triacylglycerol synthetic activity.

PubMed ID: 10432298

DOI: 10.1042/bj3420041

PubMed ID: 11773063

Title: The orphan receptor C5L2 has high affinity binding sites for complement fragments C5a and C5a des Arg(74).

PubMed ID: 11773063

DOI: 10.1074/jbc.c100714200

PubMed ID: 12540846

Title: The chemoattractant receptor-like protein C5L2 binds the C3a des-Arg77/acylation-stimulating protein.

PubMed ID: 12540846

DOI: 10.1074/jbc.m206169200

PubMed ID: 12754519

Title: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.

PubMed ID: 12754519

DOI: 10.1038/nbt827

PubMed ID: 14760718

Title: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.

PubMed ID: 14760718

DOI: 10.1002/pmic.200300556

PubMed ID: 15809665

Title: Acylation-stimulating protein: effect of acute exercise and endurance training.

PubMed ID: 15809665

DOI: 10.1038/sj.ijo.0802949

PubMed ID: 15833747

Title: C5L2 is a functional receptor for acylation-stimulating protein.

PubMed ID: 15833747

DOI: 10.1074/jbc.m406921200

PubMed ID: 16335952

Title: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.

PubMed ID: 16335952

DOI: 10.1021/pr0502065

PubMed ID: 16302015

Title: Relationships among acylation stimulating protein, adiponectin and complement C3 in lean vs obese type 2 diabetes.

PubMed ID: 16302015

DOI: 10.1038/sj.ijo.0803173

PubMed ID: 16333141

Title: Targeting the signaling pathway of acylation stimulating protein.

PubMed ID: 16333141

DOI: 10.1194/jlr.m500500-jlr200

PubMed ID: 16263699

Title: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.

PubMed ID: 16263699

DOI: 10.1074/mcp.m500324-mcp200

PubMed ID: 18805911

Title: Acylation stimulating protein but not complement C3 associates with metabolic syndrome components in Chinese children and adolescents.

PubMed ID: 18805911

DOI: 10.1530/eje-08-0467

PubMed ID: 18160402

Title: Group A streptococcal cysteine protease degrades C3 (C3b) and contributes to evasion of innate immunity.

PubMed ID: 18160402

DOI: 10.1074/jbc.m704821200

PubMed ID: 19112495

Title: The Staphylococcus aureus protein Sbi acts as a complement inhibitor and forms a tripartite complex with host complement Factor H and C3b.

PubMed ID: 19112495

DOI: 10.1371/journal.ppat.1000250

PubMed ID: 19159218

Title: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.

PubMed ID: 19159218

DOI: 10.1021/pr8008012

PubMed ID: 19615750

Title: C5a- and ASP-mediated C5L2 activation, endocytosis and recycling are lost in S323I-C5L2 mutation.

PubMed ID: 19615750

DOI: 10.1016/j.molimm.2009.06.007

PubMed ID: 20083651

Title: Mutational analyses reveal that the staphylococcal immune evasion molecule Sbi and complement receptor 2 (CR2) share overlapping contact residues on C3d: implications for the controversy regarding the CR2/C3d cocrystal structure.

PubMed ID: 20083651

DOI: 10.4049/jimmunol.0902919

PubMed ID: 20951140

Title: Delineation of the complement receptor type 2-C3d complex by site-directed mutagenesis and molecular docking.

PubMed ID: 20951140

DOI: 10.1016/j.jmb.2010.10.005

PubMed ID: 19913840

Title: Serum complement C3: a determinant of cardiometabolic risk, additive to the metabolic syndrome, in middle-aged population.

PubMed ID: 19913840

DOI: 10.1016/j.metabol.2009.09.006

PubMed ID: 21502375

Title: Staphylococcus aureus metalloprotease aureolysin cleaves complement C3 to mediate immune evasion.

PubMed ID: 21502375

DOI: 10.4049/jimmunol.1002948

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 26091039

Title: A single kinase generates the majority of the secreted phosphoproteome.

PubMed ID: 26091039

DOI: 10.1016/j.cell.2015.05.028

PubMed ID: 3260670

Title: Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: differences between crystal and solution conformations.

PubMed ID: 3260670

DOI: 10.1073/pnas.85.14.5036

PubMed ID: 9596584

Title: X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2.

PubMed ID: 9596584

DOI: 10.1126/science.280.5367.1277

PubMed ID: 11387479

Title: Structure of complement receptor 2 in complex with its C3d ligand.

PubMed ID: 11387479

DOI: 10.1126/science.1059118

PubMed ID: 15713468

Title: Solution structure of the complex between CR2 SCR 1-2 and C3d of human complement: an X-ray scattering and sedimentation modelling study.

PubMed ID: 15713468

DOI: 10.1016/j.jmb.2004.12.006

PubMed ID: 16177781

Title: Structures of complement component C3 provide insights into the function and evolution of immunity.

PubMed ID: 16177781

DOI: 10.1038/nature04005

PubMed ID: 17051160

Title: Structure of C3b reveals conformational changes that underlie complement activity.

PubMed ID: 17051160

DOI: 10.1038/nature05172

PubMed ID: 17051150

Title: Structure of C3b in complex with CRIg gives insights into regulation of complement activation.

PubMed ID: 17051150

DOI: 10.1038/nature05263

PubMed ID: 17684013

Title: Structure of compstatin in complex with complement component C3c reveals a new mechanism of complement inhibition.

PubMed ID: 17684013

DOI: 10.1074/jbc.m704587200

PubMed ID: 17351618

Title: A structural basis for complement inhibition by Staphylococcus aureus.

PubMed ID: 17351618

DOI: 10.1038/ni1450

PubMed ID: 21055811

Title: A structural basis for Staphylococcal complement subversion: X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3d.

PubMed ID: 21055811

DOI: 10.1016/j.molimm.2010.09.017

PubMed ID: 21527715

Title: A crystal structure of the complex between human complement receptor 2 and its ligand C3d.

PubMed ID: 21527715

DOI: 10.1126/science.1201954

PubMed ID: 28264884

Title: Functional and structural insight into properdin control of complement alternative pathway amplification.

PubMed ID: 28264884

DOI: 10.15252/embj.201696173

PubMed ID: 31507604

Title: Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.

PubMed ID: 31507604

DOI: 10.3389/fimmu.2019.02007

PubMed ID: 2473125

Title: The difference between human C3F and C3S results from a single amino acid change from an asparagine to an aspartate residue at position 1216 on the alpha-chain of the complement component, C3.

PubMed ID: 2473125

PubMed ID: 2584723

Title:

PubMed ID: 2584723

PubMed ID: 1976733

Title: Molecular basis of polymorphisms of human complement component C3.

PubMed ID: 1976733

DOI: 10.1084/jem.172.4.1011

PubMed ID: 7961791

Title: Inherited human complement C3 deficiency. An amino acid substitution in the beta-chain (Asp549 to Asn) impairs C3 secretion.

PubMed ID: 7961791

DOI: 10.1016/s0021-9258(18)46954-2

PubMed ID: 17634448

Title: Complement C3 variant and the risk of age-related macular degeneration.

PubMed ID: 17634448

DOI: 10.1056/nejmoa072618

PubMed ID: 18796626

Title: Mutations in complement C3 predispose to development of atypical hemolytic uremic syndrome.

PubMed ID: 18796626

DOI: 10.1182/blood-2008-01-133702

PubMed ID: 20513133

Title: Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome.

PubMed ID: 20513133

DOI: 10.1002/humu.21256

PubMed ID: 22028381

Title: Quantitative detection of single amino acid polymorphisms by targeted proteomics.

PubMed ID: 22028381

DOI: 10.1093/jmcb/mjr024

PubMed ID: 21555552

Title: Common polymorphisms in C3, factor B, and factor H collaborate to determine systemic complement activity and disease risk.

PubMed ID: 21555552

DOI: 10.1073/pnas.1019338108

PubMed ID: 21285368

Title: Dual interaction of factor H with C3d and glycosaminoglycans in host-nonhost discrimination by complement.

PubMed ID: 21285368

DOI: 10.1073/pnas.1017087108

PubMed ID: 21317894

Title: Structural basis for engagement by complement factor H of C3b on a self surface.

PubMed ID: 21317894

DOI: 10.1038/nsmb.2018

PubMed ID: 24036952

Title: Rare variants in CFI, C3 and C9 are associated with high risk of advanced age-related macular degeneration.

PubMed ID: 24036952

DOI: 10.1038/ng.2741

Sequence Information:

  • Length: 1663
  • Mass: 187148
  • Checksum: 30C2832A9E75FFC4
  • Sequence:
  • MGPTSGPSLL LLLLTHLPLA LGSPMYSIIT PNILRLESEE TMVLEAHDAQ GDVPVTVTVH 
    DFPGKKLVLS SEKTVLTPAT NHMGNVTFTI PANREFKSEK GRNKFVTVQA TFGTQVVEKV 
    VLVSLQSGYL FIQTDKTIYT PGSTVLYRIF TVNHKLLPVG RTVMVNIENP EGIPVKQDSL 
    SSQNQLGVLP LSWDIPELVN MGQWKIRAYY ENSPQQVFST EFEVKEYVLP SFEVIVEPTE 
    KFYYIYNEKG LEVTITARFL YGKKVEGTAF VIFGIQDGEQ RISLPESLKR IPIEDGSGEV 
    VLSRKVLLDG VQNPRAEDLV GKSLYVSATV ILHSGSDMVQ AERSGIPIVT SPYQIHFTKT 
    PKYFKPGMPF DLMVFVTNPD GSPAYRVPVA VQGEDTVQSL TQGDGVAKLS INTHPSQKPL 
    SITVRTKKQE LSEAEQATRT MQALPYSTVG NSNNYLHLSV LRTELRPGET LNVNFLLRMD 
    RAHEAKIRYY TYLIMNKGRL LKAGRQVREP GQDLVVLPLS ITTDFIPSFR LVAYYTLIGA 
    SGQREVVADS VWVDVKDSCV GSLVVKSGQS EDRQPVPGQQ MTLKIEGDHG ARVVLVAVDK 
    GVFVLNKKNK LTQSKIWDVV EKADIGCTPG SGKDYAGVFS DAGLTFTSSS GQQTAQRAEL 
    QCPQPAARRR RSVQLTEKRM DKVGKYPKEL RKCCEDGMRE NPMRFSCQRR TRFISLGEAC 
    KKVFLDCCNY ITELRRQHAR ASHLGLARSN LDEDIIAEEN IVSRSEFPES WLWNVEDLKE 
    PPKNGISTKL MNIFLKDSIT TWEILAVSMS DKKGICVADP FEVTVMQDFF IDLRLPYSVV 
    RNEQVEIRAV LYNYRQNQEL KVRVELLHNP AFCSLATTKR RHQQTVTIPP KSSLSVPYVI 
    VPLKTGLQEV EVKAAVYHHF ISDGVRKSLK VVPEGIRMNK TVAVRTLDPE RLGREGVQKE 
    DIPPADLSDQ VPDTESETRI LLQGTPVAQM TEDAVDAERL KHLIVTPSGC GEQNMIGMTP 
    TVIAVHYLDE TEQWEKFGLE KRQGALELIK KGYTQQLAFR QPSSAFAAFV KRAPSTWLTA 
    YVVKVFSLAV NLIAIDSQVL CGAVKWLILE KQKPDGVFQE DAPVIHQEMI GGLRNNNEKD 
    MALTAFVLIS LQEAKDICEE QVNSLPGSIT KAGDFLEANY MNLQRSYTVA IAGYALAQMG 
    RLKGPLLNKF LTTAKDKNRW EDPGKQLYNV EATSYALLAL LQLKDFDFVP PVVRWLNEQR 
    YYGGGYGSTQ ATFMVFQALA QYQKDAPDHQ ELNLDVSLQL PSRSSKITHR IHWESASLLR 
    SEETKENEGF TVTAEGKGQG TLSVVTMYHA KAKDQLTCNK FDLKVTIKPA PETEKRPQDA 
    KNTMILEICT RYRGDQDATM SILDISMMTG FAPDTDDLKQ LANGVDRYIS KYELDKAFSD 
    RNTLIIYLDK VSHSEDDCLA FKVHQYFNVE LIQPGAVKVY AYYNLEESCT RFYHPEKEDG 
    KLNKLCRDEL CRCAEENCFI QKSDDKVTLE ERLDKACEPG VDYVYKTRLV KVQLSNDFDE 
    YIMAIEQTIK SGSDEVQVGQ QRTFISPIKC REALKLEEKK HYLMWGLSSD FWGEKPNLSY 
    IIGKDTWVEH WPEEDECQDE ENQKQCQDLG AFTESMVVFG CPN

Genular Protein ID: 1271765858

Symbol: B4DR57_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 235
  • Mass: 26082
  • Checksum: 96A083386384C0CB
  • Sequence:
  • MGPTSGPSLL LLLLTHLPLA LGSPMYSIIT PNILRLESEE TMVQEAHDAQ GDVPVTVTVH 
    DFPGKKLVLS SEKTVLTPAT NHMGNVTFTI PANREFKSEK GRNKFVTVQA TFGTQVVEKV 
    VLVSLQSGYL LIQTDKTIYT PGSTVLYRIF TVNHKLLPVG RTVMVNIENP EGIPVKQDSL 
    SSQNQLGVLP LSWDIPELVN MGQWKIRAYY ENSPQQVFST EFEVKEYVLP SFEVI

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.