CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001861
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Complement C3 
Protein Synonyms/Alias
 C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1; Complement C3 beta chain; Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein; ASP; C3adesArg; Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2 
Gene Name
 C3 
Gene Synonyms/Alias
 CPAMD1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
289ISLPESLKRIPIEDGubiquitination[1]
1036DETEQWEKFGLEKRQacetylation[2]
1041WEKFGLEKRQGALELacetylation[2]
1071SAFAAFVKRAPSTWLacetylation[2]
1105QVLCGAVKWLILEKQacetylation[2]
1111VKWLILEKQKPDGVFacetylation[2]
1113WLILEKQKPDGVFQEacetylation[2]
1139GLRNNNEKDMALTAFacetylation[2]
1155LISLQEAKDICEEQVacetylation[2]
1171SLPGSITKAGDFLEAacetylation[2]
1215NKFLTTAKDKNRWEDacetylation[2]
1217FLTTAKDKNRWEDPGacetylation[2]
1225NRWEDPGKQLYNVEAacetylation[2]
1284QALAQYQKDAPDHQEacetylation[2]
Reference
 [1] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [2] Solution insights into the structure of the Efb/C3 complement inhibitory complex as revealed by lysine acetylation and mass spectrometry.
 Chen H, Schuster MC, Sfyroera G, Geisbrecht BV, Lambris JD.
 J Am Soc Mass Spectrom. 2008 Jan;19(1):55-65. [PMID: 18293486
Functional Description
 C3 plays a central role in the activation of the complement system. Its processing by C3 convertase is the central reaction in both classical and alternative complement pathways. After activation C3b can bind covalently, via its reactive thioester, to cell surface carbohydrates or immune aggregates. 
Sequence Annotation
 DOMAIN 693 728 Anaphylatoxin-like.
 DOMAIN 1518 1661 NTR.
 REGION 1424 1456 Properdin-binding.
 MOD_RES 489 489 Phosphotyrosine (By similarity).
 CARBOHYD 85 85 N-linked (GlcNAc...).
 CARBOHYD 939 939 N-linked (GlcNAc...).
 CARBOHYD 1617 1617 N-linked (GlcNAc...).
 DISULFID 559 816 Interchain (between beta and alpha
 DISULFID 627 662
 DISULFID 693 720
 DISULFID 694 727
 DISULFID 707 728
 DISULFID 873 1513
 DISULFID 1101 1158
 DISULFID 1358 1489
 DISULFID 1389 1458
 DISULFID 1506 1511
 DISULFID 1518 1590
 DISULFID 1537 1661
 DISULFID 1637 1646
 CROSSLNK 1010 1013 Isoglutamyl cysteine thioester (Cys-Gln).  
Keyword
 3D-structure; Age-related macular degeneration; Cleavage on pair of basic residues; Complement alternate pathway; Complement pathway; Complete proteome; Direct protein sequencing; Disease mutation; Disulfide bond; Fatty acid metabolism; Glycoprotein; Hemolytic uremic syndrome; Immunity; Inflammatory response; Innate immunity; Lipid metabolism; Phosphoprotein; Polymorphism; Reference proteome; Secreted; Signal; Thioester bond. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1663 AA 
Protein Sequence
MGPTSGPSLL LLLLTHLPLA LGSPMYSIIT PNILRLESEE TMVLEAHDAQ GDVPVTVTVH 60
DFPGKKLVLS SEKTVLTPAT NHMGNVTFTI PANREFKSEK GRNKFVTVQA TFGTQVVEKV 120
VLVSLQSGYL FIQTDKTIYT PGSTVLYRIF TVNHKLLPVG RTVMVNIENP EGIPVKQDSL 180
SSQNQLGVLP LSWDIPELVN MGQWKIRAYY ENSPQQVFST EFEVKEYVLP SFEVIVEPTE 240
KFYYIYNEKG LEVTITARFL YGKKVEGTAF VIFGIQDGEQ RISLPESLKR IPIEDGSGEV 300
VLSRKVLLDG VQNPRAEDLV GKSLYVSATV ILHSGSDMVQ AERSGIPIVT SPYQIHFTKT 360
PKYFKPGMPF DLMVFVTNPD GSPAYRVPVA VQGEDTVQSL TQGDGVAKLS INTHPSQKPL 420
SITVRTKKQE LSEAEQATRT MQALPYSTVG NSNNYLHLSV LRTELRPGET LNVNFLLRMD 480
RAHEAKIRYY TYLIMNKGRL LKAGRQVREP GQDLVVLPLS ITTDFIPSFR LVAYYTLIGA 540
SGQREVVADS VWVDVKDSCV GSLVVKSGQS EDRQPVPGQQ MTLKIEGDHG ARVVLVAVDK 600
GVFVLNKKNK LTQSKIWDVV EKADIGCTPG SGKDYAGVFS DAGLTFTSSS GQQTAQRAEL 660
QCPQPAARRR RSVQLTEKRM DKVGKYPKEL RKCCEDGMRE NPMRFSCQRR TRFISLGEAC 720
KKVFLDCCNY ITELRRQHAR ASHLGLARSN LDEDIIAEEN IVSRSEFPES WLWNVEDLKE 780
PPKNGISTKL MNIFLKDSIT TWEILAVSMS DKKGICVADP FEVTVMQDFF IDLRLPYSVV 840
RNEQVEIRAV LYNYRQNQEL KVRVELLHNP AFCSLATTKR RHQQTVTIPP KSSLSVPYVI 900
VPLKTGLQEV EVKAAVYHHF ISDGVRKSLK VVPEGIRMNK TVAVRTLDPE RLGREGVQKE 960
DIPPADLSDQ VPDTESETRI LLQGTPVAQM TEDAVDAERL KHLIVTPSGC GEQNMIGMTP 1020
TVIAVHYLDE TEQWEKFGLE KRQGALELIK KGYTQQLAFR QPSSAFAAFV KRAPSTWLTA 1080
YVVKVFSLAV NLIAIDSQVL CGAVKWLILE KQKPDGVFQE DAPVIHQEMI GGLRNNNEKD 1140
MALTAFVLIS LQEAKDICEE QVNSLPGSIT KAGDFLEANY MNLQRSYTVA IAGYALAQMG 1200
RLKGPLLNKF LTTAKDKNRW EDPGKQLYNV EATSYALLAL LQLKDFDFVP PVVRWLNEQR 1260
YYGGGYGSTQ ATFMVFQALA QYQKDAPDHQ ELNLDVSLQL PSRSSKITHR IHWESASLLR 1320
SEETKENEGF TVTAEGKGQG TLSVVTMYHA KAKDQLTCNK FDLKVTIKPA PETEKRPQDA 1380
KNTMILEICT RYRGDQDATM SILDISMMTG FAPDTDDLKQ LANGVDRYIS KYELDKAFSD 1440
RNTLIIYLDK VSHSEDDCLA FKVHQYFNVE LIQPGAVKVY AYYNLEESCT RFYHPEKEDG 1500
KLNKLCRDEL CRCAEENCFI QKSDDKVTLE ERLDKACEPG VDYVYKTRLV KVQLSNDFDE 1560
YIMAIEQTIK SGSDEVQVGQ QRTFISPIKC REALKLEEKK HYLMWGLSSD FWGEKPNLSY 1620
IIGKDTWVEH WPEEDECQDE ENQKQCQDLG AFTESMVVFG CPN 1663 
Gene Ontology
 GO:0005615; C:extracellular space; IEA:InterPro.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0031715; F:C5L2 anaphylatoxin chemotactic receptor binding; IDA:UniProtKB.
 GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
 GO:0006957; P:complement activation, alternative pathway; TAS:Reactome.
 GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
 GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
 GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
 GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
 GO:0010951; P:negative regulation of endopeptidase activity; IEA:GOC.
 GO:0001970; P:positive regulation of activation of membrane attack complex; IEA:Compara.
 GO:0045766; P:positive regulation of angiogenesis; IEA:Compara.
 GO:0045745; P:positive regulation of G-protein coupled receptor protein signaling pathway; IDA:UniProtKB.
 GO:0010828; P:positive regulation of glucose transport; IDA:UniProtKB.
 GO:0010884; P:positive regulation of lipid storage; IDA:UniProtKB.
 GO:0050766; P:positive regulation of phagocytosis; IEA:Compara.
 GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
 GO:0001798; P:positive regulation of type IIa hypersensitivity; IEA:Compara.
 GO:0010575; P:positive regulation vascular endothelial growth factor production; IDA:BHF-UCL.
 GO:0030449; P:regulation of complement activation; TAS:Reactome.
 GO:0010866; P:regulation of triglyceride biosynthetic process; IDA:UniProtKB. 
Interpro
 IPR009048; A-macroglobulin_rcpt-bd.
 IPR011626; A2M_comp.
 IPR002890; A2M_N.
 IPR011625; A2M_N_2.
 IPR000020; Anaphylatoxin/fibulin.
 IPR018081; Anaphylatoxin_.
 IPR001840; Anaphylatoxn.
 IPR001599; Macroglobln_a2.
 IPR019742; MacrogloblnA2_CS.
 IPR019565; MacrogloblnA2_thiol-ester-bond.
 IPR001134; Netrin_domain.
 IPR018933; Netrin_module_non-TIMP.
 IPR008930; Terpenoid_cyclase/PrenylTrfase.
 IPR008993; TIMP-like_OB-fold. 
Pfam
 PF00207; A2M
 PF07678; A2M_comp
 PF01835; A2M_N
 PF07703; A2M_N_2
 PF07677; A2M_recep
 PF01821; ANATO
 PF01759; NTR
 PF10569; Thiol-ester_cl 
SMART
 SM00104; ANATO
 SM00643; C345C 
PROSITE
 PS00477; ALPHA_2_MACROGLOBULIN
 PS01177; ANAPHYLATOXIN_1
 PS01178; ANAPHYLATOXIN_2
 PS50189; NTR 
PRINTS
 PR00004; ANAPHYLATOXN.