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Protein Page:
C3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
C3 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. Defects in C3 are the cause of complement component 3 deficiency (C3D). A rare defect of the complement classical pathway. Patients develop recurrent, severe, pyogenic infections because of ineffective opsonization of pathogens. Some patients may also develop autoimmune disorders, such as arthralgia and vasculitic rashes, lupus-like syndrome and membranoproliferative glomerulonephritis. Genetic variation in C3 is associated with susceptibility to age-related macular degeneration type 9 (ARMD9). ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin- containing structure known as Bruch membrane. Defects in C3 are a cause of susceptibility to hemolytic uremic syndrome atypical type 5 (AHUS5). An atypical form of hemolytic uremic syndrome. It is a complex genetic disease characterized by microangiopathic hemolytic anemia, thrombocytopenia, renal failure and absence of episodes of enterocolitis and diarrhea. In contrast to typical hemolytic uremic syndrome, atypical forms have a poorer prognosis, with higher death rates and frequent progression to end-stage renal disease. Susceptibility to the development of atypical hemolytic uremic syndrome can be conferred by mutations in various components of or regulatory factors in the complement cascade system. Other genes may play a role in modifying the phenotype. Increased levels of C3 and its cleavage product ASP, are associated with obesity, diabetes and coronary heart disease. Short-term endurance training reduces baseline ASP levels and subsequently fat storage. Note: This description may include information from UniProtKB.
Protein type: Inhibitor; Secreted; Secreted, signal peptide
Chromosomal Location of Human Ortholog: 19p13.3-p13.2
Cellular Component: extracellular region; extracellular space; plasma membrane
Molecular Function: C5L2 anaphylatoxin chemotactic receptor binding; protein binding; receptor binding; serine-type endopeptidase activity
Biological Process: complement activation; complement activation, alternative pathway; G-protein coupled receptor protein signaling pathway; immune response; positive regulation of G-protein coupled receptor protein signaling pathway; positive regulation of protein amino acid phosphorylation; regulation of complement activation; regulation of immune response; signal transduction
Disease: Complement Component 3 Deficiency, Autosomal Recessive; Hemolytic Uremic Syndrome, Atypical, Susceptibility To, 5; Macular Degeneration, Age-related, 9
Reference #:  P01024 (UniProtKB)
Alt. Names/Synonyms: acylation-stimulating protein cleavage product; AHUS5; ARMD9; C3; C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1; C3a anaphylatoxin; CO3; Complement C3; Complement C3 alpha chain; Complement C3 beta chain; Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3c alpha' chain fragment 2; Complement C3d fragment; Complement C3dg fragment; Complement C3f fragment; Complement C3g fragment; complement component 3; complement component C3; CPAMD1
Gene Symbols: C3
Molecular weight: 187,148 Da
Basal Isoelectric point: 6.02  Predict pI for various phosphorylation states
Select Structure to View Below

C3

Protein Structure Not Found.
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Download ChimeraX Script


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K73 KLVLSSEKTVLTPAT
0 1 R94 TFTIPANREFKSEKG
0 1 S283‑p QDGEQRIsLPEsLkR
0 1 S287‑p QRIsLPEsLkRIPIE
0 1 K289‑ub IsLPEsLkRIPIEDG
0 2 S297‑p RIPIEDGsGEVVLsR
0 1 S303‑p GsGEVVLsRKVLLDG
0 1 K305 GEVVLsRKVLLDGVQ
0 1 T329 KSLYVSATVILHSGS
0 1 K359 PYQIHFTKTPKYFKP
0 1 Q398 VQGEDTVQSLTQGDG
0 1 K408 TQGDGVAKLSINTHP
0 1 R466 SVLRTELRPGETLNV
0 1 R466 SVLRTELRPGETLNV
0 1 K486 MDRAHEAKIRYYTYL
0 1 Y489 AHEAKIRYYTYLIMN
0 1 K566 CVGSLVVKSGQSEDR
0 1 K600 VVLVAVDKGVFVLNK
0 7 S672‑p PAARRRRsVQLtEKR
0 1 T676‑p RRRsVQLtEKRMDKV
0 1 K682 LtEKRMDKVGKyPKE
0 1 Y686‑p RMDKVGKyPKELRKC
1 1 S742‑p RRQHARAsHLGLARS
0 1 K879 FCSLATTKRRHQQtV
0 1 T885‑p TKRRHQQtVTIPPKS
0 1 S892 tVTIPPKSSLSVPYV
0 1 S893 VTIPPKSSLSVPYVI
0 1 S922‑p AVYHHFIsDGVRKsL
0 1 S928‑p IsDGVRKsLKVVPEG
0 1 K930 DGVRKsLKVVPEGIR
0 1 T985 TRILLQGTPVAQMTE
1 0 T1031‑p AVHYLDEtEQWEKFG
0 1 K1050 QGALELIKKGYTQQL
0 2 Y1194‑p YTVAIAGyALAQMGR
0 1 K1215 NKFLTTAKDKNRWED
0 1 K1215 NKFLTTAKDKNRWED
0 1 K1215 NKFLTTAKDKNRWED
0 1 K1325 LLRSEETKENEGFTV
0 1 E1335 EGFTVTAEGKGQGtL
0 1 T1341‑p AEGKGQGtLsVVTMY
0 1 S1343‑p GKGQGtLsVVTMYHA
0 1 R1427 QLANGVDRYISKYEL
0 1 K1431 GVDRYISKYELDKAF
0 1 K1436 ISKYELDKAFSDRNT
0 1 S1439 YELDKAFSDRNTLII
0 1 T1443 KAFSDRNTLIIYLDK
0 1 Y1480‑p QPGAVKVyAYYNLEE
0 1 K1535 TLEERLDKACEPGVD
0 1 S1586‑p GQQRTFIsPIKCREA
  mouse

 
K74‑ub RQVLTSEkTVLTGAS
K95‑ub SIKIPASkEFNSDKE
S284 QDGDKKISLAHSLTR
S288 KKISLAHSLTRVVIE
T290 ISLAHSLTRVVIEDG
V298 RVVIEDGVGDAVLTR
T304 GVGDAVLTRkVLMEG
K306‑ub GDAVLTRkVLMEGVR
T330‑p KSLYVSVtVILHSGS
K360‑ub PYQIHFTkTPKFFKP
K398‑ub VTQGSNAkALTQDDG
K408‑ub TQDDGVAkLSINTPN
K466 SVSRMELKPGDNLNV
K466‑ub SVSRMELkPGDNLNV
K486 TDPGHEAKIRyYTYL
Y489‑p GHEAKIRyYTYLVMN
K566‑ub CIGTLVVkGDPRDNH
K599‑ub VGLVAVDkGVFVLNK
S671‑p PAARRRRsVQLMERR
M675 RRRsVQLMERRMDKA
K681 LMERRMDKAGQYTDK
Y685 RMDKAGQYTDKGLRK
H742 REQHRRDHVLGLARS
K879‑ub FCSMATAkNRYFQTI
T885 AkNRYFQTIKIPPKs
S892‑p TIKIPPKssVAVPYV
S893‑p IKIPPKssVAVPYVI
S922 AVFNHFISDGVKKTL
T928 ISDGVKKTLKVVPEG
K930 DGVKKTLKVVPEGMR
S985‑p TRIILQGsPVVQMAE
T1031 AVHYLDQTEQWEKFG
K1050 QEALELIKKGYTQQL
Y1194 YTVAIAGYALALMNK
K1215 GKFLNTAKDRNRWEE
K1215‑ub GKFLNTAkDRNRWEE
K1215‑sc GKFLNTAkDRNRWEE
K1325‑ub LLRSEETkQNEAFSL
K1335‑ub EAFSLTAkGKGRGTL
T1341 AkGKGRGTLSVVAVY
S1343 GKGRGTLSVVAVYHA
R1427‑m2 LLASGVDrYISkYEM
K1431‑ub GVDrYISkYEMNKAF
K1436 ISkYEMNKAFsNKNt
S1439‑p YEMNKAFsNKNtLII
T1443‑p KAFsNKNtLIIYLEK
Y1480 QPGSVKVYSYYNLEE
K1535‑ub NLNVRLDkACEPGVD
S1586 GQQRKFISHIKCRNA
  rat

 
K74 KQVLTSEKTVLTGAT
K95 FIKIPASKEFNADKG
S283 QDEDKKISLALSLTR
S287 KKISLALSLTRVLIE
T289 ISLALSLTRVLIEDG
S297 RVLIEDGSGEAVLSR
S303 GSGEAVLSRKVLMDG
K305 GEAVLSRKVLMDGVR
T329 KSLYVSVTVILHSGS
K359 PYQIHFTKTPKFFKP
Q397 VTQGSDAQALTQDDG
K407 TQDDGVAKLSVNTPN
K465‑ac SVSRVELkPGDNLNV
K465 SVSRVELKPGDNLNV
K485‑ac TDAGQEAkIRYYTYL
Y488 GQEAkIRYYTYLVMN
K565 CVGTLVVKGDPRDNR
K599 VGLVAVDKGVFVLNK
S671‑p PAARRRRsVQLMERR
M675 RRRsVQLMERRMDkA
K681‑ac LMERRMDkAGQYTDK
Y685 RMDkAGQYTDKGLRK
H742 REQHRRDHVLGLARS
K879 FCSMATAKKRYYQTI
T885 AKKRYYQTIEIPPKS
S892 TIEIPPKSSVAVPYV
S893 IEIPPKSSVAVPYVI
S922 AVFNHFISDGVKKIL
I928 ISDGVKKILkVVPEG
K930‑ac DGVKKILkVVPEGMR
T985 TRILLQGTPVAQMAE
T1031 AVHYLDQTEQWEKFG
K1050‑ac QEALELIkKGYTQQL
Y1194 YTVAIAGYALALMNK
K1215‑ac TKFLNTAkDRNRWEE
K1215 TKFLNTAKDRNRWEE
K1215 TKFLNTAKDRNRWEE
K1325 LLRSEETKQNEGFSL
K1335 EGFSLTAKGKGQGTL
T1341 AKGKGQGTLSVVTVY
S1343 GKGQGTLSVVTVYHA
R1427 LLSSGVDRYISKYEM
K1431 GVDRYISKYEMDkAF
K1436‑ac ISKYEMDkAFSNKNT
S1439 YEMDkAFSNKNTLII
T1443 kAFSNKNTLIIYLEK
Y1480 QPGSVKVYSYYNLEE
K1535 SLNERLDKACEPGVD
S1586 GQERRFISHVKCRNA
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