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Protein Page:
C3 (mouse)
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, signal peptide; Secreted
Cellular Component: extracellular space
Molecular Function: C5L2 anaphylatoxin chemotactic receptor binding; cofactor binding; lipid binding; protein binding
Biological Process: blood coagulation; complement activation; positive regulation of activation of membrane attack complex; positive regulation of angiogenesis; positive regulation of developmental growth; positive regulation of G-protein coupled receptor protein signaling pathway; positive regulation of phagocytosis; positive regulation of protein amino acid phosphorylation; positive regulation of type IIa hypersensitivity
Reference #:  P01027 (UniProtKB)
Alt. Names/Synonyms: acylation stimulating protein; AI255234; C3; 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 3d; complement factor 3; HSE-MSF; Plp
Gene Symbols: C3
Molecular weight: 186,484 Da
Basal Isoelectric point: 6.29  Predict pI for various phosphorylation states
Select Structure to View Below

C3

Protein Structure Not Found.
Download PyMol Script
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.


       mouse

 
0 1 K74‑ub RQVLTSEkTVLTGAS
0 1 K95‑ub SIKIPASkEFNSDKE
0 1 S284 QDGDKKISLAHSLTR
0 1 S288 KKISLAHSLTRVVIE
0 1 T290 ISLAHSLTRVVIEDG
0 1 V298 RVVIEDGVGDAVLTR
0 1 T304 GVGDAVLTRkVLMEG
0 1 K306‑ub GDAVLTRkVLMEGVR
0 1 T330‑p KSLYVSVtVILHSGS
0 1 K360‑ub PYQIHFTkTPKFFKP
0 1 K398‑ub VTQGSNAkALTQDDG
0 1 K408‑ub TQDDGVAkLSINTPN
0 1 K466 SVSRMELKPGDNLNV
0 1 K466‑ub SVSRMELkPGDNLNV
0 1 K486 TDPGHEAKIRyYTYL
0 1 Y489‑p GHEAKIRyYTYLVMN
0 1 K566‑ub CIGTLVVkGDPRDNH
0 1 K599‑ub VGLVAVDkGVFVLNK
0 6 S671‑p PAARRRRsVQLMERR
0 1 M675 RRRsVQLMERRMDKA
0 1 K681 LMERRMDKAGQYTDK
0 1 Y685 RMDKAGQYTDKGLRK
1 0 H742 REQHRRDHVLGLARS
0 1 K879‑ub FCSMATAkNRYFQTI
0 1 T885 AkNRYFQTIKIPPKs
0 1 S892‑p TIKIPPKssVAVPYV
0 1 S893‑p IKIPPKssVAVPYVI
0 1 S922 AVFNHFISDGVKKTL
0 1 T928 ISDGVKKTLKVVPEG
0 1 K930 DGVKKTLKVVPEGMR
1 0 T1031 AVHYLDQTEQWEKFG
0 1 K1050 QEALELIKKGYTQQL
0 2 Y1194 YTVAIAGYALALMNK
0 1 K1215 GKFLNTAKDRNRWEE
0 1 K1215‑ub GKFLNTAkDRNRWEE
0 1 K1215‑sc GKFLNTAkDRNRWEE
0 1 K1325‑ub LLRSEETkQNEAFSL
0 1 K1335‑ub EAFSLTAkGKGRGTL
0 1 T1341 AkGKGRGTLSVVAVY
0 1 S1343 GKGRGTLSVVAVYHA
0 1 R1427‑m2 LLASGVDrYISkYEM
0 1 K1431‑ub GVDrYISkYEMNKAF
0 1 K1436 ISkYEMNKAFsNKNt
0 1 S1439‑p YEMNKAFsNKNtLII
0 1 T1443‑p KAFsNKNtLIIYLEK
0 1 Y1480 QPGSVKVYSYYNLEE
0 1 K1535‑ub NLNVRLDkACEPGVD
0 1 S1586 GQQRKFISHIKCRNA
  human

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