CO4B_HUMAN - dbPTM
CO4B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CO4B_HUMAN
UniProt AC P0C0L5
Protein Name Complement C4-B
Gene Name C4B
Organism Homo sapiens (Human).
Sequence Length 1744
Subcellular Localization Secreted. Cell junction, synapse . Cell projection, axon . Cell projection, dendrite .
Protein Description Non-enzymatic component of the C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens, while C4B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens.; Derived from proteolytic degradation of complement C4, C4a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes..
Protein Sequence MRLLWGLIWASSFFTLSLQKPRLLLFSPSVVHLGVPLSVGVQLQDVPRGQVVKGSVFLRNPSRNNVPCSPKVDFTLSSERDFALLSLQVPLKDAKSCGLHQLLRGPEVQLVAHSPWLKDSLSRTTNIQGINLLFSSRRGHLFLQTDQPIYNPGQRVRYRVFALDQKMRPSTDTITVMVENSHGLRVRKKEVYMPSSIFQDDFVIPDISEPGTWKISARFSDGLESNSSTQFEVKKYVLPNFEVKITPGKPYILTVPGHLDEMQLDIQARYIYGKPVQGVAYVRFGLLDEDGKKTFFRGLESQTKLVNGQSHISLSKAEFQDALEKLNMGITDLQGLRLYVAAAIIESPGGEMEEAELTSWYFVSSPFSLDLSKTKRHLVPGAPFLLQALVREMSGSPASGIPVKVSATVSSPGSVPEVQDIQQNTDGSGQVSIPIIIPQTISELQLSVSAGSPHPAIARLTVAAPPSGGPGFLSIERPDSRPPRVGDTLNLNLRAVGSGATFSHYYYMILSRGQIVFMNREPKRTLTSVSVFVDHHLAPSFYFVAFYYHGDHPVANSLRVDVQAGACEGKLELSVDGAKQYRNGESVKLHLETDSLALVALGALDTALYAAGSKSHKPLNMGKVFEAMNSYDLGCGPGGGDSALQVFQAAGLAFSDGDQWTLSRKRLSCPKEKTTRKKRNVNFQKAINEKLGQYASPTAKRCCQDGVTRLPMMRSCEQRAARVQQPDCREPFLSCCQFAESLRKKSRDKGQAGLQRALEILQEEDLIDEDDIPVRSFFPENWLWRVETVDRFQILTLWLPDSLTTWEIHGLSLSKTKGLCVATPVQLRVFREFHLHLRLPMSVRRFEQLELRPVLYNYLDKNLTVSVHVSPVEGLCLAGGGGLAQQVLVPAGSARPVAFSVVPTAATAVSLKVVARGSFEFPVGDAVSKVLQIEKEGAIHREELVYELNPLDHRGRTLEIPGNSDPNMIPDGDFNSYVRVTASDPLDTLGSEGALSPGGVASLLRLPRGCGEQTMIYLAPTLAASRYLDKTEQWSTLPPETKDHAVDLIQKGYMRIQQFRKADGSYAAWLSRGSSTWLTAFVLKVLSLAQEQVGGSPEKLQETSNWLLSQQQADGSFQDLSPVIHRSMQGGLVGNDETVALTAFVTIALHHGLAVFQDEGAEPLKQRVEASISKASSFLGEKASAGLLGAHAAAITAYALTLTKAPADLRGVAHNNLMAMAQETGDNLYWGSVTGSQSNAVSPTPAPRNPSDPMPQAPALWIETTAYALLHLLLHEGKAEMADQAAAWLTRQGSFQGGFRSTQDTVIALDALSAYWIASHTTEERGLNVTLSSTGRNGFKSHALQLNNRQIRGLEEELQFSLGSKINVKVGGNSKGTLKVLRTYNVLDMKNTTCQDLQIEVTVKGHVEYTMEANEDYEDYEYDELPAKDDPDAPLQPVTPLQLFEGRRNRRRREAPKVVEEQESRVHYTVCIWRNGKVGLSGMAIADVTLLSGFHALRADLEKLTSLSDRYVSHFETEGPHVLLYFDSVPTSRECVGFEAVQEVPVGLVQPASATLYDYYNPERRCSVFYGAPSKSRLLATLCSAEVCQCAEGKCPRQRRALERGLQDEDGYRMKFACYYPRVEYGFQVKVLREDSRAAFRLFETKITQVLHFTKDVKAAANQMRNFLVRASCRLRLEPGKEYLIMGLDGATYDLEGHPQYLLDSNSWIEEMPSERLCRSTRQRAACAQLNDFLQEYGTQGCQV
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
17PhosphorylationASSFFTLSLQKPRLL
HHHHHHHCCCCCEEE		26.2024719451
77PhosphorylationPKVDFTLSSERDFAL
CCEEEEECCCCCEEE		27.3924275569
125PhosphorylationKDSLSRTTNIQGINL
HHHHCCCCCCCCCEE		29.2530087585
158PhosphorylationNPGQRVRYRVFALDQ
CCCCCEEEEEEEECC		14.3128258704
171PhosphorylationDQKMRPSTDTITVMV
CCCCCCCCCEEEEEE		39.5828258704
173PhosphorylationKMRPSTDTITVMVEN
CCCCCCCEEEEEEEC		20.7328258704
226N-linked_GlycosylationFSDGLESNSSTQFEV
ECCCCCCCCCCCEEE		30.5112754519
236PhosphorylationTQFEVKKYVLPNFEV
CCEEEEEEECCCEEE		11.0822461510
310O-linked_GlycosylationTKLVNGQSHISLSKA
CEEECCCCCEECCHH		24.9631492838
313PhosphorylationVNGQSHISLSKAEFQ
ECCCCCEECCHHHHH		22.5924719451
313O-linked_GlycosylationVNGQSHISLSKAEFQ
ECCCCCEECCHHHHH		22.5931492838
678AcetylationKEKTTRKKRNVNFQK
CCCCCCHHCCCCHHH		46.0130587339
696O-linked_GlycosylationEKLGQYASPTAKRCC
HHHHCCCCHHHHHHC		20.18OGP
696PhosphorylationEKLGQYASPTAKRCC
HHHHCCCCHHHHHHC		20.1823532336
698O-linked_GlycosylationLGQYASPTAKRCCQD
HHCCCCHHHHHHCCC		42.17OGP
812PhosphorylationTWEIHGLSLSKTKGL
CEEEECEECCCCCCE		34.8824719451
856PhosphorylationLELRPVLYNYLDKNL
HCCHHHHHHHHCCCC		11.2926074081
858PhosphorylationLRPVLYNYLDKNLTV
CHHHHHHHHCCCCEE		11.6126074081
862N-linked_GlycosylationLYNYLDKNLTVSVHV
HHHHHCCCCEEEEEE		40.38UniProtKB CARBOHYD
864PhosphorylationNYLDKNLTVSVHVSP
HHHCCCCEEEEEECC		21.8226074081
866PhosphorylationLDKNLTVSVHVSPVE
HCCCCEEEEEECCCC		10.9826074081
870PhosphorylationLTVSVHVSPVEGLCL
CEEEEEECCCCCEEE		14.3526074081
918PhosphorylationLKVVARGSFEFPVGD
EEEEECCCEEEECCH		18.9524505115
964PhosphorylationTLEIPGNSDPNMIPD
EEECCCCCCCCCCCC		61.4324505115
988PhosphorylationTASDPLDTLGSEGAL
EECCCCCCCCCCCCC		40.4723612710
991PhosphorylationDPLDTLGSEGALSPG
CCCCCCCCCCCCCCC		35.6523612710
1014PhosphorylationPRGCGEQTMIYLAPT
CCCCCCCHHHHHHCH		10.9624505115
1109PhosphorylationETSNWLLSQQQADGS
HHHHHHHHHHHCCCC		24.6319562805
1176PhosphorylationEASISKASSFLGEKA
HHHHHHHHHHHCCHH		36.7129449344
1177PhosphorylationASISKASSFLGEKAS
HHHHHHHHHHCCHHH		27.0629449344
1196PhosphorylationGAHAAAITAYALTLT
HHHHHHHHHHHHHHC		14.6422496350
1242O-linked_GlycosylationGSQSNAVSPTPAPRN
CCCCCCCCCCCCCCC		22.20OGP
1244O-linked_GlycosylationQSNAVSPTPAPRNPS
CCCCCCCCCCCCCCC		25.28OGP
1251O-linked_GlycosylationTPAPRNPSDPMPQAP
CCCCCCCCCCCCCCC		58.87OGP
1328N-linked_GlycosylationTTEERGLNVTLSSTG
CCCCCCCEEEEECCC		27.7916740002
1330PhosphorylationEERGLNVTLSSTGRN
CCCCCEEEEECCCCC		21.6124719451
1332PhosphorylationRGLNVTLSSTGRNGF
CCCEEEEECCCCCCH		19.2524719451
1334PhosphorylationLNVTLSSTGRNGFKS
CEEEEECCCCCCHHH		36.4624719451
1341PhosphorylationTGRNGFKSHALQLNN
CCCCCHHHHEEEECH		16.2519664994
1374PhosphorylationNVKVGGNSKGTLKVL
EEEECCCCCCCEEEE		35.42-
1391N-linked_GlycosylationYNVLDMKNTTCQDLQ
EEEEECCCCCCCEEE		33.7014760718
1417SulfationTMEANEDYEDYEYDE
EEECCCCCCCCCCCC		12.43-
1417SulfationTMEANEDYEDYEYDE
EEECCCCCCCCCCCC		12.433944109
1420SulfationANEDYEDYEYDELPA
CCCCCCCCCCCCCCC		12.403944109
1420SulfationANEDYEDYEYDELPA
CCCCCCCCCCCCCCC		12.40-
1422SulfationEDYEDYEYDELPAKD
CCCCCCCCCCCCCCC		14.423944109
1422SulfationEDYEDYEYDELPAKD
CCCCCCCCCCCCCCC		14.42-
1505PhosphorylationRADLEKLTSLSDRYV
HHCHHHHHCCCHHHH		38.3923403867
1506PhosphorylationADLEKLTSLSDRYVS
HCHHHHHCCCHHHHH		35.9923403867
1567PhosphorylationYNPERRCSVFYGAPS
CCCCCCEEEEECCCC		17.2828857561
1584PhosphorylationRLLATLCSAEVCQCA
HHHHHHHHHHHHHHH		30.4924505115
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 CO4B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CO4B_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 CO4B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CO2_HUMANC2physical
10946278
CO2_HUMANC2physical
11341920
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
OMIM Disease
152700Systemic lupus erythematosus (SLE)
614379Complement component 4B deficiency (C4BD)
Kegg Drug
There are no disease associations of PTM sites.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CO4B_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-linked glycoproteins in human saliva byglycoprotein capture and mass spectrometry.";
Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T.,Loo J.A.;
J. Proteome Res. 5:1493-1503(2006).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1328, AND MASSSPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1391, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-226.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory