CO4B_MOUSE - dbPTM
CO4B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CO4B_MOUSE
UniProt AC P01029
Protein Name Complement C4-B
Gene Name C4b
Organism Mus musculus (Mouse).
Sequence Length 1738
Subcellular Localization Secreted . Cell junction, synapse . Cell projection, axon . Cell projection, dendrite .
Protein Description Non-enzymatic component of 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. Catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens (By similarity)..
Protein Sequence MRLLWGLAWVFSFCASSLQKPRLLLFSPSVVNLGTPLSVGVQLLDAPPGQEVKGSVFLRNPKGGSCSPKKDFKLSSGDDFVLLSLEVPLEDVRSCGLFDLRRAPHIQLVAQSPWLRNTAFKATETQGVNLLFSSRRGHIFVQTDQPIYNPGQRVRYRVFALDQKMRPSTDFLTITVENSHGLRVLKKEIFTSTSIFQDAFTIPDISEPGTWKISARFSDGLESNRSTHFEVKKYVLPNFEVKITPWKPYILMVPSNSDEIQLDIQARYIYGKPVQGVAYTRFALMDEQGKRTFLRGLETQAKLVEGRTHISISKDQFQAALDKINIGVRDLEGLRLYAATAVIESPGGEMEEAELTSWRFVSSAFSLDLSRTKRHLVPGAHFLLQALVQEMSGSEASNVPVKVSATLVSGSDSQVLDIQQSTNGIGQVSISFPIPPTVTELRLLVSAGSLYPAIARLTVQAPPSRGTGFLSIEPLDPRSPSVGDTFILNLQPVGIPAPTFSHYYYMIISRGQIMAMGREPRKTVTSVSVLVDHQLAPSFYFVAYFYHQGHPVANSLLINIQSRDCEGKLQLKVDGAKEYRNADMMKLRIQTDSKALVALGAVDMALYAVGGRSHKPLDMSKVFEVINSYNVGCGPGGGDDALQVFQDAGLAFSDGDRLTQTREDLSCPKEKKSRQKRNVNFQKAVSEKLGQYSSPDAKRCCQDGMTKLPMKRTCEQRAARVPQQACREPFLSCCKFAEDLRRNQTRSQAHLARNNHNMLQEEDLIDEDDILVRTSFPENWLWRVEPVDSSKLLTVWLPDSMTTWEIHGVSLSKSKGLCVAKPTRVRVFRKFHLHLRLPISIRRFEQFELRPVLYNYLNDDVAVSVHVTPVEGLCLAGGGMMAQQVTVPAGSARPVAFSVVPTAAANVPLKVVARGVFDLGDAVSKILQIEKEGAIHREELVYNLDPLNNLGRTLEIPGSSDPNIVPDGDFSSLVRVTASEPLETMGSEGALSPGGVASLLRLPQGCAEQTMIYLAPTLTASNYLDRTEQWSKLSPETKDHAVDLIQKGYMRIQQFRKNDGSFGAWLHRDSSTWLTAFVLKILSLAQEQVGNSPEKLQETASWLLAQQLGDGSFHDPCPVIHRAMQGGLVGSDETVALTAFVVIALHHGLDVFQDDDAKQLKNRVEASITKANSFLGQKASAGLLGAHAAAITAYALTLTKASEDLRNVAHNSLMAMAEETGEHLYWGLVLGSQDKVVLRPTAPRSPTEPVPQAPALWIETTAYALLHLLLREGKGKMADKAASWLTHQGSFHGAFRSTQDTVVTLDALSAYWIASHTTEEKALNVTLSSMGRNGLKTHGLHLNNHQVKGLEEELKFSLGSTISVKVEGNSKGTLKILRTYNVLDMKNTTCQDLQIEVKVTGAVEYAWDANEDYEDYYDMPAADDPSVPLQPVTPLQLFEGRRSRRRREAPKVVEEQESRVQYTVCIWRNGKLGLSGMAIADITLLSGFHALRADLEKLTSLSDRYVSHFETDGPHVLLYFDSVPTTRECVGFGASQEVVVGLVQPSSAVLYDYYSPDHKCSVFYAAPTKSQLLATLCSGDVCQCAEGKCPRLLRSLERRVEDKDGYRMRFACYYPRVEYGFTVKVLREDGRAAFRLFESKITQVLHFRKDTMASIGQTRNFLSRASCRLRLEPNKEYLIMGMDGETSDNKGDPQYLLDSNTWIEEMPSEQMCKSTRHRAACFQLKDFLMEFSSRGCQV
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
224N-linked_GlycosylationFSDGLESNRSTHFEV
ECCCCCCCCCCCEEE
32.33-
272UbiquitinationQARYIYGKPVQGVAY
EHHHHCCCCCCCEEE
25.66-
302UbiquitinationRGLETQAKLVEGRTH
HHHHHHHHHHCCCCE
43.16-
314UbiquitinationRTHISISKDQFQAAL
CCEEEECHHHHHHHH
54.61-
323UbiquitinationQFQAALDKINIGVRD
HHHHHHHHCCCCCCC
38.20-
451PhosphorylationLVSAGSLYPAIARLT
HHHHCCHHHEEEEEE
7.72-
683UbiquitinationKRNVNFQKAVSEKLG
HHCCCHHHHHHHHHC
46.77-
688UbiquitinationFQKAVSEKLGQYSSP
HHHHHHHHHCCCCCC
50.87-
743N-linked_GlycosylationFAEDLRRNQTRSQAH
HHHHHHHCHHHHHHH
40.93-
810PhosphorylationTWEIHGVSLSKSKGL
CEEEEEEEECCCCCE
31.3622324799
812PhosphorylationEIHGVSLSKSKGLCV
EEEEEEECCCCCEEE
27.6322324799
818S-palmitoylationLSKSKGLCVAKPTRV
ECCCCCEEEECCCEE
3.6926165157
910UbiquitinationAAANVPLKVVARGVF
CCCCCCCEEEEEEEC
28.70-
925UbiquitinationDLGDAVSKILQIEKE
CHHHHHHHHHHHHHC
40.62-
1034PhosphorylationTEQWSKLSPETKDHA
HHHHHHCCHHHHHHH
25.1523737553
1192PhosphorylationGAHAAAITAYALTLT
HHHHHHHHHHHHHHH
14.64-
1194PhosphorylationHAAAITAYALTLTKA
HHHHHHHHHHHHHHC
8.09-
1315PhosphorylationLSAYWIASHTTEEKA
HHHHHHHCCCCCHHH
16.54-
1324N-linked_GlycosylationTTEEKALNVTLSSMG
CCCHHHHCEEHHHCC
29.5917330941
1387N-linked_GlycosylationYNVLDMKNTTCQDLQ
EEEEECCCCCCCCEE
33.70-
1413SulfationAWDANEDYEDYYDMP
EEECCCCCHHHCCCC
12.43-
1413SulfationAWDANEDYEDYYDMP
EEECCCCCHHHCCCC
12.43-
1416SulfationANEDYEDYYDMPAAD
CCCCCHHHCCCCCCC
6.88-
1416SulfationANEDYEDYYDMPAAD
CCCCCHHHCCCCCCC
6.88-
1417SulfationNEDYEDYYDMPAADD
CCCCHHHCCCCCCCC
20.35-
1417SulfationNEDYEDYYDMPAADD
CCCCHHHCCCCCCCC
20.35-

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CO4B_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CO4B_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CO4B_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides.";
Bernhard O.K., Kapp E.A., Simpson R.J.;
J. Proteome Res. 6:987-995(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1324, AND MASSSPECTROMETRY.

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