CO3_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CO3_MOUSE
• UniProt AC: P01027
• Protein Name: Complement C3
• Gene Name: C3
• Organism: Mus musculus (Mouse).
• Sequence Length: 1663
• Subcellular Localization: Secreted.
• Protein 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.; Derived from proteolytic degradation of complement C3, C3a anaphylatoxin is a mediator of local inflammatory process. In chronic inflammation, acts as a chemoattractant for neutrophils (By similarity). It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes. The short isoform has B-cell stimulatory activity.; C3-beta-c: Acts as a chemoattractant for neutrophils in chronic inflammation.; Acylation stimulating protein: adipogenic hormone that stimulates triglyceride (TG) synthesis and glucose transport in adipocytes, regulating fat storage and playing a role in postprandial TG clearance. Appears to stimulate TG synthesis via activation of the PLC, MAPK and AKT signaling pathways. Ligand for C5AR2. Promotes the phosphorylation, ARRB2-mediated internalization and recycling of C5AR2..
• Protein Sequence: MGPASGSQLLVLLLLLASSPLALGIPMYSIITPNVLRLESEETIVLEAHDAQGDIPVTVTVQDFLKRQVLTSEKTVLTGASGHLRSVSIKIPASKEFNSDKEGHKYVTVVANFGETVVEKAVMVSFQSGYLFIQTDKTIYTPGSTVLYRIFTVDNNLLPVGKTVVILIETPDGIPVKRDILSSNNQHGILPLSWNIPELVNMGQWKIRAFYEHAPKQIFSAEFEVKEYVLPSFEVRVEPTETFYYIDDPNGLEVSIIAKFLYGKNVDGTAFVIFGVQDGDKKISLAHSLTRVVIEDGVGDAVLTRKVLMEGVRPSNADALVGKSLYVSVTVILHSGSDMVEAERSGIPIVTSPYQIHFTKTPKFFKPAMPFDLMVFVTNPDGSPASKVLVVTQGSNAKALTQDDGVAKLSINTPNSRQPLTITVRTKKDTLPESRQATKTMEAHPYSTMHNSNNYLHLSVSRMELKPGDNLNVNFHLRTDPGHEAKIRYYTYLVMNKGKLLKAGRQVREPGQDLVVLSLPITPEFIPSFRLVAYYTLIGASGQREVVADSVWVDVKDSCIGTLVVKGDPRDNHLAPGQQTTLRIEGNQGARVGLVAVDKGVFVLNKKNKLTQSKIWDVVEKADIGCTPGSGKNYAGVFMDAGLAFKTSQGLQTEQRADLECTKPAARRRRSVQLMERRMDKAGQYTDKGLRKCCEDGMRDIPMRYSCQRRARLITQGENCIKAFIDCCNHITKLREQHRRDHVLGLARSELEEDIIPEEDIISRSHFPQSWLWTIEELKEPEKNGISTKVMNIFLKDSITTWEILAVSLSDKKGICVADPYEIRVMQDFFIDLRLPYSVVRNEQVEIRAVLFNYREQEELKVRVELLHNPAFCSMATAKNRYFQTIKIPPKSSVAVPYVIVPLKIGQQEVEVKAAVFNHFISDGVKKTLKVVPEGMRINKTVAIHTLDPEKLGQGGVQKVDVPAADLSDQVPDTDSETRIILQGSPVVQMAEDAVDGERLKHLIVTPAGCGEQNMIGMTPTVIAVHYLDQTEQWEKFGIEKRQEALELIKKGYTQQLAFKQPSSAYAAFNNRPPSTWLTAYVVKVFSLAANLIAIDSHVLCGAVKWLILEKQKPDGVFQEDGPVIHQEMIGGFRNAKEADVSLTAFVLIALQEARDICEGQVNSLPGSINKAGEYIEASYMNLQRPYTVAIAGYALALMNKLEEPYLGKFLNTAKDRNRWEEPDQQLYNVEATSYALLALLLLKDFDSVPPVVRWLNEQRYYGGGYGSTQATFMVFQALAQYQTDVPDHKDLNMDVSFHLPSRSSATTFRLLWENGNLLRSEETKQNEAFSLTAKGKGRGTLSVVAVYHAKLKSKVTCKKFDLRVSIRPAPETAKKPEEAKNTMFLEICTKYLGDVDATMSILDISMMTGFAPDTKDLELLASGVDRYISKYEMNKAFSNKNTLIIYLEKISHTEEDCLTFKVHQYFNVGLIQPGSVKVYSYYNLEESCTRFYHPEKDDGMLSKLCHSEMCRCAEENCFMQQSQEKINLNVRLDKACEPGVDYVYKTELTNIELLDDFDEYTMTIQQVIKSGSDEVQAGQQRKFISHIKCRNALKLQKGKKYLMWGLSSDLWGEKPNTSYIIGKDTWVEHWPEAEECQDQKYQKQCEELGAFTESMVVYGCPN

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
40	Phosphorylation	PNVLRLESEETIVLE CCEEECCCCEEEEEE	45.37	-
74	Ubiquitination	RQVLTSEKTVLTGAS HHCCCCCCEEEECCC	43.64	22790023
90	Ubiquitination	HLRSVSIKIPASKEF CCEEEEEEECCCCCC	34.82	27667366
95	Ubiquitination	SIKIPASKEFNSDKE EEEECCCCCCCCCCC	69.31	22790023
126	Ubiquitination	EKAVMVSFQSGYLFI EEEEEEEECCCEEEE	4.57	27667366
306	Ubiquitination	GDAVLTRKVLMEGVR CHHHHHHHHHHHCCC	34.19	22790023
330	Phosphorylation	KSLYVSVTVILHSGS CEEEEEEEEEEECCC	8.36	-
360	Ubiquitination	PYQIHFTKTPKFFKP CEEEEEECCCCCCCC	62.98	22790023
398	Ubiquitination	VTQGSNAKALTQDDG EECCCCCEEECCCCC	48.45	22790023
408	Ubiquitination	TQDDGVAKLSINTPN CCCCCEEEEEECCCC	40.12	22790023
466	Ubiquitination	SVSRMELKPGDNLNV EEEEEEECCCCCEEE	33.38	22790023
480	Ubiquitination	VNFHLRTDPGHEAKI EEEEEECCCCCHHHH	40.52	27667366
489	Phosphorylation	GHEAKIRYYTYLVMN CCHHHHEEEEEEEEE	12.02	17203969
495	Oxidation	RYYTYLVMNKGKLLK EEEEEEEEECCCHHH	3.86	17203969
566	Ubiquitination	CIGTLVVKGDPRDNH EEEEEEEECCCCCCC	50.55	22790023
599	Ubiquitination	VGLVAVDKGVFVLNK EEEEEEECCEEEEEC	50.83	22790023
671	Phosphorylation	PAARRRRSVQLMERR HHHHHHHHHHHHHHH	16.65	22817900
688	Ubiquitination	KAGQYTDKGLRKCCE HHCCCCHHHHHHHCH	52.63	27667366
720	S-palmitoylation	LITQGENCIKAFIDC HHHCCHHHHHHHHHH	2.69	28526873
749	Phosphorylation	HVLGLARSELEEDII HHHHHHHHHHHHCCC	40.71	26525534
816	S-palmitoylation	LSDKKGICVADPYEI CCCCCCEEECCCCEE	2.55	28526873
861	Ubiquitination	YREQEELKVRVELLH HHCHHHHEEEEEHHC	31.13	27667366
873	S-nitrosylation	LLHNPAFCSMATAKN HHCCCCCCCHHHCCC	2.71	22178444
873	S-palmitoylation	LLHNPAFCSMATAKN HHCCCCCCCHHHCCC	2.71	26165157
879	Ubiquitination	FCSMATAKNRYFQTI CCCHHHCCCCCEEEE	37.29	22790023
892	Phosphorylation	TIKIPPKSSVAVPYV EEECCCCCCCCCCEE	35.50	21454597
893	Phosphorylation	IKIPPKSSVAVPYVI EECCCCCCCCCCEEE	21.88	21454597
936	Sulfoxidation	LKVVPEGMRINKTVA EEECCCCCCCCCEEE	3.56	21406390
939	N-linked_Glycosylation	VPEGMRINKTVAIHT CCCCCCCCCEEEEEE	24.47	-
968	Phosphorylation	DVPAADLSDQVPDTD CCCHHHCCCCCCCCC	26.92	26525534
974	Phosphorylation	LSDQVPDTDSETRII CCCCCCCCCCCCEEE	35.04	26525534
976	Phosphorylation	DQVPDTDSETRIILQ CCCCCCCCCCEEEEE	42.85	26525534
985	Phosphorylation	TRIILQGSPVVQMAE CEEEEECCCCEEECC	11.10	24719451
1188	Phosphorylation	MNLQRPYTVAIAGYA CCCCCCHHHHHHHHH	13.22	28978645
1194	Phosphorylation	YTVAIAGYALALMNK HHHHHHHHHHHHHHH	6.87	28978645
1215	Succinylation	GKFLNTAKDRNRWEE HHHHCCHHHCCCCCC	56.00	23954790
1215	Ubiquitination	GKFLNTAKDRNRWEE HHHHCCHHHCCCCCC	56.00	27667366
1321	Phosphorylation	ENGNLLRSEETKQNE HCCCCCCCCCCCCCC	39.49	-
1325	Ubiquitination	LLRSEETKQNEAFSL CCCCCCCCCCCCEEE	55.17	22790023
1335	Ubiquitination	EAFSLTAKGKGRGTL CCEEEEECCCCCCEE	56.79	22790023
1360	Acetylation	KSKVTCKKFDLRVSI CCCCEEEECEEEEEE	46.38	24062335
1427	Dimethylation	LLASGVDRYISKYEM HHHHCHHHHHHHHHH	28.42	-
1431	Ubiquitination	GVDRYISKYEMNKAF CHHHHHHHHHHHHHH	35.35	22790023
1439	Phosphorylation	YEMNKAFSNKNTLII HHHHHHHCCCCEEEE	52.32	-
1443	Phosphorylation	KAFSNKNTLIIYLEK HHHCCCCEEEEEEEE	22.42	-
1535	Ubiquitination	NLNVRLDKACEPGVD CCCHHHHCCCCCCCC	60.57	22790023
1537	S-palmitoylation	NVRLDKACEPGVDYV CHHHHCCCCCCCCEE	8.81	26165157
1573	Phosphorylation	QQVIKSGSDEVQAGQ HHHHHHCCCCCHHHH	37.37	-
1617	N-linked_Glycosylation	DLWGEKPNTSYIIGK CCCCCCCCCEEEEEC	53.37	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of CO3_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CO3_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of CO3_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CO3_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-489, AND MASSSPECTROMETRY.
PubMed: 17203969