dbPTM

CO5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CO5_HUMAN
UniProt AC	P01031
Protein Name	Complement C5
Gene Name	C5
Organism	Homo sapiens (Human).
Sequence Length	1676
Subcellular Localization	Secreted.
Protein Description	Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled.; Derived from proteolytic degradation of complement C5, C5 anaphylatoxin is a mediator of local inflammatory process. Binding to the receptor C5AR1 induces a variety of responses including intracellular calcium release, contraction of smooth muscle, increased vascular permeability, and histamine release from mast cells and basophilic leukocytes. [PubMed: 8182049 C5a is also a potent chemokine which stimulates the locomotion of polymorphonuclear leukocytes and directs their migration toward sites of inflammation.]
Protein Sequence	MGLLGILCFLIFLGKTWGQEQTYVISAPKIFRVGASENIVIQVYGYTEAFDATISIKSYPDKKFSYSSGHVHLSSENKFQNSAILTIQPKQLPGGQNPVSYVYLEVVSKHFSKSKRMPITYDNGFLFIHTDKPVYTPDQSVKVRVYSLNDDLKPAKRETVLTFIDPEGSEVDMVEEIDHIGIISFPDFKIPSNPRYGMWTIKAKYKEDFSTTGTAYFEVKEYVLPHFSVSIEPEYNFIGYKNFKNFEITIKARYFYNKVVTEADVYITFGIREDLKDDQKEMMQTAMQNTMLINGIAQVTFDSETAVKELSYYSLEDLNNKYLYIAVTVIESTGGFSEEAEIPGIKYVLSPYKLNLVATPLFLKPGIPYPIKVQVKDSLDQLVGGVPVTLNAQTIDVNQETSDLDPSKSVTRVDDGVASFVLNLPSGVTVLEFNVKTDAPDLPEENQAREGYRAIAYSSLSQSYLYIDWTDNHKALLVGEHLNIIVTPKSPYIDKITHYNYLILSKGKIIHFGTREKFSDASYQSINIPVTQNMVPSSRLLVYYIVTGEQTAELVSDSVWLNIEEKCGNQLQVHLSPDADAYSPGQTVSLNMATGMDSWVALAAVDSAVYGVQRGAKKPLERVFQFLEKSDLGCGAGGGLNNANVFHLAGLTFLTNANADDSQENDEPCKEILRPRRTLQKKIEEIAAKYKHSVVKKCCYDGACVNNDETCEQRAARISLGPRCIKAFTECCVVASQLRANISHKDMQLGRLHMKTLLPVSKPEIRSYFPESWLWEVHLVPRRKQLQFALPDSLTTWEIQGVGISNTGICVADTVKAKVFKDVFLEMNIPYSVVRGEQIQLKGTVYNYRTSGMQFCVKMSAVEGICTSESPVIDHQGTKSSKCVRQKVEGSSSHLVTFTVLPLEIGLHNINFSLETWFGKEILVKTLRVVPEGVKRESYSGVTLDPRGIYGTISRRKEFPYRIPLDLVPKTEIKRILSVKGLLVGEILSAVLSQEGINILTHLPKGSAEAELMSVVPVFYVFHYLETGNHWNIFHSDPLIEKQKLKKKLKEGMLSIMSYRNADYSYSVWKGGSASTWLTAFALRVLGQVNKYVEQNQNSICNSLLWLVENYQLDNGSFKENSQYQPIKLQGTLPVEARENSLYLTAFTVIGIRKAFDICPLVKIDTALIKADNFLLENTLPAQSTFTLAISAYALSLGDKTHPQFRSIVSALKREALVKGNPPIYRFWKDNLQHKDSSVPNTGTARMVETTAYALLTSLNLKDINYVNPVIKWLSEEQRYGGGFYSTQDTINAIEGLTEYSLLVKQLRLSMDIDVSYKHKGALHNYKMTDKNFLGRPVEVLLNDDLIVSTGFGSGLATVHVTTVVHKTSTSEEVCSFYLKIDTQDIEASHYRGYGNSDYKRIVACASYKPSREESSSGSSHAVMDISLPTGISANEEDLKALVEGVDQLFTDYQIKDGHVILQLNSIPSSDFLCVRFRIFELFEVGFLSPATFTVYEYHRPDKQCTMFYSTSNIKIQKVCEGAACKCVEADCGQMQEELDLTISAETRKQTACKPEIAYAYKVSITSITVENVFVKYKATLLDIYKTGEAVAEKDSEITFIKKVTCTNAELVKGRQYLIMGKEALQIKYNFSFRYIYPLDSLTWIEYWPRDTTCSSCQAFLANLDEFAEDIFLNGC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
114	Phosphorylation	VSKHFSKSKRMPITY HHHHCCCCCCCCEEE	25.05	-
120	Phosphorylation	KSKRMPITYDNGFLF CCCCCCEEEECCEEE	20.96	-
121	Phosphorylation	SKRMPITYDNGFLFI CCCCCEEEECCEEEE	14.23	-
146	Phosphorylation	QSVKVRVYSLNDDLK CCEEEEEEECCCCCC	9.25	23917254
147	Phosphorylation	SVKVRVYSLNDDLKP CEEEEEEECCCCCCC	20.17	23917254
282	Ubiquitination	LKDDQKEMMQTAMQN CCCHHHHHHHHHHHH	2.88	-
290	Phosphorylation	MQTAMQNTMLINGIA HHHHHHHHHEECCEE	9.10	24505115
505	Phosphorylation	HYNYLILSKGKIIHF CCCEEEEECCCEEEE	32.16	28060719
506	Acetylation	YNYLILSKGKIIHFG CCEEEEECCCEEEEE	61.86	25953088
508	Ubiquitination	YLILSKGKIIHFGTR EEEEECCCEEEEECC	42.07	-
514	Phosphorylation	GKIIHFGTREKFSDA CCEEEEECCCCCCCC	34.41	29052541
662	Phosphorylation	TNANADDSQENDEPC CCCCCCCCCCCCCCH	39.68	27130503
668	Phosphorylation	DSQENDEPCKEILRP CCCCCCCCHHHHHHH	37.03	-
690	Phosphorylation	IEEIAAKYKHSVVKK HHHHHHHCCCHHHHH	14.81	-
693	Phosphorylation	IAAKYKHSVVKKCCY HHHHCCCHHHHHHCC	25.18	-
700	Nitration	SVVKKCCYDGACVNN HHHHHHCCCCCCCCC	27.21	-
700	Phosphorylation	SVVKKCCYDGACVNN HHHHHHCCCCCCCCC	27.21	-
719	Phosphorylation	EQRAARISLGPRCIK HHHHHHHCCCHHHHH	23.01	24719451
725	Phosphorylation	ISLGPRCIKAFTECC HCCCHHHHHHHHHHH	3.68	-
729	O-linked_Glycosylation	PRCIKAFTECCVVAS HHHHHHHHHHHHHHH	32.73	OGP
729	Phosphorylation	PRCIKAFTECCVVAS HHHHHHHHHHHHHHH	32.73	-
736	Phosphorylation	TECCVVASQLRANIS HHHHHHHHHHHHHCC	20.38	-
741	N-linked_Glycosylation	VASQLRANISHKDMQ HHHHHHHHCCCCHHC	29.84	16335952
743	Phosphorylation	SQLRANISHKDMQLG HHHHHHCCCCHHCCC	25.04	22964224
747	N-linked_Glycosylation	ANISHKDMQLGRLHM HHCCCCHHCCCCEEE	4.17	16335952
749	Phosphorylation	ISHKDMQLGRLHMKT CCCCHHCCCCEEEHH	3.28	-
844	Phosphorylation	EQIQLKGTVYNYRTS CEEEEEEEEEEECCC	20.45	27174698
846	Phosphorylation	IQLKGTVYNYRTSGM EEEEEEEEEECCCCC	13.30	27174698
848	Phosphorylation	LKGTVYNYRTSGMQF EEEEEEEECCCCCEE	9.51	27174698
911	N-linked_Glycosylation	EIGLHNINFSLETWF EECCCCCCEEEEECC	26.27	21217642
917	N-linked_Glycosylation	INFSLETWFGKEILV CCEEEEECCCHHHHH	7.22	16335952
938	Phosphorylation	PEGVKRESYSGVTLD CCCCCCCCCCCCEEC	28.73	29449344
939	Phosphorylation	EGVKRESYSGVTLDP CCCCCCCCCCCEECC	12.51	29083192
940	Phosphorylation	GVKRESYSGVTLDPR CCCCCCCCCCEECCC	35.75	29083192
943	Phosphorylation	RESYSGVTLDPRGIY CCCCCCCEECCCCCC	29.03	29449344
943	O-linked_Glycosylation	RESYSGVTLDPRGIY CCCCCCCEECCCCCC	29.03	OGP
950	Phosphorylation	TLDPRGIYGTISRRK EECCCCCCEEEECCC	15.84	29449344
952	O-linked_Glycosylation	DPRGIYGTISRRKEF CCCCCCEEEECCCCC	9.98	OGP
952	Phosphorylation	DPRGIYGTISRRKEF CCCCCCEEEECCCCC	9.98	29083192
954	Phosphorylation	RGIYGTISRRKEFPY CCCCEEEECCCCCCC	26.35	29083192
954	O-linked_Glycosylation	RGIYGTISRRKEFPY CCCCEEEECCCCCCC	26.35	OGP
961	Phosphorylation	SRRKEFPYRIPLDLV ECCCCCCCCCCCCCC	26.88	26657352
971	Phosphorylation	PLDLVPKTEIKRILS CCCCCCHHHHHHHHC	36.55	-
978	Phosphorylation	TEIKRILSVKGLLVG HHHHHHHCCCCHHHH	21.29	24719451
1115	N-linked_Glycosylation	VENYQLDNGSFKENS HHHCCCCCCCCCCCC	57.51	UniProtKB CARBOHYD
1250	Phosphorylation	GTARMVETTAYALLT CCCHHHHHHHHHHHH	12.81	29083192
1251	Phosphorylation	TARMVETTAYALLTS CCHHHHHHHHHHHHH	12.26	29083192
1253	Phosphorylation	RMVETTAYALLTSLN HHHHHHHHHHHHHCC	8.83	25954137
1257	Phosphorylation	TTAYALLTSLNLKDI HHHHHHHHHCCCCCC	31.83	25954137
1258	Phosphorylation	TAYALLTSLNLKDIN HHHHHHHHCCCCCCC	18.41	25954137
1311	Ubiquitination	VKQLRLSMDIDVSYK HHHHHHHCCCCCCCC	6.57	-
1317	Phosphorylation	SMDIDVSYKHKGALH HCCCCCCCCCCCCCC	19.57	-
1326	Phosphorylation	HKGALHNYKMTDKNF CCCCCCCEECCCCCC	7.44	30622161
1329	Phosphorylation	ALHNYKMTDKNFLGR CCCCEECCCCCCCCC	39.40	30622161
1368	O-linked_Glycosylation	VTTVVHKTSTSEEVC EEEEEEECCCCHHEE	23.51	OGP
1369	O-linked_Glycosylation	TTVVHKTSTSEEVCS EEEEEECCCCHHEEE	34.44	OGP
1370	O-linked_Glycosylation	TVVHKTSTSEEVCSF EEEEECCCCHHEEEE	45.44	OGP
1371	O-linked_Glycosylation	VVHKTSTSEEVCSFY EEEECCCCHHEEEEE	31.37	OGP
1599	Phosphorylation	AEKDSEITFIKKVTC HCCCCCCEEEEEEEE	18.43	-
1630	N-linked_Glycosylation	EALQIKYNFSFRYIY CEEEEEEEEEEEEEE	22.53	16335952
1632	Phosphorylation	LQIKYNFSFRYIYPL EEEEEEEEEEEEEEC	12.74	24719451
1636	N-linked_Glycosylation	YNFSFRYIYPLDSLT EEEEEEEEEECCCCE	2.20	16335952

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 CO5_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CO5_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 CO5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CO6_HUMAN	C6	physical	1387399
CO7_HUMAN	C7	physical	1387399
CO8B_HUMAN	C8B	physical	3624872
CR3L1_HUMAN	CREB3L1	physical	25416956

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609536	Complement component 5 deficiency (C5D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CO5_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex."; Laursen N.S., Andersen K.R., Braren I., Spillner E.,Sottrup-Jensen L., Andersen G.R.; EMBO J. 30:606-616(2011). Cited for: X-RAY CRYSTALLOGRAPHY (4.30 ANGSTROMS) OF 20-1676, GLYCOSYLATION ATASN-911, AND DISULFIDE BONDS.	21217642 [Abstract]
"Structure of and influence of a tick complement inhibitor on humancomplement component 5."; Fredslund F., Laursen N.S., Roversi P., Jenner L., Oliveira C.L.P.,Pedersen J.S., Nunn M.A., Lea S.M., Discipio R., Sottrup-Jensen L.,Andersen G.R.; Nat. Immunol. 9:753-760(2008). Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), INTERACTION WITH TICKCOMPLEMENT INHIBITOR, GLYCOSYLATION AT ASN-741 AND ASN-911, ANDDISULFIDE BONDS.	18536718 [Abstract]
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-741; ASN-911 AND ASN-1630,AND MASS SPECTROMETRY.	16335952 [Abstract]