MCP_HUMAN - dbPTM
MCP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCP_HUMAN
UniProt AC P15529
Protein Name Membrane cofactor protein
Gene Name CD46
Organism Homo sapiens (Human).
Sequence Length 392
Subcellular Localization Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane
Single-pass type I membrane protein . Inner acrosomal membrane of spermatozoa. Internalized upon binding of Measles virus, Herpesvirus 6 or Neisseria gonorrhoeae, which results in an i
Protein Description Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-cells which induces the differentiation of CD4+ into T-regulatory 1 cells. T-regulatory 1 cells suppress immune responses by secreting interleukin-10, and therefore are thought to prevent autoimmunity.; (Microbial infection) A number of viral and bacterial pathogens seem to bind MCP in order to exploit its immune regulation property and directly induce an immunosuppressive phenotype in T-cells.; (Microbial infection) Acts as a receptor for Adenovirus subgroup B2 and Ad3.; (Microbial infection) Acts as a receptor for cultured Measles virus.; (Microbial infection) Acts as a receptor for Herpesvirus 6/HHV-6.; (Microbial infection) May act as a receptor for pathogenic bacteria Neisseria and Streptococcus pyogenes. [PubMed: 7708671]
Protein Sequence MEPPGRRECPFPSWRFPGLLLAAMVLLLYSFSDACEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAVPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAIWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWDPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPTYKPPVSNYPGYPKPEEGILDSLDVWVIAVIVIAIVVGVAVICVVPYRYLQRRKKKGTYLTDETHREVKFTSL
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
13PhosphorylationRRECPFPSWRFPGLL
CCCCCCCCCCCHHHH		31.1226091039
51UbiquitinationMELIGKPKPYYEIGE
HHHHCCCCCCCCCCC		49.4929967540
66UbiquitinationRVDYKCKKGYFYIPP
CCCEECCCCEEECCC		69.21-
66 (in isoform 2)Ubiquitination-69.21-
83N-linked_GlycosylationTHTICDRNHTWLPVS
EEEECCCCCCEEECC		24.56UniProtKB CARBOHYD
114N-linked_GlycosylationNGQAVPANGTYEFGY
CCCEECCCCEEEECC		36.95UniProtKB CARBOHYD
153UbiquitinationSVAIWSGKPPICEKV
CEEEECCCCCCCEEE		41.9529967540
153AcetylationSVAIWSGKPPICEKV
CEEEECCCCCCCEEE		41.9526051181
159UbiquitinationGKPPICEKVLCTPPP
CCCCCCEEEEECCCC		35.7829967540
159AcetylationGKPPICEKVLCTPPP
CCCCCCEEEEECCCC		35.7826051181
163O-linked_GlycosylationICEKVLCTPPPKIKN
CCEEEEECCCCCCCC		34.37UniProtKB CARBOHYD
163PhosphorylationICEKVLCTPPPKIKN
CCEEEEECCCCCCCC		34.3724719451
167UbiquitinationVLCTPPPKIKNGKHT
EEECCCCCCCCCCCC		72.5729967540
224UbiquitinationSRAAPECKVVKCRFP
HCCCCCCCEEEEECE		48.6927667366
224 (in isoform 2)Ubiquitination-48.69-
237UbiquitinationFPVVENGKQISGFGK
CEEEECCEEECCCCC		56.9229967540
2442-HydroxyisobutyrylationKQISGFGKKFYYKAT
EEECCCCCCEEEEEE		37.13-
273N-linked_GlycosylationDTIVCDSNSTWDPPV
CEEEECCCCCCCCCC		30.1517660510
290O-linked_GlycosylationCLKVLPPSSTKPPAL
EEEECCCCCCCCCCC		49.01UniProtKB CARBOHYD
291O-linked_GlycosylationLKVLPPSSTKPPALS
EEECCCCCCCCCCCC		46.34UniProtKB CARBOHYD
292O-linked_GlycosylationKVLPPSSTKPPALSH
EECCCCCCCCCCCCC		52.48UniProtKB CARBOHYD
293UbiquitinationVLPPSSTKPPALSHS
ECCCCCCCCCCCCCE		51.4527667366
298O-linked_GlycosylationSTKPPALSHSVSTSS
CCCCCCCCCEEECCC		18.80UniProtKB CARBOHYD
298PhosphorylationSTKPPALSHSVSTSS
CCCCCCCCCEEECCC		18.8030242111
300O-linked_GlycosylationKPPALSHSVSTSSTT
CCCCCCCEEECCCCC		17.87UniProtKB CARBOHYD
300PhosphorylationKPPALSHSVSTSSTT
CCCCCCCEEECCCCC		17.8730242111
302O-linked_GlycosylationPALSHSVSTSSTTKS
CCCCCEEECCCCCCC		26.11UniProtKB CARBOHYD
302PhosphorylationPALSHSVSTSSTTKS
CCCCCEEECCCCCCC		26.1130242111
303O-linked_GlycosylationALSHSVSTSSTTKSP
CCCCEEECCCCCCCC		25.25UniProtKB CARBOHYD
303PhosphorylationALSHSVSTSSTTKSP
CCCCEEECCCCCCCC		25.2530242111
304O-linked_GlycosylationLSHSVSTSSTTKSPA
CCCEEECCCCCCCCC		20.41UniProtKB CARBOHYD
304PhosphorylationLSHSVSTSSTTKSPA
CCCEEECCCCCCCCC		20.4130242111
305O-linked_GlycosylationSHSVSTSSTTKSPAS
CCEEECCCCCCCCCC		39.94UniProtKB CARBOHYD
305PhosphorylationSHSVSTSSTTKSPAS
CCEEECCCCCCCCCC		39.9430242111
306O-linked_GlycosylationHSVSTSSTTKSPASS
CEEECCCCCCCCCCC		37.70UniProtKB CARBOHYD
306PhosphorylationHSVSTSSTTKSPASS
CEEECCCCCCCCCCC		37.7030242111
307O-linked_GlycosylationSVSTSSTTKSPASSA
EEECCCCCCCCCCCC		31.32UniProtKB CARBOHYD
307PhosphorylationSVSTSSTTKSPASSA
EEECCCCCCCCCCCC		31.3230242111
308UbiquitinationVSTSSTTKSPASSAS
EECCCCCCCCCCCCC		55.3127667366
309O-linked_GlycosylationSTSSTTKSPASSASG
ECCCCCCCCCCCCCC		24.49UniProtKB CARBOHYD
312O-linked_GlycosylationSTTKSPASSASGPRP
CCCCCCCCCCCCCCC		29.80UniProtKB CARBOHYD
313O-linked_GlycosylationTTKSPASSASGPRPT
CCCCCCCCCCCCCCC		28.67UniProtKB CARBOHYD
314 (in isoform 16)Ubiquitination-18.9321890473
315O-linked_GlycosylationKSPASSASGPRPTYK
CCCCCCCCCCCCCCC		51.80UniProtKB CARBOHYD
320O-linked_GlycosylationSASGPRPTYKPPVSN
CCCCCCCCCCCCCCC		45.52UniProtKB CARBOHYD
320PhosphorylationSASGPRPTYKPPVSN
CCCCCCCCCCCCCCC		45.52-
321 (in isoform 16)Phosphorylation-24.9527273156
323 (in isoform 16)Phosphorylation-24.9027273156
324 (in isoform 16)Phosphorylation-37.7125159151
326O-linked_GlycosylationPTYKPPVSNYPGYPK
CCCCCCCCCCCCCCC		36.10UniProtKB CARBOHYD
326 (in isoform 16)Phosphorylation-36.1028152594
327 (in isoform 16)Ubiquitination-47.4521890473
328 (in isoform 16)Phosphorylation-7.1929514088
329UbiquitinationKPPVSNYPGYPKPEE
CCCCCCCCCCCCCCC		39.8423000965
329 (in isoform 16)Phosphorylation-39.8429514088
330UbiquitinationPPVSNYPGYPKPEEG
CCCCCCCCCCCCCCC		40.8023000965
330 (in isoform 16)Phosphorylation-40.8029514088
331UbiquitinationPVSNYPGYPKPEEGI
CCCCCCCCCCCCCCC		11.9923000965
333UbiquitinationSNYPGYPKPEEGILD
CCCCCCCCCCCCCHH		57.4827667366
333 (in isoform 7)Ubiquitination-57.4821890473
340 (in isoform 7)Phosphorylation-45.2827273156
342 (in isoform 7)Phosphorylation-6.5127273156
343UbiquitinationEGILDSLDVWVIAVI
CCCHHHHHHHHHHHH		35.8623000965
343 (in isoform 7)Phosphorylation-35.8625159151
344UbiquitinationGILDSLDVWVIAVIV
CCHHHHHHHHHHHHH		5.5123000965
345UbiquitinationILDSLDVWVIAVIVI
CHHHHHHHHHHHHHH		3.8823000965
345 (in isoform 7)Phosphorylation-3.8828152594
346UbiquitinationLDSLDVWVIAVIVIA
HHHHHHHHHHHHHHH		1.7023000965
346 (in isoform 7)Ubiquitination-1.7021890473
347UbiquitinationDSLDVWVIAVIVIAI
HHHHHHHHHHHHHHH		1.1627667366
347 (in isoform 7)Phosphorylation-1.1629514088
347 (in isoform 4)Ubiquitination-1.1621890473
348UbiquitinationSLDVWVIAVIVIAIV
HHHHHHHHHHHHHHH		3.8627667366
348 (in isoform 7)Phosphorylation-3.8629514088
348 (in isoform 6)Ubiquitination-3.8621890473
349 (in isoform 7)Phosphorylation-2.1729514088
354 (in isoform 4)Phosphorylation-1.4527273156
355 (in isoform 6)Phosphorylation-1.9627273156
356 (in isoform 4)Phosphorylation-4.1127273156
357 (in isoform 4)Phosphorylation-7.2625159151
357 (in isoform 6)Phosphorylation-7.2627273156
358UbiquitinationVIAIVVGVAVICVVP
HHHHHHHHHHHHHHH		2.3123000965
358 (in isoform 6)Phosphorylation-2.3125159151
359UbiquitinationIAIVVGVAVICVVPY
HHHHHHHHHHHHHHH		4.5023000965
359 (in isoform 4)Phosphorylation-4.5028152594
360UbiquitinationAIVVGVAVICVVPYR
HHHHHHHHHHHHHHH		3.0323000965
360 (in isoform 6)Phosphorylation-3.0328152594
360 (in isoform 4)Ubiquitination-3.0321890473
361UbiquitinationIVVGVAVICVVPYRY
HHHHHHHHHHHHHHH		0.7723000965
361 (in isoform 4)Phosphorylation-0.7729514088
361 (in isoform 6)Ubiquitination-0.7721890473
362UbiquitinationVVGVAVICVVPYRYL
HHHHHHHHHHHHHHH		1.7127667366
362 (in isoform 4)Phosphorylation-1.7129514088
362 (in isoform 6)Phosphorylation-1.7129514088
362 (in isoform 3)Ubiquitination-1.7121890473
363UbiquitinationVGVAVICVVPYRYLQ
HHHHHHHHHHHHHHH		3.1427667366
363 (in isoform 4)Phosphorylation-3.1429514088
363 (in isoform 6)Phosphorylation-3.1429514088
363 (in isoform 5)Ubiquitination-3.1421890473
364 (in isoform 6)Phosphorylation-2.7529514088
368PhosphorylationICVVPYRYLQRRKKK
HHHHHHHHHHHHHCC		11.0111901164
369 (in isoform 3)Phosphorylation-2.0627273156
370 (in isoform 5)Phosphorylation-33.9127273156
371 (in isoform 3)Phosphorylation-50.2027273156
372 (in isoform 3)Phosphorylation-42.0325159151
372 (in isoform 5)Phosphorylation-42.0327273156
373UbiquitinationYRYLQRRKKKGTYLT
HHHHHHHHCCCCCCC		62.1123000965
373 (in isoform 5)Phosphorylation-62.1125159151
374UbiquitinationRYLQRRKKKGTYLTD
HHHHHHHCCCCCCCC		55.4123000965
374 (in isoform 3)Phosphorylation-55.4128152594
375UbiquitinationYLQRRKKKGTYLTDE
HHHHHHCCCCCCCCC		60.5623000965
375 (in isoform 5)Phosphorylation-60.5628152594
375 (in isoform 3)Ubiquitination-60.5621890473
376UbiquitinationLQRRKKKGTYLTDET
HHHHHCCCCCCCCCC		28.5923000965
376 (in isoform 3)Phosphorylation-28.5929514088
376 (in isoform 5)Ubiquitination-28.5921890473
377UbiquitinationQRRKKKGTYLTDETH
HHHHCCCCCCCCCCC		25.0027667366
377PhosphorylationQRRKKKGTYLTDETH
HHHHCCCCCCCCCCC		25.0028152594
377 (in isoform 3)Phosphorylation-25.0029514088
377 (in isoform 5)Phosphorylation-25.0029514088
377 (in isoform 2)Ubiquitination-25.0021890473
378PhosphorylationRRKKKGTYLTDETHR
HHHCCCCCCCCCCCC		19.1024702127
378 (in isoform 3)Phosphorylation-19.1029514088
378 (in isoform 5)Phosphorylation-19.1029514088
379 (in isoform 5)Phosphorylation-4.9629514088
380PhosphorylationKKKGTYLTDETHREV
HCCCCCCCCCCCCEE		22.7524702127
384 (in isoform 2)Phosphorylation-23.1227273156
386 (in isoform 2)Phosphorylation-42.3227273156
387 (in isoform 2)Phosphorylation-6.6125159151
388UbiquitinationDETHREVKFTSL---
CCCCCEEECCCC---		37.8723000965
389 (in isoform 2)Phosphorylation-7.2928152594
390UbiquitinationTHREVKFTSL-----
CCCEEECCCC-----		24.3323000965
390 (in isoform 2)Ubiquitination-24.3321890473
391PhosphorylationHREVKFTSL------
CCEEECCCC------		34.9028450419
391 (in isoform 2)Phosphorylation-34.9029514088
392 (in isoform 2)Phosphorylation-8.0629514088
393 (in isoform 2)Phosphorylation-29514088
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
354YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
83NGlycosylation

8764003
114NGlycosylation

8764003
114NGlycosylation

8764003
114NGlycosylation

8764003
273NGlycosylation

8764003
273NGlycosylation

8764003
273NGlycosylation

8764003
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 MCP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD9_HUMANCD9physical
10741407
CD151_HUMANCD151physical
10741407
ITB1_HUMANITGB1physical
10741407
MOES_HUMANMSNphysical
7884872
DLG4_HUMANDLG4physical
11714708
YES_HUMANYES1physical
11901164
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612922Hemolytic uremic syndrome atypical 2 (AHUS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MCP_HUMAN

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Related Literatures of Post-Translational Modification

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