MCTP2_HUMAN - dbPTM
MCTP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCTP2_HUMAN
UniProt AC Q6DN12
Protein Name Multiple C2 and transmembrane domain-containing protein 2
Gene Name MCTP2
Organism Homo sapiens (Human).
Sequence Length 878
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Might play a role in the development of cardiac outflow tract..
Protein Sequence MDLDKPSVWGSLKQRTRPLLINLSKKKVKKNPSKPPDLRARHHLDRRLSLSVPDLLEAEALAPEGRPYSGPQSSYTSVPSSLSTAGIFPKSSSSSLKQSEEELDWSQEEASHLHVVETDSEEAYASPAERRRVSSNGIFDLQKTSLGGDAPEEPEKLCGSSDLNASMTSQHFEEQSVPGEASDGLSNLPSPFAYLLTIHLKEGRNLVVRDRCGTSDPYVKFKLNGKTLYKSKVIYKNLNPVWDEIVVLPIQSLDQKLRVKVYDRDLTTSDFMGSAFVILSDLELNRTTEHILKLEDPNSLEDDMGVIVLNLNLVVKQGDFKRHRWSNRKRLSASKSSLIRNLRLSESLKKNQLWNGIISITLLEGKNVSGGSMTEMFVQLKLGDQRYKSKTLCKSANPQWQEQFDFHYFSDRMGILDIEVWGKDNKKHEERLGTCKVDISALPLKQANCLELPLDSCLGALLMLVTLTPCAGVSVSDLCVCPLADLSERKQITQRYCLQNSLKDVKDVGILQVKVLKAADLLAADFSGKSDPFCLLELGNDRLQTHTVYKNLNPEWNKVFTFPIKDIHDVLEVTVFDEDGDKPPDFLGKVAIPLLSIRDGQPNCYVLKNKDLEQAFKGVIYLEMDLIYNPVKASIRTFTPREKRFVEDSRKLSKKILSRDVDRVKRITMAIWNTMQFLKSCFQWESTLRSTIAFAVFLITVWNFELYMIPLALLLIFVYNFIRPVKGKVSSIQDSQESTDIDDEEDEDDKESEKKGLIERIYMVQDIVSTVQNVLEEIASFGERIKNTFNWTVPFLSSLACLILAAATIILYFIPLRYIILIWGINKFTKKLRNPYSIDNNELLDFLSRVPSDVQKVQYAELKLCSSHSPLRKKRSAL
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
7Phosphorylation-MDLDKPSVWGSLKQ
-CCCCCCCHHHHHHH
35.9226074081
11PhosphorylationDKPSVWGSLKQRTRP
CCCCHHHHHHHHHHC
19.3828355574
13MethylationPSVWGSLKQRTRPLL
CCHHHHHHHHHHCEE
39.16115972899
24UbiquitinationRPLLINLSKKKVKKN
HCEEEECCHHHHCCC
37.6329967540
24PhosphorylationRPLLINLSKKKVKKN
HCEEEECCHHHHCCC
37.6325159151
27AcetylationLINLSKKKVKKNPSK
EEECCHHHHCCCCCC
64.127674197
30AcetylationLSKKKVKKNPSKPPD
CCHHHHCCCCCCCCC
76.667674207
33PhosphorylationKKVKKNPSKPPDLRA
HHHCCCCCCCCCHHH
68.1628464451
49PhosphorylationHHLDRRLSLSVPDLL
HHHHHCCCCCHHHHH
19.4526657352
51PhosphorylationLDRRLSLSVPDLLEA
HHHCCCCCHHHHHHH
28.3826657352
69PhosphorylationAPEGRPYSGPQSSYT
CCCCCCCCCCCCCCC
46.8323898821
75PhosphorylationYSGPQSSYTSVPSSL
CCCCCCCCCCCCCCC
14.3127642862
76PhosphorylationSGPQSSYTSVPSSLS
CCCCCCCCCCCCCCC
25.79-
80PhosphorylationSSYTSVPSSLSTAGI
CCCCCCCCCCCCCCC
41.58-
94UbiquitinationIFPKSSSSSLKQSEE
CCCCCCCCCHHHCHH
41.4529967540
102UbiquitinationSLKQSEEELDWSQEE
CHHHCHHHCCCCHHH
48.2329967540
105UbiquitinationQSEEELDWSQEEASH
HCHHHCCCCHHHHHC
17.9729967540
111PhosphorylationDWSQEEASHLHVVET
CCCHHHHHCCEEEEC
29.8427642862
117UbiquitinationASHLHVVETDSEEAY
HHCCEEEECCCHHHC
45.8929967540
118PhosphorylationSHLHVVETDSEEAYA
HCCEEEECCCHHHCC
32.9627642862
124PhosphorylationETDSEEAYASPAERR
ECCCHHHCCCHHHHC
15.7627642862
134PhosphorylationPAERRRVSSNGIFDL
HHHHCCCCCCCCEEE
19.1023401153
135PhosphorylationAERRRVSSNGIFDLQ
HHHCCCCCCCCEEEC
35.9025159151
138UbiquitinationRRVSSNGIFDLQKTS
CCCCCCCCEEECCCC
2.5829967540
143UbiquitinationNGIFDLQKTSLGGDA
CCCEEECCCCCCCCC
47.5929967540
144PhosphorylationGIFDLQKTSLGGDAP
CCEEECCCCCCCCCC
19.0725159151
145PhosphorylationIFDLQKTSLGGDAPE
CEEECCCCCCCCCCC
31.8625159151
170UbiquitinationLNASMTSQHFEEQSV
CCHHHHHHHHHHCCC
35.8029967540
196UbiquitinationPSPFAYLLTIHLKEG
CCHHHHEEEEEECCC
2.4829967540
198UbiquitinationPFAYLLTIHLKEGRN
HHHHEEEEEECCCCC
3.4629967540
214PhosphorylationVVRDRCGTSDPYVKF
EEECCCCCCCCEEEE
33.3222210691
215PhosphorylationVRDRCGTSDPYVKFK
EECCCCCCCCEEEEE
23.1322210691
218PhosphorylationRCGTSDPYVKFKLNG
CCCCCCCEEEEEECC
22.6622210691
332PhosphorylationWSNRKRLSASKSSLI
CCCCCCCCCCHHHHH
34.2320873877
334PhosphorylationNRKRLSASKSSLIRN
CCCCCCCCHHHHHHH
29.6923312004
335AcetylationRKRLSASKSSLIRNL
CCCCCCCHHHHHHHH
43.727668679
335UbiquitinationRKRLSASKSSLIRNL
CCCCCCCHHHHHHHH
43.7229967540
336PhosphorylationKRLSASKSSLIRNLR
CCCCCCHHHHHHHHH
28.0723312004
337PhosphorylationRLSASKSSLIRNLRL
CCCCCHHHHHHHHHH
31.3924719451
345PhosphorylationLIRNLRLSESLKKNQ
HHHHHHHCHHHHHCC
20.7825159151
347PhosphorylationRNLRLSESLKKNQLW
HHHHHCHHHHHCCCC
41.9628857561
350UbiquitinationRLSESLKKNQLWNGI
HHCHHHHHCCCCCCE
56.04-
374PhosphorylationNVSGGSMTEMFVQLK
CCCCCCHHEEEEEEC
26.46-
436UbiquitinationEERLGTCKVDISALP
HHHHCCCCCCCCCCC
42.6629967540
493PhosphorylationLSERKQITQRYCLQN
HHHHHHHHHHHHHHH
12.4224719451
496PhosphorylationRKQITQRYCLQNSLK
HHHHHHHHHHHHHCC
6.4124719451
506UbiquitinationQNSLKDVKDVGILQV
HHHCCCCHHCCHHHH
57.7529967540
514UbiquitinationDVGILQVKVLKAADL
HCCHHHHEHHHHHHH
28.9629967540
517UbiquitinationILQVKVLKAADLLAA
HHHHEHHHHHHHHHH
44.5129967540
527PhosphorylationDLLAADFSGKSDPFC
HHHHHCCCCCCCCEE
45.95-
529UbiquitinationLAADFSGKSDPFCLL
HHHCCCCCCCCEEEE
50.9529967540
550UbiquitinationLQTHTVYKNLNPEWN
CCEECEECCCCCHHH
51.1029967540
582UbiquitinationVFDEDGDKPPDFLGK
EECCCCCCCCCHHCC
65.0729967540
608UbiquitinationQPNCYVLKNKDLEQA
CCCEEEECCCCHHHH
52.4829967540
610UbiquitinationNCYVLKNKDLEQAFK
CEEEECCCCHHHHHC
63.2029967540
730PhosphorylationRPVKGKVSSIQDSQE
HCCCCCCCCCCCCCC
25.8030108239
731PhosphorylationPVKGKVSSIQDSQES
CCCCCCCCCCCCCCC
27.5330108239
735PhosphorylationKVSSIQDSQESTDID
CCCCCCCCCCCCCCC
21.3326657352
738PhosphorylationSIQDSQESTDIDDEE
CCCCCCCCCCCCCCC
24.6030108239
739PhosphorylationIQDSQESTDIDDEED
CCCCCCCCCCCCCCC
35.9023401153
752PhosphorylationEDEDDKESEKKGLIE
CCCCCHHHHHHHHHH
61.5325841592
801UbiquitinationPFLSSLACLILAAAT
HHHHHHHHHHHHHHH
2.7029967540
818PhosphorylationLYFIPLRYIILIWGI
HHHHHHHHHHHHHCH
10.45-
856UbiquitinationRVPSDVQKVQYAELK
CCCCCHHHHHHHHHH
31.0229967540
866PhosphorylationYAELKLCSSHSPLRK
HHHHHHHHCCCCHHH
41.3330108239
867PhosphorylationAELKLCSSHSPLRKK
HHHHHHHCCCCHHHH
27.3030108239
869PhosphorylationLKLCSSHSPLRKKRS
HHHHHCCCCHHHHHH
27.8123927012

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 MCTP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCTP2_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 MCTP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MCTP2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-144 AND SER-145, ANDMASS SPECTROMETRY.

TOP