MSD2_HUMAN - dbPTM
MSD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MSD2_HUMAN
UniProt AC Q6P1R3
Protein Name Myb/SANT-like DNA-binding domain-containing protein 2
Gene Name MSANTD2
Organism Homo sapiens (Human).
Sequence Length 559
Subcellular Localization
Protein Description
Protein Sequence MAAPCGSELPANSPLKIPKMEVLSPASPGGLSDGNPSLSDPSTPRGASPLGPGSAAGSGAAASGGLGLGLGGRSAASSSVSFSPGGGGGGAAAAAAAACRGMSWTPAETNALIAVWGNERLVEARYQQLEGAGTVFGSKAPGPAMYERVSRALAELGYERTPSQCRERIKTLRRCYSRVKEHGVGKRKSSYTFEQLEQVFGQGGWDAQPCQPVLINSSGLYQELESDGSTMEDYSQEDWGNHSQDLHGYPTDQELDEIPVTKRTLKIKQESSEEAQKRDIMQNIVQILESVQLKWELFQSWTDFSRLHLSNKLAIFGIGYNTRWKEDIRYHYAEISSQVPLGKRLREYFNSEKPEGRIIMTRVQKMNWKNVYYKFLEITISEARCLELHMEIDWIPIAHSKPTGGNVVQYLLPGGIPKSPGLYAIGYEECIERPLSPHMEQSSLDPGKEGRVDLETLSAQASLQVEIEPTRIIYCYLGIAEVRTLQQCLFLHFQANTKTFSKDWVGINGFLSQNCIVDPGVSPKSIYIKFVEVERDFLSAGSLVECLEKAIGYPLKFNN
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-MAAPCGSELPANSP
-CCCCCCCCCCCCCC
42.5529255136
13PhosphorylationGSELPANSPLKIPKM
CCCCCCCCCCCCCCE
33.4429255136
24PhosphorylationIPKMEVLSPASPGGL
CCCEEEECCCCCCCC
24.4829255136
27PhosphorylationMEVLSPASPGGLSDG
EEEECCCCCCCCCCC
27.7129255136
32PhosphorylationPASPGGLSDGNPSLS
CCCCCCCCCCCCCCC
46.9029255136
37PhosphorylationGLSDGNPSLSDPSTP
CCCCCCCCCCCCCCC
44.5028450419
39PhosphorylationSDGNPSLSDPSTPRG
CCCCCCCCCCCCCCC
52.3828450419
42PhosphorylationNPSLSDPSTPRGASP
CCCCCCCCCCCCCCC
56.9128450419
43PhosphorylationPSLSDPSTPRGASPL
CCCCCCCCCCCCCCC
23.5328450419
48PhosphorylationPSTPRGASPLGPGSA
CCCCCCCCCCCCCCC
24.3929255136
54PhosphorylationASPLGPGSAAGSGAA
CCCCCCCCCCCCCCH
20.3423927012
58PhosphorylationGPGSAAGSGAAASGG
CCCCCCCCCCHHCCC
22.1130278072
63PhosphorylationAGSGAAASGGLGLGL
CCCCCHHCCCCCCCC
28.7723403867
74PhosphorylationGLGLGGRSAASSSVS
CCCCCCCCCCCCEEE
31.3126552605
77PhosphorylationLGGRSAASSSVSFSP
CCCCCCCCCEEEECC
23.9026552605
78PhosphorylationGGRSAASSSVSFSPG
CCCCCCCCEEEECCC
29.9926552605
79PhosphorylationGRSAASSSVSFSPGG
CCCCCCCEEEECCCC
21.2026552605
81PhosphorylationSAASSSVSFSPGGGG
CCCCCEEEECCCCCC
23.1926552605
83PhosphorylationASSSVSFSPGGGGGG
CCCEEEECCCCCCHH
18.3528985074
161PhosphorylationAELGYERTPSQCRER
HHCCCCCCHHHHHHH
18.4928555341
268SumoylationTKRTLKIKQESSEEA
CCCEEEECCCCCHHH
46.5628112733
268UbiquitinationTKRTLKIKQESSEEA
CCCEEEECCCCCHHH
46.56-
268SumoylationTKRTLKIKQESSEEA
CCCEEEECCCCCHHH
46.56-
300PhosphorylationLKWELFQSWTDFSRL
HHHHHHHCCCHHHHH
25.3027174698
302PhosphorylationWELFQSWTDFSRLHL
HHHHHCCCHHHHHHH
32.2027174698
305PhosphorylationFQSWTDFSRLHLSNK
HHCCCHHHHHHHCCC
36.4227174698
323MethylationFGIGYNTRWKEDIRY
EEECCCCCCHHHHHH
38.54115483855
325UbiquitinationIGYNTRWKEDIRYHY
ECCCCCCHHHHHHHH
42.07-
330PhosphorylationRWKEDIRYHYAEISS
CCHHHHHHHHHHHHC
10.2628270605
332PhosphorylationKEDIRYHYAEISSQV
HHHHHHHHHHHHCCC
9.3028270605
336PhosphorylationRYHYAEISSQVPLGK
HHHHHHHHCCCCHHH
13.2628270605
337PhosphorylationYHYAEISSQVPLGKR
HHHHHHHCCCCHHHH
40.6428270605
343SumoylationSSQVPLGKRLREYFN
HCCCCHHHHHHHHHC
56.8128112733
348PhosphorylationLGKRLREYFNSEKPE
HHHHHHHHHCCCCCC
11.13-
384PhosphorylationEITISEARCLELHME
EEEECHHHHHHHCEE
22.8527251275
419PhosphorylationLPGGIPKSPGLYAIG
ECCCCCCCCCEEEEC
20.8826434776
423PhosphorylationIPKSPGLYAIGYEEC
CCCCCCEEEECHHHH
11.3326434776
427PhosphorylationPGLYAIGYEECIERP
CCEEEECHHHHHCCC
11.4825159151
436PhosphorylationECIERPLSPHMEQSS
HHHCCCCCCCCCHHC
18.5525159151
442PhosphorylationLSPHMEQSSLDPGKE
CCCCCCHHCCCCCCC
21.4029978859
443PhosphorylationSPHMEQSSLDPGKEG
CCCCCHHCCCCCCCC
36.1629978859

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 MSD2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MSD2_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 MSD2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERCC3_HUMANERCC3physical
21988832

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MSD2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-54, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.

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