SCNM1_HUMAN - dbPTM
SCNM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCNM1_HUMAN
UniProt AC Q9BWG6
Protein Name Sodium channel modifier 1
Gene Name SCNM1
Organism Homo sapiens (Human).
Sequence Length 230
Subcellular Localization Nucleus. Nucleus speckle. Colocalizes with LUC7L2 and SNRNP70 in nuclear speckles..
Protein Description Plays a role in RNA splicing, possibly contributing to the recognition of non-consensus donor sites..
Protein Sequence MSFKREGDDWSQLNVLKKRRVGDLLASYIPEDEALMLRDGRFACAICPHRPVLDTLAMLTAHRAGKKHLSSLQLFYGKKQPGKERKQNPKHQNELRREETKAEAPLLTQTRLITQSALHRAPHYNSCCRRKYRPEAPGPSVSLSPMPPSEVKLQSGKISREPEPAAGPQAEESATVSAPAPMSPTRRRALDHYLTLRSSGWIPDGRGRWVKDENVEFDSDEEEPPDLPLD
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
2Phosphorylation------MSFKREGDD
------CCCCCCCCC		39.2028464451
17UbiquitinationWSQLNVLKKRRVGDL
HHHHHHHHHCCHHHH		39.6929967540
18UbiquitinationSQLNVLKKRRVGDLL
HHHHHHHHCCHHHHH		41.08-
66UbiquitinationLTAHRAGKKHLSSLQ
HHHHHHCHHHHHHHH		35.7132015554
67SumoylationTAHRAGKKHLSSLQL
HHHHHCHHHHHHHHH		49.1928112733
76PhosphorylationLSSLQLFYGKKQPGK
HHHHHHHCCCCCCCC		36.31-
101UbiquitinationELRREETKAEAPLLT
HHHHHHHHHHHCHHH		47.7332015554
116PhosphorylationQTRLITQSALHRAPH
HHHHHCHHHHHHCCC		24.9328555341
126PhosphorylationHRAPHYNSCCRRKYR
HHCCCCCCCCCCCCC		13.8728555341
142PhosphorylationEAPGPSVSLSPMPPS
CCCCCCCCCCCCCHH		27.7127732954
144PhosphorylationPGPSVSLSPMPPSEV
CCCCCCCCCCCHHHC		16.2025159151
148PhosphorylationVSLSPMPPSEVKLQS
CCCCCCCHHHCCCCC		36.5532142685
149PhosphorylationSLSPMPPSEVKLQSG
CCCCCCHHHCCCCCC		49.5028555341
157AcetylationEVKLQSGKISREPEP
HCCCCCCCCCCCCCC		42.6325953088
159PhosphorylationKLQSGKISREPEPAA
CCCCCCCCCCCCCCC		33.7924732914
173PhosphorylationAGPQAEESATVSAPA
CCCCCCCCCEECCCC		22.2729255136
175PhosphorylationPQAEESATVSAPAPM
CCCCCCCEECCCCCC		25.0329255136
177PhosphorylationAEESATVSAPAPMSP
CCCCCEECCCCCCCH		24.9529255136
183PhosphorylationVSAPAPMSPTRRRAL
ECCCCCCCHHHHHHH		23.2829255136
185PhosphorylationAPAPMSPTRRRALDH
CCCCCCHHHHHHHHE		29.5129255136
193PhosphorylationRRRALDHYLTLRSSG
HHHHHHEEHHHHHCC		10.8828796482
195PhosphorylationRALDHYLTLRSSGWI
HHHHEEHHHHHCCCC		16.98-
219PhosphorylationDENVEFDSDEEEPPD
CCCCCCCCCCCCCCC		52.8525159151
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 SCNM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCNM1_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 SCNM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CCD33_HUMANCCDC33physical
25416956
CEP44_HUMANCEP44physical
25416956
LZTS2_HUMANLZTS2physical
25416956
UBX11_HUMANUBXN11physical
25416956
SYCE1_HUMANSYCE1physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
MIPO1_HUMANMIPOL1physical
25416956
SPERT_HUMANSPERTphysical
25416956
TRI42_HUMANTRIM42physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
INCA1_HUMANINCA1physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
YBEY_HUMANYBEYphysical
26186194
PMVK_HUMANPMVKphysical
26186194
SNX3_HUMANSNX3physical
26186194
F192A_HUMANFAM192Aphysical
26186194
TCAL1_HUMANTCEAL1physical
26186194
TCAL1_HUMANTCEAL1physical
28514442
SNX3_HUMANSNX3physical
28514442
PMVK_HUMANPMVKphysical
28514442
DOHH_HUMANDOHHphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SCNM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 AND SER-219, ANDMASS SPECTROMETRY.
"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-183, AND MASSSPECTROMETRY.

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