SMBT1_HUMAN - dbPTM
SMBT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMBT1_HUMAN
UniProt AC Q9UHJ3
Protein Name Scm-like with four MBT domains protein 1
Gene Name SFMBT1
Organism Homo sapiens (Human).
Sequence Length 866
Subcellular Localization Nucleus .
Protein Description Histone-binding protein, which is part of various corepressor complexes. Mediates the recruitment of corepressor complexes to target genes, followed by chromatin compaction and repression of transcription. Plays a role during myogenesis: required for the maintenance of undifferentiated states of myogenic progenitor cells via interaction with MYOD1. Interaction with MYOD1 leads to the recruitment of associated corepressors and silencing of MYOD1 target genes. Part of the SLC complex in germ cells, where it may play a role during spermatogenesis..
Protein Sequence MNGEQQLDADAGSGMEEVELSWEDYLEETGSTAVPYGSFKHVDTRLQNGFAPGMKLEVAVRTDPETYWVATVITTCEQLLLLRYDGYGEDRRADFWCDIRKADLYPIGWCEQNKKTLEAPEGIRDKVSDWDEFLRQTLIGACSPPVPLLEGLRNGRNPLDLIAPGSRLECQAFQDSLSTWIVTVVENIGGRLKLRYEGLESSDNYEHWLYYLDPFLHHVGWAAQQGYELQPPSAIRHLKNEAEWQEILAKVKEEEEEPLPSYLFKDKQVIGIHTFSVNMKLEAVDPWSPFGISPATVVKVFDEKYFLVEMDDLRPENHARRSFVCHADSPGIFPVQWSLKNGLHISPPPGYPSQDFDWADYLKQCGAEAAPQRCFPPLISEHEFKENMKLEAVNPILPEEVCVATITAVRGSYLWLQLEGSKKPIPECIVSVESMDIFPLGWCETNGHPLSTPRRARVYKQRKIAVVQPEKQVPSSRTVHEGLRNQELNSTESVMINGKYCCPKIYFNHRCFSGPYLNKGRIAELPQCVGPGNCVLVLREVLTLLINAAYKPSRVLRELQLDKDSVWHGCGEVLKAKYKGKSYRATVEIVKTADRVTEFCRQTCIKLECCPNLFGPRMVLDKCSENCSVLTKTKYTHYYGKKKNKRIGRPPGGHSNLACALKKASKRRKRRKNVFVHKKKRSSASVDNTPAGSPQGSGGEDEDDPDEGDDDSLSEGSTSEQQDELQEESEMSEKKSCSSSPTQSEISTSLPPDRQRRKRELRTFSFSDDENKPPSPKEIRIEVAERLHLDSNPLKWSVADVVRFIRSTDCAPLARIFLDQEIDGQALLLLTLPTVQECMDLKLGPAIKLCHHIERIKFAFYEQFAN
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
62PhosphorylationKLEVAVRTDPETYWV
EEEEEEECCHHHEEE		49.6726074081
66PhosphorylationAVRTDPETYWVATVI
EEECCHHHEEEEEHH		28.2426074081
67PhosphorylationVRTDPETYWVATVIT
EECCHHHEEEEEHHH		9.0226074081
71PhosphorylationPETYWVATVITTCEQ
HHHEEEEEHHHCHHH		11.6526074081
74PhosphorylationYWVATVITTCEQLLL
EEEEEHHHCHHHHHH		22.5126074081
75PhosphorylationWVATVITTCEQLLLL
EEEEHHHCHHHHHHH		11.7026074081
84PhosphorylationEQLLLLRYDGYGEDR
HHHHHHCCCCCCCCC		17.4326074081
87PhosphorylationLLLRYDGYGEDRRAD
HHHCCCCCCCCCCCC		17.9126074081
105PhosphorylationDIRKADLYPIGWCEQ
ECCCCCEEECCCCCC		8.05-
114UbiquitinationIGWCEQNKKTLEAPE
CCCCCCCCCCCCCCC		46.99-
115UbiquitinationGWCEQNKKTLEAPEG
CCCCCCCCCCCCCCC		66.93-
116PhosphorylationWCEQNKKTLEAPEGI
CCCCCCCCCCCCCCH		31.29-
143PhosphorylationQTLIGACSPPVPLLE
HHHHHHCCCCHHHHH		31.5328348404
250UbiquitinationEWQEILAKVKEEEEE
HHHHHHHHHHHHCCC		50.85-
252UbiquitinationQEILAKVKEEEEEPL
HHHHHHHHHHCCCCC		59.72-
265UbiquitinationPLPSYLFKDKQVIGI
CCCCHHCCCCEEEEE		62.51-
361PhosphorylationQDFDWADYLKQCGAE
CCCCHHHHHHHHCCC		14.19-
363UbiquitinationFDWADYLKQCGAEAA
CCHHHHHHHHCCCCC		37.00-
407PhosphorylationEVCVATITAVRGSYL
HHHEEEEEEEECCEE		18.10-
445PhosphorylationFPLGWCETNGHPLST
EECCCCCCCCCCCCC		43.28-
451PhosphorylationETNGHPLSTPRRARV
CCCCCCCCCHHHHHH		40.59-
452PhosphorylationTNGHPLSTPRRARVY
CCCCCCCCHHHHHHH		28.62-
471UbiquitinationIAVVQPEKQVPSSRT
EEEECCCCCCCCCCC		64.38-
476PhosphorylationPEKQVPSSRTVHEGL
CCCCCCCCCCCCHHH		26.3823403867
478PhosphorylationKQVPSSRTVHEGLRN
CCCCCCCCCCHHHCC		28.3223403867
553PhosphorylationINAAYKPSRVLRELQ
HHHHCCHHHHHHHHC		30.76-
582PhosphorylationKAKYKGKSYRATVEI
HHHHCCCCEEEEEEE		28.6423403867
583PhosphorylationAKYKGKSYRATVEIV
HHHCCCCEEEEEEEE		14.0423403867
592PhosphorylationATVEIVKTADRVTEF
EEEEEEEHHHHHHHH		23.93-
639PhosphorylationKTKYTHYYGKKKNKR
CCCCCCCCCCCCCCC		18.1822817900
641AcetylationKYTHYYGKKKNKRIG
CCCCCCCCCCCCCCC		44.4419816931
642AcetylationYTHYYGKKKNKRIGR
CCCCCCCCCCCCCCC		58.1619816939
693PhosphorylationVDNTPAGSPQGSGGE
CCCCCCCCCCCCCCC		19.0222468782
697PhosphorylationPAGSPQGSGGEDEDD
CCCCCCCCCCCCCCC		38.0822468782
738PhosphorylationMSEKKSCSSSPTQSE
HHHHHCCCCCCCHHH		40.7327050516
742PhosphorylationKSCSSSPTQSEISTS
HCCCCCCCHHHHHHC		46.8325627689
744PhosphorylationCSSSPTQSEISTSLP
CCCCCCHHHHHHCCC		39.1025159151
749PhosphorylationTQSEISTSLPPDRQR
CHHHHHHCCCCCHHH		31.89-
763PhosphorylationRRKRELRTFSFSDDE
HHHHHHCCCCCCCCC		35.9330266825
765PhosphorylationKRELRTFSFSDDENK
HHHHCCCCCCCCCCC		24.1930266825
765 (in isoform 2)Phosphorylation-24.1929743597
767PhosphorylationELRTFSFSDDENKPP
HHCCCCCCCCCCCCC		42.8430266825
767 (in isoform 2)Phosphorylation-42.8425849741
775PhosphorylationDDENKPPSPKEIRIE
CCCCCCCCCCEEEEE		58.0723592795
775 (in isoform 2)Phosphorylation-58.0725849741
791PhosphorylationAERLHLDSNPLKWSV
HHHHCCCCCCCCCCH		46.86-
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 SMBT1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMBT1_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 SMBT1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H31_HUMANHIST1H3Aphysical
17599839
ZCH10_HUMANZCCHC10physical
25416956
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 SMBT1_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-765; SER-767 ANDSER-775, AND MASS SPECTROMETRY.

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