SCMH1_HUMAN - dbPTM
SCMH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCMH1_HUMAN
UniProt AC Q96GD3
Protein Name Polycomb protein SCMH1
Gene Name SCMH1 {ECO:0000312|EMBL:CAH72793.1}
Organism Homo sapiens (Human).
Sequence Length 660
Subcellular Localization Nucleus .
Protein Description Associates with Polycomb group (PcG) multiprotein complexes; the complex class is required to maintain the transcriptionally repressive state of some genes..
Protein Sequence MLVCYSVLACEILWDLPCSIMGSPLGHFTWDKYLKETCSVPAPVHCFKQSYTPPSNEFKISMKLEAQDPRNTTSTCIATVVGLTGARLRLRLDGSDNKNDFWRLVDSAEIQPIGNCEKNGGMLQPPLGFRLNASSWPMFLLKTLNGAEMAPIRIFHKEPPSPSHNFFKMGMKLEAVDRKNPHFICPATIGEVRGSEVLVTFDGWRGAFDYWCRFDSRDIFPVGWCSLTGDNLQPPGTKVVIPKNPYPASDVNTEKPSIHSSTKTVLEHQPGQRGRKPGKKRGRTPKTLISHPISAPSKTAEPLKFPKKRGPKPGSKRKPRTLLNPPPASPTTSTPEPDTSTVPQDAATIPSSAMQAPTVCIYLNKNGSTGPHLDKKKVQQLPDHFGPARASVVLQQAVQACIDCAYHQKTVFSFLKQGHGGEVISAVFDREQHTLNLPAVNSITYVLRFLEKLCHNLRSDNLFGNQPFTQTHLSLTAIEYSHSHDRYLPGETFVLGNSLARSLEPHSDSMDSASNPTNLVSTSQRHRPLLSSCGLPPSTASAVRRLCSRGVLKGSNERRDMESFWKLNRSPGSDRYLESRDASRLSGRDPSSWTVEDVMQFVREADPQLGPHADLFRKHEIDGKALLLLRSDMMMKYMGLKLGPALKLSYHIDRLKQGKF
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
23PhosphorylationLPCSIMGSPLGHFTW
CCCHHCCCCCCCCCH		10.2827499020
48UbiquitinationPAPVHCFKQSYTPPS
CCCEEEEECCCCCCC		43.67-
50PhosphorylationPVHCFKQSYTPPSNE
CEEEEECCCCCCCCC		31.4023663014
51PhosphorylationVHCFKQSYTPPSNEF
EEEEECCCCCCCCCE		22.2923663014
52PhosphorylationHCFKQSYTPPSNEFK
EEEECCCCCCCCCEE		33.6923663014
55PhosphorylationKQSYTPPSNEFKISM
ECCCCCCCCCEEEEE		50.6323663014
61PhosphorylationPSNEFKISMKLEAQD
CCCCEEEEEEEEECC		15.5123663014
72PhosphorylationEAQDPRNTTSTCIAT
EECCCCCCHHHHHHH		24.3326434552
73PhosphorylationAQDPRNTTSTCIATV
ECCCCCCHHHHHHHH		26.1126434552
74PhosphorylationQDPRNTTSTCIATVV
CCCCCCHHHHHHHHH		21.1724275748
75PhosphorylationDPRNTTSTCIATVVG
CCCCCHHHHHHHHHH		13.0728111955
79PhosphorylationTTSTCIATVVGLTGA
CHHHHHHHHHHHCCC		8.87-
84PhosphorylationIATVVGLTGARLRLR
HHHHHHHCCCEEEEE		23.90-
95PhosphorylationLRLRLDGSDNKNDFW
EEEEECCCCCCCCCE		37.36-
134PhosphorylationLGFRLNASSWPMFLL
CCEECCCCCCCEEHH		31.6825627689
135PhosphorylationGFRLNASSWPMFLLK
CEECCCCCCCEEHHH		32.5625627689
142MethylationSWPMFLLKTLNGAEM
CCCEEHHHHCCCCEE		53.78115977595
157UbiquitinationAPIRIFHKEPPSPSH
CCEEEEECCCCCCCC		62.25-
276AcetylationQPGQRGRKPGKKRGR
CCCCCCCCCCCCCCC		62.0320167786
279AcetylationQRGRKPGKKRGRTPK
CCCCCCCCCCCCCCC		48.0720167786
290PhosphorylationRTPKTLISHPISAPS
CCCCCCCCCCCCCCC		26.7324905233
294PhosphorylationTLISHPISAPSKTAE
CCCCCCCCCCCCCCC		38.2824905233
297PhosphorylationSHPISAPSKTAEPLK
CCCCCCCCCCCCCCC		42.2124905233
329PhosphorylationLLNPPPASPTTSTPE
CCCCCCCCCCCCCCC		28.6628348404
331PhosphorylationNPPPASPTTSTPEPD
CCCCCCCCCCCCCCC		30.7728348404
332PhosphorylationPPPASPTTSTPEPDT
CCCCCCCCCCCCCCC		33.7128348404
333PhosphorylationPPASPTTSTPEPDTS
CCCCCCCCCCCCCCC		44.4328348404
334PhosphorylationPASPTTSTPEPDTST
CCCCCCCCCCCCCCC		29.5828348404
339PhosphorylationTSTPEPDTSTVPQDA
CCCCCCCCCCCCCCC		36.6928348404
340PhosphorylationSTPEPDTSTVPQDAA
CCCCCCCCCCCCCCC		34.4828348404
341PhosphorylationTPEPDTSTVPQDAAT
CCCCCCCCCCCCCCC		37.9928348404
348PhosphorylationTVPQDAATIPSSAMQ
CCCCCCCCCCHHHCC		34.8328348404
413PhosphorylationYHQKTVFSFLKQGHG
HHHHHHHHHHHHCCC		25.9024719451
507PhosphorylationARSLEPHSDSMDSAS
HHHCCCCCCCCCCCC		41.9421601212
509PhosphorylationSLEPHSDSMDSASNP
HCCCCCCCCCCCCCC		27.7524247654
531PhosphorylationQRHRPLLSSCGLPPS
HHCCCCHHHCCCCHH		31.1225332170
539PhosphorylationSCGLPPSTASAVRRL
HCCCCHHHHHHHHHH		30.3325332170
541PhosphorylationGLPPSTASAVRRLCS
CCCHHHHHHHHHHHH		27.6425332170
555O-linked_GlycosylationSRGVLKGSNERRDME
HCCCCCCCCCCCCHH		33.6530379171
561PhosphorylationGSNERRDMESFWKLN
CCCCCCCHHHHHHHC		4.3927251275
573PhosphorylationKLNRSPGSDRYLESR
HHCCCCCCHHHCCCC		23.4627251275
641SumoylationMMKYMGLKLGPALKL
HHHHHCCCHHHHHHH		45.74-
641SumoylationMMKYMGLKLGPALKL
HHHHHCCCHHHHHHH		45.74-
649PhosphorylationLGPALKLSYHIDRLK
HHHHHHHHHHHHHHH		17.0518491316
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 SCMH1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCMH1_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 SCMH1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SCMH1_HUMANSCMH1physical
16169070
MAML3_HUMANMAML3physical
20211142
UBQL1_HUMANUBQLN1physical
25416956
ACTBL_HUMANACTBL2physical
28514442
ACTA_HUMANACTA2physical
28514442
PGK2_HUMANPGK2physical
28514442
GBB2_HUMANGNB2physical
28514442
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 SCMH1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND MASSSPECTROMETRY.

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