SETD3_HUMAN - dbPTM
SETD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SETD3_HUMAN
UniProt AC Q86TU7
Protein Name Histone-lysine N-methyltransferase setd3
Gene Name SETD3
Organism Homo sapiens (Human).
Sequence Length 594
Subcellular Localization Nucleus .
Protein Description Histone methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3 (H3K4me and H3K36me). Acts as a transcriptional activator. Plays an important role in the transcriptional regulation of muscle cell differentiation via interaction with MYOD1..
Protein Sequence MGKKSRVKTQKSGTGATATVSPKEILNLTSELLQKCSSPAPGPGKEWEEYVQIRTLVEKIRKKQKGLSVTFDGKREDYFPDLMKWASENGASVEGFEMVNFKEEGFGLRATRDIKAEELFLWVPRKLLMTVESAKNSVLGPLYSQDRILQAMGNIALAFHLLCERASPNSFWQPYIQTLPSEYDTPLYFEEDEVRYLQSTQAIHDVFSQYKNTARQYAYFYKVIQTHPHANKLPLKDSFTYEDYRWAVSSVMTRQNQIPTEDGSRVTLALIPLWDMCNHTNGLITTGYNLEDDRCECVALQDFRAGEQIYIFYGTRSNAEFVIHSGFFFDNNSHDRVKIKLGVSKSDRLYAMKAEVLARAGIPTSSVFALHFTEPPISAQLLAFLRVFCMTEEELKEHLLGDSAIDRIFTLGNSEFPVSWDNEVKLWTFLEDRASLLLKTYKTTIEEDKSVLKNHDLSVRAKMAIKLRLGEKEILEKAVKSAAVNREYYRQQMEEKAPLPKYEESNLGLLESSVGDSRLPLVLRNLEEEAGVQDALNIREAISKAKATENGLVNGENSIPNGTRSENESLNQESKRAVEDAKGSSSDSTAGVKE
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
11UbiquitinationKSRVKTQKSGTGATA
CCCCCCCCCCCCCCC		56.96-
12PhosphorylationSRVKTQKSGTGATAT
CCCCCCCCCCCCCCC		31.5922617229
12 (in isoform 2)Phosphorylation-31.59-
14 (in isoform 2)Phosphorylation-30.63-
14PhosphorylationVKTQKSGTGATATVS
CCCCCCCCCCCCCCC		30.6325159151
17 (in isoform 2)Phosphorylation-24.98-
17PhosphorylationQKSGTGATATVSPKE
CCCCCCCCCCCCHHH		24.9816094384
19PhosphorylationSGTGATATVSPKEIL
CCCCCCCCCCHHHHH		19.7028450419
21PhosphorylationTGATATVSPKEILNL
CCCCCCCCHHHHHHH		26.3725849741
23UbiquitinationATATVSPKEILNLTS
CCCCCCHHHHHHHHH		50.29-
35UbiquitinationLTSELLQKCSSPAPG
HHHHHHHHCCCCCCC		35.73-
38PhosphorylationELLQKCSSPAPGPGK
HHHHHCCCCCCCCCC		34.2523312004
74UbiquitinationLSVTFDGKREDYFPD
CEEEECCCCHHHCHH		55.23-
742-HydroxyisobutyrylationLSVTFDGKREDYFPD
CEEEECCCCHHHCHH		55.23-
115UbiquitinationLRATRDIKAEELFLW
CEECCCCCHHHHHHE		54.77-
133PhosphorylationKLLMTVESAKNSVLG
HHHHHHHHHHHCCCC		39.9630631047
181PhosphorylationPYIQTLPSEYDTPLY
HHHHCCCCCCCCCCC		52.4826074081
183PhosphorylationIQTLPSEYDTPLYFE
HHCCCCCCCCCCCCC		29.4726074081
217PhosphorylationYKNTARQYAYFYKVI
HHHHHHHHHHHHHHH		9.5629083192
219PhosphorylationNTARQYAYFYKVIQT
HHHHHHHHHHHHHHH		11.5128555341
221PhosphorylationARQYAYFYKVIQTHP
HHHHHHHHHHHHHCC		7.5328555341
232UbiquitinationQTHPHANKLPLKDSF
HHCCCCCCCCCCCCC		52.87-
244PhosphorylationDSFTYEDYRWAVSSV
CCCCHHHHHHHHHHH		8.98-
249PhosphorylationEDYRWAVSSVMTRQN
HHHHHHHHHHHHHCC		14.9623403867
250PhosphorylationDYRWAVSSVMTRQNQ
HHHHHHHHHHHHCCC		14.8723403867
253PhosphorylationWAVSSVMTRQNQIPT
HHHHHHHHHCCCCCC		27.2623403867
340AcetylationSHDRVKIKLGVSKSD
CCCCEEEEECCCHHH		33.2125953088
345UbiquitinationKIKLGVSKSDRLYAM
EEEECCCHHHHHHHH		54.70-
350PhosphorylationVSKSDRLYAMKAEVL
CCHHHHHHHHHHHHH		12.9221406692
439UbiquitinationDRASLLLKTYKTTIE
HHHHHHHHHHHHHHH		50.18-
440PhosphorylationRASLLLKTYKTTIEE
HHHHHHHHHHHHHHH		30.16-
453UbiquitinationEEDKSVLKNHDLSVR
HHHHHHHHCCCCHHH		50.51-
466UbiquitinationVRAKMAIKLRLGEKE
HHHHHHHHHHCCCHH		20.30-
472UbiquitinationIKLRLGEKEILEKAV
HHHHCCCHHHHHHHH		48.53-
477UbiquitinationGEKEILEKAVKSAAV
CCHHHHHHHHHHHHH		55.84-
480UbiquitinationEILEKAVKSAAVNRE
HHHHHHHHHHHHCHH		38.96-
501UbiquitinationEEKAPLPKYEESNLG
HHHCCCCCHHHCCCC		73.34-
512PhosphorylationSNLGLLESSVGDSRL
CCCCCHHCCCCCCHH		30.2322199227
513PhosphorylationNLGLLESSVGDSRLP
CCCCHHCCCCCCHHH		22.2728442573
517PhosphorylationLESSVGDSRLPLVLR
HHCCCCCCHHHHHHH		29.7729978859
558PhosphorylationGLVNGENSIPNGTRS
CCCCCCCCCCCCCCC		34.8127251275
569PhosphorylationGTRSENESLNQESKR
CCCCCCCCCCHHHHH		44.1721815630
584PhosphorylationAVEDAKGSSSDSTAG
HHHHHCCCCCCCCCC		26.4330624053
585PhosphorylationVEDAKGSSSDSTAGV
HHHHCCCCCCCCCCC		47.0030624053
586PhosphorylationEDAKGSSSDSTAGVK
HHHCCCCCCCCCCCC		36.9630624053
588PhosphorylationAKGSSSDSTAGVKE-
HCCCCCCCCCCCCC-		23.3127794612
589PhosphorylationKGSSSDSTAGVKE--
CCCCCCCCCCCCC--		32.2128985074
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 SETD3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SETD3_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 SETD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYOD1_HUMANMYOD1physical
21832073
A4_HUMANAPPphysical
21832049
RFC4_HUMANRFC4physical
26186194
SNX3_HUMANSNX3physical
26186194
RFC2_HUMANRFC2physical
26186194
SNX3_HUMANSNX3physical
28514442
PMVK_HUMANPMVKphysical
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 SETD3_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-513, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17, AND MASSSPECTROMETRY.

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