Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Lysine-specific demethylase 3B  

UniProtKB / Swiss-Prot ID :  KDM3B_HUMAN

Gene Name (Synonyms) : 
KDM3B, C5orf7, JHDM2B, JMJD1B, KIAA1082  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). 

Protein Function :  Histone demethylase that specifically demethylates 'Lys- 9' of histone H3, thereby playing a central role in histone code. Demethylation of Lys residue generates formaldehyde and succinate. May have tumor suppressor activity. 

Protein Sequence MADAAASPVGKRLLLLFADTAASASASAPAAAAASGDPGPALRTRAWRAGTVRAMSGAVPQDLAIFVEFD...
Predicted Secondary Structure  -
Protein Variant
LocationDescription
256A -> T (in dbSNP:rs6865472). VAR_026221
1201S -> N (in dbSNP:rs7706614). VAR_026222
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
289PhosphoserineRRRKSASDS
31.06HPRD
Link-
291PhosphoserineRKSASDSGC
39.12PhosphoELM
Link-
291PhosphoserineRKSASDSGC
39.12Phosphositeplus
Link-
291Phosphoserine.RKSASDSGC
39.12UniProtKB
Link-
311PhosphoserineGEVDSNGSD
48.55Phosphositeplus
Link-
314PhosphoserineDSNGSDGGE
37.01Phosphositeplus
Link-
361N6-acetyllysineATYTKENGR
38.48HPRD
Link-
361N6-acetyllysineATYTKENGR
38.48Phosphositeplus
Link-
361N6-acetyllysine.ATYTKENGR
38.48UniProtKB
Link-
614PhosphothreonineLNARTPENH
32.32PhosphoELM
Link-
614PhosphothreonineLNARTPENH
32.32Phosphositeplus
Link-
647PhosphoserineKVEHSPFSS
17.71HPRD
Link-
647PhosphoserineKVEHSPFSS
17.71PhosphoELM
Link-
654PhosphoserineSSFASQASG
25.03HPRD
Link-
654PhosphoserineSSFASQASG
25.03PhosphoELM
Link-
725PhosphoserineGNGRSSSPT
36.24HPRD
Link-
725PhosphoserineGNGRSSSPT
36.24PhosphoELM
Link-
726PhosphoserineNGRSSSPTS
38.69HPRD
Link-
726PhosphoserineNGRSSSPTS
38.69PhosphoELM
Link-
727PhosphoserineGRSSSPTSS
33.18HPRD
Link-
727PhosphoserineGRSSSPTSS
33.18PhosphoELM
Link-
729PhosphothreonineSSSPTSSLT
32.66HPRD
Link-
729PhosphothreonineSSSPTSSLT
32.66PhosphoELM
Link-
730PhosphoserineSSPTSSLTQ
27.08HPRD
Link-
730PhosphoserineSSPTSSLTQ
27.08PhosphoELM
Link-
730PhosphoserineSSPTSSLTQ
27.08Phosphositeplus
Link-
731PhosphoserineSPTSSLTQP
37.60HPRD
Link-
731PhosphoserineSPTSSLTQP
37.60PhosphoELM
Link-
731PhosphoserineSPTSSLTQP
37.60Phosphositeplus
Link-
733PhosphothreonineTSSLTQPIE
33.96Phosphositeplus
Link-
742PhosphoserineMPTLSSSPT
31.11HPRD
Link-
742PhosphoserineMPTLSSSPT
31.11PhosphoELM
Link-
743PhosphoserinePTLSSSPTE
43.37HPRD
Link-
743PhosphoserinePTLSSSPTE
43.37PhosphoELM
Link-
744PhosphoserineTLSSSPTEE
32.25HPRD
Link-
744PhosphoserineTLSSSPTEE
32.25PhosphoELM
Link-
744PhosphoserineTLSSSPTEE
32.25Phosphositeplus
Link-
766PhosphoserineLKTFSNVFG
37.00HPRD
Link-
766PhosphoserineLKTFSNVFG
37.00Phosphositeplus
Link-
766PhosphoserineLKTFSNVFG
37.00SysPTM
Link-
766Phosphoserine.LKTFSNVFG
37.00UniProtKB
Link-
773PhosphoserineFGRHSGGFL
38.97HPRD
Link-
773PhosphoserineFGRHSGGFL
38.97PhosphoELM
Link-
773PhosphoserineFGRHSGGFL
38.97Phosphositeplus
Link-
773PhosphoserineFGRHSGGFL
38.97SysPTM
Link-
773Phosphoserine.FGRHSGGFL
38.97UniProtKB
Link-
778PhosphoserineGGFLSSPAD
31.82HPRD
Link-
778PhosphoserineGGFLSSPAD
31.82PhosphoELM
Link-
779PhosphoserineGFLSSPADF
26.67HPRD
Link-
779PhosphoserineGFLSSPADF
26.67PhosphoELM
Link-
779PhosphoserineGFLSSPADF
26.67Phosphositeplus
Link-
779PhosphoserineGFLSSPADF
26.67SysPTM
Link-
779Phosphoserine.GFLSSPADF
26.67UniProtKB
Link-
798PhosphoserineVKRFSLDER
38.66HPRD
Link-
798PhosphoserineVKRFSLDER
38.66PhosphoELM
Link-
798PhosphoserineVKRFSLDER
38.66Phosphositeplus
Link-
798PhosphoserineVKRFSLDER
38.66SysPTM
Link-
798Phosphoserine.VKRFSLDER
38.66UniProtKB
Link-
810PhosphoserineCRQDSDSST
30.93HPRD
Link-
814PhosphothreonineSDSSTNSDL
42.57HPRD
Link-
819PhosphoserineNSDLSDLSD
41.31HPRD
Link-
822PhosphoserineLSDLSDSEE
44.04HPRD
Link-
832PhosphothreonineLQAKTGLKG
51.25HPRD
Link-
1193Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EEPLKTDSS
62.09Phosphositeplus
Link-
1249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SVLNKESHS
57.33Phosphositeplus
Link-
1251PhosphoserineLNKESHSPF
30.76HPRD
Link-
1253PhosphoserineKESHSPFGL
31.07HPRD
Link-
1253PhosphoserineKESHSPFGL
31.07PhosphoELM
Link-
1253PhosphoserineKESHSPFGL
31.07Phosphositeplus
Link-
1267PhosphoserineTAKVSPLTP
17.31HPRD
Link-
1267PhosphoserineTAKVSPLTP
17.31Phosphositeplus
Link-
1270PhosphothreonineVSPLTPKLF
23.04HPRD
Link-
1270PhosphothreonineVSPLTPKLF
23.04Phosphositeplus
Link-
1272Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PLTPKLFNS
61.55Phosphositeplus
Link-
1287Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ASNNKTEGS
52.80Phosphositeplus
Link-
1303Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SGPGKLPQT
61.19Phosphositeplus
Link-
1327Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SAGVKSKAS
45.37Phosphositeplus
Link-
1516Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PEYTKRDGR
47.81Phosphositeplus
Link
1600Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DEVTKQRIH
42.63Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-361, AND MASS SPECTROMETRY.
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-798, AND MASSSPECTROMETRY.
"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-773 AND SER-779, ANDMASS SPECTROMETRY.
"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-766, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures