KDM4B_HUMAN - dbPTM
KDM4B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KDM4B_HUMAN
UniProt AC O94953
Protein Name Lysine-specific demethylase 4B
Gene Name KDM4B
Organism Homo sapiens (Human).
Sequence Length 1096
Subcellular Localization Nucleus .
Protein Description Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Only able to demethylate trimethylated H3 'Lys-9', with a weaker activity than KDM4A, KDM4C and KDM4D. Demethylation of Lys residue generates formaldehyde and succinate..
Protein Sequence MGSEDHGAQNPSCKIMTFRPTMEEFKDFNKYVAYIESQGAHRAGLAKIIPPKEWKPRQTYDDIDDVVIPAPIQQVVTGQSGLFTQYNIQKKAMTVGEYRRLANSEKYCTPRHQDFDDLERKYWKNLTFVSPIYGADISGSLYDDDVAQWNIGSLRTILDMVERECGTIIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAIGFFPGSSQGCDAFLRHKMTLISPIILKKYGIPFSRITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATLRWIDYGKVATQCTCRKDMVKISMDVFVRILQPERYELWKQGKDLTVLDHTRPTALTSPELSSWSASRASLKAKLLRRSHRKRSQPKKPKPEDPKFPGEGTAGAALLEEAGGSVKEEAGPEVDPEEEEEEPQPLPHGREAEGAEEDGRGKLRPTKAKSERKKKSFGLLPPQLPPPPAHFPSEEALWLPSPLEPPVLGPGPAAMEESPLPAPLNVVPPEVPSEELEAKPRPIIPMLYVVPRPGKAAFNQEHVSCQQAFEHFAQKGPTWKEPVSPMELTGPEDGAASSGAGRMETKARAGEGQAPSTFSKLKMEIKKSRRHPLGRPPTRSPLSVVKQEASSDEEASPFSGEEDVSDPDALRPLLSLQWKNRAASFQAERKFNAAAARTEPYCAICTLFYPYCQALQTEKEAPIASLGKGCPATLPSKSRQKTRPLIPEMCFTSGGENTEPLPANSYIGDDGTSPLIACGKCCLQVHASCYGIRPELVNEGWTCSRCAAHAWTAECCLCNLRGGALQMTTDRRWIHVICAIAVPEARFLNVIERHPVDISAIPEQRWKLKCVYCRKRMKKVSGACIQCSYEHCSTSFHVTCAHAAGVLMEPDDWPYVVSITCLKHKSGGHAVQLLRAVSLGQVVITKNRNGLYYRCRVIGAASQTCYEVNFDDGSYSDNLYPESITSRDCVQLGPPSEGELVELRWTDGNLYKAKFISSVTSHIYQVEFEDGSQLTVKRGDIFTLEEELPKRVRSRLSLSTGAPQEPAFSGEEAKAAKRPRVGTPLATEDSGRSQDYVAFVESLLQVQGRPGAPF
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
12PhosphorylationDHGAQNPSCKIMTFR
CCCCCCCCCEEEEEC		35.2822985185
26UbiquitinationRPTMEEFKDFNKYVA
CCCHHHHHCHHHHHH		65.77-
30UbiquitinationEEFKDFNKYVAYIES
HHHHCHHHHHHHHHC		40.89-
31PhosphorylationEFKDFNKYVAYIESQ
HHHCHHHHHHHHHCC		7.45-
34PhosphorylationDFNKYVAYIESQGAH
CHHHHHHHHHCCCCC		8.65-
37PhosphorylationKYVAYIESQGAHRAG
HHHHHHHCCCCCCCC		25.10-
52UbiquitinationLAKIIPPKEWKPRQT
CCCCCCCCCCCCCCC		71.50-
80PhosphorylationQQVVTGQSGLFTQYN
HHEEECCCCEEEEHH		38.5222210691
91UbiquitinationTQYNIQKKAMTVGEY
EEHHHHCCCCCHHHH		27.32-
94PhosphorylationNIQKKAMTVGEYRRL
HHHCCCCCHHHHHHH		30.1622210691
98PhosphorylationKAMTVGEYRRLANSE
CCCCHHHHHHHHCCC		8.6322210691
106UbiquitinationRRLANSEKYCTPRHQ
HHHHCCCCCCCCCCC		45.50-
153PhosphorylationVAQWNIGSLRTILDM
HHHCCHHHHHHHHHH		15.7524719451
184PhosphorylationLYFGMWKTTFAWHTE
EEEEEEEEEEEEECC		16.1926552605
185PhosphorylationYFGMWKTTFAWHTED
EEEEEEEEEEEECCC		13.9726552605
190PhosphorylationKTTFAWHTEDMDLYS
EEEEEEECCCCCEEE		23.9926552605
196PhosphorylationHTEDMDLYSINYLHF
ECCCCCEEEEEEEEC		11.8424719451
197PhosphorylationTEDMDLYSINYLHFG
CCCCCEEEEEEEECC		16.2024719451
200PhosphorylationMDLYSINYLHFGEPK
CCEEEEEEEECCCCC		10.4124719451
242UbiquitinationCDAFLRHKMTLISPI
HHHHHHHHHHHHHHH		27.44-
252UbiquitinationLISPIILKKYGIPFS
HHHHHHHHHHCCCHH		33.28-
253UbiquitinationISPIILKKYGIPFSR
HHHHHHHHHCCCHHH		45.31-
302UbiquitinationLRWIDYGKVATQCTC
EEEEEHHHEECEEEE		23.59-
305PhosphorylationIDYGKVATQCTCRKD
EEHHHEECEEEECHH		27.45-
334UbiquitinationPERYELWKQGKDLTV
HHHHHHHHCCCCCEE		62.89-
337UbiquitinationYELWKQGKDLTVLDH
HHHHHCCCCCEEECC		47.25-
340PhosphorylationWKQGKDLTVLDHTRP
HHCCCCCEEECCCCC		29.2026434776
345PhosphorylationDLTVLDHTRPTALTS
CCEEECCCCCCCCCC		37.7022199227
348PhosphorylationVLDHTRPTALTSPEL
EECCCCCCCCCCCCH		30.8926434776
351PhosphorylationHTRPTALTSPELSSW
CCCCCCCCCCCHHHC		39.5122199227
352PhosphorylationTRPTALTSPELSSWS
CCCCCCCCCCHHHCC		19.7522199227
356PhosphorylationALTSPELSSWSASRA
CCCCCCHHHCCCCHH		28.2626434776
357PhosphorylationLTSPELSSWSASRAS
CCCCCHHHCCCCHHH		37.3626434776
359PhosphorylationSPELSSWSASRASLK
CCCHHHCCCCHHHHH		20.5126434776
361PhosphorylationELSSWSASRASLKAK
CHHHCCCCHHHHHHH		23.9026434776
364PhosphorylationSWSASRASLKAKLLR
HCCCCHHHHHHHHHH		29.3226434776
381AcetylationHRKRSQPKKPKPEDP
HHHCCCCCCCCCCCC		74.2530589577
384AcetylationRSQPKKPKPEDPKFP
CCCCCCCCCCCCCCC		70.6730589583
389UbiquitinationKPKPEDPKFPGEGTA
CCCCCCCCCCCCCHH		76.22-
409AcetylationEEAGGSVKEEAGPEV
HHCCCCCCHHCCCCC		52.0830589589
409SumoylationEEAGGSVKEEAGPEV
HHCCCCCCHHCCCCC		52.08-
537UbiquitinationYVVPRPGKAAFNQEH
EEECCCCCCCCCCHH		38.94-
557UbiquitinationAFEHFAQKGPTWKEP
HHHHHHHHCCCCCCC		64.53-
560PhosphorylationHFAQKGPTWKEPVSP
HHHHHCCCCCCCCCC		58.8128464451
562UbiquitinationAQKGPTWKEPVSPME
HHHCCCCCCCCCCCC		55.40-
566PhosphorylationPTWKEPVSPMELTGP
CCCCCCCCCCCCCCC		29.2830278072
571PhosphorylationPVSPMELTGPEDGAA
CCCCCCCCCCCCCCC		37.0727794612
579PhosphorylationGPEDGAASSGAGRME
CCCCCCCCCCCCCCC		28.8626074081
580PhosphorylationPEDGAASSGAGRMET
CCCCCCCCCCCCCCH		28.1226074081
602AcetylationQAPSTFSKLKMEIKK
CCCCHHHHHHHHHHH		48.1919608861
602UbiquitinationQAPSTFSKLKMEIKK
CCCCHHHHHHHHHHH		48.1919608861
620PhosphorylationHPLGRPPTRSPLSVV
CCCCCCCCCCCCHHH		46.6028348404
622PhosphorylationLGRPPTRSPLSVVKQ
CCCCCCCCCCHHHEE		32.4430266825
625PhosphorylationPPTRSPLSVVKQEAS
CCCCCCCHHHEECCC		28.4030266825
632PhosphorylationSVVKQEASSDEEASP
HHHEECCCCCCCCCC		37.2522777824
633PhosphorylationVVKQEASSDEEASPF
HHEECCCCCCCCCCC		56.9726657352
638PhosphorylationASSDEEASPFSGEED
CCCCCCCCCCCCCCC		29.7423909892
641PhosphorylationDEEASPFSGEEDVSD
CCCCCCCCCCCCCCC		48.9922115753
647PhosphorylationFSGEEDVSDPDALRP
CCCCCCCCCHHHHHH		56.6022115753
657PhosphorylationDALRPLLSLQWKNRA
HHHHHHHCHHHHHHH		26.6327251275
666PhosphorylationQWKNRAASFQAERKF
HHHHHHHHHHHHHHH		19.5327251275
672UbiquitinationASFQAERKFNAAAAR
HHHHHHHHHHHHHHC		34.18-
707PhosphorylationEKEAPIASLGKGCPA
CCCCCCCCCCCCCCC		38.07-
718PhosphorylationGCPATLPSKSRQKTR
CCCCCCCCCCCCCCC		46.5024719451
723UbiquitinationLPSKSRQKTRPLIPE
CCCCCCCCCCCCCCC		45.45-
851UbiquitinationPEQRWKLKCVYCRKR
CHHHCEEEEEEHHHH		20.23-
907UbiquitinationSITCLKHKSGGHAVQ
EEEEEECCCCCCHHH		49.57-
908PhosphorylationITCLKHKSGGHAVQL
EEEEECCCCCCHHHH		50.1328555341
920PhosphorylationVQLLRAVSLGQVVIT
HHHHHHHHCCCEEEE		26.2930108239
928UbiquitinationLGQVVITKNRNGLYY
CCCEEEEECCCCCEE		42.67-
1017PhosphorylationFEDGSQLTVKRGDIF
ECCCCEEEEECCCEE		19.1523532336
1032UbiquitinationTLEEELPKRVRSRLS
EECHHHCHHHHHHHC		75.93-
1036PhosphorylationELPKRVRSRLSLSTG
HHCHHHHHHHCCCCC		34.4128387310
1039PhosphorylationKRVRSRLSLSTGAPQ
HHHHHHHCCCCCCCC		21.1128450419
1041PhosphorylationVRSRLSLSTGAPQEP
HHHHHCCCCCCCCCC		22.7828387310
1042PhosphorylationRSRLSLSTGAPQEPA
HHHHCCCCCCCCCCC		42.5328450419
1051PhosphorylationAPQEPAFSGEEAKAA
CCCCCCCCHHHHHHC		47.6128985074
1056 (in isoform 1)Ubiquitination-52.7521906983
1056UbiquitinationAFSGEEAKAAKRPRV
CCCHHHHHHCCCCCC		52.7521906983
1065PhosphorylationAKRPRVGTPLATEDS
CCCCCCCCCCCCCCC		16.5729255136
1069PhosphorylationRVGTPLATEDSGRSQ
CCCCCCCCCCCCCCH		48.27-
1078PhosphorylationDSGRSQDYVAFVESL
CCCCCHHHHHHHHHH		6.00-
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
305TPhosphorylationKinaseMAPK1P28482
GPS
352SPhosphorylationKinaseMAPK1P28482
GPS
566SPhosphorylationKinaseMAPK1P28482
GPS
622SPhosphorylationKinaseMAPK1P28482
GPS
1065TPhosphorylationKinaseMAPK1P28482
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KDM4B_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 KDM4B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KMT2D_HUMANKMT2Dphysical
21502505
ASH2L_HUMANASH2Lphysical
21502505
RBBP5_HUMANRBBP5physical
21502505
WDR5_HUMANWDR5physical
21502505
HNRPU_HUMANHNRNPUphysical
21502505
HSP74_HUMANHSPA4physical
21502505
ESR1_HUMANESR1physical
21502505
KMT2C_HUMANKMT2Cphysical
21502505
SMU1_HUMANSMU1physical
22939629
ENPL_HUMANHSP90B1physical
23589305
DDX3X_HUMANDDX3Xphysical
26344197
KDM4A_HUMANKDM4Aphysical
28514442
TCPG_HUMANCCT3physical
28514442
TCPD_HUMANCCT4physical
28514442
TCPW_HUMANCCT6Bphysical
28514442
TCPB_HUMANCCT2physical
28514442
TCPH_HUMANCCT7physical
28514442
CC85C_HUMANCCDC85Cphysical
28514442
TCPE_HUMANCCT5physical
28514442
TCPA_HUMANTCP1physical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
TCPQ_HUMANCCT8physical
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 KDM4B_HUMAN

loading...

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-602, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-566 AND THR-1065, ANDMASS SPECTROMETRY.
"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-566 AND SER-622, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory