KDM1B_HUMAN - dbPTM
KDM1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KDM1B_HUMAN
UniProt AC Q8NB78
Protein Name Lysine-specific histone demethylase 1B
Gene Name KDM1B
Organism Homo sapiens (Human).
Sequence Length 822
Subcellular Localization Nucleus.
Protein Description Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for de novo DNA methylation of a subset of imprinted genes during oogenesis. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. Has no effect on tri-methylated 'Lys-4', mono-, di- or tri-methylated 'Lys-9', mono-, di- or tri-methylated 'Lys-27', mono-, di- or tri-methylated 'Lys-36' of histone H3, or on mono-, di- or tri-methylated 'Lys-20' of histone H4..
Protein Sequence MATPRGRTKKKASFDHSPDSLPLRSSGRQAKKKATETTDEDEDGGSEKKYRKCEKAGCTATCPVCFASASERCAKNGYTSRWYHLSCGEHFCNECFDHYYRSHKDGYDKYTTWKKIWTSNGKTEPSPKAFMADQQLPYWVQCTKPECRKWRQLTKEIQLTPQIAKTYRCGMKPNTAIKPETSDHCSLPEDLRVLEVSNHWWYSMLILPPLLKDSVAAPLLSAYYPDCVGMSPSCTSTNRAAATGNASPGKLEHSKAALSVHVPGMNRYFQPFYQPNECGKALCVRPDVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEALTPQKCIPHIIVRGLVRIRCVQEVERILYFMTRKGLINTGVLSVGADQYLLPKDYHNKSVIIIGAGPAGLAAARQLHNFGIKVTVLEAKDRIGGRVWDDKSFKGVTVGRGAQIVNGCINNPVALMCEQLGISMHKFGERCDLIQEGGRITDPTIDKRMDFHFNALLDVVSEWRKDKTQLQDVPLGEKIEEIYKAFIKESGIQFSELEGQVLQFHLSNLEYACGSNLHQVSARSWDHNEFFAQFAGDHTLLTPGYSVIIEKLAEGLDIQLKSPVQCIDYSGDEVQVTTTDGTGYSAQKVLVTVPLALLQKGAIQFNPPLSEKKMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPPSASKRGLFAVFYDMDPQKKHSVLMSVIAGEAVASVRTLDDKQVLQQCMATLRELFKEQEVPDPTKYFVTRWSTDPWIQMAYSFVKTGGSGEAYDIIAEDIQGTVFFAGEATNRHFPQTVTGAYLSGVREASKIAAF
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
13 (in isoform 2)Phosphorylation-39.8324719451
13PhosphorylationGRTKKKASFDHSPDS
CCCCCCCCCCCCCCC		39.8323927012
17 (in isoform 2)Phosphorylation-32.0424719451
17PhosphorylationKKASFDHSPDSLPLR
CCCCCCCCCCCCCCC		32.0429255136
20PhosphorylationSFDHSPDSLPLRSSG
CCCCCCCCCCCCCCC		34.9623927012
25 (in isoform 2)Phosphorylation-44.8427251275
25PhosphorylationPDSLPLRSSGRQAKK
CCCCCCCCCCCCCHH		44.8425159151
26PhosphorylationDSLPLRSSGRQAKKK
CCCCCCCCCCCCHHH		31.4025159151
35PhosphorylationRQAKKKATETTDEDE
CCCHHHHCCCCCCCC		42.6230624053
37PhosphorylationAKKKATETTDEDEDG
CHHHHCCCCCCCCCC		34.8828985074
38PhosphorylationKKKATETTDEDEDGG
HHHHCCCCCCCCCCC		31.0329414761
109UbiquitinationSHKDGYDKYTTWKKI
HCCCCCCCCCCCHHH		35.6921890473
109 (in isoform 1)Ubiquitination-35.6921890473
109 (in isoform 2)Ubiquitination-35.6921890473
109 (in isoform 4)Ubiquitination-35.6921890473
109UbiquitinationSHKDGYDKYTTWKKI
HCCCCCCCCCCCHHH		35.6921890473
109UbiquitinationSHKDGYDKYTTWKKI
HCCCCCCCCCCCHHH		35.6921890473
118PhosphorylationTTWKKIWTSNGKTEP
CCCHHHCCCCCCCCC		18.7829083192
119PhosphorylationTWKKIWTSNGKTEPS
CCHHHCCCCCCCCCC		28.7029083192
122AcetylationKIWTSNGKTEPSPKA
HHCCCCCCCCCCCCC		54.7026051181
123PhosphorylationIWTSNGKTEPSPKAF
HCCCCCCCCCCCCCH		55.3029083192
126PhosphorylationSNGKTEPSPKAFMAD
CCCCCCCCCCCHHCC		32.5723532336
155UbiquitinationRKWRQLTKEIQLTPQ
HHHHHHHHHHCCCHH		62.50-
165UbiquitinationQLTPQIAKTYRCGMK
CCCHHHHHHHCCCCC		47.95-
165AcetylationQLTPQIAKTYRCGMK
CCCHHHHHHHCCCCC		47.9526051181
178AcetylationMKPNTAIKPETSDHC
CCCCCCCCCCCCCCC		34.0525953088
243PhosphorylationSTNRAAATGNASPGK
CCCCHHHCCCCCCCC		26.6622167270
246 (in isoform 4)Ubiquitination-20.6021890473
246UbiquitinationRAAATGNASPGKLEH
CHHHCCCCCCCCCCC		20.6021890473
246 (in isoform 2)Ubiquitination-20.6021890473
247PhosphorylationAAATGNASPGKLEHS
HHHCCCCCCCCCCCC		37.8829255136
250UbiquitinationTGNASPGKLEHSKAA
CCCCCCCCCCCCCEE		54.83-
254PhosphorylationSPGKLEHSKAALSVH
CCCCCCCCCEEEEEC		18.0222167270
327PhosphorylationTNCKEALTPQKCIPH
HCHHHHCCCCCCCCH		30.6224719451
374PhosphorylationLSVGADQYLLPKDYH
CCCCCCEEECCCCCC		15.6846164807
378 (in isoform 1)Ubiquitination-71.5321890473
378UbiquitinationADQYLLPKDYHNKSV
CCEEECCCCCCCCEE		71.5321890473
378UbiquitinationADQYLLPKDYHNKSV
CCEEECCCCCCCCEE		71.5321890473
414UbiquitinationKVTVLEAKDRIGGRV
EEEEEEECCCCCCCC		37.86-
417 (in isoform 4)Ubiquitination-11.1421890473
417UbiquitinationVLEAKDRIGGRVWDD
EEEECCCCCCCCCCC		11.1421890473
418 (in isoform 2)Ubiquitination-20.8121890473
425UbiquitinationGGRVWDDKSFKGVTV
CCCCCCCCCCCCCEE		56.15-
428UbiquitinationVWDDKSFKGVTVGRG
CCCCCCCCCCEECCC		60.61-
481 (in isoform 1)Ubiquitination-45.8521890473
481UbiquitinationITDPTIDKRMDFHFN
CCCCCCCHHHHHHHH		45.8521906983
518 (in isoform 1)Ubiquitination-42.3421890473
518UbiquitinationEKIEEIYKAFIKESG
HHHHHHHHHHHHHHC		42.3421890473
518UbiquitinationEKIEEIYKAFIKESG
HHHHHHHHHHHHHHC		42.3421890473
644PhosphorylationIQFNPPLSEKKMKAI
CCCCCCCCHHHHHHH		53.8246164789
649UbiquitinationPLSEKKMKAINSLGA
CCCHHHHHHHHHCCC		55.802189047
650 (in isoform 1)Ubiquitination-11.6021890473
650UbiquitinationLSEKKMKAINSLGAG
CCHHHHHHHHHCCCC		11.6021890473
668PhosphorylationKIALQFPYRFWDSKV
HHHHHCCHHHCCCCC		21.5227067055
673PhosphorylationFPYRFWDSKVQGADF
CCHHHCCCCCCCCCC		25.8927067055
711PhosphorylationKKHSVLMSVIAGEAV
HCCHHHHHHHCCCHH		13.2546164795
720PhosphorylationIAGEAVASVRTLDDK
HCCCHHEECCCCCHH		12.9246164801
736PhosphorylationVLQQCMATLRELFKE
HHHHHHHHHHHHHHH		10.2420201521
750PhosphorylationEQEVPDPTKYFVTRW
HCCCCCCCCEEEEEE		45.8410964131
755PhosphorylationDPTKYFVTRWSTDPW
CCCCEEEEEECCCHH		19.2710964141
768PhosphorylationPWIQMAYSFVKTGGS
HHHHHHHHHHHCCCC		17.6410964151
811PhosphorylationTVTGAYLSGVREASK
HHHHHHHHCHHHHHH		23.6724719451
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 KDM1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KDM1B_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 KDM1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NSD3_HUMANWHSC1L1physical
20670891
EHMT2_HUMANEHMT2physical
20670891
PAXI1_HUMANPAXIP1physical
20670891
CCNT1_HUMANCCNT1physical
20670891
WDR5_HUMANWDR5physical
20670891
DC1I2_HUMANDYNC1I2physical
26496610
BAP1_HUMANBAP1physical
26496610
COX5A_HUMANCOX5Aphysical
26496610
CASC3_HUMANCASC3physical
26496610
CPSF3_HUMANCPSF3physical
26496610
NSD3_HUMANWHSC1L1physical
26496610
HEAT3_HUMANHEATR3physical
26496610
ASXL2_HUMANASXL2physical
26496610
KDM1B_HUMANKDM1Bphysical
25773598
UB2D3_HUMANUBE2D3physical
25773598
OGT1_HUMANOGTphysical
25773598
H31T_HUMANHIST3H3physical
25773598
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 KDM1B_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-17, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASSSPECTROMETRY.

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