KDM1B_MOUSE - dbPTM
KDM1B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KDM1B_MOUSE
UniProt AC Q8CIG3
Protein Name Lysine-specific histone demethylase 1B
Gene Name Kdm1b
Organism Mus musculus (Mouse).
Sequence Length 826
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 MAASRGRSKKRSNLELSPDNLPLRSSGRQAKKKAVEIPDEDEDGSSEKKYRKCEKAGCTAAYPVCFASASERCAKNGYTSRWYHLSCGEHFCNECFDHYYRSHKDGYDKYSAWKRVWTSNGKTEPSPKAFMADQQLPYWVQCTKPECGKWRQLTKEIQLTPHMARTYRCGMKPNTITKPDTPDHCSFPEDLRVLEVSNHWWYPMLIQPPLLKDSVAAPLLSAYYPDCVGMSPSCTSTHRATVTAATTTTGSASPGEMEPSKAAPSSLVLGMNRYFQPFYQPNECGKALCVRPDVMELDELYEFPEYSRDPTMYLALRNLILALWYTNCKEALTPQKCIPHIIVRGLVRIRCVQEVERILYFMTRKGLINTGVLTVAAGQHLLPKHYHNKSVLVVGAGPAGLAAARQLHNFGMKVTVLEAKDRIGGRVWDDKSFKGVVVGRGPQIVNGCINNPVALMCEQLGISMRKLGERCDLIQEGGRITDPTVDKRMDFHFNALLDVVSEWRKDKTLLQDVPLGEKIEEIYRAFVKESGIQFSELEGQVLQFHLSNLEYACGSSLHQVSARSWDHNEFFAQFAGDHTLLTPGYSTIIEKLAEGLDIRLKSPVQSIDYTGDEVQVTTTDGMGHSAQKVLVTVPLAILQRGAIQFNPPLSEKKMKAINSLGAGIIEKIALQFPYRFWDSKVQGADFFGHVPPSASQRGLFAVFYDMDSQQSVLMSVITGEAVASLRTMDDKQVLQQCMGILRELFKEQEIPEPTKYFVTRWSTEPWIQMAYSFVKTFGSGEAYDIIAEEIQGTVFFAGEATNRHFPQTVTGAYLSGVREASKIAAF
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
12PhosphorylationRGRSKKRSNLELSPD
CCCCCCCCCCCCCCC
55.4325777480
17PhosphorylationKRSNLELSPDNLPLR
CCCCCCCCCCCCCCC
22.3426824392
26PhosphorylationDNLPLRSSGRQAKKK
CCCCCCCCCCCCCCC
31.40-
45PhosphorylationPDEDEDGSSEKKYRK
CCCCCCCCCHHHHHH
47.8725338131
241PhosphorylationCTSTHRATVTAATTT
CCCCCEEEEEEEEEE
20.5325619855
243PhosphorylationSTHRATVTAATTTTG
CCCEEEEEEEEEECC
13.2525619855
246PhosphorylationRATVTAATTTTGSAS
EEEEEEEEEECCCCC
23.3925619855
247PhosphorylationATVTAATTTTGSASP
EEEEEEEEECCCCCC
20.0325619855
248PhosphorylationTVTAATTTTGSASPG
EEEEEEEECCCCCCC
25.4625619855
249PhosphorylationVTAATTTTGSASPGE
EEEEEEECCCCCCCC
27.3525619855
251PhosphorylationAATTTTGSASPGEME
EEEEECCCCCCCCCC
24.3925619855
253PhosphorylationTTTTGSASPGEMEPS
EEECCCCCCCCCCCC
34.8225521595
260PhosphorylationSPGEMEPSKAAPSSL
CCCCCCCCCCCCCCE
22.9425619855
632PhosphorylationSAQKVLVTVPLAILQ
CCCEEEEHHHHHHHH
16.5551460277
655UbiquitinationPLSEKKMKAINSLGA
CCCHHHHHHHHHCCC
55.8022790023

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KDM1B_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of KDM1B_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KDM1B_MOUSE

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Related Literatures of Post-Translational Modification

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