UniProt ID | KDM3B_MOUSE | |
---|---|---|
UniProt AC | Q6ZPY7 | |
Protein Name | Lysine-specific demethylase 3B | |
Gene Name | Kdm3b | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 1562 | |
Subcellular Localization | Nucleus. | |
Protein Description | 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 (By similarity).. | |
Protein Sequence | MADAAASPVGKRLLLLFADPTASASASAPTAAAVVSGDPGPALRTRAWRAGTVRAMSGAVPQDLAIFVEFDGCNWKQHSWVKVHAEDVLALLLEGSLVWAPRKDPVLLQGTRVPVAQWPALTFTPLVDKLGLGSVVPVEYLVDRELRFLSDANGMHLFQMGTDVQNQILLEHAALRETVNALISDQKLQEIFSRGPYSVQGHRVKVYQPEGEEVWLCGVVSRQDSVTRLMEVSITETGEVKSVDPRLTHVMLMDSSTPQSENSRNSSLASSGFGVSLSSLSQPLTFGSGRSQSNGVLATDNKPLGFSFSCSSASESQKDSDLSKNLFFQCMSQNVPSTNYLSRVSESVADDSSSRDSFTQSLESLTSGLCKGRSVLGADTQPGPKAGSSVDRKVPAESMPTLTPAFPRSLLNTRTPENHENLFLQPPKLSREEPSNPFLAFVEKVEHSPFSSFVSQASGSSSSATSVTSKATASWPESHSSAESAPLAKKKPLFITTDSSKLVSGVLGSALSTGSPSLSAVGNGRSSSPTNSLTQPIEMPTLSSSPTEERPTVGPGQQDNPLLKTFSTVFGRHSGSFLSAPAEFAQENKAPFEAVKRFSLDERSLACRQDSDSSTNSDLSDLSDSEEQLQAKSGLKGIPEHLMGKLGPNGERSAELLLGKGKGKQAPKGRPRTAPLKVGQSVLKDVSKVRKLKQSGEPFLQDGSCINVAPHLHKCRECRLERYRKFKEQEQDDSTVACRFFHFRRLVFTRKGVLRVEGFLSPQQSDPDAMNLWIPSSSLAEGIDLETSKYILANVGDQFCQLVMSEKEAMMMVEPHQKVAWKRAVRGVREMCDVCETTLFNIHWVCRKCGFGVCLDCYRLRKSRPRSETEEMGDEEVFSWLKCAKGQSHEPENLMPTQIIPGTALYNIGDMVHAARGKWGIKANCPCISRQSKSVLRPAVTNGISQLPSVTPSASSGNETTFSSGGGAAAVTNPEPDQVPKGAGTDGRSEEPLKAEGSASNSNSELKAIRPPCPDTAPPSSALHWLADLATQKAKEETKDAGSLRSVLNKESHSPFGLDSFNSTAKVSPLTPKLFNSLLLGPTASNSKTEGSSLRDLLHSGPGKLPQTPLDTGIPFPPVFSSSSAVAKSKASLPDFLDHIIASVVENKKTSDPSKRSCNLTDTQKEVKEMAMGLNVLDPHTSHSWLCDGRLLCLHDPSNKNNWKIFRECWKQGQPVLVSGVHKKLKSELWKPEAFSQEFGDQDVDLVNCRNCAIISDVKVRDFWDGFEIICKRLRSEDGQPMVLKLKDWPPGEDFRDMMPTRFEDLMENLPLPEYTKRDGRLNLASRLPSYFVRPDLGPKMYNAYGLITAEDRRVGTTNLHLDVSDAVNVMVYVGIPVGEGAHDEEVLKTIDEGDADEVTKQRIHDGKEKPGALWHIYAAKDAEKIRELLRKVGEEQGQENPPDHDPIHDQSWYLDQILRKRLFEEYGVQGWAIVQFLGDAVFIPAGAPHQVHNLYSCIKVAEDFVSPEHVKHCFRLTQEFRHLSNTHTNHEDKLQVKNIIYHAVKDAVGTLKAHESKLARS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MADAAASPV ------CCCHHCCCC | 26.84 | - | |
7 | Phosphorylation | -MADAAASPVGKRLL -CCCHHCCCCHHEEE | 18.52 | - | |
242 | Phosphorylation | TETGEVKSVDPRLTH ECCCCEEECCCCCEE | 36.61 | - | |
248 | Phosphorylation | KSVDPRLTHVMLMDS EECCCCCEEEEEECC | 17.44 | - | |
255 | Phosphorylation | THVMLMDSSTPQSEN EEEEEECCCCCCCCC | 23.34 | - | |
293 | Phosphorylation | FGSGRSQSNGVLATD CCCCCCCCCCEEECC | 36.48 | 27841257 | |
345 | Phosphorylation | TNYLSRVSESVADDS CCHHHHHCHHHCCCC | 24.04 | 25619855 | |
347 | Phosphorylation | YLSRVSESVADDSSS HHHHHCHHHCCCCCC | 18.33 | 25619855 | |
352 | Phosphorylation | SESVADDSSSRDSFT CHHHCCCCCCCHHHH | 30.66 | 21082442 | |
353 | Phosphorylation | ESVADDSSSRDSFTQ HHHCCCCCCCHHHHH | 36.07 | 25619855 | |
354 | Phosphorylation | SVADDSSSRDSFTQS HHCCCCCCCHHHHHH | 44.02 | 27087446 | |
357 | Phosphorylation | DDSSSRDSFTQSLES CCCCCCHHHHHHHHH | 29.14 | 27087446 | |
359 | Phosphorylation | SSSRDSFTQSLESLT CCCCHHHHHHHHHHH | 22.62 | 27087446 | |
361 | Phosphorylation | SRDSFTQSLESLTSG CCHHHHHHHHHHHCC | 30.92 | 25619855 | |
364 | Phosphorylation | SFTQSLESLTSGLCK HHHHHHHHHHCCCCC | 42.09 | 25619855 | |
366 | Phosphorylation | TQSLESLTSGLCKGR HHHHHHHHCCCCCCC | 29.99 | 25619855 | |
367 | Phosphorylation | QSLESLTSGLCKGRS HHHHHHHCCCCCCCC | 34.75 | 25619855 | |
409 | Phosphorylation | LTPAFPRSLLNTRTP CCCCCCHHHCCCCCC | 37.13 | 26643407 | |
413 | Phosphorylation | FPRSLLNTRTPENHE CCHHHCCCCCCCCCC | 35.57 | 26643407 | |
415 | Phosphorylation | RSLLNTRTPENHENL HHHCCCCCCCCCCCC | 32.68 | 26643407 | |
448 | Phosphorylation | FVEKVEHSPFSSFVS HHEECCCCCCHHHHH | 17.71 | 26643407 | |
451 | Phosphorylation | KVEHSPFSSFVSQAS ECCCCCCHHHHHHCC | 26.67 | 26643407 | |
452 | Phosphorylation | VEHSPFSSFVSQASG CCCCCCHHHHHHCCC | 30.01 | 26643407 | |
455 | Phosphorylation | SPFSSFVSQASGSSS CCCHHHHHHCCCCCC | 20.30 | 26643407 | |
497 | O-linked_Glycosylation | KKPLFITTDSSKLVS CCCEEEECCHHHHHH | 29.12 | 55412337 | |
497 | Phosphorylation | KKPLFITTDSSKLVS CCCEEEECCHHHHHH | 29.12 | - | |
504 | Phosphorylation | TDSSKLVSGVLGSAL CCHHHHHHHHHHHHH | 33.35 | 22942356 | |
509 | Phosphorylation | LVSGVLGSALSTGSP HHHHHHHHHHHCCCC | 23.13 | 26643407 | |
512 | Phosphorylation | GVLGSALSTGSPSLS HHHHHHHHCCCCCCH | 30.36 | 26643407 | |
513 | Phosphorylation | VLGSALSTGSPSLSA HHHHHHHCCCCCCHH | 42.39 | 26643407 | |
515 | Phosphorylation | GSALSTGSPSLSAVG HHHHHCCCCCCHHCC | 16.05 | 27180971 | |
517 | Phosphorylation | ALSTGSPSLSAVGNG HHHCCCCCCHHCCCC | 36.33 | 26745281 | |
519 | Phosphorylation | STGSPSLSAVGNGRS HCCCCCCHHCCCCCC | 25.83 | 26643407 | |
526 | Phosphorylation | SAVGNGRSSSPTNSL HHCCCCCCCCCCCCC | 36.24 | 25521595 | |
527 | Phosphorylation | AVGNGRSSSPTNSLT HCCCCCCCCCCCCCC | 38.69 | 24453211 | |
528 | Phosphorylation | VGNGRSSSPTNSLTQ CCCCCCCCCCCCCCC | 36.67 | 24925903 | |
530 | Phosphorylation | NGRSSSPTNSLTQPI CCCCCCCCCCCCCCC | 39.11 | 24925903 | |
532 | Phosphorylation | RSSSPTNSLTQPIEM CCCCCCCCCCCCCCC | 34.96 | 24925903 | |
534 | Phosphorylation | SSPTNSLTQPIEMPT CCCCCCCCCCCCCCC | 31.92 | 24925903 | |
541 | Phosphorylation | TQPIEMPTLSSSPTE CCCCCCCCCCCCCCC | 37.65 | 24925903 | |
543 | Phosphorylation | PIEMPTLSSSPTEER CCCCCCCCCCCCCCC | 31.11 | 24925903 | |
544 | Phosphorylation | IEMPTLSSSPTEERP CCCCCCCCCCCCCCC | 43.37 | 24925903 | |
545 | Phosphorylation | EMPTLSSSPTEERPT CCCCCCCCCCCCCCC | 32.25 | 25521595 | |
547 | Phosphorylation | PTLSSSPTEERPTVG CCCCCCCCCCCCCCC | 53.04 | 24925903 | |
552 | Phosphorylation | SPTEERPTVGPGQQD CCCCCCCCCCCCCCC | 44.29 | 24925903 | |
565 | Phosphorylation | QDNPLLKTFSTVFGR CCCHHHHHHHHHHCC | 23.84 | 26643407 | |
567 | Phosphorylation | NPLLKTFSTVFGRHS CHHHHHHHHHHCCCC | 28.97 | 27600695 | |
568 | Phosphorylation | PLLKTFSTVFGRHSG HHHHHHHHHHCCCCC | 18.70 | 26643407 | |
574 | Phosphorylation | STVFGRHSGSFLSAP HHHHCCCCCCCCCCC | 34.47 | 29899451 | |
576 | Phosphorylation | VFGRHSGSFLSAPAE HHCCCCCCCCCCCHH | 26.48 | 26643407 | |
579 | Phosphorylation | RHSGSFLSAPAEFAQ CCCCCCCCCCHHHHH | 30.14 | 26643407 | |
599 | Phosphorylation | FEAVKRFSLDERSLA HHHHHHCCCCHHHHH | 38.66 | 26824392 | |
1052 | Phosphorylation | RSVLNKESHSPFGLD HHHHCCCCCCCCCCC | 30.76 | 26745281 | |
1054 | Phosphorylation | VLNKESHSPFGLDSF HHCCCCCCCCCCCCC | 31.07 | 25266776 | |
1060 | Phosphorylation | HSPFGLDSFNSTAKV CCCCCCCCCCCCCCC | 31.22 | 26643407 | |
1068 | Phosphorylation | FNSTAKVSPLTPKLF CCCCCCCCCCCHHHH | 17.31 | 28066266 | |
1071 | Phosphorylation | TAKVSPLTPKLFNSL CCCCCCCCHHHHHHH | 23.04 | 29514104 | |
1073 | Ubiquitination | KVSPLTPKLFNSLLL CCCCCCHHHHHHHHC | 61.55 | - | |
1088 | Ubiquitination | GPTASNSKTEGSSLR CCCCCCCCCCCCCHH | 55.64 | - | |
1187 | S-nitrosylation | HTSHSWLCDGRLLCL CCCCCCCCCCEEEEE | 4.19 | 22178444 | |
1187 | S-nitrosocysteine | HTSHSWLCDGRLLCL CCCCCCCCCCEEEEE | 4.19 | - | |
1507 | Phosphorylation | KVAEDFVSPEHVKHC HHHHCCCCHHHHHHH | 25.27 | 26745281 |
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 KDM3B_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KDM3B_MOUSE !! |
* 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 KDM3B_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of KDM3B_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599, AND MASSSPECTROMETRY. |