UniProt ID | KDM4B_MOUSE | |
---|---|---|
UniProt AC | Q91VY5 | |
Protein Name | Lysine-specific demethylase 4B | |
Gene Name | Kdm4b | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 1086 | |
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 (By similarity).. | |
Protein Sequence | MGSEDHSAQNPSCKIMTFRPTMDEFRDFNRYVAYIESQGAHRAGLAKIIPPKEWKPRQTYDDIDDVVIPAPIQQVVTGQSGLFTQYNIQKKAMTVGEYRRLANSEKYCTPRHQDFDDLERKYWKNLTFVSPIYGADISGSLYDDDVAQWNIGNLRTILDMVERECGTIIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAIGFFPGSSQGCDAFLRHKMTLISPIILKKYGIPFSRITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATLRWIDYGKVATQCTCRKDMVKISMDVFVRILQPERYEQWKQGRDLTVLDHTRPTALSSPELSSWSASRTSIKAKLLRRQISVKESRPWRKAEEERRREPTRRPGPASHRRRSQPKKSKPEESRSPGEATAGVSTLDEARGCSRGEAMPEDEEEEELLPSQGHEAEGVEEDGRGKPRPTKARNKKKTPSPSSPPLLSAPPALFPTEEVLRPPPQPKSPGPAMGPMAAEGGPPPTPLNVVPPGAPVEEAEVRPRPIIPMLYVLPRTSSTDGDREHSAHAQLAPMELGPEEENQAQAGDSQGTTPFSKLKVEIKKSRRHPLGRPPTRSPLSVVKQEASSDEEAFLFSGEDDVTDPEALRSLLSLQWKNKAASFQAERKFNAAAALSEPYCAICTLFYPYSQSVQTERDSAVQPPSKSGQRTRPLIPEMCFTSSGENTEPLPANSYVGEDGTSPLISCAHCCLQVHASCYGVRPELAKEGWTCSRCAAHAWTAECCLCNLRGGALQRTTEHRWIHVICAIAVPEVRFLNVIERNPVDVSAIPEQRWKLKCIYCRKRMKRVSGACIQCSYEHCSTSFHVTCAHAAGVLMEPDDWPYVVSITCLKHRASGAGGQLLRTVSLGQIVITKNRNGLYYRCRVIGTTAQTFYEVNFDDGSYSDNLYPESITSRDCLRLGPPPEGELVELRWTDGNLYRARFISMATSLIYQVEFEDGSQLTVKRGDIFTLEEELPKRVRSRLSLSTGTPQEPSFSGDDVKAAKRPRVASVLATTTEDTGRSPEYLSFMESLLQAQGRPGAPF | |
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 |
---|---|---|---|---|---|
305 | Phosphorylation | IDYGKVATQCTCRKD EEHHHEECEEEECHH | 27.45 | 17203969 | |
317 | Phosphorylation | RKDMVKISMDVFVRI CHHHEEEEHHHHHHH | 11.83 | 20531401 | |
375 | Phosphorylation | KLLRRQISVKESRPW HHHHHCCCCCCCCCC | 20.85 | - | |
394 | Phosphorylation | EERRREPTRRPGPAS HHHHCCCCCCCCCHH | 34.26 | 23140645 | |
401 | Phosphorylation | TRRPGPASHRRRSQP CCCCCCHHHCCCCCC | 22.21 | 22817900 | |
411 | Phosphorylation | RRSQPKKSKPEESRS CCCCCCCCCCHHHCC | 60.62 | 25619855 | |
416 | Phosphorylation | KKSKPEESRSPGEAT CCCCCHHHCCCCCCC | 36.07 | 25619855 | |
418 | Phosphorylation | SKPEESRSPGEATAG CCCHHHCCCCCCCCC | 46.68 | 27149854 | |
423 | Phosphorylation | SRSPGEATAGVSTLD HCCCCCCCCCCCHHH | 21.46 | 25619855 | |
427 | Phosphorylation | GEATAGVSTLDEARG CCCCCCCCHHHHHCC | 23.49 | 25619855 | |
428 | Phosphorylation | EATAGVSTLDEARGC CCCCCCCHHHHHCCC | 35.50 | 25619855 | |
453 | Phosphorylation | EEEELLPSQGHEAEG HHHHHCCCCCCCCCC | 49.08 | 22006019 | |
480 | Phosphorylation | KARNKKKTPSPSSPP CCCCCCCCCCCCCCC | 37.57 | 26643407 | |
482 | Phosphorylation | RNKKKTPSPSSPPLL CCCCCCCCCCCCCCC | 42.52 | 26643407 | |
484 | Phosphorylation | KKKTPSPSSPPLLSA CCCCCCCCCCCCCCC | 60.87 | 26643407 | |
485 | Phosphorylation | KKTPSPSSPPLLSAP CCCCCCCCCCCCCCC | 33.64 | 25266776 | |
490 | Phosphorylation | PSSPPLLSAPPALFP CCCCCCCCCCCCCCC | 46.54 | 26643407 | |
498 | Phosphorylation | APPALFPTEEVLRPP CCCCCCCCHHHCCCC | 37.13 | 22817900 | |
510 | Phosphorylation | RPPPQPKSPGPAMGP CCCCCCCCCCCCCCC | 41.60 | 26643407 | |
558 (in isoform 2) | Phosphorylation | - | 25.70 | 25338131 | |
558 | Phosphorylation | MLYVLPRTSSTDGDR EEEEEECCCCCCCCC | 25.70 | 25338131 | |
560 (in isoform 2) | Phosphorylation | - | 29.88 | 25338131 | |
568 | Phosphorylation | TDGDREHSAHAQLAP CCCCCCCCCCCEECC | 19.59 | 25338131 | |
599 | Acetylation | QGTTPFSKLKVEIKK CCCCCHHHHEEEEEH | 53.35 | - | |
617 | Phosphorylation | HPLGRPPTRSPLSVV CCCCCCCCCCCCHHH | 46.60 | 26060331 | |
619 | Phosphorylation | LGRPPTRSPLSVVKQ CCCCCCCCCCHHHEE | 32.44 | 26239621 | |
622 | Phosphorylation | PPTRSPLSVVKQEAS CCCCCCCHHHEECCC | 28.40 | 26239621 | |
629 | Phosphorylation | SVVKQEASSDEEAFL HHHEECCCCCCCCEE | 37.25 | 26239621 | |
630 | Phosphorylation | VVKQEASSDEEAFLF HHEECCCCCCCCEEE | 56.97 | 26239621 | |
638 | Phosphorylation | DEEAFLFSGEDDVTD CCCCEEECCCCCCCC | 43.34 | 25293948 | |
908 | Phosphorylation | GQLLRTVSLGQIVIT CCEEEEEECCCEEEE | 26.60 | 26239621 | |
1024 | Phosphorylation | ELPKRVRSRLSLSTG HHCHHHHHHHCCCCC | 34.41 | 25338131 | |
1027 | Phosphorylation | KRVRSRLSLSTGTPQ HHHHHHHCCCCCCCC | 21.11 | - | |
1037 | Phosphorylation | TGTPQEPSFSGDDVK CCCCCCCCCCCHHHH | 31.15 | 26745281 | |
1039 | Phosphorylation | TPQEPSFSGDDVKAA CCCCCCCCCHHHHHH | 45.72 | 26745281 | |
1053 | Phosphorylation | AKRPRVASVLATTTE HCCCCEEEEEEEECC | 18.14 | 25266776 |
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 KDM4B_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of KDM4B_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 KDM4B_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ESR1_MOUSE | Esr1 | physical | 21445275 | |
SMCA4_MOUSE | Smarca4 | physical | 21445275 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-305, AND MASSSPECTROMETRY. |