Lysine-specific demethylase 4A

NameLysine-specific demethylase 4A
Synonyms1.14.11.- JHDM3A JmjC domain-containing histone demethylation protein 3A JMJD2 JMJD2A Jumonji domain-containing protein 2A KIAA0677
Gene NameKDM4A
OrganismHuman
Amino acid sequence
>lcl|BSEQ0008939|Lysine-specific demethylase 4A
MASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASYD
DIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERK
YWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFGM
WKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRH
KMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYG
KQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESELP
PRAGNEEECPEEDMEGVEDGEEGDLKTSLAKHRIGTKRHRVCLEIPQEVSQSELFPKEDL
SSEQYEMTECPAALAPVRPTHSSVRQVEDGLTFPDYSDSTEVKFEELKNVKLEEEDEEEE
QAAAALDLSVNPASVGGRLVFSGSKKKSSSSLGSGSSRDSISSDSETSEPLSCRAQGQTG
VLTVHSYAKGDGRVTVGEPCTRKKGSAARSFSERELAEVADEYMFSLEENKKSKGRRQPL
SKLPRHHPLVLQECVSDDETSEQLTPEEEAEETEAWAKPLSQLWQNRPPNFEAEKEFNET
MAQQAPHCAVCMIFQTYHQVEFGGFNQNCGNASDLAPQKQRTKPLIPEMCFTSTGCSTDI
NLSTPYLEEDGTSILVSCKKCSVRVHASCYGVPPAKASEDWMCSRCSANALEEDCCLCSL
RGGALQRANDDRWVHVSCAVAILEARFVNIAERSPVDVSKIPLPRFKLKCIFCKKRRKRT
AGCCVQCSHGRCPTAFHVSCAQAAGVMMQPDDWPFVVFITCFRHKIPNLERAKGALQSIT
AGQKVISKHKNGRFYQCEVVRLTTETFYEVNFDDGSFSDNLYPEDIVSQDCLQFGPPAEG
EVVQVRWTDGQVYGAKFVASHPIQMYQVEFEDGSQLVVKRDDVYTLDEELPKRVKSRLSV
ASDMRFNEIFTEKEVKQEKKRQRVINSRYREDYIEPALYRAIME
Number of residues1064
Molecular Weight120661.265
Theoretical pINone
GO Classification
Functions
    methylated histone binding
histone demethylase activity (H3-K36 specific)
ubiquitin protein ligase binding
zinc ion binding
Processes
    cardiac muscle hypertrophy in response to stress
double-strand break repair
histone demethylation
histone H3-K36 demethylation
transcription, DNA-templated
negative regulation of gene expression
negative regulation of transcription, DNA-templated
viral process
negative regulation of autophagy
chromatin organization
DNA repair
Components
    nucleolus
nucleoplasm
cytoplasm
nucleus
General FunctionZinc ion binding
Specific FunctionHistone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.
Transmembrane Regions
GenBank Protein ID
UniProtKB IDO75164
UniProtKB Entry NameKDM4A_HUMAN
Cellular LocationNucleus
Gene sequence
>lcl|BSEQ0017640|Lysine-specific demethylase 4A (KDM4A)
ATGGCTTCTGAGTCTGAAACTCTGAATCCCAGTGCTAGGATAATGACCTTTTATCCAACT
ATGGAAGAGTTCCGAAACTTCAGTAGATACATTGCCTACATTGAATCCCAAGGAGCTCAT
CGGGCAGGGCTAGCCAAGGTTGTTCCTCCAAAAGAGTGGAAGCCACGAGCATCCTATGAT
GACATTGATGATTTGGTCATTCCTGCCCCCATTCAACAGCTGGTGACGGGGCAGTCTGGC
CTCTTTACTCAGTACAACATACAGAAGAAAGCCATGACTGTTCGAGAGTTCCGCAAGATA
GCCAATAGCGATAAGTACTGTACCCCACGCTATAGTGAGTTTGAAGAGCTCGAGCGGAAA
TACTGGAAAAATCTTACATTCAATCCTCCAATCTATGGTGCAGATGTGAATGGTACCCTC
TATGAAAAGCATGTTGATGAGTGGAATATTGGCCGGCTGAGAACAATCCTGGACTTGGTG
GAAAAGGAGAGTGGGATCACCATTGAGGGTGTGAACACCCCATACCTGTACTTTGGCATG
TGGAAGACATCCTTTGCTTGGCACACTGAAGACATGGACCTCTACAGCATCAACTACCTG
CACTTTGGAGAACCAAAGTCCTGGTACTCTGTTCCACCTGAGCATGGAAAGCGGTTGGAA
CGCCTCGCCAAAGGCTTTTTCCCAGGAAGTGCTCAAAGCTGTGAGGCATTTCTCCGCCAC
AAGATGACCCTGATTTCCCCGTTAATGCTGAAGAAATATGGAATTCCCTTTGACAAGGTG
ACTCAAGAGGCTGGAGAGTTTATGATCACTTTCCCTTATGGTTACCATGCCGGCTTTAAC
CATGGTTTTAACTGTGCGGAGTCTACCAATTTTGCTACCCGTCGGTGGATTGAGTACGGC
AAGCAAGCTGTGCTGTGCTCCTGTAGAAAGGACATGGTGAAGATCTCCATGGATGTGTTT
GTGAGAAAGTTCCAGCCAGAAAGGTACAAACTTTGGAAAGCTGGGAAGGACAACACAGTT
ATTGACCATACTCTGCCCACGCCAGAAGCAGCTGAGTTTCTTAAGGAGAGTGAACTGCCT
CCAAGAGCTGGCAACGAGGAGGAGTGCCCAGAGGAGGACATGGAAGGGGTGGAGGATGGA
GAGGAAGGAGACCTGAAGACAAGCCTGGCCAAGCACCGAATAGGGACAAAGAGGCACCGA
GTTTGTCTTGAAATACCACAGGAGGTGAGTCAGAGTGAGCTCTTCCCCAAGGAGGATCTG
AGTTCTGAGCAGTATGAGATGACGGAGTGCCCGGCAGCCCTCGCCCCTGTGAGGCCCACC
CATAGCTCTGTGCGGCAAGTTGAGGATGGTCTTACCTTCCCAGATTATTCTGACTCCACT
GAAGTCAAATTTGAAGAGCTTAAAAATGTCAAACTAGAAGAGGAGGATGAGGAGGAAGAA
CAAGCAGCAGCTGCCTTGGATCTTTCTGTGAATCCTGCGTCTGTAGGGGGACGCCTTGTC
TTCTCAGGCTCCAAAAAGAAATCATCTTCTAGCCTGGGCTCTGGCTCTTCACGGGATTCT
ATCTCTTCTGATTCAGAAACTAGTGAGCCTCTCTCCTGCCGAGCCCAAGGGCAAACGGGA
GTTCTCACTGTGCACAGTTATGCCAAAGGGGATGGCAGGGTCACTGTGGGAGAGCCATGC
ACGAGGAAGAAAGGAAGCGCCGCTAGAAGTTTCAGTGAGCGGGAGCTGGCAGAGGTTGCA
GATGAATACATGTTTTCCCTAGAAGAGAATAAGAAGTCCAAGGGACGCCGTCAGCCTTTA
AGCAAGCTCCCCCGCCATCACCCACTTGTGCTGCAGGAGTGTGTCAGTGATGATGAGACA
TCTGAACAGCTGACCCCTGAGGAAGAGGCTGAGGAGACAGAGGCCTGGGCCAAGCCTCTG
AGCCAACTGTGGCAGAACCGACCTCCAAACTTTGAGGCTGAGAAGGAATTCAATGAGACC
ATGGCCCAACAGGCCCCTCACTGCGCTGTCTGTATGATCTTCCAGACTTATCATCAGGTT
GAATTTGGAGGCTTTAATCAGAACTGTGGAAATGCTTCAGATTTAGCCCCCCAGAAGCAG
AGGACCAAGCCATTGATTCCAGAAATGTGCTTCACTTCGACTGGCTGCAGCACGGACATC
AACCTTTCTACTCCTTATCTTGAGGAGGATGGCACCAGCATACTCGTTTCCTGCAAGAAG
TGCAGCGTCCGGGTCCATGCCAGTTGCTATGGGGTCCCCCCTGCAAAGGCTTCTGAAGAC
TGGATGTGTTCTCGGTGTTCAGCCAATGCCCTAGAGGAGGACTGCTGTTTATGCTCATTA
CGAGGAGGGGCCCTGCAGAGAGCAAATGATGACAGGTGGGTCCACGTTTCATGTGCTGTG
GCAATTCTGGAAGCAAGGTTTGTCAACATTGCAGAAAGAAGTCCGGTGGATGTGAGCAAA
ATCCCCCTGCCCCGCTTCAAACTGAAATGTATCTTCTGTAAGAAGCGGAGGAAAAGAACT
GCTGGCTGCTGTGTGCAGTGTTCTCACGGCCGCTGCCCAACTGCCTTCCATGTGAGCTGC
GCCCAGGCTGCCGGTGTGATGATGCAGCCTGACGACTGGCCTTTTGTGGTCTTCATTACC
TGCTTTCGGCACAAGATTCCTAATTTGGAGCGTGCCAAGGGGGCCTTGCAAAGCATCACT
GCAGGCCAGAAAGTCATTAGCAAGCATAAGAACGGGCGCTTCTACCAGTGTGAAGTGGTC
AGGCTCACCACCGAGACCTTCTATGAAGTCAACTTTGATGATGGCTCCTTCAGCGACAAT
CTTTATCCTGAGGACATAGTGAGCCAGGACTGTCTCCAGTTTGGTCCTCCTGCTGAAGGG
GAAGTGGTCCAAGTGAGATGGACAGACGGCCAAGTCTATGGAGCCAAGTTTGTGGCCTCC
CACCCTATCCAAATGTACCAGGTGGAGTTTGAGGATGGCTCACAACTTGTGGTTAAGAGA
GATGATGTATACACACTGGATGAAGAGCTTCCCAAGAGAGTCAAATCTAGACTGTCAGTA
GCCTCAGACATGCGCTTCAATGAGATTTTCACAGAGAAAGAGGTTAAGCAAGAAAAGAAA
CGGCAACGAGTTATCAACTCAAGATACCGGGAAGATTATATTGAGCCTGCACTATACCGG
GCCATCATGGAGTAG
GenBank Gene ID
GeneCard IDNone
GenAtlas ID
HGNC IDHGNC:22978
Chromosome Location1
LocusNone
References
  1. Huang Y, Fang J, Bedford MT, Zhang Y, Xu RM: Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science. 2006 May 5;312(5774):748-51. Epub 2006 Apr 6.[16601153 ]
  2. Gray SG, Iglesias AH, Lizcano F, Villanueva R, Camelo S, Jingu H, Teh BT, Koibuchi N, Chin WW, Kokkotou E, Dangond F: Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. J Biol Chem. 2005 Aug 5;280(31):28507-18. Epub 2005 May 31.[15927959 ]
  3. Zhang D, Yoon HG, Wong J: JMJD2A is a novel N-CoR-interacting protein and is involved in repression of the human transcription factor achaete scute-like homologue 2 (ASCL2/Hash2). Mol Cell Biol. 2005 Aug;25(15):6404-14.[16024779 ]
  4. Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76.[9734811 ]
  5. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21.[16710414 ]
  6. Whetstine JR, Nottke A, Lan F, Huarte M, Smolikov S, Chen Z, Spooner E, Li E, Zhang G, Colaiacovo M, Shi Y: Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. Cell. 2006 May 5;125(3):467-81. Epub 2006 Apr 6.[16603238 ]
  7. Kim J, Daniel J, Espejo A, Lake A, Krishna M, Xia L, Zhang Y, Bedford MT: Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO Rep. 2006 Apr;7(4):397-403. Epub 2006 Jan 13.[16415788 ]
  8. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31.[18669648 ]
  9. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309.[19413330 ]
  10. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570.[21406692 ]
  11. Mallette FA, Mattiroli F, Cui G, Young LC, Hendzel MJ, Mer G, Sixma TK, Richard S: RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites. EMBO J. 2012 Apr 18;31(8):1865-78. doi: 10.1038/emboj.2012.47. Epub 2012 Feb 28.[22373579 ]
  12. Verrier L, Escaffit F, Chailleux C, Trouche D, Vandromme M: A new isoform of the histone demethylase JMJD2A/KDM4A is required for skeletal muscle differentiation. PLoS Genet. 2011 Jun;7(6):e1001390. doi: 10.1371/journal.pgen.1001390. Epub 2011 Jun 2.[21694756 ]
  13. Chen Z, Zang J, Whetstine J, Hong X, Davrazou F, Kutateladze TG, Simpson M, Mao Q, Pan CH, Dai S, Hagman J, Hansen K, Shi Y, Zhang G: Structural insights into histone demethylation by JMJD2 family members. Cell. 2006 May 19;125(4):691-702. Epub 2006 May 4.[16677698 ]
  14. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7.[15489334 ]

Related FRC

FRCD ID Name Exact Mass Structure




F04252



Nickelocene


188.883




F03310



Nickel


58.693




F02409



Nickel chloride


129.593