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O75164 (KDM4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysine-specific demethylase 4A

EC=1.14.11.-
Alternative name(s):
JmjC domain-containing histone demethylation protein 3A
Jumonji domain-containing protein 2A
Gene names
Name:KDM4A
Synonyms:JHDM3A, JMJD2, JMJD2A, KIAA0677
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1064 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone 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. Ref.5 Ref.6 Ref.12

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. Ref.5 Ref.6 Ref.12

Cofactor

Binds 1 Fe2+ ion per subunit. Ref.6

Subunit structure

Interacts with histone deacetylase proteins HDAC1, HDAC2 and HDAC3. Interacts with RB and NCOR1. Interacts with HTLV-1 Tax protein. Ref.4 Ref.5

Subcellular location

Nucleus Ref.4 Ref.5.

Tissue specificity

Ubiquitous. Ref.4

Domain

The 2 Tudor domains recognize and bind methylated histone H3 'Lys-4' residue (H3K4me). Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails. Trimethylated H3 'Lys-4' (H3K4me3) is bound in a cage of 3 aromatic residues, 2 of which are from the Tudor domain 2, while the binding specificity is determined by side-chain interactions involving residues from the Tudor domain 1. The Tudor domains are also able to bind trimethylated histone H3 'Lys-9' (H3K9me3), di- and trimethylated H4 'Lys-20' (H4K20me2 and H4K20me3). Has high affinity for H4K20me2, blocking recruitment of proteins such as TP53BP1. Ref.6 Ref.7 Ref.11 Ref.14

Post-translational modification

Ubiquitinated by RNF8 and RNF168 following DNA damage, leading to its degradation. Degradation promotes accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited. Ref.11

Sequence similarities

Belongs to the JHDM3 histone demethylase family.

Contains 1 JmjC domain.

Contains 1 JmjN domain.

Contains 2 PHD-type zinc fingers.

Contains 2 Tudor domains.

Sequence caution

The sequence BAA31652.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandIron
Metal-binding
Zinc
   Molecular functionChromatin regulator
Dioxygenase
Oxidoreductase
   PTMAcetylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac muscle hypertrophy in response to stress

Inferred from electronic annotation. Source: Ensembl

histone H3-K36 demethylation

Inferred from direct assay Ref.5. Source: GOC

histone demethylation

Inferred from direct assay Ref.5. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.5. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functionhistone demethylase activity (H3-K36 specific)

Inferred from direct assay Ref.5. Source: UniProtKB

methylated histone binding

Inferred from direct assay Ref.11. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7Ref.6PubMed 17567753Ref.11. Source: IntAct

ubiquitin protein ligase binding

Inferred from physical interaction Ref.11. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75164-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O75164-2)

Also known as: deltaN-JMJD2A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-583: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 10641063Lysine-specific demethylase 4A
PRO_0000183172

Regions

Domain14 – 5643JmjN
Domain142 – 308167JmjC
Domain897 – 95458Tudor 1
Domain955 – 101157Tudor 2
Zinc finger709 – 76759PHD-type 1
Zinc finger829 – 88557PHD-type 2
Region597 – 63842Interaction with NCOR1

Sites

Metal binding1881Iron; catalytic
Metal binding1901Iron; catalytic
Metal binding2341Zinc
Metal binding2401Zinc
Metal binding2761Iron; catalytic
Metal binding3061Zinc
Metal binding3081Zinc
Binding site1321Alpha-ketoglutarate
Binding site1981Alpha-ketoglutarate
Binding site2061Alpha-ketoglutarate
Binding site9451Histone H3K4me3
Binding site9671Histone H3K4me3
Binding site9731Histone H3K4me3

Amino acid modifications

Modified residue21N-acetylalanine Ref.9

Natural variations

Alternative sequence1 – 583583Missing in isoform 2.
VSP_044239
Natural variant4821A → E. Ref.1 Ref.3
Corresponds to variant rs586339 [ dbSNP | Ensembl ].
VAR_023775
Natural variant8771V → G.
Corresponds to variant rs12759032 [ dbSNP | Ensembl ].
VAR_031217

Experimental info

Mutagenesis1331G → A: Abolishes histone demethylase activity; when associated with A-138. Ref.13
Mutagenesis1381G → A: Abolishes histone demethylase activity; when associated with A-138. Ref.13
Mutagenesis1651G → A: Abolishes histone demethylase activity; when associated with A-165. Ref.13
Mutagenesis1701G → A: Abolishes histone demethylase activity; when associated with A-165. Ref.13
Mutagenesis1881H → A: Abolishes histone demethylase activity without affecting ability to bind H4K20me2. Ref.6 Ref.11
Mutagenesis288 – 2892ST → AI: Displays histone demethylase activity for both dimethylated and H3-K9Me3.
Mutagenesis288 – 2892ST → TV, NV or GG: Abolishes histone demethylase activity.
Mutagenesis9391D → R: Impairs binding to H4K20me2, promoting partial recruitment of TP53BP1. Ref.11
Mutagenesis9451D → A: Impairs binding to H3K4me3. Ref.14
Mutagenesis9451D → R: Abolishes binding to H3K4me3. Ref.14
Mutagenesis9671W → H: Abolishes binding to H3K4me3. Ref.14
Mutagenesis9731Y → A: Abolishes binding to H3K4me3. Ref.13 Ref.14

Secondary structure

................................................................................................ 1064
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 4A811BEECFEDC6B3

FASTA1,064120,662
        10         20         30         40         50         60 
MASESETLNP SARIMTFYPT MEEFRNFSRY IAYIESQGAH RAGLAKVVPP KEWKPRASYD 

        70         80         90        100        110        120 
DIDDLVIPAP IQQLVTGQSG LFTQYNIQKK AMTVREFRKI ANSDKYCTPR YSEFEELERK 

       130        140        150        160        170        180 
YWKNLTFNPP IYGADVNGTL YEKHVDEWNI GRLRTILDLV EKESGITIEG VNTPYLYFGM 

       190        200        210        220        230        240 
WKTSFAWHTE DMDLYSINYL HFGEPKSWYS VPPEHGKRLE RLAKGFFPGS AQSCEAFLRH 

       250        260        270        280        290        300 
KMTLISPLML KKYGIPFDKV TQEAGEFMIT FPYGYHAGFN HGFNCAESTN FATRRWIEYG 

       310        320        330        340        350        360 
KQAVLCSCRK DMVKISMDVF VRKFQPERYK LWKAGKDNTV IDHTLPTPEA AEFLKESELP 

       370        380        390        400        410        420 
PRAGNEEECP EEDMEGVEDG EEGDLKTSLA KHRIGTKRHR VCLEIPQEVS QSELFPKEDL 

       430        440        450        460        470        480 
SSEQYEMTEC PAALAPVRPT HSSVRQVEDG LTFPDYSDST EVKFEELKNV KLEEEDEEEE 

       490        500        510        520        530        540 
QAAAALDLSV NPASVGGRLV FSGSKKKSSS SLGSGSSRDS ISSDSETSEP LSCRAQGQTG 

       550        560        570        580        590        600 
VLTVHSYAKG DGRVTVGEPC TRKKGSAARS FSERELAEVA DEYMFSLEEN KKSKGRRQPL 

       610        620        630        640        650        660 
SKLPRHHPLV LQECVSDDET SEQLTPEEEA EETEAWAKPL SQLWQNRPPN FEAEKEFNET 

       670        680        690        700        710        720 
MAQQAPHCAV CMIFQTYHQV EFGGFNQNCG NASDLAPQKQ RTKPLIPEMC FTSTGCSTDI 

       730        740        750        760        770        780 
NLSTPYLEED GTSILVSCKK CSVRVHASCY GVPPAKASED WMCSRCSANA LEEDCCLCSL 

       790        800        810        820        830        840 
RGGALQRAND DRWVHVSCAV AILEARFVNI AERSPVDVSK IPLPRFKLKC IFCKKRRKRT 

       850        860        870        880        890        900 
AGCCVQCSHG RCPTAFHVSC AQAAGVMMQP DDWPFVVFIT CFRHKIPNLE RAKGALQSIT 

       910        920        930        940        950        960 
AGQKVISKHK NGRFYQCEVV RLTTETFYEV NFDDGSFSDN LYPEDIVSQD CLQFGPPAEG 

       970        980        990       1000       1010       1020 
EVVQVRWTDG QVYGAKFVAS HPIQMYQVEF EDGSQLVVKR DDVYTLDEEL PKRVKSRLSV 

      1030       1040       1050       1060 
ASDMRFNEIF TEKEVKQEKK RQRVINSRYR EDYIEPALYR AIME 

« Hide

Isoform 2 (deltaN-JMJD2A) [UniParc].

Checksum: 394B208A6E5483FB
Show »

FASTA48154,697

References

« Hide 'large scale' references
[1]"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."
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-482.
Tissue: Brain.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLU-482.
Tissue: Placenta.
[4]"Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein."
Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H., Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.
J. Biol. Chem. 280:28507-28518(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH HDAC1; HDAC2; HDAC3; RB1 AND HTLV-1 TAX.
[5]"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)."
Zhang D., Yoon H.-G., Wong J.
Mol. Cell. Biol. 25:6404-6414(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NCOR1.
[6]"Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases."
Whetstine J.R., Nottke A., Lan F., Huarte M., Smolikov S., Chen Z., Spooner E., Li E., Zhang G., Colaiacovo M., Shi Y.
Cell 125:467-481(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, MUTAGENESIS OF HIS-188.
[7]"Tudor, MBT and chromo domains gauge the degree of lysine methylation."
Kim J., Daniel J., Espejo A., Lake A., Krishna M., Xia L., Zhang Y., Bedford M.T.
EMBO Rep. 7:397-403(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN.
[8]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites."
Mallette F.A., Mattiroli F., Cui G., Young L.C., Hendzel M.J., Mer G., Sixma T.K., Richard S.
EMBO J. 31:1865-1878(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, DOMAIN, MUTAGENESIS OF HIS-188 AND ASP-939.
[12]"A new isoform of the histone demethylase JMJD2A/KDM4A is required for skeletal muscle differentiation."
Verrier L., Escaffit F., Chailleux C., Trouche D., Vandromme M.
PLoS Genet. 7:E1001390-E1001390(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2), FUNCTION (ISOFORM 2).
[13]"Structural insights into histone demethylation by JMJD2 family members."
Chen Z., Zang J., Whetstine J., Hong X., Davrazou F., Kutateladze T.G., Simpson M., Mao Q., Pan C.-H., Dai S., Hagman J., Hansen K., Shi Y., Zhang G.
Cell 125:691-702(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 1-350 IN COMPLEX WITH IRON AND ALPHA-KETOGLUTARATE, ZINC-BINDING, MUTAGENESIS OF GLY-133; GLY-138; GLY-165; GLY-170; 279-SER-THR-280 AND TYR-973.
[14]"Recognition of histone H3 lysine-4 methylation by the double Tudor domain of JMJD2A."
Huang Y., Fang J., Bedford M.T., Zhang Y., Xu R.-M.
Science 312:748-751(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 895-1011 IN COMPLEX WITH TRIMETHYLATED H3 'LYS-4', DOMAIN, MUTAGENESIS OF ASP-945; TRP-967 AND TYR-973.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB014577 mRNA. Translation: BAA31652.2. Different initiation.
AL451062, AC092815 Genomic DNA. Translation: CAH71021.1.
BC002558 mRNA. Translation: AAH02558.1.
CCDSCCDS491.1. [O75164-1]
RefSeqNP_055478.2. NM_014663.2. [O75164-1]
XP_005271411.1. XM_005271354.1. [O75164-1]
XP_005271412.1. XM_005271355.1. [O75164-1]
UniGeneHs.155983.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2GF7X-ray2.20A/B/C/D895-1011[»]
2GFAX-ray2.10A/B895-1011[»]
2GP3X-ray2.35A/B2-350[»]
2GP5X-ray2.28A/B2-350[»]
2OQ6X-ray2.00A/B1-359[»]
2OQ7X-ray2.15A/B1-359[»]
2OS2X-ray2.30A/B1-359[»]
2OT7X-ray2.13A/B1-359[»]
2OX0X-ray1.95A/B1-359[»]
2P5BX-ray1.99A/B2-350[»]
2PXJX-ray2.00A/B2-348[»]
2Q8CX-ray2.05A/B1-350[»]
2Q8DX-ray2.29A/B1-350[»]
2Q8EX-ray2.05A/B1-350[»]
2QQRX-ray1.80A/B897-1011[»]
2QQSX-ray2.82A/B897-1011[»]
2VD7X-ray2.25A/B1-359[»]
2WWJX-ray2.60A/B7-353[»]
2YBKX-ray2.40A/B1-359[»]
2YBPX-ray2.02A/B1-359[»]
2YBSX-ray2.32A/B1-359[»]
3NJYX-ray2.60A/B1-359[»]
3PDQX-ray1.99A/B1-359[»]
3RVHX-ray2.25A/B1-359[»]
3U4SX-ray2.15A/B1-359[»]
4AI9X-ray2.25A/B1-359[»]
4BISX-ray2.49A/B1-359[»]
4GD4X-ray2.33A/B1-359[»]
ProteinModelPortalO75164.
SMRO75164. Positions 7-355, 821-869, 897-1011.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115035. 19 interactions.
DIPDIP-29372N.
IntActO75164. 28 interactions.
MINTMINT-2829088.
STRING9606.ENSP00000361473.

Chemistry

BindingDBO75164.
ChEMBLCHEMBL5896.

PTM databases

PhosphoSiteO75164.

Proteomic databases

MaxQBO75164.
PaxDbO75164.
PRIDEO75164.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372396; ENSP00000361473; ENSG00000066135. [O75164-1]
GeneID9682.
KEGGhsa:9682.
UCSCuc001cjx.3. human. [O75164-1]

Organism-specific databases

CTD9682.
GeneCardsGC01P044115.
H-InvDBHIX0020610.
HGNCHGNC:22978. KDM4A.
HPAHPA007610.
MIM609764. gene.
neXtProtNX_O75164.
PharmGKBPA164721403.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5141.
HOGENOMHOG000231125.
InParanoidO75164.
KOK06709.
OMARKRTAGC.
OrthoDBEOG7TQV03.
PhylomeDBO75164.
TreeFamTF106449.

Gene expression databases

ArrayExpressO75164.
BgeeO75164.
CleanExHS_JMJD2A.
GenevestigatorO75164.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR003347. JmjC_dom.
IPR003349. TF_JmjN.
IPR002999. Tudor.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
[Graphical view]
SMARTSM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 2 hits.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKdm4A. human.
EvolutionaryTraceO75164.
GeneWikiJMJD2A.
GenomeRNAi9682.
NextBio36361.
PROO75164.
SOURCESearch...

Entry information

Entry nameKDM4A_HUMAN
AccessionPrimary (citable) accession number: O75164
Secondary accession number(s): Q5VVB1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM