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Protein

Lysine-specific demethylase 4A

Gene

KDM4A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.
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.

Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei132Alpha-ketoglutarate1 Publication1
Metal bindingi188Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi190Iron; catalyticPROSITE-ProRule annotation1 Publication1
Binding sitei198Alpha-ketoglutarate1 Publication1
Binding sitei206Alpha-ketoglutarate1 Publication1
Metal bindingi234Zinc1
Metal bindingi240Zinc1
Metal bindingi276Iron; catalyticPROSITE-ProRule annotation1 Publication1
Metal bindingi306Zinc1
Metal bindingi308Zinc1
Binding sitei945Histone H3K4me31
Binding sitei967Histone H3K4me31
Binding sitei973Histone H3K4me31

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri709 – 767PHD-type 1Add BLAST59
Zinc fingeri772 – 805C2HC pre-PHD-typePROSITE-ProRule annotationAdd BLAST34
Zinc fingeri828 – 885PHD-type 2PROSITE-ProRule annotationAdd BLAST58

GO - Molecular functioni

  • double-stranded DNA binding Source: Ensembl
  • histone demethylase activity Source: Reactome
  • histone demethylase activity (H3-K36 specific) Source: UniProtKB
  • methylated histone binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000066135-MONOMER.
BRENDAi1.14.11.27. 2681.
1.14.11.B1. 2681.
1.14.11.B2. 2681.
ReactomeiR-HSA-3214842. HDMs demethylate histones.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:KDM4A
Synonyms:JHDM3A, JMJD2, JMJD2A, KIAA0677
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:22978. KDM4A.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • pericentric heterochromatin Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi133G → A: Abolishes histone demethylase activity; when associated with A-138. 1 Publication1
Mutagenesisi138G → A: Abolishes histone demethylase activity; when associated with A-138. 1 Publication1
Mutagenesisi165G → A: Abolishes histone demethylase activity; when associated with A-165. 1 Publication1
Mutagenesisi170G → A: Abolishes histone demethylase activity; when associated with A-165. 1 Publication1
Mutagenesisi188H → A: Abolishes histone demethylase activity without affecting ability to bind H4K20me2. 2 Publications1
Mutagenesisi288 – 289ST → AI: Displays histone demethylase activity for both dimethylated and H3-K9Me3. 2
Mutagenesisi288 – 289ST → TV, NV or GG: Abolishes histone demethylase activity. 2
Mutagenesisi939D → R: Impairs binding to H4K20me2, promoting partial recruitment of TP53BP1. 1 Publication1
Mutagenesisi945D → A: Impairs binding to H3K4me3. 1 Publication1
Mutagenesisi945D → R: Abolishes binding to H3K4me3. 1 Publication1
Mutagenesisi967W → H: Abolishes binding to H3K4me3. 1 Publication1
Mutagenesisi973Y → A: Abolishes binding to H3K4me3. 2 Publications1

Organism-specific databases

DisGeNETi9682.
OpenTargetsiENSG00000066135.
PharmGKBiPA164721403.

Chemistry databases

ChEMBLiCHEMBL5896.
GuidetoPHARMACOLOGYi2675.

Polymorphism and mutation databases

BioMutaiKDM4A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001831722 – 1064Lysine-specific demethylase 4AAdd BLAST1063

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei523PhosphoserineCombined sources1

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO75164.
MaxQBiO75164.
PaxDbiO75164.
PeptideAtlasiO75164.
PRIDEiO75164.

PTM databases

iPTMnetiO75164.
PhosphoSitePlusiO75164.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000066135.
CleanExiHS_JMJD2A.
GenevisibleiO75164. HS.

Organism-specific databases

HPAiHPA007610.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST1H3DP684317EBI-936709,EBI-79722
HIST2H4BP628057EBI-936709,EBI-302023
HIST3H3Q166956EBI-936709,EBI-358900

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi115035. 26 interactors.
DIPiDIP-29372N.
IntActiO75164. 28 interactors.
MINTiMINT-2829088.
STRINGi9606.ENSP00000361473.

Chemistry databases

BindingDBiO75164.

Structurei

Secondary structure

11064
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni4 – 6Combined sources3
Beta strandi7 – 9Combined sources3
Helixi10 – 12Combined sources3
Beta strandi15 – 17Combined sources3
Helixi21 – 24Combined sources4
Helixi27 – 36Combined sources10
Helixi39 – 42Combined sources4
Beta strandi43 – 47Combined sources5
Beta strandi55 – 57Combined sources3
Beta strandi59 – 61Combined sources3
Helixi62 – 64Combined sources3
Beta strandi66 – 69Combined sources4
Beta strandi71 – 78Combined sources8
Beta strandi81 – 88Combined sources8
Helixi94 – 101Combined sources8
Turni104 – 106Combined sources3
Helixi114 – 124Combined sources11
Beta strandi131 – 137Combined sources7
Helixi150 – 152Combined sources3
Helixi156 – 158Combined sources3
Helixi159 – 162Combined sources4
Beta strandi163 – 165Combined sources3
Turni169 – 171Combined sources3
Beta strandi175 – 179Combined sources5
Beta strandi184 – 188Combined sources5
Helixi191 – 193Combined sources3
Beta strandi195 – 204Combined sources10
Beta strandi206 – 211Combined sources6
Helixi213 – 215Combined sources3
Helixi216 – 226Combined sources11
Helixi228 – 233Combined sources6
Helixi237 – 240Combined sources4
Beta strandi243 – 245Combined sources3
Helixi247 – 252Combined sources6
Beta strandi258 – 262Combined sources5
Beta strandi267 – 270Combined sources4
Beta strandi275 – 280Combined sources6
Beta strandi282 – 291Combined sources10
Helixi296 – 302Combined sources7
Beta strandi308 – 311Combined sources4
Helixi318 – 324Combined sources7
Helixi326 – 333Combined sources8
Beta strandi343 – 345Combined sources3
Helixi348 – 353Combined sources6
Beta strandi904 – 908Combined sources5
Beta strandi912 – 932Combined sources21
Beta strandi937 – 941Combined sources5
Helixi943 – 945Combined sources3
Helixi951 – 954Combined sources4
Beta strandi962 – 966Combined sources5
Beta strandi972 – 990Combined sources19
Beta strandi995 – 998Combined sources4
Helixi1000 – 1002Combined sources3
Beta strandi1003 – 1005Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4URAX-ray2.23A/B1-359[»]
4V2VX-ray2.00A/B1-359[»]
4V2WX-ray1.81A/B1-359[»]
5A7NX-ray2.39A/B1-359[»]
5A7OX-ray2.15A/B1-359[»]
5A7PX-ray2.28A/B1-359[»]
5A7QX-ray2.00A/B1-359[»]
5A7SX-ray2.20A/B1-359[»]
5A7WX-ray2.27A/B1-359[»]
5A80X-ray2.28A/B1-359[»]
5ANQX-ray2.00A/B1-359[»]
5D6WX-ray1.99A/B/C/D895-1011[»]
5D6XX-ray2.15A/B895-1011[»]
5D6YX-ray2.29A/B/C/D/E/F895-1011[»]
5F2SX-ray2.08A/B/C/D1-359[»]
5F2WX-ray2.60A/B/C/D1-359[»]
5F32X-ray2.05A/B/C/D1-359[»]
5F37X-ray2.22A/B/C/D1-359[»]
5F39X-ray2.65A/B/C/D1-359[»]
5F3CX-ray2.06A/B/C/D1-359[»]
5F3EX-ray2.16A/B/C/D1-359[»]
5F3GX-ray2.50A/B/C/D1-359[»]
5F3IX-ray2.24A/B/C/D1-359[»]
5F5IX-ray2.63A/B1-359[»]
5FPVX-ray2.44A/B/C/D/E/F/G/H1-359[»]
5FWEX-ray2.05A/B1-359[»]
5FY8X-ray2.34A/B1-359[»]
5FYCX-ray2.26A/B1-359[»]
5FYHX-ray2.35A/B1-359[»]
5FYIX-ray2.10A/B1-359[»]
ProteinModelPortaliO75164.
SMRiO75164.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75164.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini14 – 56JmjNPROSITE-ProRule annotationAdd BLAST43
Domaini142 – 308JmjCPROSITE-ProRule annotationAdd BLAST167
Domaini897 – 954Tudor 1Add BLAST58
Domaini955 – 1011Tudor 2Add BLAST57

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni597 – 638Interaction with NCOR11 PublicationAdd BLAST42

Domaini

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 TP53BP1.4 Publications

Sequence similaritiesi

Belongs to the JHDM3 histone demethylase family.Curated
Contains 1 C2HC pre-PHD-type zinc finger.PROSITE-ProRule annotation
Contains 1 JmjC domain.PROSITE-ProRule annotation
Contains 1 JmjN domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation
Contains 2 Tudor domains.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri709 – 767PHD-type 1Add BLAST59
Zinc fingeri772 – 805C2HC pre-PHD-typePROSITE-ProRule annotationAdd BLAST34
Zinc fingeri828 – 885PHD-type 2PROSITE-ProRule annotationAdd BLAST58

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IT40. Eukaryota.
COG5141. LUCA.
GeneTreeiENSGT00530000063342.
HOGENOMiHOG000231125.
InParanoidiO75164.
KOiK06709.
OMAiCRAQGQT.
OrthoDBiEOG091G01FR.
PhylomeDBiO75164.
TreeFamiTF106449.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003347. JmjC_dom.
IPR003349. JmjN.
IPR002999. Tudor.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 2 hits.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51805. EPHD. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75164-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MASESETLNP SARIMTFYPT MEEFRNFSRY IAYIESQGAH RAGLAKVVPP
60 70 80 90 100
KEWKPRASYD DIDDLVIPAP IQQLVTGQSG LFTQYNIQKK AMTVREFRKI
110 120 130 140 150
ANSDKYCTPR YSEFEELERK YWKNLTFNPP IYGADVNGTL YEKHVDEWNI
160 170 180 190 200
GRLRTILDLV EKESGITIEG VNTPYLYFGM WKTSFAWHTE DMDLYSINYL
210 220 230 240 250
HFGEPKSWYS VPPEHGKRLE RLAKGFFPGS AQSCEAFLRH KMTLISPLML
260 270 280 290 300
KKYGIPFDKV TQEAGEFMIT FPYGYHAGFN HGFNCAESTN FATRRWIEYG
310 320 330 340 350
KQAVLCSCRK DMVKISMDVF VRKFQPERYK LWKAGKDNTV IDHTLPTPEA
360 370 380 390 400
AEFLKESELP PRAGNEEECP EEDMEGVEDG EEGDLKTSLA KHRIGTKRHR
410 420 430 440 450
VCLEIPQEVS QSELFPKEDL SSEQYEMTEC PAALAPVRPT HSSVRQVEDG
460 470 480 490 500
LTFPDYSDST EVKFEELKNV KLEEEDEEEE QAAAALDLSV NPASVGGRLV
510 520 530 540 550
FSGSKKKSSS SLGSGSSRDS ISSDSETSEP LSCRAQGQTG VLTVHSYAKG
560 570 580 590 600
DGRVTVGEPC TRKKGSAARS FSERELAEVA DEYMFSLEEN KKSKGRRQPL
610 620 630 640 650
SKLPRHHPLV LQECVSDDET SEQLTPEEEA EETEAWAKPL SQLWQNRPPN
660 670 680 690 700
FEAEKEFNET MAQQAPHCAV CMIFQTYHQV EFGGFNQNCG NASDLAPQKQ
710 720 730 740 750
RTKPLIPEMC FTSTGCSTDI NLSTPYLEED GTSILVSCKK CSVRVHASCY
760 770 780 790 800
GVPPAKASED WMCSRCSANA LEEDCCLCSL RGGALQRAND DRWVHVSCAV
810 820 830 840 850
AILEARFVNI AERSPVDVSK IPLPRFKLKC IFCKKRRKRT AGCCVQCSHG
860 870 880 890 900
RCPTAFHVSC AQAAGVMMQP DDWPFVVFIT CFRHKIPNLE RAKGALQSIT
910 920 930 940 950
AGQKVISKHK NGRFYQCEVV RLTTETFYEV NFDDGSFSDN LYPEDIVSQD
960 970 980 990 1000
CLQFGPPAEG EVVQVRWTDG QVYGAKFVAS HPIQMYQVEF EDGSQLVVKR
1010 1020 1030 1040 1050
DDVYTLDEEL PKRVKSRLSV ASDMRFNEIF TEKEVKQEKK RQRVINSRYR
1060
EDYIEPALYR AIME
Length:1,064
Mass (Da):120,662
Last modified:October 5, 2010 - v2
Checksum:i4A811BEECFEDC6B3
GO
Isoform 2 (identifier: O75164-2) [UniParc]FASTAAdd to basket
Also known as: deltaN-JMJD2A

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

Show »
Length:481
Mass (Da):54,697
Checksum:i394B208A6E5483FB
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023775482A → E.2 PublicationsCorresponds to variant rs586339dbSNPEnsembl.1
Natural variantiVAR_031217877V → G.Corresponds to variant rs12759032dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0442391 – 583Missing in isoform 2. CuratedAdd BLAST583

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014577 mRNA. Translation: BAA31652.2. Different initiation.
AL451062, AC092815 Genomic DNA. Translation: CAH71021.1.
BC002558 mRNA. Translation: AAH02558.1.
CCDSiCCDS491.1. [O75164-1]
RefSeqiNP_055478.2. NM_014663.2. [O75164-1]
XP_005271411.1. XM_005271354.3. [O75164-1]
XP_005271412.1. XM_005271355.3. [O75164-1]
UniGeneiHs.155983.

Genome annotation databases

EnsembliENST00000372396; ENSP00000361473; ENSG00000066135. [O75164-1]
GeneIDi9682.
KEGGihsa:9682.
UCSCiuc001cjx.4. human. [O75164-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014577 mRNA. Translation: BAA31652.2. Different initiation.
AL451062, AC092815 Genomic DNA. Translation: CAH71021.1.
BC002558 mRNA. Translation: AAH02558.1.
CCDSiCCDS491.1. [O75164-1]
RefSeqiNP_055478.2. NM_014663.2. [O75164-1]
XP_005271411.1. XM_005271354.3. [O75164-1]
XP_005271412.1. XM_005271355.3. [O75164-1]
UniGeneiHs.155983.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4URAX-ray2.23A/B1-359[»]
4V2VX-ray2.00A/B1-359[»]
4V2WX-ray1.81A/B1-359[»]
5A7NX-ray2.39A/B1-359[»]
5A7OX-ray2.15A/B1-359[»]
5A7PX-ray2.28A/B1-359[»]
5A7QX-ray2.00A/B1-359[»]
5A7SX-ray2.20A/B1-359[»]
5A7WX-ray2.27A/B1-359[»]
5A80X-ray2.28A/B1-359[»]
5ANQX-ray2.00A/B1-359[»]
5D6WX-ray1.99A/B/C/D895-1011[»]
5D6XX-ray2.15A/B895-1011[»]
5D6YX-ray2.29A/B/C/D/E/F895-1011[»]
5F2SX-ray2.08A/B/C/D1-359[»]
5F2WX-ray2.60A/B/C/D1-359[»]
5F32X-ray2.05A/B/C/D1-359[»]
5F37X-ray2.22A/B/C/D1-359[»]
5F39X-ray2.65A/B/C/D1-359[»]
5F3CX-ray2.06A/B/C/D1-359[»]
5F3EX-ray2.16A/B/C/D1-359[»]
5F3GX-ray2.50A/B/C/D1-359[»]
5F3IX-ray2.24A/B/C/D1-359[»]
5F5IX-ray2.63A/B1-359[»]
5FPVX-ray2.44A/B/C/D/E/F/G/H1-359[»]
5FWEX-ray2.05A/B1-359[»]
5FY8X-ray2.34A/B1-359[»]
5FYCX-ray2.26A/B1-359[»]
5FYHX-ray2.35A/B1-359[»]
5FYIX-ray2.10A/B1-359[»]
ProteinModelPortaliO75164.
SMRiO75164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115035. 26 interactors.
DIPiDIP-29372N.
IntActiO75164. 28 interactors.
MINTiMINT-2829088.
STRINGi9606.ENSP00000361473.

Chemistry databases

BindingDBiO75164.
ChEMBLiCHEMBL5896.
GuidetoPHARMACOLOGYi2675.

PTM databases

iPTMnetiO75164.
PhosphoSitePlusiO75164.

Polymorphism and mutation databases

BioMutaiKDM4A.

Proteomic databases

EPDiO75164.
MaxQBiO75164.
PaxDbiO75164.
PeptideAtlasiO75164.
PRIDEiO75164.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372396; ENSP00000361473; ENSG00000066135. [O75164-1]
GeneIDi9682.
KEGGihsa:9682.
UCSCiuc001cjx.4. human. [O75164-1]

Organism-specific databases

CTDi9682.
DisGeNETi9682.
GeneCardsiKDM4A.
H-InvDBHIX0020610.
HGNCiHGNC:22978. KDM4A.
HPAiHPA007610.
MIMi609764. gene.
neXtProtiNX_O75164.
OpenTargetsiENSG00000066135.
PharmGKBiPA164721403.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IT40. Eukaryota.
COG5141. LUCA.
GeneTreeiENSGT00530000063342.
HOGENOMiHOG000231125.
InParanoidiO75164.
KOiK06709.
OMAiCRAQGQT.
OrthoDBiEOG091G01FR.
PhylomeDBiO75164.
TreeFamiTF106449.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000066135-MONOMER.
BRENDAi1.14.11.27. 2681.
1.14.11.B1. 2681.
1.14.11.B2. 2681.
ReactomeiR-HSA-3214842. HDMs demethylate histones.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.

Miscellaneous databases

ChiTaRSiKDM4A. human.
EvolutionaryTraceiO75164.
GeneWikiiJMJD2A.
GenomeRNAii9682.
PROiO75164.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000066135.
CleanExiHS_JMJD2A.
GenevisibleiO75164. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003347. JmjC_dom.
IPR003349. JmjN.
IPR002999. Tudor.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 2 hits.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51805. EPHD. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKDM4A_HUMAN
AccessioniPrimary (citable) accession number: O75164
Secondary accession number(s): Q5VVB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 22, 2003
Last sequence update: October 5, 2010
Last modified: November 2, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.