UniProtKB - O75164 (KDM4A_HUMAN)
Lysine-specific demethylase 4A
KDM4A
Functioni
Histone demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code (PubMed:26741168).
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.
3 PublicationsCrucial 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.
1 PublicationCatalytic activityi
- 2 2-oxoglutarate + N6,N6,N6-trimethyl-L-lysyl9-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N6-methyl-L-lysyl9-[histone H3] + 2 succinate1 PublicationEC:1.14.11.661 Publication
- 2 2-oxoglutarate + N6,N6,N6-trimethyl-L-lysyl36-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N6-methyl-L-lysyl36-[histone H3] + 2 succinate1 PublicationEC:1.14.11.691 Publication
Cofactori
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 132 | 2-oxoglutarate1 Publication | 1 | |
Metal bindingi | 188 | Iron; catalyticPROSITE-ProRule annotation1 Publication1 Publication | 1 | |
Metal bindingi | 190 | Iron; catalytic1 Publication1 Publication | 1 | |
Binding sitei | 198 | 2-oxoglutarate1 Publication | 1 | |
Binding sitei | 206 | 2-oxoglutarate1 Publication | 1 | |
Metal bindingi | 234 | ZincCombined sources | 1 | |
Metal bindingi | 240 | Zinc; via tele nitrogenCombined sources | 1 | |
Binding sitei | 241 | 2-oxoglutarateBy similarity | 1 | |
Metal bindingi | 276 | Iron; catalyticPROSITE-ProRule annotation1 Publication1 Publication | 1 | |
Metal bindingi | 306 | ZincCombined sources | 1 | |
Metal bindingi | 308 | ZincCombined sources | 1 | |
Sitei | 945 | Histone H3K4me3 binding | 1 | |
Sitei | 967 | Histone H3K4me3 binding | 1 | |
Sitei | 973 | Histone H3K4me3 binding | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 709 – 767 | PHD-type 1Add BLAST | 59 | |
Zinc fingeri | 772 – 805 | C2HC pre-PHD-typePROSITE-ProRule annotationAdd BLAST | 34 | |
Zinc fingeri | 828 – 885 | PHD-type 2PROSITE-ProRule annotationAdd BLAST | 58 |
GO - Molecular functioni
- histone demethylase activity Source: GO_Central
- histone H3-methyl-lysine-36 demethylase activity Source: UniProtKB
- histone H3-methyl-lysine-9 demethylase activity Source: UniProtKB
- histone H3-tri/dimethyl-lysine-36 demethylase activity Source: UniProtKB-EC
- histone H3-tri/dimethyl-lysine-9 demethylase activity Source: UniProtKB-EC
- methylated histone binding Source: UniProtKB
- ubiquitin protein ligase binding Source: UniProtKB
- zinc ion binding Source: UniProtKB
GO - Biological processi
- cardiac muscle hypertrophy in response to stress Source: Ensembl
- chromatin remodeling Source: GO_Central
- histone demethylation Source: UniProtKB
- histone H3-K36 demethylation Source: UniProtKB
- histone H3-K9 demethylation Source: UniProtKB
- negative regulation of astrocyte differentiation Source: Ensembl
- negative regulation of autophagy Source: ParkinsonsUK-UCL
- negative regulation of cell death Source: Ensembl
- negative regulation of gene expression Source: ParkinsonsUK-UCL
- negative regulation of histone H3-K9 trimethylation Source: Ensembl
- negative regulation of transcription, DNA-templated Source: UniProtKB
- positive regulation of gene expression Source: Ensembl
- positive regulation of neuron differentiation Source: Ensembl
- response to nutrient levels Source: Ensembl
Keywordsi
Molecular function | Chromatin regulator, Dioxygenase, Oxidoreductase |
Biological process | Host-virus interaction, Transcription, Transcription regulation |
Ligand | Iron, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 1.14.11.27, 2681 1.14.11.66, 2681 1.14.11.67, 2681 1.14.11.69, 2681 1.14.99.66, 2681 |
PathwayCommonsi | O75164 |
Reactomei | R-HSA-3214842, HDMs demethylate histones R-HSA-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks R-HSA-9029569, NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux |
SignaLinki | O75164 |
Names & Taxonomyi
Protein namesi | Recommended name: Lysine-specific demethylase 4A (EC:1.14.11.661 Publication, EC:1.14.11.691 Publication)Alternative name(s): JmjC domain-containing histone demethylation protein 3A Jumonji domain-containing protein 2A [histone H3]-trimethyl-L-lysine(36) demethylase 4ACurated [histone H3]-trimethyl-L-lysine(9) demethylase 4ACurated |
Gene namesi | Name:KDM4A Synonyms:JHDM3A, JMJD2, JMJD2A, KIAA0677 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:22978, KDM4A |
MIMi | 609764, gene |
neXtProti | NX_O75164 |
VEuPathDBi | HostDB:ENSG00000066135 |
Subcellular locationi
Nucleus
- Nucleus PROSITE-ProRule annotation2 Publications
Cytosol
- cytosol Source: HPA
Nucleus
- fibrillar center Source: HPA
- nucleoplasm Source: HPA
- nucleus Source: UniProtKB
Other locations
- pericentric heterochromatin Source: Ensembl
Keywords - Cellular componenti
NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 133 | G → A: Abolishes histone demethylase activity; when associated with A-138. 1 Publication | 1 | |
Mutagenesisi | 138 | G → A: Abolishes histone demethylase activity; when associated with A-138. 1 Publication | 1 | |
Mutagenesisi | 165 | G → A: Abolishes histone demethylase activity; when associated with A-165. 1 Publication | 1 | |
Mutagenesisi | 170 | G → A: Abolishes histone demethylase activity; when associated with A-165. 1 Publication | 1 | |
Mutagenesisi | 188 | H → A: Abolishes histone demethylase activity without affecting ability to bind H4K20me2. 2 Publications | 1 | |
Mutagenesisi | 288 – 289 | ST → AI: Displays histone demethylase activity for both dimethylated and H3-K9Me3. | 2 | |
Mutagenesisi | 288 – 289 | ST → TV, NV or GG: Abolishes histone demethylase activity. | 2 | |
Mutagenesisi | 939 | D → R: Impairs binding to H4K20me2, promoting partial recruitment of TP53BP1. 1 Publication | 1 | |
Mutagenesisi | 945 | D → A: Impairs binding to H3K4me3. 1 Publication | 1 | |
Mutagenesisi | 945 | D → R: Abolishes binding to H3K4me3. 1 Publication | 1 | |
Mutagenesisi | 967 | W → H: Abolishes binding to H3K4me3. 1 Publication | 1 | |
Mutagenesisi | 973 | Y → A: Abolishes binding to H3K4me3. 2 Publications | 1 |
Organism-specific databases
DisGeNETi | 9682 |
OpenTargetsi | ENSG00000066135 |
PharmGKBi | PA164721403 |
Miscellaneous databases
Pharosi | O75164, Tchem |
Chemistry databases
ChEMBLi | CHEMBL5896 |
GuidetoPHARMACOLOGYi | 2675 |
Genetic variation databases
BioMutai | KDM4A |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000183172 | 2 – 1064 | Lysine-specific demethylase 4AAdd BLAST | 1063 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineCombined sources | 1 | |
Modified residuei | 523 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | O75164 |
jPOSTi | O75164 |
MassIVEi | O75164 |
MaxQBi | O75164 |
PaxDbi | O75164 |
PeptideAtlasi | O75164 |
PRIDEi | O75164 |
ProteomicsDBi | 49829 [O75164-1] |
PTM databases
iPTMneti | O75164 |
PhosphoSitePlusi | O75164 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000066135, Expressed in cortical plate and 230 other tissues |
ExpressionAtlasi | O75164, baseline and differential |
Genevisiblei | O75164, HS |
Organism-specific databases
HPAi | ENSG00000066135, Low tissue specificity |
Interactioni
Subunit structurei
Interacts with histone deacetylase proteins HDAC1, HDAC2 and HDAC3.
Interacts with RB and NCOR1.
4 Publications(Microbial infection) Interacts with HTLV-1 Tax protein.
1 PublicationBinary interactionsi
O75164
With | #Exp. | IntAct |
---|---|---|
ERG [P11308] | 2 | EBI-936709,EBI-79704 |
H3-4 [Q16695] | 6 | EBI-936709,EBI-358900 |
H3C12 [P68431] | 7 | EBI-936709,EBI-79722 |
H4C9 [P62805] | 7 | EBI-936709,EBI-302023 |
GO - Molecular functioni
- methylated histone binding Source: UniProtKB
- ubiquitin protein ligase binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 115035, 55 interactors |
CORUMi | O75164 |
DIPi | DIP-29372N |
IntActi | O75164, 54 interactors |
MINTi | O75164 |
STRINGi | 9606.ENSP00000361473 |
Chemistry databases
BindingDBi | O75164 |
Miscellaneous databases
RNActi | O75164, protein |
Structurei
Secondary structure
3D structure databases
PCDDBi | O75164 |
SMRi | O75164 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O75164 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 14 – 56 | JmjNPROSITE-ProRule annotationAdd BLAST | 43 | |
Domaini | 142 – 308 | JmjCPROSITE-ProRule annotationAdd BLAST | 167 | |
Domaini | 897 – 954 | Tudor 1Add BLAST | 58 | |
Domaini | 955 – 1011 | Tudor 2Add BLAST | 57 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 358 – 384 | DisorderedSequence analysisAdd BLAST | 27 | |
Regioni | 501 – 537 | DisorderedSequence analysisAdd BLAST | 37 | |
Regioni | 597 – 638 | Interaction with NCOR11 PublicationAdd BLAST | 42 | |
Regioni | 616 – 641 | DisorderedSequence analysisAdd BLAST | 26 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 503 – 537 | Polar residuesSequence analysisAdd BLAST | 35 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 709 – 767 | PHD-type 1Add BLAST | 59 | |
Zinc fingeri | 772 – 805 | C2HC pre-PHD-typePROSITE-ProRule annotationAdd BLAST | 34 | |
Zinc fingeri | 828 – 885 | PHD-type 2PROSITE-ProRule annotationAdd BLAST | 58 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG0958, Eukaryota |
GeneTreei | ENSGT00940000159643 |
HOGENOMi | CLU_001442_0_1_1 |
InParanoidi | O75164 |
OMAi | AQQPPYC |
OrthoDBi | 1186832at2759 |
PhylomeDBi | O75164 |
TreeFami | TF106449 |
Family and domain databases
CDDi | cd04508, TUDOR, 2 hits |
Gene3Di | 3.30.40.10, 2 hits |
IDEALi | IID00360 |
InterProi | View protein in InterPro IPR034732, EPHD IPR003347, JmjC_dom IPR003349, JmjN IPR040477, KDM4_Tudor_2 IPR002999, Tudor IPR011011, Znf_FYVE_PHD IPR001965, Znf_PHD IPR013083, Znf_RING/FYVE/PHD |
Pfami | View protein in Pfam PF02373, JmjC, 1 hit PF02375, JmjN, 1 hit PF18104, Tudor_2, 2 hits |
SMARTi | View protein in SMART SM00558, JmjC, 1 hit SM00545, JmjN, 1 hit SM00249, PHD, 2 hits SM00333, TUDOR, 2 hits |
SUPFAMi | SSF57903, SSF57903, 1 hit |
PROSITEi | View protein in PROSITE PS51805, EPHD, 1 hit PS51184, JMJC, 1 hit PS51183, JMJN, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A2R8YDF7 | A0A2R8YDF7_HUMAN | Lysine-specific demethylase 4A | KDM4A | 281 | Annotation score: | ||
A0A2R8Y7L1 | A0A2R8Y7L1_HUMAN | Lysine-specific demethylase 4A | KDM4A | 8 | Annotation score: |
Sequence cautioni
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_023775 | 482 | A → E2 PublicationsCorresponds to variant dbSNP:rs586339Ensembl. | 1 | |
Natural variantiVAR_031217 | 877 | V → G. Corresponds to variant dbSNP:rs12759032Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_044239 | 1 – 583 | Missing in isoform 2. CuratedAdd BLAST | 583 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB014577 mRNA Translation: BAA31652.2 Different initiation. AC092815 Genomic DNA No translation available. AL451062 Genomic DNA No translation available. BC002558 mRNA Translation: AAH02558.1 |
CCDSi | CCDS491.1 [O75164-1] |
RefSeqi | NP_055478.2, NM_014663.2 [O75164-1] XP_005271411.1, XM_005271354.3 [O75164-1] XP_005271412.1, XM_005271355.3 [O75164-1] |
Genome annotation databases
Ensembli | ENST00000372396; ENSP00000361473; ENSG00000066135 |
GeneIDi | 9682 |
KEGGi | hsa:9682 |
MANE-Selecti | ENST00000372396.4; ENSP00000361473.3; NM_014663.3; NP_055478.2 |
UCSCi | uc001cjx.4, human [O75164-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AB014577 mRNA Translation: BAA31652.2 Different initiation. AC092815 Genomic DNA No translation available. AL451062 Genomic DNA No translation available. BC002558 mRNA Translation: AAH02558.1 |
CCDSi | CCDS491.1 [O75164-1] |
RefSeqi | NP_055478.2, NM_014663.2 [O75164-1] XP_005271411.1, XM_005271354.3 [O75164-1] XP_005271412.1, XM_005271355.3 [O75164-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2GF7 | X-ray | 2.20 | A/B/C/D | 895-1011 | [»] | |
2GFA | X-ray | 2.10 | A/B | 895-1011 | [»] | |
2GP3 | X-ray | 2.35 | A/B | 2-350 | [»] | |
2GP5 | X-ray | 2.28 | A/B | 2-350 | [»] | |
2OQ6 | X-ray | 2.00 | A/B | 1-359 | [»] | |
2OQ7 | X-ray | 2.15 | A/B | 1-359 | [»] | |
2OS2 | X-ray | 2.30 | A/B | 1-359 | [»] | |
2OT7 | X-ray | 2.13 | A/B | 1-359 | [»] | |
2OX0 | X-ray | 1.95 | A/B | 1-359 | [»] | |
2P5B | X-ray | 1.99 | A/B | 2-350 | [»] | |
2PXJ | X-ray | 2.00 | A/B | 2-348 | [»] | |
2Q8C | X-ray | 2.05 | A/B | 1-350 | [»] | |
2Q8D | X-ray | 2.29 | A/B | 1-350 | [»] | |
2Q8E | X-ray | 2.05 | A/B | 1-350 | [»] | |
2QQR | X-ray | 1.80 | A/B | 897-1011 | [»] | |
2QQS | X-ray | 2.82 | A/B | 897-1011 | [»] | |
2VD7 | X-ray | 2.25 | A/B | 1-359 | [»] | |
2WWJ | X-ray | 2.60 | A/B | 7-353 | [»] | |
2YBK | X-ray | 2.40 | A/B | 1-359 | [»] | |
2YBP | X-ray | 2.02 | A/B | 1-359 | [»] | |
2YBS | X-ray | 2.32 | A/B | 1-359 | [»] | |
3NJY | X-ray | 2.60 | A/B | 1-359 | [»] | |
3PDQ | X-ray | 1.99 | A/B | 1-359 | [»] | |
3RVH | X-ray | 2.25 | A/B | 1-359 | [»] | |
3U4S | X-ray | 2.15 | A/B | 1-359 | [»] | |
4AI9 | X-ray | 2.25 | A/B | 1-359 | [»] | |
4BIS | X-ray | 2.49 | A/B | 1-359 | [»] | |
4GD4 | X-ray | 2.33 | A/B | 1-359 | [»] | |
4URA | X-ray | 2.23 | A/B | 1-359 | [»] | |
4V2V | X-ray | 2.00 | A/B | 1-359 | [»] | |
4V2W | X-ray | 1.81 | A/B | 1-359 | [»] | |
5A7N | X-ray | 2.39 | A/B | 1-359 | [»] | |
5A7O | X-ray | 2.15 | A/B | 1-359 | [»] | |
5A7P | X-ray | 2.28 | A/B | 1-359 | [»] | |
5A7Q | X-ray | 2.00 | A/B | 1-359 | [»] | |
5A7S | X-ray | 2.20 | A/B | 1-359 | [»] | |
5A7W | X-ray | 2.27 | A/B | 1-359 | [»] | |
5A80 | X-ray | 2.28 | A/B | 1-359 | [»] | |
5ANQ | X-ray | 2.00 | A/B | 1-359 | [»] | |
5D6W | X-ray | 1.99 | A/B/C/D | 895-1011 | [»] | |
5D6X | X-ray | 2.15 | A/B | 895-1011 | [»] | |
5D6Y | X-ray | 2.29 | A/B/C/D/E/F | 895-1011 | [»] | |
5F2S | X-ray | 2.08 | A/B/C/D | 1-359 | [»] | |
5F2W | X-ray | 2.60 | A/B/C/D | 1-359 | [»] | |
5F32 | X-ray | 2.05 | A/B/C/D | 1-359 | [»] | |
5F37 | X-ray | 2.22 | A/B/C/D | 1-359 | [»] | |
5F39 | X-ray | 2.65 | A/B/C/D | 1-359 | [»] | |
5F3C | X-ray | 2.06 | A/B/C/D | 1-359 | [»] | |
5F3E | X-ray | 2.16 | A/B/C/D | 1-359 | [»] | |
5F3G | X-ray | 2.50 | A/B/C/D | 1-359 | [»] | |
5F3I | X-ray | 2.24 | A/B/C/D | 1-359 | [»] | |
5F5I | X-ray | 2.63 | A/B | 1-359 | [»] | |
5FPV | X-ray | 2.44 | A/B/C/D/E/F/G/H | 1-359 | [»] | |
5FWE | X-ray | 2.05 | A/B | 1-359 | [»] | |
5FY8 | X-ray | 2.34 | A/B | 1-359 | [»] | |
5FYC | X-ray | 2.26 | A/B | 1-359 | [»] | |
5FYH | X-ray | 2.35 | A/B | 1-359 | [»] | |
5FYI | X-ray | 2.10 | A/B | 1-359 | [»] | |
5LY1 | X-ray | 2.50 | A/B/C/D | 1-359 | [»] | |
5LY2 | X-ray | 2.43 | A/B/C/D | 1-359 | [»] | |
5TVR | X-ray | 2.09 | A/B | 1-359 | [»] | |
5TVS | X-ray | 2.75 | A/B | 1-359 | [»] | |
5VAR | X-ray | 1.83 | A | 897-1011 | [»] | |
5VGI | X-ray | 2.07 | A/B/C/D | 5-354 | [»] | |
5VMP | X-ray | 2.48 | A/B/C/D | 5-354 | [»] | |
6CG1 | X-ray | 2.16 | A/B/C/D | 5-354 | [»] | |
6CG2 | X-ray | 2.34 | A/B/C/D | 5-354 | [»] | |
6G5W | X-ray | 1.83 | A/B | 1-359 | [»] | |
6G5X | X-ray | 1.78 | A/B | 1-359 | [»] | |
6H4O | X-ray | 2.25 | A/B/C/D | 1-359 | [»] | |
6H4P | X-ray | 2.19 | A/B/C/D | 1-359 | [»] | |
6H4Q | X-ray | 2.31 | A/B/C/D | 1-359 | [»] | |
6H4R | X-ray | 2.14 | A/B/C/D | 1-359 | [»] | |
6H4S | X-ray | 2.45 | A/B/C/D | 1-359 | [»] | |
6H4T | X-ray | 2.38 | A/B/C/D | 1-359 | [»] | |
6H4U | X-ray | 2.21 | A/B/C/D | 1-359 | [»] | |
6H4V | X-ray | 2.15 | A/B/C/D | 1-359 | [»] | |
6H4W | X-ray | 2.81 | A/B/C/D | 1-359 | [»] | |
6H4X | X-ray | 2.34 | A/B/C/D | 1-359 | [»] | |
6H4Y | X-ray | 2.38 | A/B/C/D | 1-359 | [»] | |
6H8P | X-ray | 1.98 | A/B | 1-359 | [»] | |
6HGT | X-ray | 2.33 | A/B/C/D | 1-359 | [»] | |
7D4A | X-ray | 2.20 | A | 898-1011 | [»] | |
PCDDBi | O75164 | |||||
SMRi | O75164 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 115035, 55 interactors |
CORUMi | O75164 |
DIPi | DIP-29372N |
IntActi | O75164, 54 interactors |
MINTi | O75164 |
STRINGi | 9606.ENSP00000361473 |
Chemistry databases
BindingDBi | O75164 |
ChEMBLi | CHEMBL5896 |
GuidetoPHARMACOLOGYi | 2675 |
PTM databases
iPTMneti | O75164 |
PhosphoSitePlusi | O75164 |
Genetic variation databases
BioMutai | KDM4A |
Proteomic databases
EPDi | O75164 |
jPOSTi | O75164 |
MassIVEi | O75164 |
MaxQBi | O75164 |
PaxDbi | O75164 |
PeptideAtlasi | O75164 |
PRIDEi | O75164 |
ProteomicsDBi | 49829 [O75164-1] |
Protocols and materials databases
ABCDi | O75164, 10 sequenced antibodies |
Antibodypediai | 1997, 445 antibodies from 43 providers |
DNASUi | 9682 |
Genome annotation databases
Ensembli | ENST00000372396; ENSP00000361473; ENSG00000066135 |
GeneIDi | 9682 |
KEGGi | hsa:9682 |
MANE-Selecti | ENST00000372396.4; ENSP00000361473.3; NM_014663.3; NP_055478.2 |
UCSCi | uc001cjx.4, human [O75164-1] |
Organism-specific databases
CTDi | 9682 |
DisGeNETi | 9682 |
GeneCardsi | KDM4A |
HGNCi | HGNC:22978, KDM4A |
HPAi | ENSG00000066135, Low tissue specificity |
MIMi | 609764, gene |
neXtProti | NX_O75164 |
OpenTargetsi | ENSG00000066135 |
PharmGKBi | PA164721403 |
VEuPathDBi | HostDB:ENSG00000066135 |
HUGEi | Search... |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0958, Eukaryota |
GeneTreei | ENSGT00940000159643 |
HOGENOMi | CLU_001442_0_1_1 |
InParanoidi | O75164 |
OMAi | AQQPPYC |
OrthoDBi | 1186832at2759 |
PhylomeDBi | O75164 |
TreeFami | TF106449 |
Enzyme and pathway databases
BRENDAi | 1.14.11.27, 2681 1.14.11.66, 2681 1.14.11.67, 2681 1.14.11.69, 2681 1.14.99.66, 2681 |
PathwayCommonsi | O75164 |
Reactomei | R-HSA-3214842, HDMs demethylate histones R-HSA-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks R-HSA-9029569, NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux |
SignaLinki | O75164 |
Miscellaneous databases
BioGRID-ORCSi | 9682, 38 hits in 1057 CRISPR screens |
ChiTaRSi | KDM4A, human |
EvolutionaryTracei | O75164 |
GeneWikii | JMJD2A |
GenomeRNAii | 9682 |
Pharosi | O75164, Tchem |
PROi | PR:O75164 |
RNActi | O75164, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000066135, Expressed in cortical plate and 230 other tissues |
ExpressionAtlasi | O75164, baseline and differential |
Genevisiblei | O75164, HS |
Family and domain databases
CDDi | cd04508, TUDOR, 2 hits |
Gene3Di | 3.30.40.10, 2 hits |
IDEALi | IID00360 |
InterProi | View protein in InterPro IPR034732, EPHD IPR003347, JmjC_dom IPR003349, JmjN IPR040477, KDM4_Tudor_2 IPR002999, Tudor IPR011011, Znf_FYVE_PHD IPR001965, Znf_PHD IPR013083, Znf_RING/FYVE/PHD |
Pfami | View protein in Pfam PF02373, JmjC, 1 hit PF02375, JmjN, 1 hit PF18104, Tudor_2, 2 hits |
SMARTi | View protein in SMART SM00558, JmjC, 1 hit SM00545, JmjN, 1 hit SM00249, PHD, 2 hits SM00333, TUDOR, 2 hits |
SUPFAMi | SSF57903, SSF57903, 1 hit |
PROSITEi | View protein in PROSITE PS51805, EPHD, 1 hit PS51184, JMJC, 1 hit PS51183, JMJN, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | KDM4A_HUMAN | |
Accessioni | O75164Primary (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: | February 23, 2022 | |
This is version 195 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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, Reference proteomeDocuments
- Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families