Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O75164

- KDM4A_HUMAN

UniProt

O75164 - KDM4A_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Lysine-specific demethylase 4A

Gene

KDM4A

Organism
Homo sapiens (Human)
Status
Reviewed - 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 Fe(2+) ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei132 – 1321Alpha-ketoglutarate1 Publication
Metal bindingi188 – 1881Iron; catalytic1 PublicationPROSITE-ProRule annotation
Metal bindingi190 – 1901Iron; catalytic1 PublicationPROSITE-ProRule annotation
Binding sitei198 – 1981Alpha-ketoglutarate1 Publication
Binding sitei206 – 2061Alpha-ketoglutarate1 Publication
Metal bindingi234 – 2341Zinc
Metal bindingi240 – 2401Zinc
Metal bindingi276 – 2761Iron; catalytic1 PublicationPROSITE-ProRule annotation
Metal bindingi306 – 3061Zinc
Metal bindingi308 – 3081Zinc
Binding sitei945 – 9451Histone H3K4me3
Binding sitei967 – 9671Histone H3K4me3
Binding sitei973 – 9731Histone H3K4me3

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri709 – 76759PHD-type 1Add
BLAST
Zinc fingeri829 – 88557PHD-type 2Add
BLAST

GO - Molecular functioni

  1. histone demethylase activity (H3-K36 specific) Source: UniProtKB
  2. methylated histone binding Source: UniProtKB
  3. ubiquitin protein ligase binding Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. cardiac muscle hypertrophy in response to stress Source: Ensembl
  2. histone demethylation Source: UniProtKB
  3. histone H3-K36 demethylation Source: GOC
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. transcription, DNA-templated Source: UniProtKB-KW
  6. viral process Source: UniProtKB-KW
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

ReactomeiREACT_228178. HDMs demethylate histones.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:22978. KDM4A.

Subcellular locationi

Nucleus 2 PublicationsPROSITE-ProRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleolus Source: HPA
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi133 – 1331G → A: Abolishes histone demethylase activity; when associated with A-138. 1 Publication
Mutagenesisi138 – 1381G → A: Abolishes histone demethylase activity; when associated with A-138. 1 Publication
Mutagenesisi165 – 1651G → A: Abolishes histone demethylase activity; when associated with A-165. 1 Publication
Mutagenesisi170 – 1701G → A: Abolishes histone demethylase activity; when associated with A-165. 1 Publication
Mutagenesisi188 – 1881H → A: Abolishes histone demethylase activity without affecting ability to bind H4K20me2. 2 Publications
Mutagenesisi288 – 2892ST → AI: Displays histone demethylase activity for both dimethylated and H3-K9Me3.
Mutagenesisi288 – 2892ST → TV, NV or GG: Abolishes histone demethylase activity.
Mutagenesisi939 – 9391D → R: Impairs binding to H4K20me2, promoting partial recruitment of TP53BP1. 1 Publication
Mutagenesisi945 – 9451D → A: Impairs binding to H3K4me3. 1 Publication
Mutagenesisi945 – 9451D → R: Abolishes binding to H3K4me3. 1 Publication
Mutagenesisi967 – 9671W → H: Abolishes binding to H3K4me3. 1 Publication
Mutagenesisi973 – 9731Y → A: Abolishes binding to H3K4me3. 2 Publications

Organism-specific databases

PharmGKBiPA164721403.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 10641063Lysine-specific demethylase 4APRO_0000183172Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

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, Ubl conjugation

Proteomic databases

MaxQBiO75164.
PaxDbiO75164.
PRIDEiO75164.

PTM databases

PhosphoSiteiO75164.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiO75164.
CleanExiHS_JMJD2A.
ExpressionAtlasiO75164. baseline and differential.
GenevestigatoriO75164.

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

Protein-protein interaction databases

BioGridi115035. 19 interactions.
DIPiDIP-29372N.
IntActiO75164. 28 interactions.
MINTiMINT-2829088.
STRINGi9606.ENSP00000361473.

Structurei

Secondary structure

1
1064
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 73Combined sources
Turni9 – 113Combined sources
Beta strandi15 – 173Combined sources
Helixi21 – 244Combined sources
Helixi27 – 3610Combined sources
Helixi39 – 424Combined sources
Beta strandi43 – 475Combined sources
Beta strandi59 – 613Combined sources
Helixi62 – 643Combined sources
Beta strandi66 – 694Combined sources
Beta strandi71 – 788Combined sources
Beta strandi81 – 888Combined sources
Helixi94 – 1029Combined sources
Turni104 – 1063Combined sources
Helixi114 – 12411Combined sources
Beta strandi131 – 1377Combined sources
Helixi156 – 1583Combined sources
Helixi159 – 1646Combined sources
Turni169 – 1713Combined sources
Beta strandi175 – 1795Combined sources
Beta strandi184 – 1885Combined sources
Helixi191 – 1933Combined sources
Beta strandi195 – 20410Combined sources
Beta strandi206 – 2116Combined sources
Helixi213 – 2153Combined sources
Helixi216 – 22611Combined sources
Helixi228 – 2336Combined sources
Helixi237 – 2404Combined sources
Beta strandi243 – 2453Combined sources
Helixi247 – 2526Combined sources
Beta strandi258 – 2625Combined sources
Beta strandi267 – 2704Combined sources
Beta strandi275 – 2806Combined sources
Beta strandi282 – 29110Combined sources
Helixi296 – 3027Combined sources
Beta strandi308 – 3114Combined sources
Helixi318 – 3247Combined sources
Helixi326 – 3283Combined sources
Helixi329 – 3335Combined sources
Helixi348 – 3503Combined sources
Helixi351 – 3544Combined sources
Beta strandi904 – 9085Combined sources
Beta strandi912 – 93221Combined sources
Beta strandi937 – 9415Combined sources
Helixi943 – 9453Combined sources
Helixi951 – 9544Combined sources
Beta strandi962 – 9665Combined sources
Beta strandi972 – 99019Combined sources
Beta strandi995 – 9984Combined sources
Helixi1000 – 10023Combined sources
Beta strandi1003 – 10053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliO75164.
SMRiO75164. Positions 7-355, 821-869, 897-1011.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75164.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 5643JmjNPROSITE-ProRule annotationAdd
BLAST
Domaini142 – 308167JmjCPROSITE-ProRule annotationAdd
BLAST
Domaini897 – 95458Tudor 1Add
BLAST
Domaini955 – 101157Tudor 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni597 – 63842Interaction with NCOR1Add
BLAST

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 JmjC domain.PROSITE-ProRule annotation
Contains 1 JmjN domain.PROSITE-ProRule annotation
Contains 2 PHD-type zinc fingers.Curated
Contains 2 Tudor domains.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri709 – 76759PHD-type 1Add
BLAST
Zinc fingeri829 – 88557PHD-type 2Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5141.
GeneTreeiENSGT00530000063342.
HOGENOMiHOG000231125.
InParanoidiO75164.
KOiK06709.
OMAiRKRTAGC.
OrthoDBiEOG7TQV03.
PhylomeDBiO75164.
TreeFamiTF106449.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003347. JmjC_dom.
IPR003349. TF_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.
PROSITEiPS51184. 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. Align

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti482 – 4821A → E.2 Publications
Corresponds to variant rs586339 [ dbSNP | Ensembl ].
VAR_023775
Natural varianti877 – 8771V → G.
Corresponds to variant rs12759032 [ dbSNP | Ensembl ].
VAR_031217

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 583583Missing in isoform 2. CuratedVSP_044239Add
BLAST

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_005271354.1. [O75164-1]
XP_005271412.1. XM_005271355.1. [O75164-1]
UniGeneiHs.155983.

Genome annotation databases

EnsembliENST00000372396; ENSP00000361473; ENSG00000066135. [O75164-1]
GeneIDi9682.
KEGGihsa:9682.
UCSCiuc001cjx.3. 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 .
CCDSi CCDS491.1. [O75164-1 ]
RefSeqi NP_055478.2. NM_014663.2. [O75164-1 ]
XP_005271411.1. XM_005271354.1. [O75164-1 ]
XP_005271412.1. XM_005271355.1. [O75164-1 ]
UniGenei Hs.155983.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali O75164.
SMRi O75164. Positions 7-355, 821-869, 897-1011.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115035. 19 interactions.
DIPi DIP-29372N.
IntActi O75164. 28 interactions.
MINTi MINT-2829088.
STRINGi 9606.ENSP00000361473.

Chemistry

BindingDBi O75164.
ChEMBLi CHEMBL5896.

PTM databases

PhosphoSitei O75164.

Proteomic databases

MaxQBi O75164.
PaxDbi O75164.
PRIDEi O75164.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372396 ; ENSP00000361473 ; ENSG00000066135 . [O75164-1 ]
GeneIDi 9682.
KEGGi hsa:9682.
UCSCi uc001cjx.3. human. [O75164-1 ]

Organism-specific databases

CTDi 9682.
GeneCardsi GC01P044115.
H-InvDB HIX0020610.
HGNCi HGNC:22978. KDM4A.
HPAi HPA007610.
MIMi 609764. gene.
neXtProti NX_O75164.
PharmGKBi PA164721403.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5141.
GeneTreei ENSGT00530000063342.
HOGENOMi HOG000231125.
InParanoidi O75164.
KOi K06709.
OMAi RKRTAGC.
OrthoDBi EOG7TQV03.
PhylomeDBi O75164.
TreeFami TF106449.

Enzyme and pathway databases

Reactomei REACT_228178. HDMs demethylate histones.

Miscellaneous databases

ChiTaRSi KDM4A. human.
EvolutionaryTracei O75164.
GeneWikii JMJD2A.
GenomeRNAii 9682.
NextBioi 36361.
PROi O75164.
SOURCEi Search...

Gene expression databases

Bgeei O75164.
CleanExi HS_JMJD2A.
ExpressionAtlasi O75164. baseline and differential.
Genevestigatori O75164.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi IPR003347. JmjC_dom.
IPR003349. TF_JmjN.
IPR002999. Tudor.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
[Graphical view ]
SMARTi SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 2 hits.
SM00333. TUDOR. 2 hits.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

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 26, 2014
This is version 135 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

External Data

Dasty 3