UniProtKB - O75164 (KDM4A_HUMAN)

>sp|O75164|KDM4A_HUMAN Lysine-specific demethylase 4A OS=Homo sapiens OX=9606 GN=KDM4A PE=1 SV=2
MASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASYD
DIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERK
YWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFGM
WKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRH
KMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYG
KQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESELP
PRAGNEEECPEEDMEGVEDGEEGDLKTSLAKHRIGTKRHRVCLEIPQEVSQSELFPKEDL
SSEQYEMTECPAALAPVRPTHSSVRQVEDGLTFPDYSDSTEVKFEELKNVKLEEEDEEEE
QAAAALDLSVNPASVGGRLVFSGSKKKSSSSLGSGSSRDSISSDSETSEPLSCRAQGQTG
VLTVHSYAKGDGRVTVGEPCTRKKGSAARSFSERELAEVADEYMFSLEENKKSKGRRQPL
SKLPRHHPLVLQECVSDDETSEQLTPEEEAEETEAWAKPLSQLWQNRPPNFEAEKEFNET
MAQQAPHCAVCMIFQTYHQVEFGGFNQNCGNASDLAPQKQRTKPLIPEMCFTSTGCSTDI
NLSTPYLEEDGTSILVSCKKCSVRVHASCYGVPPAKASEDWMCSRCSANALEEDCCLCSL
RGGALQRANDDRWVHVSCAVAILEARFVNIAERSPVDVSKIPLPRFKLKCIFCKKRRKRT
AGCCVQCSHGRCPTAFHVSCAQAAGVMMQPDDWPFVVFITCFRHKIPNLERAKGALQSIT
AGQKVISKHKNGRFYQCEVVRLTTETFYEVNFDDGSFSDNLYPEDIVSQDCLQFGPPAEG
EVVQVRWTDGQVYGAKFVASHPIQMYQVEFEDGSQLVVKRDDVYTLDEELPKRVKSRLSV
ASDMRFNEIFTEKEVKQEKKRQRVINSRYREDYIEPALYRAIME

Entry version 177 (08 May 2019)
Sequence version 2 (05 Oct 2010)
Previous versions | rss

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Protein

Lysine-specific demethylase 4A

Gene

KDM4A

Organism

Homo sapiens (Human)

Status

Reviewed-Annotation score: -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 (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 Publications

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.1 Publication

Cofactorⁱ

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

Activity regulationⁱ

Several specific inhibitors are being developed and tested.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	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
Binding siteⁱ	945	Histone H3K4me3	1
Binding siteⁱ	967	Histone H3K4me3	1
Binding siteⁱ	973	Histone H3K4me3	1

Regions

Feature key	Position(s)	DescriptionActions	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

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

View the complete GO annotation on QuickGO ...

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.B1 2681 1.14.11.B2 2681
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

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database More...HGNCⁱ	HGNC:22978 KDM4A
MIMⁱ	609764 gene
neXtProtⁱ	NX_O75164

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	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

DisGeNET More...DisGeNETⁱ	9682
Open Targets More...OpenTargetsⁱ	ENSG00000066135
PharmGKBⁱ	PA164721403

Chemistry databases

ChEMBLⁱ	CHEMBL5896
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	2675

Polymorphism and mutation databases

BioMutaⁱ	KDM4A

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

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

EPDⁱ	O75164
jPOSTⁱ	O75164
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O75164
PaxDbⁱ	O75164
PeptideAtlas More...PeptideAtlasⁱ	O75164
PRIDEⁱ	O75164
ProteomicsDBⁱ	49829

PTM databases

iPTMnetⁱ	O75164
PhosphoSitePlusⁱ	O75164

Expressionⁱ

Tissue specificityⁱ

Ubiquitous.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000066135 Expressed in 218 organ(s), highest expression level in lung
ExpressionAtlasⁱ	O75164 baseline and differential
Genevisibleⁱ	O75164 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA007610

HPAⁱ

HPA007610

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 Publication

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
ERG	P11308	2	EBI-936709,EBI-79704
HIST1H3D	P68431	7	EBI-936709,EBI-79722
HIST2H4B	P62805	7	EBI-936709,EBI-302023
HIST3H3	Q16695	6	EBI-936709,EBI-358900

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	115035, 30 interactors
CORUMⁱ	O75164
Database of interacting proteins More...DIPⁱ	DIP-29372N
IntActⁱ	O75164, 29 interactors
Molecular INTeraction database More...MINTⁱ	O75164
STRINGⁱ	9606.ENSP00000361473

Chemistry databases

BindingDBⁱ

O75164

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	4 – 6	Combined sources	3
Beta strandⁱ	7 – 9	Combined sources	3
Helixⁱ	10 – 12	Combined sources	3
Beta strandⁱ	15 – 17	Combined sources	3
Helixⁱ	21 – 24	Combined sources	4
Helixⁱ	27 – 36	Combined sources	10
Helixⁱ	39 – 42	Combined sources	4
Beta strandⁱ	43 – 47	Combined sources	5
Beta strandⁱ	55 – 57	Combined sources	3
Turnⁱ	61 – 64	Combined sources	4
Beta strandⁱ	66 – 69	Combined sources	4
Beta strandⁱ	71 – 78	Combined sources	8
Beta strandⁱ	81 – 88	Combined sources	8
Helixⁱ	94 – 101	Combined sources	8
Turnⁱ	104 – 106	Combined sources	3
Helixⁱ	114 – 124	Combined sources	11
Beta strandⁱ	131 – 137	Combined sources	7
Helixⁱ	150 – 152	Combined sources	3
Helixⁱ	156 – 158	Combined sources	3
Helixⁱ	159 – 162	Combined sources	4
Beta strandⁱ	163 – 165	Combined sources	3
Turnⁱ	169 – 171	Combined sources	3
Beta strandⁱ	175 – 179	Combined sources	5
Beta strandⁱ	184 – 188	Combined sources	5
Helixⁱ	191 – 193	Combined sources	3
Beta strandⁱ	195 – 204	Combined sources	10
Beta strandⁱ	206 – 211	Combined sources	6
Helixⁱ	213 – 215	Combined sources	3
Helixⁱ	216 – 226	Combined sources	11
Helixⁱ	228 – 233	Combined sources	6
Helixⁱ	237 – 240	Combined sources	4
Beta strandⁱ	243 – 245	Combined sources	3
Helixⁱ	247 – 252	Combined sources	6
Beta strandⁱ	258 – 262	Combined sources	5
Beta strandⁱ	267 – 270	Combined sources	4
Beta strandⁱ	275 – 280	Combined sources	6
Beta strandⁱ	282 – 291	Combined sources	10
Helixⁱ	296 – 302	Combined sources	7
Beta strandⁱ	308 – 311	Combined sources	4
Helixⁱ	318 – 324	Combined sources	7
Helixⁱ	326 – 333	Combined sources	8
Beta strandⁱ	343 – 345	Combined sources	3
Helixⁱ	348 – 353	Combined sources	6
Beta strandⁱ	904 – 908	Combined sources	5
Beta strandⁱ	912 – 932	Combined sources	21
Beta strandⁱ	937 – 941	Combined sources	5
Helixⁱ	943 – 945	Combined sources	3
Helixⁱ	951 – 954	Combined sources	4
Beta strandⁱ	962 – 966	Combined sources	5
Beta strandⁱ	972 – 990	Combined sources	19
Beta strandⁱ	995 – 998	Combined sources	4
Helixⁱ	1000 – 1002	Combined sources	3
Beta strandⁱ	1003 – 1005	Combined sources	3

Show more details

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...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	[»]
6H8P	X-ray	1.98	A/B	1-359	[»]
SMRⁱ	O75164
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	O75164

EvolutionaryTraceⁱ

O75164

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	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	597 – 638	Interaction with NCOR11 PublicationAdd BLAST		42

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

Zinc finger

Feature key	Position(s)	DescriptionActions	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-finger

Phylogenomic databases

eggNOGⁱ	ENOG410IT40 Eukaryota COG5141 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000159643
HOGENOMⁱ	HOG000231125
InParanoidⁱ	O75164
KEGG Orthology (KO) More...KOⁱ	K06709
OMAⁱ	TAGCCVQ
Database of Orthologous Groups More...OrthoDBⁱ	482696at2759
PhylomeDBⁱ	O75164
TreeFamⁱ	TF106449

Family and domain databases

Gene3Dⁱ	3.30.40.10, 2 hits
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
Pfam protein domain database More...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

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 Add to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: O75164-1) [UniParc]FASTA Add 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

Isoform 2 (identifier: O75164-2) [UniParc]FASTA Add to basket

Also known as: deltaN-JMJD2A

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

« Hide

        10         20         30         40         50
MFSLEENKKS KGRRQPLSKL PRHHPLVLQE CVSDDETSEQ LTPEEEAEET 
        60         70         80         90        100
EAWAKPLSQL WQNRPPNFEA EKEFNETMAQ QAPHCAVCMI FQTYHQVEFG 
       110        120        130        140        150
GFNQNCGNAS DLAPQKQRTK PLIPEMCFTS TGCSTDINLS TPYLEEDGTS 
       160        170        180        190        200
ILVSCKKCSV RVHASCYGVP PAKASEDWMC SRCSANALEE DCCLCSLRGG 
       210        220        230        240        250
ALQRANDDRW VHVSCAVAIL EARFVNIAER SPVDVSKIPL PRFKLKCIFC 
       260        270        280        290        300
KKRRKRTAGC CVQCSHGRCP TAFHVSCAQA AGVMMQPDDW PFVVFITCFR 
       310        320        330        340        350
HKIPNLERAK GALQSITAGQ KVISKHKNGR FYQCEVVRLT TETFYEVNFD 
       360        370        380        390        400
DGSFSDNLYP EDIVSQDCLQ FGPPAEGEVV QVRWTDGQVY GAKFVASHPI 
       410        420        430        440        450
QMYQVEFEDG SQLVVKRDDV YTLDEELPKR VKSRLSVASD MRFNEIFTEK 
       460        470        480 
EVKQEKKRQR VINSRYREDY IEPALYRAIM E

Show »

Length:481

Mass (Da):54,697

Checksum:ⁱ394B208A6E5483FB

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A2R8YDF7	A0A2R8YDF7_HUMAN	Lysine-specific demethylase 4A Lysine-specific demethylase 4A	KDM4A	281	Annotation score:
A0A2R8Y7L1	A0A2R8Y7L1_HUMAN	Lysine-specific demethylase 4A Lysine-specific demethylase 4A	KDM4A	8	Annotation score:

Sequence cautionⁱ

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

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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS491.1 [O75164-1]
NCBI Reference Sequences More...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 [O75164-1]
GeneIDⁱ	9682
KEGGⁱ	hsa:9682
UCSC genome browser More...UCSCⁱ	uc001cjx.4 human [O75164-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O75164	cDNA FLJ60248, highly similar to JmjC domain-containing histone demethylation protein 3A		HUMAN		303	UniRef100_O75164
Isoform 2 of Lysine-specific demethylase 4A		HUMAN		481

Protein	Similar proteins		Species	Score	Length	Source
O75164	cDNA FLJ60248, highly similar to JmjC domain-containing histone demethylation protein 3A		HUMAN		303	UniRef90_O75164
lysine-specific demethylase 4A isoform X1		PHYMC		1073
lysine-specific demethylase 4A isoform X1		BALAS		1072
Uncharacterized protein		SHEEP		1071
LOW QUALITY PROTEIN: lysine-specific demethylase 4A		LIPVE		1069
+151

Protein	Similar proteins		Species	Score	Length	Source
O75164	cDNA FLJ60248, highly similar to JmjC domain-containing histone demethylation protein 3A		HUMAN		303	UniRef50_O75164
lysine-specific demethylase 4A isoform X1		PHYMC		1073
lysine-specific demethylase 4A isoform X1		BALAS		1072
Uncharacterized protein		SHEEP		1071
LOW QUALITY PROTEIN: lysine-specific demethylase 4A		LIPVE		1069
+462

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	[»]
6H8P	X-ray	1.98	A/B	1-359	[»]
SMRⁱ	O75164
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	115035, 30 interactors
CORUMⁱ	O75164
DIPⁱ	DIP-29372N
IntActⁱ	O75164, 29 interactors
MINTⁱ	O75164
STRINGⁱ	9606.ENSP00000361473

Chemistry databases

BindingDBⁱ	O75164
ChEMBLⁱ	CHEMBL5896
GuidetoPHARMACOLOGYⁱ	2675

PTM databases

iPTMnetⁱ	O75164
PhosphoSitePlusⁱ	O75164

Polymorphism and mutation databases

BioMutaⁱ	KDM4A

BioMutaⁱ

KDM4A

Proteomic databases

EPDⁱ	O75164
jPOSTⁱ	O75164
MaxQBⁱ	O75164
PaxDbⁱ	O75164
PeptideAtlasⁱ	O75164
PRIDEⁱ	O75164
ProteomicsDBⁱ	49829

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000372396; ENSP00000361473; ENSG00000066135 [O75164-1]
GeneIDⁱ	9682
KEGGⁱ	hsa:9682
UCSCⁱ	uc001cjx.4 human [O75164-1]

Organism-specific databases

CTDⁱ	9682
DisGeNETⁱ	9682
GeneCardsⁱ	KDM4A
H-InvDBⁱ	HIX0020610
HGNCⁱ	HGNC:22978 KDM4A
HPAⁱ	HPA007610
MIMⁱ	609764 gene
neXtProtⁱ	NX_O75164
OpenTargetsⁱ	ENSG00000066135
PharmGKBⁱ	PA164721403
HUGEⁱ	Search...
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410IT40 Eukaryota COG5141 LUCA
GeneTreeⁱ	ENSGT00940000159643
HOGENOMⁱ	HOG000231125
InParanoidⁱ	O75164
KOⁱ	K06709
OMAⁱ	TAGCCVQ
OrthoDBⁱ	482696at2759
PhylomeDBⁱ	O75164
TreeFamⁱ	TF106449

Enzyme and pathway databases

BRENDAⁱ	1.14.11.27 2681 1.14.11.B1 2681 1.14.11.B2 2681
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

Miscellaneous databases

ChiTaRSⁱ	KDM4A human
EvolutionaryTraceⁱ	O75164
GeneWikiⁱ	JMJD2A
GenomeRNAiⁱ	9682
Protein Ontology More...PROⁱ	PR:O75164
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000066135 Expressed in 218 organ(s), highest expression level in lung
ExpressionAtlasⁱ	O75164 baseline and differential
Genevisibleⁱ	O75164 HS

Family and domain databases

Gene3Dⁱ	3.30.40.10, 2 hits
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
ProtoNetⁱ	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:	May 8, 2019
	This is version 177 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, Complete proteome, Reference proteome

Documents

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

UniProtKB

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UniProtKB - O75164 (KDM4A_HUMAN)

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Lysine-specific demethylase 4A

KDM4A

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Cytosol

Nucleus

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ