Q6ZMT4 (KDM7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lysine-specific demethylase 7
EC=1.14.11.-

Alternative name(s):
JmjC domain-containing histone demethylation protein 1D

Gene names

Name:	JHDM1D
Synonyms:	KDM7, KIAA1718

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	941 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone demethylase required for brain development. Specifically demethylates dimethylated 'Lys-9' and 'Lys-27' (H3K9me2 and H3K27me2, respectively) of histone H3 and monomethylated histone H4 'Lys-20' residue (H4K20Me1), thereby playing a central role in histone code. Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: in presence of H3K4me3, it has no demethylase activity toward H3K9me2, while it has high activity toward H3K27me2. Demethylates H3K9me2 in absence of H3K4me3. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate. Ref.6 Ref.7 Ref.8
Cofactor	Binds 1 Fe2+ ion per subunit. Ref.6 Ref.8
Subcellular location	Nucleus.
Domain	The PHD-type zinc finger mediates the binding to H3K4me3. Binding to H3K4me3 prevents its access to H3K9me2. Ref.8 The linker region is a critical determinant of demethylase specificity. It prevents the active site of JmjC to reach the target H3K9me2 when the PHD-type zinc finger binds to H3K4me3, while it favors selectivity toward H3K27me2. Ref.8
Sequence similarities	Belongs to the JHDM1 histone demethylase family. JHDM1D subfamily. Contains 1 JmjC domain. Contains 1 PHD-type zinc finger.
Biophysicochemical properties	Kinetic parameters: KM=1.2 µM for histone H3 H3K9Me2 Ref.8
Sequence caution	The sequence BAD18641.1 differs from that shown. Reason: Frameshift at position 902. The sequence EAL24032.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Iron Metal-binding Zinc
Molecular function	Chromatin regulator Dioxygenase Oxidoreductase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	midbrain development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleolus Inferred from direct assay. Source: HPA
Molecular_function	histone demethylase activity (H3-K27 specific) Inferred from direct assay Ref.8Ref.6Ref.7. Source: UniProtKB histone demethylase activity (H3-K36 specific) Inferred from direct assay Ref.7. Source: UniProtKB histone demethylase activity (H3-K9 specific) Inferred from direct assay Ref.8Ref.6Ref.7. Source: UniProtKB histone demethylase activity (H4-K20 specific) Inferred from direct assay Ref.7. Source: UniProtKB iron ion binding Inferred from direct assay Ref.8. Source: UniProtKB methylated histone residue binding Inferred from direct assay Ref.8. Source: UniProtKB oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q6ZMT4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q6ZMT4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     792-809: GYHVKTEDPDLRTSSWIK → ETRSHLCCPDWSPTPELK
     810-941: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 941

941

Lysine-specific demethylase 7

PRO_0000226771

Regions

Domain

230 – 386

157

JmjC

Zinc finger

37 – 88

52

PHD-type

Region

97 – 114

18

Linker

Compositional bias

2 – 31

30

Ala-rich

Sites

Metal binding

282

1

Iron; catalytic

Metal binding

284

1

Iron; catalytic

Metal binding

354

1

Iron; catalytic

Binding site

279

1

Substrate By similarity

Binding site

299

1

Substrate By similarity

Natural variations

Alternative sequence

792 – 809

18

GYHVK…SSWIK → ETRSHLCCPDWSPTPELK in isoform 2.

VSP_017458

Alternative sequence

810 – 941

132

Missing in isoform 2.

VSP_017459

Natural variant

392

1

D → Y.
Corresponds to variant rs5020212 [ dbSNP | Ensembl ].

VAR_049652

Natural variant

644

1

R → S. Ref.4
Corresponds to variant rs6950119 [ dbSNP | Ensembl ].

VAR_049653

Experimental info

Mutagenesis

282

1

H → A: Abolishes enzymatic activity. Ref.6

Sequence conflict

677

1

T → I in CAE46011. Ref.5

Secondary structure

1

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941

Helix Strand Turn

Details...

Turn

40 – 43

4

Beta strand

52 – 55

4

Turn

56 – 58

3

Beta strand

61 – 63

3

Helix

64 – 67

4

Helix

71 – 76

6

Beta strand

77 – 80

4

Helix

83 – 89

7

Beta strand

100 – 104

5

Helix

120 – 128

9

Helix

134 – 136

3

Turn

143 – 145

3

Helix

148 – 154

7

Beta strand

160 – 164

5

Turn

166 – 168

3

Helix

179 – 186

8

Turn

187 – 189

3

Beta strand

190 – 196

7

Turn

197 – 200

4

Beta strand

201 – 206

6

Helix

207 – 215

9

Beta strand

216 – 218

3

Beta strand

223 – 229

7

Beta strand

231 – 233

3

Helix

234 – 238

5

Helix

243 – 248

6

Helix

250 – 254

5

Beta strand

269 – 273

5

Beta strand

278 – 282

5

Helix

285 – 287

3

Beta strand

289 – 304

16

Helix

308 – 318

11

Helix

321 – 325

5

Helix

328 – 331

4

Beta strand

336 – 341

6

Beta strand

345 – 348

4

Beta strand

353 – 369

17

Helix

375 – 388

14

Helix

391 – 395

5

Helix

399 – 418

20

Turn

419 – 421

3

Helix

426 – 442

17

Turn

445 – 447

3

Helix

448 – 450

3

Helix

452 – 454

3

Beta strand

457 – 459

3

Helix

461 – 477

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: AB8161020D157F11	FASTA	941	106,557
	10 20 30 40 50 60 MAGAAAAVAA GAAAGAAAAA VSVAAPGRAS APPPPPPVYC VCRQPYDVNR FMIECDICKD 70 80 90 100 110 120 WFHGSCVGVE EHHAVDIDLY HCPNCAVLHG SSLMKKRRNW HRHDYTEIDD GSKPVQAGTR 130 140 150 160 170 180 TFIKELRSRV FPSADEIIIK MHGSQLTQRY LEKHGFDVPI MVPKLDDLGL RLPSPTFSVM 190 200 210 220 230 240 DVERYVGGDK VIDVIDVARQ ADSKMTLHNY VKYFMNPNRP KVLNVISLEF SDTKMSELVE 250 260 270 280 290 300 VPDIAKKLSW VENYWPDDSV FPKPFVQKYC LMGVQDSYTD FHIDFGGTSV WYHVLWGEKI 310 320 330 340 350 360 FYLIKPTDEN LARYESWSSS VTQSEVFFGD KVDKCYKCVV KQGHTLFVPT GWIHAVLTSQ 370 380 390 400 410 420 DCMAFGGNFL HNLNIGMQLR CYEMEKRLKT PDLFKFPFFE AICWFVAKNL LETLKELRED 430 440 450 460 470 480 GFQPQTYLVQ GVKALHTALK LWMKKELVSE HAFEIPDNVR PGHLIKELSK VIRAIEEENG 490 500 510 520 530 540 KPVKSQGIPI VCPVSRSSNE ATSPYHSRRK MRKLRDHNVR TPSNLDILEL HTREVLKRLE 550 560 570 580 590 600 MCPWEEDILS SKLNGKFNKH LQPSSTVPEW RAKDNDLRLL LTNGRIIKDE RQPFADQSLY 610 620 630 640 650 660 TADSENEEDK RRTKKAKMKI EESSGVEGVE HEESQKPLNG FFTRVKSELR SRSSGYSDIS 670 680 690 700 710 720 ESEDSGPECT ALKSIFTTEE SESSGDEKKQ EITSNFKEES NVMRNFLQKS QKPSRSEIPI 730 740 750 760 770 780 KRECPTSTST EEEAIQGMLS MAGLHYSTCL QRQIQSTDCS GERNSLQDPS SCHGSNHEVR 790 800 810 820 830 840 QLYRYDKPVE CGYHVKTEDP DLRTSSWIKQ FDTSRFHPQD LSRSQKCIRK EGSSEISQRV 850 860 870 880 890 900 QSRNYVDSSG SSLQNGKYMQ NSNLTSGACQ ISNGSLSPER PVGETSFSVP LHPTKRPASN 910 920 930 940 PPPISNQATK GKRPKKGMAT AKQRLGKILK LNRNGHARFF V
	Isoform 2 [UniParc]. Checksum: 1561533C92AB3466	FASTA	809	92,001
	10 20 30 40 50 60 MAGAAAAVAA GAAAGAAAAA VSVAAPGRAS APPPPPPVYC VCRQPYDVNR FMIECDICKD 70 80 90 100 110 120 WFHGSCVGVE EHHAVDIDLY HCPNCAVLHG SSLMKKRRNW HRHDYTEIDD GSKPVQAGTR 130 140 150 160 170 180 TFIKELRSRV FPSADEIIIK MHGSQLTQRY LEKHGFDVPI MVPKLDDLGL RLPSPTFSVM 190 200 210 220 230 240 DVERYVGGDK VIDVIDVARQ ADSKMTLHNY VKYFMNPNRP KVLNVISLEF SDTKMSELVE 250 260 270 280 290 300 VPDIAKKLSW VENYWPDDSV FPKPFVQKYC LMGVQDSYTD FHIDFGGTSV WYHVLWGEKI 310 320 330 340 350 360 FYLIKPTDEN LARYESWSSS VTQSEVFFGD KVDKCYKCVV KQGHTLFVPT GWIHAVLTSQ 370 380 390 400 410 420 DCMAFGGNFL HNLNIGMQLR CYEMEKRLKT PDLFKFPFFE AICWFVAKNL LETLKELRED 430 440 450 460 470 480 GFQPQTYLVQ GVKALHTALK LWMKKELVSE HAFEIPDNVR PGHLIKELSK VIRAIEEENG 490 500 510 520 530 540 KPVKSQGIPI VCPVSRSSNE ATSPYHSRRK MRKLRDHNVR TPSNLDILEL HTREVLKRLE 550 560 570 580 590 600 MCPWEEDILS SKLNGKFNKH LQPSSTVPEW RAKDNDLRLL LTNGRIIKDE RQPFADQSLY 610 620 630 640 650 660 TADSENEEDK RRTKKAKMKI EESSGVEGVE HEESQKPLNG FFTRVKSELR SRSSGYSDIS 670 680 690 700 710 720 ESEDSGPECT ALKSIFTTEE SESSGDEKKQ EITSNFKEES NVMRNFLQKS QKPSRSEIPI 730 740 750 760 770 780 KRECPTSTST EEEAIQGMLS MAGLHYSTCL QRQIQSTDCS GERNSLQDPS SCHGSNHEVR 790 800 QLYRYDKPVE CETRSHLCCP DWSPTPELK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Trachea.
[2]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O. DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 565-941 (ISOFORM 1), VARIANT SER-644.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 407-941 (ISOFORM 2). Tissue: Fetal kidney.
[6]	"KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development." Tsukada Y., Ishitani T., Nakayama K.I. Genes Dev. 24:432-437(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF HIS-282.
[7]	"Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development." Qi H.H., Sarkissian M., Hu G.Q., Wang Z., Bhattacharjee A., Gordon D.B., Gonzales M., Lan F., Ongusaha P.P., Huarte M., Yaghi N.K., Lim H., Garcia B.A., Brizuela L., Zhao K., Roberts T.M., Shi Y. Nature 466:503-507(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases." Horton J.R., Upadhyay A.K., Qi H.H., Zhang X., Shi Y., Cheng X. Nat. Struct. Mol. Biol. 17:38-43(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-488 IN COMPLEX WITH IRON AND N-OXALYLGLYCINE, ZINC-BINDING, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, DOMAIN LINKER AND PHD-FINGER.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK131497 mRNA. Translation: BAD18641.1. Frameshift.
AC004849 Genomic DNA. No translation available.
CH236950 Genomic DNA. Translation: EAL24032.1. Sequence problems.
AB051505 mRNA. Translation: BAB21809.1.
BX641017 mRNA. Translation: CAE46011.1.

IPI

IPI00418567.
IPI00738581.

RefSeq

NP_085150.1. NM_030647.1.

UniGene

Hs.308710.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3KV5	X-ray	2.39	A/D	1-488	[»]
3KV6	X-ray	2.89	A/D	1-488	[»]
3KV9	X-ray	2.29	A	92-488	[»]
3KVA	X-ray	2.79	A	92-488	[»]
3KVB	X-ray	2.69	A	92-488	[»]
3U78	X-ray	2.69	A	92-488	[»]

ProteinModelPortal

Q6ZMT4.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q6ZMT4. 1 interaction.

STRING

9606.ENSP00000380692.

PTM databases

PhosphoSite

Q6ZMT4.

Polymorphism databases

DMDM

90111764.

Proteomic databases

PaxDb

Q6ZMT4.

PRIDE

Q6ZMT4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000006967; ENSP00000006967; ENSG00000006459.
ENST00000397560; ENSP00000380692; ENSG00000006459.

GeneID

80853.

KEGG

hsa:80853.

UCSC

uc003vvm.3. human.

Organism-specific databases

CTD

80853.

GeneCards

GC07M139784.

H-InvDB

HIX0007139.

HGNC

HGNC:22224. JHDM1D.

HPA

HPA012114.

neXtProt

NX_Q6ZMT4.

PharmGKB

PA162392512.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG290496.

HOGENOM

HOG000231232.

HOVERGEN

HBG045631.

InParanoid

Q6ZMT4.

KO

K11445.

OMA

QDPSSCH.

OrthoDB

EOG46HG90.

PhylomeDB

Q6ZMT4.

Gene expression databases

Bgee

Q6ZMT4.

CleanEx

HS_JHDM1D.

Genevestigator

Q6ZMT4.

GermOnline

ENSG00000006459. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR003347. JmjC_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Pfam

PF02373. JmjC. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]

SMART

SM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS51184. JMJC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q6ZMT4.

GenomeRNAi

80853.

NextBio

71296.

Entry information

Entry name

KDM7_HUMAN

Accession

Primary (citable) accession number: Q6ZMT4
Secondary accession number(s): A4D1S9 , C9JJH9, C9JQU2, Q6MZL8, Q9C0E5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.