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Q6ZMT4

- KDM7A_HUMAN

UniProt

Q6ZMT4 - KDM7A_HUMAN

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Protein

Lysine-specific demethylase 7A

Gene
KDM7A, JHDM1D, KDM7, KIAA1718
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Cofactori

Binds 1 Fe2+ ion per subunit.2 Publications

Kineticsi

  1. KM=1.2 µM for histone H3 H3K9Me21 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei279 – 2791Substrate By similarity
Metal bindingi282 – 2821Iron; catalytic
Metal bindingi284 – 2841Iron; catalytic
Binding sitei299 – 2991Substrate By similarity
Metal bindingi354 – 3541Iron; catalytic

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri37 – 8852PHD-typeAdd
BLAST

GO - Molecular functioni

  1. histone demethylase activity (H3-K27 specific) Source: UniProtKB
  2. histone demethylase activity (H3-K36 specific) Source: UniProtKB
  3. histone demethylase activity (H3-K9 specific) Source: UniProtKB
  4. histone demethylase activity (H4-K20 specific) Source: UniProtKB
  5. iron ion binding Source: UniProtKB
  6. methylated histone binding Source: UniProtKB
  7. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Source: UniProtKB
  8. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. histone H3-K27 demethylation Source: UniProtKB
  2. histone H3-K36 demethylation Source: UniProtKB
  3. histone H3-K9 demethylation Source: UniProtKB
  4. histone H4-K20 demethylation Source: UniProtKB
  5. midbrain development Source: UniProtKB
  6. positive regulation of transcription, DNA-templated Source: Ensembl
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific demethylase 7A (EC:1.14.11.-)
Alternative name(s):
JmjC domain-containing histone demethylation protein 1D
Lysine-specific demethylase 7
Gene namesi
Name:KDM7A
Synonyms:JHDM1D, KDM7, KIAA1718
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:22224. KDM7A.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi282 – 2821H → A: Abolishes enzymatic activity. 1 Publication

Organism-specific databases

PharmGKBiPA162392512.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 941941Lysine-specific demethylase 7APRO_0000226771Add
BLAST

Proteomic databases

PaxDbiQ6ZMT4.
PRIDEiQ6ZMT4.

PTM databases

PhosphoSiteiQ6ZMT4.

Expressioni

Gene expression databases

BgeeiQ6ZMT4.
CleanExiHS_JHDM1D.
GenevestigatoriQ6ZMT4.

Organism-specific databases

HPAiHPA012114.

Interactioni

Protein-protein interaction databases

BioGridi123331. 1 interaction.
IntActiQ6ZMT4. 1 interaction.
STRINGi9606.ENSP00000380692.

Structurei

Secondary structure

1
941
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni40 – 434
Beta strandi52 – 554
Turni56 – 583
Beta strandi61 – 633
Helixi64 – 674
Helixi71 – 766
Beta strandi77 – 804
Helixi83 – 897
Beta strandi100 – 1045
Helixi120 – 1289
Helixi134 – 1363
Turni143 – 1453
Helixi148 – 1547
Beta strandi160 – 1645
Turni166 – 1683
Helixi179 – 1868
Turni187 – 1893
Beta strandi190 – 1967
Turni197 – 2004
Beta strandi201 – 2066
Helixi207 – 2159
Beta strandi216 – 2183
Beta strandi223 – 2297
Beta strandi231 – 2333
Helixi234 – 2385
Helixi243 – 2486
Helixi250 – 2545
Beta strandi269 – 2735
Beta strandi278 – 2825
Helixi285 – 2873
Beta strandi289 – 30416
Helixi308 – 31811
Helixi321 – 3255
Helixi328 – 3314
Beta strandi336 – 3416
Beta strandi345 – 3484
Beta strandi353 – 36917
Helixi375 – 38814
Helixi391 – 3955
Helixi399 – 41820
Turni419 – 4213
Helixi426 – 44217
Turni445 – 4473
Helixi448 – 4503
Helixi452 – 4543
Beta strandi457 – 4593
Helixi461 – 47717

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KV5X-ray2.39A/D1-488[»]
3KV6X-ray2.89A/D1-488[»]
3KV9X-ray2.29A92-488[»]
3KVAX-ray2.79A92-488[»]
3KVBX-ray2.69A92-488[»]
3U78X-ray2.69A92-488[»]
ProteinModelPortaliQ6ZMT4.
SMRiQ6ZMT4. Positions 38-479.

Miscellaneous databases

EvolutionaryTraceiQ6ZMT4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini230 – 386157JmjCAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 11418LinkerAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 3130Ala-richAdd
BLAST

Domaini

The PHD-type zinc finger mediates the binding to H3K4me3. Binding to H3K4me3 prevents its access to H3K9me2.1 Publication
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 H3K27me2.1 Publication

Sequence similaritiesi

Contains 1 JmjC domain.

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri37 – 8852PHD-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG290496.
HOGENOMiHOG000231232.
HOVERGENiHBG045631.
InParanoidiQ6ZMT4.
KOiK11445.
OMAiLWMKKEL.
OrthoDBiEOG73JKV9.
PhylomeDBiQ6ZMT4.
TreeFamiTF106480.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR003347. 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]
PfamiPF02373. JmjC. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS51184. JMJC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6ZMT4-1) [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

MAGAAAAVAA GAAAGAAAAA VSVAAPGRAS APPPPPPVYC VCRQPYDVNR    50
FMIECDICKD WFHGSCVGVE EHHAVDIDLY HCPNCAVLHG SSLMKKRRNW 100
HRHDYTEIDD GSKPVQAGTR TFIKELRSRV FPSADEIIIK MHGSQLTQRY 150
LEKHGFDVPI MVPKLDDLGL RLPSPTFSVM DVERYVGGDK VIDVIDVARQ 200
ADSKMTLHNY VKYFMNPNRP KVLNVISLEF SDTKMSELVE VPDIAKKLSW 250
VENYWPDDSV FPKPFVQKYC LMGVQDSYTD FHIDFGGTSV WYHVLWGEKI 300
FYLIKPTDEN LARYESWSSS VTQSEVFFGD KVDKCYKCVV KQGHTLFVPT 350
GWIHAVLTSQ DCMAFGGNFL HNLNIGMQLR CYEMEKRLKT PDLFKFPFFE 400
AICWFVAKNL LETLKELRED GFQPQTYLVQ GVKALHTALK LWMKKELVSE 450
HAFEIPDNVR PGHLIKELSK VIRAIEEENG KPVKSQGIPI VCPVSRSSNE 500
ATSPYHSRRK MRKLRDHNVR TPSNLDILEL HTREVLKRLE MCPWEEDILS 550
SKLNGKFNKH LQPSSTVPEW RAKDNDLRLL LTNGRIIKDE RQPFADQSLY 600
TADSENEEDK RRTKKAKMKI EESSGVEGVE HEESQKPLNG FFTRVKSELR 650
SRSSGYSDIS ESEDSGPECT ALKSIFTTEE SESSGDEKKQ EITSNFKEES 700
NVMRNFLQKS QKPSRSEIPI KRECPTSTST EEEAIQGMLS MAGLHYSTCL 750
QRQIQSTDCS GERNSLQDPS SCHGSNHEVR QLYRYDKPVE CGYHVKTEDP 800
DLRTSSWIKQ FDTSRFHPQD LSRSQKCIRK EGSSEISQRV QSRNYVDSSG 850
SSLQNGKYMQ NSNLTSGACQ ISNGSLSPER PVGETSFSVP LHPTKRPASN 900
PPPISNQATK GKRPKKGMAT AKQRLGKILK LNRNGHARFF V 941
Length:941
Mass (Da):106,557
Last modified:March 7, 2006 - v2
Checksum:iAB8161020D157F11
GO
Isoform 2 (identifier: Q6ZMT4-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:809
Mass (Da):92,001
Checksum:i1561533C92AB3466
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti392 – 3921D → Y.
Corresponds to variant rs5020212 [ dbSNP | Ensembl ].
VAR_049652
Natural varianti644 – 6441R → S.1 Publication
Corresponds to variant rs6950119 [ dbSNP | Ensembl ].
VAR_049653

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei792 – 80918GYHVK…SSWIK → ETRSHLCCPDWSPTPELK in isoform 2. VSP_017458Add
BLAST
Alternative sequencei810 – 941132Missing in isoform 2. VSP_017459Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti677 – 6771T → I in CAE46011. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS43658.1. [Q6ZMT4-1]
RefSeqiNP_085150.1. NM_030647.1. [Q6ZMT4-1]
UniGeneiHs.308710.

Genome annotation databases

EnsembliENST00000006967; ENSP00000006967; ENSG00000006459. [Q6ZMT4-2]
ENST00000397560; ENSP00000380692; ENSG00000006459. [Q6ZMT4-1]
GeneIDi80853.
KEGGihsa:80853.
UCSCiuc003vvm.3. human. [Q6ZMT4-1]

Polymorphism databases

DMDMi90111764.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS43658.1. [Q6ZMT4-1 ]
RefSeqi NP_085150.1. NM_030647.1. [Q6ZMT4-1 ]
UniGenei Hs.308710.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q6ZMT4.
SMRi Q6ZMT4. Positions 38-479.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123331. 1 interaction.
IntActi Q6ZMT4. 1 interaction.
STRINGi 9606.ENSP00000380692.

Chemistry

ChEMBLi CHEMBL3038496.
GuidetoPHARMACOLOGYi 2686.

PTM databases

PhosphoSitei Q6ZMT4.

Polymorphism databases

DMDMi 90111764.

Proteomic databases

PaxDbi Q6ZMT4.
PRIDEi Q6ZMT4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000006967 ; ENSP00000006967 ; ENSG00000006459 . [Q6ZMT4-2 ]
ENST00000397560 ; ENSP00000380692 ; ENSG00000006459 . [Q6ZMT4-1 ]
GeneIDi 80853.
KEGGi hsa:80853.
UCSCi uc003vvm.3. human. [Q6ZMT4-1 ]

Organism-specific databases

CTDi 80853.
GeneCardsi GC07M139784.
H-InvDB HIX0007139.
HGNCi HGNC:22224. KDM7A.
HPAi HPA012114.
neXtProti NX_Q6ZMT4.
PharmGKBi PA162392512.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG290496.
HOGENOMi HOG000231232.
HOVERGENi HBG045631.
InParanoidi Q6ZMT4.
KOi K11445.
OMAi LWMKKEL.
OrthoDBi EOG73JKV9.
PhylomeDBi Q6ZMT4.
TreeFami TF106480.

Miscellaneous databases

EvolutionaryTracei Q6ZMT4.
GenomeRNAii 80853.
NextBioi 71296.
PROi Q6ZMT4.

Gene expression databases

Bgeei Q6ZMT4.
CleanExi HS_JHDM1D.
Genevestigatori Q6ZMT4.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi 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 ]
Pfami PF02373. JmjC. 1 hit.
PF00628. PHD. 1 hit.
[Graphical view ]
SMARTi SM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 1 hit.
PROSITEi PS51184. JMJC. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiKDM7A_HUMAN
AccessioniPrimary (citable) accession number: Q6ZMT4
Secondary accession number(s): A4D1S9
, C9JJH9, C9JQU2, Q6MZL8, Q9C0E5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 91 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 7
    Human chromosome 7: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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