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Q6NYC1 (JMJD6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6

EC=1.14.11.-
Alternative name(s):
Histone arginine demethylase JMJD6
JmjC domain-containing protein 6
Jumonji domain-containing protein 6
Lysyl-hydroxylase JMJD6
Peptide-lysine 5-dioxygenase JMJD6
Phosphatidylserine receptor
Short name=Protein PTDSR
Gene names
Name:JMJD6
Synonyms:KIAA0585, PTDSR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length403 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Acts as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. Has no histone lysine demethylase activity. Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65. Seems to be necessary for the regulation of macrophage cytokine responses. Ref.10 Ref.11 Ref.12 Ref.15 Ref.16

Cofactor

Binds 1 Fe2+ ion per subunit. Ref.11

Subunit structure

Interacts with LUC7L2, LUC7L3 and U2AF2/U2AF65. Interacts with BRD4. Ref.11 Ref.14

Subcellular location

Nucleusnucleoplasm. Nucleusnucleolus. Note: Mainly found throughout the nucleoplasm outside of regions containing heterochromatic DNA, with some localization in nucleolus. During mitosis, excluded from the nucleus and reappears in the telophase of the cell cycle. Ref.7 Ref.12

Tissue specificity

Highly expressed in the heart, skeletal muscle and kidney. Expressed at moderate or low level in brain, placenta, lung, liver, pancreas, spleen, thymus, prostate, testis and ovary. Up-regulated in many patients with chronic pancreatitis. Expressed in nursing thymic epithelial cells. Ref.2 Ref.8 Ref.9

Induction

Up-regulated upon cytokine treatment, but not upon TNF treatment. Ref.8

Domain

The nuclear localization signal motifs are necessary and sufficient to target it into the nucleus.

Sequence similarities

Belongs to the JMJD6 family.

Contains 1 JmjC domain.

Caution

Was initially thought to constitute the phosphatidylserine receptor, a receptor that mediates recognition of phosphatidylserine, a specific marker only present at the surface of apoptotic cells. Phosphatidylserine receptor probably participates in apoptotic cell phagocytosis. This protein was identified using phage display expressing mAb 217, an antibody that specifically recognizes phosphatidylserine receptor. However, its nuclear localization and the fact that mAb 217 antibody still recognizes the phosphatidylserine receptor in mice lacking JMJD6, strongly suggest that it does not constitute the receptor for phosphatidylserine and is not involved in apoptotic cell removal.

Biophysicochemical properties

Kinetic parameters:

KM=39 µM for 2-oxoglutarate Ref.15

Sequence caution

The sequence AAH47003.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA25511.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processDifferentiation
mRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandIron
Metal-binding
RNA-binding
   Molecular functionChromatin regulator
Developmental protein
Dioxygenase
Oxidoreductase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

T cell differentiation in thymus

Inferred from electronic annotation. Source: Ensembl

cell surface receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

erythrocyte development

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

histone H3-R2 demethylation

Inferred from direct assay Ref.10. Source: BHF-UCL

histone H4-R3 demethylation

Inferred from direct assay Ref.10. Source: BHF-UCL

kidney development

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

macrophage activation

Inferred from electronic annotation. Source: Ensembl

peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine

Inferred from direct assay Ref.11. Source: UniProtKB

phosphatidylserine exposure on apoptotic cell surface

Inferred from electronic annotation. Source: Ensembl

recognition of apoptotic cell

Inferred from electronic annotation. Source: Ensembl

regulation of mRNA splicing, via spliceosome

Inferred from mutant phenotype Ref.11. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

retina development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

sprouting angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from direct assay Ref.12. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.12. Source: UniProtKB

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA binding

Traceable author statement Ref.12. Source: UniProtKB

histone demethylase activity (H3-R2 specific)

Inferred from direct assay Ref.10. Source: UniProtKB

histone demethylase activity (H4-R3 specific)

Inferred from direct assay Ref.10. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 24360279. Source: IntAct

iron ion binding

Inferred from direct assay Ref.16. Source: UniProtKB

peptidyl-lysine 5-dioxygenase activity

Inferred from direct assay Ref.11. Source: UniProtKB

receptor activity

Inferred from electronic annotation. Source: Ensembl

single-stranded RNA binding

Inferred from direct assay Ref.16. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6NYC1-1)

Also known as: Alpha;

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: Q6NYC1-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     361-402: Missing.
     403-403: R → RIRDTCGGRAHP
Isoform 3 (identifier: Q6NYC1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     403-403: R → RIRDTCGGRAHP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 403403Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6
PRO_0000129369

Regions

Domain141 – 305165JmjC
Motif6 – 105Nuclear localization signal 1 Ref.7
Motif91 – 955Nuclear localization signal 2 Ref.7
Motif141 – 1455Nuclear localization signal 3 Ref.7
Motif167 – 1704Nuclear localization signal 4 Ref.7
Motif373 – 3786Nuclear localization signal 5 Ref.7
Compositional bias340 – 36526Ser-rich

Sites

Metal binding1871Iron; catalytic
Metal binding1891Iron; catalytic
Metal binding2731Iron; catalytic
Binding site1841Substrate By similarity
Binding site19712-oxoglutarate
Binding site2041Substrate By similarity
Binding site28512-oxoglutarate

Natural variations

Alternative sequence361 – 40242Missing in isoform 2.
VSP_014022
Alternative sequence4031R → RIRDTCGGRAHP in isoform 2 and isoform 3.
VSP_014023

Experimental info

Mutagenesis1311Y → F: Abolishes 2-oxoglutarate-binding and enzyme activity. Ref.15
Mutagenesis1871H → A: Loss of catalytic activity; when associated with A-189 and A-273. Ref.10 Ref.11
Mutagenesis1891D → A: Loss of catalytic activity; when associated with A-187 and A-273. Ref.10 Ref.11
Mutagenesis2041K → A: Impairs enzyme activity without affecting 2-oxoglutarate-binding. Ref.15
Mutagenesis2311E → A: Impairs both hydroxylation activity and 2-oxoglutarate turnover assays. Ref.15
Mutagenesis2731H → A: Loss of catalytic activity; when associated with A-187 and A-189. Ref.10
Mutagenesis2851T → A: Impairs enzyme activity and 2-oxoglutarate-binding. Ref.15
Mutagenesis2871N → A: Impairs enzyme activity. Ref.15
Sequence conflict1361S → G in BAG51050. Ref.3

Secondary structure

........................................................................... 403
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 9C9AADA98B24B035

FASTA40346,462
        10         20         30         40         50         60 
MNHKSKKRIR EAKRSARPEL KDSLDWTRHN YYESFSLSPA AVADNVERAD ALQLSVEEFV 

        70         80         90        100        110        120 
ERYERPYKPV VLLNAQEGWS AQEKWTLERL KRKYRNQKFK CGEDNDGYSV KMKMKYYIEY 

       130        140        150        160        170        180 
MESTRDDSPL YIFDSSYGEH PKRRKLLEDY KVPKFFTDDL FQYAGEKRRP PYRWFVMGPP 

       190        200        210        220        230        240 
RSGTGIHIDP LGTSAWNALV QGHKRWCLFP TSTPRELIKV TRDEGGNQQD EAITWFNVIY 

       250        260        270        280        290        300 
PRTQLPTWPP EFKPLEILQK PGETVFVPGG WWHVVLNLDT TIAITQNFAS STNFPVVWHK 

       310        320        330        340        350        360 
TVRGRPKLSR KWYRILKQEH PELAVLADSV DLQESTGIAS DSSSDSSSSS SSSSSDSDSE 

       370        380        390        400 
CESGSEGDGT VHRRKKRRTC SMVGNGDTTS QDDCVSKERS SSR 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: 14154B874F1983DF
Show »

FASTA37243,109
Isoform 3 [UniParc].

Checksum: CD586580857C6C46
Show »

FASTA41447,626

References

« Hide 'large scale' references
[1]"Identification of an alternative form of phosphatidylserine receptor."
Izawa M., Takahashi M.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Stomach cancer.
[2]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
Tissue: Brain.
[3]"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. expand/collapse author list , 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] (ISOFORMS 1 AND 3).
Tissue: Brain and Embryo.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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).
Tissue: Skin and Uterus.
[7]"Nuclear localization of the phosphatidylserine receptor protein via multiple nuclear localization signals."
Cui P., Qin B., Liu N., Pan G., Pei D.
Exp. Cell Res. 293:154-163(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNALS.
[8]"Phosphatidylserine receptor cooperates with high-density lipoprotein receptor in recognition of apoptotic cells by thymic nurse cells."
Cao W.M., Murao K., Imachi H., Hiramine C., Abe H., Yu X., Dobashi H., Wong N.C.W., Takahara J., Ishida T.
J. Mol. Endocrinol. 32:497-505(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[9]"Phosphatidylserine receptor in chronic pancreatitis: evidence for a macrophage independent role."
Koeninger J., Balaz P., Wagner M., Shi X., Cima I., Zimmermann A., di Sebastiano P., Buechler M.W., Friess H.
Ann. Surg. 241:144-151(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"JMJD6 is a histone arginine demethylase."
Chang B., Chen Y., Zhao Y., Bruick R.K.
Science 318:444-447(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS HISTONE DEMETHYLASE, MUTAGENESIS OF HIS-187; ASP-189 AND HIS-273.
[11]"Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing."
Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B., Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M., Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J., Boettger A.
Science 325:90-93(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS LYSYL-HYDROXYLASE, COFACTOR, INTERACTION WITH LUC7L2; LUC7L3 AND U2AF2, MUTAGENESIS OF HIS-187 AND ASP-189.
[12]"Analysis of Jmjd6 cellular localization and testing for its involvement in histone demethylation."
Hahn P., Wegener I., Burrells A., Bose J., Wolf A., Erck C., Butler D., Schofield C.J., Bottger A., Lengeling A.
PLoS ONE 5:E13769-E13769(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, RNA-BINDING, FUNCTION.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3."
Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W., Howley P.M.
Mol. Cell. Biol. 31:2641-2652(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BRD4.
[15]"Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6."
Mantri M., Krojer T., Bagg E.A., Webby C.J., Butler D.S., Kochan G., Kavanagh K.L., Oppermann U., McDonough M.A., Schofield C.J.
J. Mol. Biol. 401:211-222(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-335 IN COMPLEX WITH NICKEL IONS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-131; LYS-204; GLU-231; THR-285 AND ASN-287.
[16]"Interaction of JMJD6 with single-stranded RNA."
Hong X., Zang J., White J., Wang C., Pan C.H., Zhao R., Murphy R.C., Dai S., Henson P., Kappler J.W., Hagman J., Zhang G.
Proc. Natl. Acad. Sci. U.S.A. 107:14568-14572(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-334 IN COMPLEX WITH IRON IONS AND 2-OXOGLUTARATE, POSSIBLE FUNCTION, RNA-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB073711 mRNA. Translation: BAC16755.1.
AB011157 mRNA. Translation: BAA25511.1. Different initiation.
AK021780 mRNA. Translation: BAG51050.1.
AK294816 mRNA. Translation: BAG57932.1.
AC005837 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89434.1.
BC047003 mRNA. Translation: AAH47003.1. Different initiation.
BC066654 mRNA. Translation: AAH66654.1.
RefSeqNP_001074930.1. NM_001081461.1.
NP_055982.2. NM_015167.2.
UniGeneHs.514505.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3K2OX-ray1.75A/B1-335[»]
3LD8X-ray2.70A1-334[»]
3LDBX-ray2.70A1-334[»]
ProteinModelPortalQ6NYC1.
SMRQ6NYC1. Positions 1-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116817. 51 interactions.
IntActQ6NYC1. 29 interactions.
MINTMINT-3086431.
STRING9606.ENSP00000394085.

PTM databases

PhosphoSiteQ6NYC1.

Polymorphism databases

DMDM67461014.

Proteomic databases

PaxDbQ6NYC1.
PRIDEQ6NYC1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000397625; ENSP00000380750; ENSG00000070495. [Q6NYC1-1]
ENST00000445478; ENSP00000394085; ENSG00000070495. [Q6NYC1-3]
GeneID23210.
KEGGhsa:23210.
UCSCuc002jsn.1. human. [Q6NYC1-3]
uc002jso.3. human. [Q6NYC1-1]

Organism-specific databases

CTD23210.
GeneCardsGC17M074708.
HGNCHGNC:19355. JMJD6.
HPACAB004548.
MIM604914. gene.
neXtProtNX_Q6NYC1.
PharmGKBPA162392513.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG124833.
HOGENOMHOG000265824.
HOVERGENHBG054774.
InParanoidQ6NYC1.
KOK11323.
PhylomeDBQ6NYC1.
TreeFamTF314988.

Gene expression databases

ArrayExpressQ6NYC1.
BgeeQ6NYC1.
CleanExHS_JMJD6.
GenevestigatorQ6NYC1.

Family and domain databases

InterProIPR003347. JmjC_dom.
[Graphical view]
PfamPF02373. JmjC. 1 hit.
[Graphical view]
SMARTSM00558. JmjC. 1 hit.
[Graphical view]
PROSITEPS51184. JMJC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ6NYC1.
GeneWikiJMJD6.
GenomeRNAi23210.
NextBio44753.
PROQ6NYC1.
SOURCESearch...

Entry information

Entry nameJMJD6_HUMAN
AccessionPrimary (citable) accession number: Q6NYC1
Secondary accession number(s): B3KMN8 expand/collapse secondary AC list , B4DGX1, Q86VY0, Q8IUM5, Q9Y4E2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM