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Q6NYC1

- JMJD6_HUMAN

UniProt

Q6NYC1 - JMJD6_HUMAN

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Protein

Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6

Gene

JMJD6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Cofactori

Fe2+1 PublicationNote: Binds 1 Fe(2+) ion per subunit.1 Publication

Kineticsi

  1. KM=39 µM for 2-oxoglutarate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei184 – 1841SubstrateBy similarity
Metal bindingi187 – 1871Iron; catalytic
Metal bindingi189 – 1891Iron; catalytic
Binding sitei197 – 19712-oxoglutarate1 Publication
Binding sitei204 – 2041SubstrateBy similarity
Metal bindingi273 – 2731Iron; catalytic
Binding sitei285 – 28512-oxoglutarate1 Publication

GO - Molecular functioni

  1. histone demethylase activity (H3-R2 specific) Source: UniProtKB
  2. histone demethylase activity (H4-R3 specific) Source: UniProtKB
  3. identical protein binding Source: IntAct
  4. iron ion binding Source: UniProtKB
  5. peptidyl-lysine 5-dioxygenase activity Source: UniProtKB
  6. receptor activity Source: Ensembl
  7. RNA binding Source: UniProtKB
  8. single-stranded RNA binding Source: UniProtKB

GO - Biological processi

  1. cell surface receptor signaling pathway Source: Ensembl
  2. erythrocyte development Source: Ensembl
  3. heart development Source: Ensembl
  4. histone H3-R2 demethylation Source: BHF-UCL
  5. histone H4-R3 demethylation Source: BHF-UCL
  6. kidney development Source: Ensembl
  7. lung development Source: Ensembl
  8. macrophage activation Source: Ensembl
  9. mRNA processing Source: UniProtKB-KW
  10. peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine Source: UniProtKB
  11. recognition of apoptotic cell Source: Ensembl
  12. regulation of mRNA splicing, via spliceosome Source: UniProtKB
  13. regulation of transcription, DNA-templated Source: UniProtKB-KW
  14. retina development in camera-type eye Source: Ensembl
  15. RNA splicing Source: UniProtKB-KW
  16. sprouting angiogenesis Source: UniProtKB
  17. T cell differentiation in thymus Source: Ensembl
  18. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Differentiation, mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:JMJD6
Synonyms:KIAA0585, PTDSR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:19355. JMJD6.

Subcellular locationi

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.

GO - Cellular componenti

  1. nucleolus Source: UniProtKB
  2. nucleoplasm Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311Y → F: Abolishes 2-oxoglutarate-binding and enzyme activity. 1 Publication
Mutagenesisi187 – 1871H → A: Loss of catalytic activity; when associated with A-189 and A-273. 2 Publications
Mutagenesisi189 – 1891D → A: Loss of catalytic activity; when associated with A-187 and A-273. 2 Publications
Mutagenesisi204 – 2041K → A: Impairs enzyme activity without affecting 2-oxoglutarate-binding. 1 Publication
Mutagenesisi231 – 2311E → A: Impairs both hydroxylation activity and 2-oxoglutarate turnover assays. 1 Publication
Mutagenesisi273 – 2731H → A: Loss of catalytic activity; when associated with A-187 and A-189. 1 Publication
Mutagenesisi285 – 2851T → A: Impairs enzyme activity and 2-oxoglutarate-binding. 1 Publication
Mutagenesisi287 – 2871N → A: Impairs enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA162392513.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 403403Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6PRO_0000129369Add
BLAST

Proteomic databases

MaxQBiQ6NYC1.
PaxDbiQ6NYC1.
PRIDEiQ6NYC1.

PTM databases

PhosphoSiteiQ6NYC1.

Expressioni

Tissue specificityi

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.3 Publications

Inductioni

Up-regulated upon cytokine treatment, but not upon TNF treatment.1 Publication

Gene expression databases

BgeeiQ6NYC1.
CleanExiHS_JMJD6.
ExpressionAtlasiQ6NYC1. baseline and differential.
GenevestigatoriQ6NYC1.

Organism-specific databases

HPAiCAB004548.

Interactioni

Subunit structurei

Interacts with LUC7L2, LUC7L3 and U2AF2/U2AF65. Interacts with BRD4.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-8464037,EBI-8464037
BRD4O6088510EBI-8464037,EBI-723869
CDK9P507505EBI-8464037,EBI-1383449
PRPF38AQ8NAV12EBI-8464037,EBI-715374
U2AF1Q010812EBI-8464037,EBI-632461
ZCCHC17Q9NP642EBI-8464037,EBI-746345

Protein-protein interaction databases

BioGridi116817. 58 interactions.
DIPiDIP-60686N.
IntActiQ6NYC1. 29 interactions.
MINTiMINT-3086431.
STRINGi9606.ENSP00000394085.

Structurei

Secondary structure

1
403
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1614Combined sources
Helixi23 – 275Combined sources
Helixi31 – 344Combined sources
Helixi39 – 413Combined sources
Beta strandi48 – 503Combined sources
Helixi51 – 533Combined sources
Helixi56 – 627Combined sources
Turni63 – 675Combined sources
Beta strandi70 – 745Combined sources
Turni75 – 784Combined sources
Helixi81 – 844Combined sources
Helixi87 – 937Combined sources
Beta strandi98 – 1036Combined sources
Beta strandi109 – 1135Combined sources
Helixi114 – 12310Combined sources
Beta strandi132 – 1354Combined sources
Helixi137 – 1393Combined sources
Helixi143 – 1497Combined sources
Helixi154 – 1563Combined sources
Helixi160 – 1645Combined sources
Turni166 – 1683Combined sources
Beta strandi173 – 1786Combined sources
Beta strandi183 – 1875Combined sources
Helixi190 – 1923Combined sources
Beta strandi194 – 2029Combined sources
Beta strandi204 – 2096Combined sources
Helixi215 – 2184Combined sources
Helixi222 – 2254Combined sources
Helixi226 – 2283Combined sources
Helixi232 – 2387Combined sources
Helixi240 – 2445Combined sources
Helixi250 – 2523Combined sources
Beta strandi255 – 2595Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi272 – 2798Combined sources
Beta strandi281 – 2888Combined sources
Turni291 – 2933Combined sources
Helixi294 – 30411Combined sources
Helixi306 – 31914Combined sources
Helixi321 – 33313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3K2OX-ray1.75A/B2-335[»]
3LD8X-ray2.70A1-334[»]
3LDBX-ray2.70A1-334[»]
ProteinModelPortaliQ6NYC1.
SMRiQ6NYC1. Positions 1-335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6NYC1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini141 – 305165JmjCPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi6 – 105Nuclear localization signal 11 Publication
Motifi91 – 955Nuclear localization signal 21 Publication
Motifi141 – 1455Nuclear localization signal 31 Publication
Motifi167 – 1704Nuclear localization signal 41 Publication
Motifi373 – 3786Nuclear localization signal 51 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi340 – 36526Ser-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the JMJD6 family.Curated
Contains 1 JmjC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG124833.
GeneTreeiENSGT00530000063579.
HOGENOMiHOG000265824.
HOVERGENiHBG054774.
InParanoidiQ6NYC1.
KOiK11323.
OMAiANLIAIE.
PhylomeDBiQ6NYC1.
TreeFamiTF314988.

Family and domain databases

InterProiIPR003347. JmjC_dom.
[Graphical view]
PfamiPF02373. JmjC. 1 hit.
[Graphical view]
SMARTiSM00558. JmjC. 1 hit.
[Graphical view]
PROSITEiPS51184. JMJC. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6NYC1-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MNHKSKKRIR EAKRSARPEL KDSLDWTRHN YYESFSLSPA AVADNVERAD
60 70 80 90 100
ALQLSVEEFV ERYERPYKPV VLLNAQEGWS AQEKWTLERL KRKYRNQKFK
110 120 130 140 150
CGEDNDGYSV KMKMKYYIEY MESTRDDSPL YIFDSSYGEH PKRRKLLEDY
160 170 180 190 200
KVPKFFTDDL FQYAGEKRRP PYRWFVMGPP RSGTGIHIDP LGTSAWNALV
210 220 230 240 250
QGHKRWCLFP TSTPRELIKV TRDEGGNQQD EAITWFNVIY PRTQLPTWPP
260 270 280 290 300
EFKPLEILQK PGETVFVPGG WWHVVLNLDT TIAITQNFAS STNFPVVWHK
310 320 330 340 350
TVRGRPKLSR KWYRILKQEH PELAVLADSV DLQESTGIAS DSSSDSSSSS
360 370 380 390 400
SSSSSDSDSE CESGSEGDGT VHRRKKRRTC SMVGNGDTTS QDDCVSKERS

SSR
Length:403
Mass (Da):46,462
Last modified:July 5, 2004 - v1
Checksum:i9C9AADA98B24B035
GO
Isoform 2 (identifier: Q6NYC1-2) [UniParc]FASTAAdd to Basket

Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     361-402: Missing.
     403-403: R → RIRDTCGGRAHP

Show »
Length:372
Mass (Da):43,109
Checksum:i14154B874F1983DF
GO
Isoform 3 (identifier: Q6NYC1-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:414
Mass (Da):47,626
Checksum:iCD586580857C6C46
GO

Sequence cautioni

The sequence AAH47003.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA25511.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti136 – 1361S → G in BAG51050. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei361 – 40242Missing in isoform 2. 1 PublicationVSP_014022Add
BLAST
Alternative sequencei403 – 4031R → RIRDTCGGRAHP in isoform 2 and isoform 3. 3 PublicationsVSP_014023

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS42383.1. [Q6NYC1-3]
CCDS42384.1. [Q6NYC1-1]
RefSeqiNP_001074930.1. NM_001081461.1. [Q6NYC1-3]
NP_055982.2. NM_015167.2. [Q6NYC1-1]
UniGeneiHs.514505.

Genome annotation databases

EnsembliENST00000397625; ENSP00000380750; ENSG00000070495. [Q6NYC1-1]
ENST00000445478; ENSP00000394085; ENSG00000070495. [Q6NYC1-3]
GeneIDi23210.
KEGGihsa:23210.
UCSCiuc002jsn.1. human. [Q6NYC1-3]
uc002jso.3. human. [Q6NYC1-1]

Polymorphism databases

DMDMi67461014.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS42383.1. [Q6NYC1-3 ]
CCDS42384.1. [Q6NYC1-1 ]
RefSeqi NP_001074930.1. NM_001081461.1. [Q6NYC1-3 ]
NP_055982.2. NM_015167.2. [Q6NYC1-1 ]
UniGenei Hs.514505.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3K2O X-ray 1.75 A/B 2-335 [» ]
3LD8 X-ray 2.70 A 1-334 [» ]
3LDB X-ray 2.70 A 1-334 [» ]
ProteinModelPortali Q6NYC1.
SMRi Q6NYC1. Positions 1-335.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116817. 58 interactions.
DIPi DIP-60686N.
IntActi Q6NYC1. 29 interactions.
MINTi MINT-3086431.
STRINGi 9606.ENSP00000394085.

PTM databases

PhosphoSitei Q6NYC1.

Polymorphism databases

DMDMi 67461014.

Proteomic databases

MaxQBi Q6NYC1.
PaxDbi Q6NYC1.
PRIDEi Q6NYC1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000397625 ; ENSP00000380750 ; ENSG00000070495 . [Q6NYC1-1 ]
ENST00000445478 ; ENSP00000394085 ; ENSG00000070495 . [Q6NYC1-3 ]
GeneIDi 23210.
KEGGi hsa:23210.
UCSCi uc002jsn.1. human. [Q6NYC1-3 ]
uc002jso.3. human. [Q6NYC1-1 ]

Organism-specific databases

CTDi 23210.
GeneCardsi GC17M074708.
HGNCi HGNC:19355. JMJD6.
HPAi CAB004548.
MIMi 604914. gene.
neXtProti NX_Q6NYC1.
PharmGKBi PA162392513.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG124833.
GeneTreei ENSGT00530000063579.
HOGENOMi HOG000265824.
HOVERGENi HBG054774.
InParanoidi Q6NYC1.
KOi K11323.
OMAi ANLIAIE.
PhylomeDBi Q6NYC1.
TreeFami TF314988.

Miscellaneous databases

EvolutionaryTracei Q6NYC1.
GeneWikii JMJD6.
GenomeRNAii 23210.
NextBioi 44753.
PROi Q6NYC1.
SOURCEi Search...

Gene expression databases

Bgeei Q6NYC1.
CleanExi HS_JMJD6.
ExpressionAtlasi Q6NYC1. baseline and differential.
Genevestigatori Q6NYC1.

Family and domain databases

InterProi IPR003347. JmjC_dom.
[Graphical view ]
Pfami PF02373. JmjC. 1 hit.
[Graphical view ]
SMARTi SM00558. JmjC. 1 hit.
[Graphical view ]
PROSITEi PS51184. JMJC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-334 IN COMPLEX WITH IRON IONS AND 2-OXOGLUTARATE, POSSIBLE FUNCTION, RNA-BINDING.

Entry informationi

Entry nameiJMJD6_HUMAN
AccessioniPrimary (citable) accession number: Q6NYC1
Secondary accession number(s): B3KMN8
, B4DGX1, Q86VY0, Q8IUM5, Q9Y4E2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 106 of the entry and version 1 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

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.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3