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Protein

Lysine-specific demethylase 8

Gene

Kdm8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Histone demethylase required for G2/M phase cell cycle progression. Specifically demethylates dimethylated 'Lys-36' (H3K36me2) of histone H3, an epigenetic repressive mark, thereby acting as a transcription activator. Regulates expression of CCNA1 (cyclin-A1) (By similarity).By similarity

Catalytic activityi

Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2.
Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2.

Cofactori

Fe2+By similarityNote: Binds 1 Fe2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi319 – 3191Iron; catalyticPROSITE-ProRule annotation
Metal bindingi321 – 3211Iron; catalyticPROSITE-ProRule annotation
Metal bindingi398 – 3981Iron; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific demethylase 8 (EC:1.14.11.27)
Alternative name(s):
JmjC domain-containing protein 5
Jumonji domain-containing protein 5
Gene namesi
Name:Kdm8
Synonyms:Jmjd5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1924285. Kdm8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Lysine-specific demethylase 8PRO_0000292011Add
BLAST

Proteomic databases

EPDiQ9CXT6.
MaxQBiQ9CXT6.
PaxDbiQ9CXT6.
PRIDEiQ9CXT6.

PTM databases

PhosphoSiteiQ9CXT6.

Expressioni

Gene expression databases

BgeeiQ9CXT6.
CleanExiMM_JMJD5.
ExpressionAtlasiQ9CXT6. baseline and differential.
GenevisibleiQ9CXT6. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033010.

Structurei

3D structure databases

ProteinModelPortaliQ9CXT6.
SMRiQ9CXT6. Positions 182-414.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini269 – 414146JmjCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 JmjC domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2132. Eukaryota.
ENOG410XQDR. LUCA.
GeneTreeiENSGT00530000062914.
HOVERGENiHBG105493.
InParanoidiQ9CXT6.
KOiK10277.
OMAiPHSKEDL.
OrthoDBiEOG7KWSJQ.
PhylomeDBiQ9CXT6.
TreeFamiTF315056.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9CXT6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEDTTEPLV GSSTLWKELR TLLPDKEEEL KLDLGEKVDR SVAALLRQAV
60 70 80 90 100
GLFYAGHWQG CLQASEAVLD YSWEKLNTGP WRDVDKEWRR VYSFGCLLKA
110 120 130 140 150
LCLCQAPQKA TTVVEALRVC DMGLLMGAAI LEDILLKVVA VLQTHQLPGK
160 170 180 190 200
QPARGPHQDQ PATKKAKCDA SPAPDVMLER MVPRLRCPPL QYFKQHFLVP
210 220 230 240 250
GRPVILEGVA DHWPCMKKWS LQYIQEIAGC RTVPVEVGSR YTDEDWSQTL
260 270 280 290 300
MTVDEFIQKF ILSEAKDVGY LAQHQLFDQI PELKRDISIP DYCCLGNGEE
310 320 330 340 350
EEITINAWFG PQGTISPLHQ DPQQNFLVQV LGRKYIRLYS PQESEAVYPH
360 370 380 390 400
ETHILHNTSQ VDVENPDLEK FPKFTEAPFL SCILSPGDTL FIPAKYWHYV
410
RSLDLSFSVS FWWS
Length:414
Mass (Da):47,145
Last modified:June 1, 2001 - v1
Checksum:i4C794D0F5E9EC996
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014006 mRNA. Translation: BAB29111.1.
BC024807 mRNA. Translation: AAH24807.1.
CCDSiCCDS21821.1.
RefSeqiNP_084118.1. NM_029842.5.
UniGeneiMm.307239.

Genome annotation databases

EnsembliENSMUST00000033010; ENSMUSP00000033010; ENSMUSG00000030752.
GeneIDi77035.
KEGGimmu:77035.
UCSCiuc009jpz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014006 mRNA. Translation: BAB29111.1.
BC024807 mRNA. Translation: AAH24807.1.
CCDSiCCDS21821.1.
RefSeqiNP_084118.1. NM_029842.5.
UniGeneiMm.307239.

3D structure databases

ProteinModelPortaliQ9CXT6.
SMRiQ9CXT6. Positions 182-414.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033010.

PTM databases

PhosphoSiteiQ9CXT6.

Proteomic databases

EPDiQ9CXT6.
MaxQBiQ9CXT6.
PaxDbiQ9CXT6.
PRIDEiQ9CXT6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033010; ENSMUSP00000033010; ENSMUSG00000030752.
GeneIDi77035.
KEGGimmu:77035.
UCSCiuc009jpz.2. mouse.

Organism-specific databases

CTDi79831.
MGIiMGI:1924285. Kdm8.

Phylogenomic databases

eggNOGiKOG2132. Eukaryota.
ENOG410XQDR. LUCA.
GeneTreeiENSGT00530000062914.
HOVERGENiHBG105493.
InParanoidiQ9CXT6.
KOiK10277.
OMAiPHSKEDL.
OrthoDBiEOG7KWSJQ.
PhylomeDBiQ9CXT6.
TreeFamiTF315056.

Miscellaneous databases

NextBioi346338.
PROiQ9CXT6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CXT6.
CleanExiMM_JMJD5.
ExpressionAtlasiQ9CXT6. baseline and differential.
GenevisibleiQ9CXT6. MM.

Family and domain databases

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

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiKDM8_MOUSE
AccessioniPrimary (citable) accession number: Q9CXT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.