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Q62315 (JARD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Protein Jumonji
Alternative name(s):
Jumonji/ARID domain-containing protein 2
Gene names
Name:Jarid2
Synonyms:Jmj
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1234 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulator of histone methyltransferase complexes that plays an essential role in embryonic development, including heart and liver development, neural tube fusion process and hematopoiesis. Acts by modulating histone methyltransferase activity and promoting the recruitment of histone methyltransferase complexes to their target genes. Binds DNA and mediates the recruitment of the PRC2 complex to target genes in embryonic stem cells. Does not have histone demethylase activity but regulates activity of various histone methyltransferase complexes. In embryonic stem cells, it associates with the PRC2 complex and inhibits trimethylation of 'Lys-27' of histone H3 (H3K27me3) by the PRC2 complex, thereby playing a key role in differentiation of embryonic stem cells and normal development. In cardiac cells, it is required to repress expression of cyclin-D1 (CCND1) by activating methylation of 'Lys-9' of histone H3 (H3K9me) by the GLP1/EHMT1 and G9a/EHMT2 histone methyltransferases. Also acts as a transcriptional repressor of ANF via its interaction with GATA4 and NKX2-5. Participates in the negative regulation of cell proliferation signaling. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Subunit structure

Associates with the PRC2 complex, which includes EED, EZH1, EZH2, SUZ12, RBBP4 and AEBP2; JARID2 is probably not a core component of the PRC2 complex and associates to PRC2 via its interaction with SUZ12. Associates with a histone methyltransferase complex containing GLP1/EHMT1 and G9a/EHMT2. Interacts with SUZ12; the interaction is direct. Interacts with GATA4 (via the N-terminal region). Interacts with NKX2-5 (via the C-terminal region). Interacts with RB1. Interacts with ZNF496. Ref.11 Ref.12 Ref.13 Ref.15

Subcellular location

Nucleus. Note: Colocalizes with the PRC2 complex on chromatin. Ref.7 Ref.8 Ref.14 Ref.15

Tissue specificity

Widely expressed in embryos. In adults, expressed at high levels in heart, skeletal muscle, brain and thymus. Ref.8

Domain

The ARID domain is required to target the PRC2 complex to its target genes. Ref.15 Ref.17

The GSGFP motif is required for the interaction with SUZ12. Ref.15 Ref.17

Disruption phenotype

Embryos die before 15.5 dpc and show severe cardiac morphological defects and altered heart-specific gene expression. Some, but not all, of the homozygotes develop an abnormal groove in a region just anterior to the midbrain-hindbrain boundary on the neural plate at 8-8.5 dpc and show a defect in neural tube closure in the midbrain region. Variable phenotypes are observed depending on the genetic backgrounds: mutant mice with a C57BL/6J X 129S1/Sv genetic background die upon birth and show cardiac defects such as ventricular septal defects, double-outlet right ventricle, and thin ventricular wall at later embryonic stages. In addition to the thin ventricular wall, mutant embryos with a pure BALB/c background show deficient cell growth in the liver, thymus, and spleen. In contrast, mutant mice with a C3H/He genetic background die at 11.5 dpc, which exhibit hyperplasia and increased cyclin-D1 (CCND1) expression in the trabecular layer of the ventricle at 10.5 dpc. Ref.1 Ref.5 Ref.6 Ref.8

Miscellaneous

'Jumonji' means 'cruciform' in Japanese.

Sequence similarities

Belongs to the JARID2 family.

Contains 1 ARID domain.

Contains 1 JmjC domain.

Contains 1 JmjN domain.

Caution

Despite the presence of a JmjC domain, lacks the conserved residues that bind the iron cofactor, explaining the absence of histone methyltransferase activity.

Sequence caution

The sequence BAE27780.1 differs from that shown. Reason: Frameshift at position 11.

The sequence EDL41007.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processDifferentiation
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   Molecular functionChromatin regulator
Developmental protein
Repressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

liver development

Inferred from mutant phenotype Ref.5. Source: MGI

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.13. Source: MGI

negative regulation of histone methylation

Inferred from direct assay Ref.15Ref.14. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction Ref.13. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.16. Source: UniProtKB

positive regulation of histone H3-K9 methylation

Inferred from direct assay Ref.16. Source: UniProtKB

regulation of cell proliferation

Inferred from mutant phenotype PubMed 11301191. Source: MGI

spleen development

Inferred from mutant phenotype Ref.5. Source: MGI

stem cell differentiation

Inferred from mutant phenotype Ref.15Ref.14Ref.17. Source: UniProtKB

thymus development

Inferred from mutant phenotype Ref.5. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentESC/E(Z) complex

Inferred from electronic annotation. Source: Ensembl

histone methyltransferase complex

Inferred from direct assay Ref.16. Source: UniProtKB

nucleus

Inferred from direct assay Ref.15Ref.14. Source: UniProtKB

   Molecular_functionDNA binding

Traceable author statement Ref.17. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.15Ref.14. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12Ref.16Ref.15. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q62315-1)

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: Q62315-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MSKERPKRNI...GLAGSLKAVN → MAAPRVCQVQFLVAYLEEPGIE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12341234Protein Jumonji
PRO_0000200592

Regions

Domain555 – 59642JmjN
Domain619 – 71193ARID
Domain882 – 1046165JmjC
Motif104 – 1107Nuclear localization signal Ref.10
Motif872 – 8765GSGFP motif

Amino acid modifications

Modified residue781Phosphoserine By similarity
Modified residue3781N6-acetyllysine By similarity
Modified residue4491Phosphoserine By similarity

Natural variations

Alternative sequence1 – 6060MSKER…LKAVN → MAAPRVCQVQFLVAYLEEPG IE in isoform 2.
VSP_038758

Experimental info

Mutagenesis106 – 1072RK → AA: Leads to cytoplasmic relocalization. Ref.10
Sequence conflict8731S → G in BAE37641. Ref.2
Sequence conflict10961L → Q in AAH03374. Ref.4

Secondary structure

............... 1234
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1997. Version 1.
Checksum: B56E172C5E5745B5

FASTA1,234137,445
        10         20         30         40         50         60 
MSKERPKRNI IQKKYDDSDG IPWSEERVVR KVLYLSLKEF KNAQKRQHGE GLAGSLKAVN 

        70         80         90        100        110        120 
GLLGNAQAKA LGPASEQSEN EKDDASQVSS TSNDVSSSDF EEGPSRKRPR LQAQRKFAQS 

       130        140        150        160        170        180 
QPNSPSTTPV KIVEPLLPPP ATQISDLSKR KPKTEDFLTF LCLRGSPALP NSMVYFGSSQ 

       190        200        210        220        230        240 
DEEDVEEEDD ETEDVKATTN NASSSCQSTP RKGKTHKHVH NGHVFNGSSR SAREKEPAHK 

       250        260        270        280        290        300 
HRSKEATPGK EKHSEPRADS RREQASGAQP TAASAAASSA KGLAANHQPP PSHRSAQDLR 

       310        320        330        340        350        360 
KQVSKVNGVT RMSSLGAGTN SAKKIREVRP SPSKTVKYTA TVTKGTVTYT KAKRELVKET 

       370        380        390        400        410        420 
KPNHHKPSSA VNHTISGKTE SSNAKTRKQV LSLGGASKST GPAASGLKAS SRLNPKSCTK 

       430        440        450        460        470        480 
EVGGRQLREG LRNSKRRLEE AQQVDKPQSP PKKMKGVAGN AEAPGKKASA ASGEKSLLNG 

       490        500        510        520        530        540 
HVKKEVPERS LERNRPKRAA AGKNMLGKQA HGKTEGTPCE NRSTSQPESS HKPHDPQGKP 

       550        560        570        580        590        600 
EKGSGKSGWA AMDEIPVLRP SAKEFHDPLI YIESVRAQVE KYGMCRVIPP PDWRPECKLN 

       610        620        630        640        650        660 
DEMRFVTQIQ HIHKLGRRWG PNVQRLACIK KHLRSQGITM DELPLIGGCE LDLACFFRLI 

       670        680        690        700        710        720 
NEMGGMQQVT DLKKWNKLAD MLRIPKTAQD RLAKLQEAYC QYLLSYDSLS PEEHRRLEKE 

       730        740        750        760        770        780 
VLMEKEILEK RKGPLEGHTE SDHHKFHSLP RFEPKNGLVH GVTPRNGFRS KLKEVGRAPL 

       790        800        810        820        830        840 
KTGRRRLFAQ EKEVVKEEEE DKGVLNDFHK CIYKGRSVSL TTFYRTARNI MNMCFSKEPA 

       850        860        870        880        890        900 
PAEIEQEYWR LVEEKDCHVA VHCGKVDTNT HGSGFPVGKS EPFSRHGWNL TVLPNNTGSI 

       910        920        930        940        950        960 
LRHLGAVPGV TIPWLNIGMV FSTSCWSRDQ NHLPYIDYLH TGADCIWYCI PAEEENKLED 

       970        980        990       1000       1010       1020 
VVHTLLQGNG TPGLQMLESN VMISPEVLCK KGIKVHRTVQ QSGQFVVCFP GSFVSKVCCG 

      1030       1040       1050       1060       1070       1080 
YNVSETVHFA TTQWTSMGFE TAKEMKRRHI AKPFSMEKLL YQIAQAEAKK ENGPTLSTIS 

      1090       1100       1110       1120       1130       1140 
ALLDELRDTE LRQRRLLFEA GLHSSARYGS HDGNSTVADG KKKPRKWLQL ETSERRCQIC 

      1150       1160       1170       1180       1190       1200 
QHLCYLSMVV QENENVVFCL ECALRHVEKQ KSCRGLKLMY RYDEEQIISL VNQICGKVSG 

      1210       1220       1230 
KHGGIENCLN KPTPKRGPRK RATVDVPPSR LPSS 

« Hide

Isoform 2 [UniParc].

Checksum: DE32BC3F7733C6F5
Show »

FASTA1,196132,938

References

« Hide 'large scale' references
[1]"Gene trap capture of a novel mouse gene, jumonji, required for neural tube formation."
Takeuchi T., Yamazaki Y., Katoh-Fukui Y., Tsuchiya R., Kondo S., Motoyama J., Higashinakagawa T.
Genes Dev. 9:1211-1222(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DISRUPTION PHENOTYPE.
Strain: 129/Ola.
[2]"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. expand/collapse author list , 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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1068 (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Embryo, Placenta and Spinal cord.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: C57BL/6 and Czech II.
Tissue: Brain and Mammary gland.
[5]"Organogenesis of the liver, thymus and spleen is affected in jumonji mutant mice."
Motoyama J., Kitajima K., Kojima M., Kondo S., Takeuchi T.
Mech. Dev. 66:27-37(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[6]"jumonji gene is essential for the neurulation and cardiac development of mouse embryos with a C3H/He background."
Takeuchi T., Kojima M., Nakajima K., Kondo S.
Mech. Dev. 86:29-38(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[7]"Jumonji is a nuclear protein that participates in the negative regulation of cell growth."
Toyoda M., Kojima M., Takeuchi T.
Biochem. Biophys. Res. Commun. 274:332-336(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Jumonji, a nuclear protein that is necessary for normal heart development."
Lee Y., Song A.J., Baker R., Micales B., Conway S.J., Lyons G.E.
Circ. Res. 86:932-938(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[9]"jumonji downregulates cardiac cell proliferation by repressing cyclin D1 expression."
Toyoda M., Shirato H., Nakajima K., Kojima M., Takahashi M., Kubota M., Suzuki-Migishima R., Motegi Y., Yokoyama M., Takeuchi T.
Dev. Cell 5:85-97(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"JUMONJI, a critical factor for cardiac development, functions as a transcriptional repressor."
Kim T.-G., Kraus J.C., Chen J., Lee Y.
J. Biol. Chem. 278:42247-42255(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 106-ARG-LYS-107.
[11]"Jumonji represses atrial natriuretic factor gene expression by inhibiting transcriptional activities of cardiac transcription factors."
Kim T.-G., Chen J., Sadoshima J., Lee Y.
Mol. Cell. Biol. 24:10151-10160(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH GATA4 AND NKX2-5.
[12]"Characterization of zinc finger protein 496 that interacts with Jumonji/JARID2."
Mysliwiec M.R., Kim T.G., Lee Y.
FEBS Lett. 581:2633-2640(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF496.
[13]"Jumonji regulates cardiomyocyte proliferation via interaction with retinoblastoma protein."
Jung J., Kim T.G., Lyons G.E., Kim H.R., Lee Y.
J. Biol. Chem. 280:30916-30923(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RB1.
[14]"Jumonji modulates polycomb activity and self-renewal versus differentiation of stem cells."
Shen X., Kim W., Fujiwara Y., Simon M.D., Liu Y., Mysliwiec M.R., Yuan G.C., Lee Y., Orkin S.H.
Cell 139:1303-1314(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, LACK OF HISTONE DEMETHYLASE ACTIVITY, SUBCELLULAR LOCATION, ASSOCIATION WITH THE PRC2 COMPLEX.
[15]"Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and target gene occupancy in pluripotent cells."
Peng J.C., Valouev A., Swigut T., Zhang J., Zhao Y., Sidow A., Wysocka J.
Cell 139:1290-1302(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE PRC2 COMPLEX, DOMAIN GSGFP MOTIF, INTERACTION WITH SUZ12.
[16]"A jumonji (Jarid2) protein complex represses cyclin D1 expression by methylation of histone H3-K9."
Shirato H., Ogawa S., Nakajima K., Inagawa M., Kojima M., Tachibana M., Shinkai Y., Takeuchi T.
J. Biol. Chem. 284:733-739(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"JARID2 regulates binding of the Polycomb repressive complex 2 to target genes in ES cells."
Pasini D., Cloos P.A., Walfridsson J., Olsson L., Bukowski J.P., Johansen J.V., Bak M., Tommerup N., Rappsilber J., Helin K.
Nature 464:306-310(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DNA-BINDING, DOMAIN ARID.
[18]"Solution structure of the AT-rich interaction domain of Jumonji/JARID2."
Kusunoki H., Takeuchi T., Kohno T.
Proteins 76:1023-1028(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 615-730.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D31967 mRNA. Translation: BAA06736.1.
AK045214 mRNA. Translation: BAC32264.1.
AK147226 mRNA. Translation: BAE27780.1. Frameshift.
AK164134 mRNA. Translation: BAE37641.1.
CH466546 Genomic DNA. Translation: EDL41007.1. Sequence problems.
BC003374 mRNA. Translation: AAH03374.1.
BC052444 mRNA. Translation: AAH52444.1.
BC060695 mRNA. Translation: AAH60695.1.
CCDSCCDS36646.1. [Q62315-1]
PIRT30254.
RefSeqNP_001191972.1. NM_001205043.1. [Q62315-1]
NP_001191973.1. NM_001205044.1. [Q62315-1]
NP_068678.1. NM_021878.3. [Q62315-1]
XP_006516918.1. XM_006516855.1. [Q62315-1]
XP_006516919.1. XM_006516856.1. [Q62315-1]
XP_006516920.1. XM_006516857.1. [Q62315-1]
XP_006516921.1. XM_006516858.1. [Q62315-2]
XP_006516922.1. XM_006516859.1.
XP_006516923.1. XM_006516860.1.
UniGeneMm.25059.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RQ5NMR-A615-730[»]
ProteinModelPortalQ62315.
SMRQ62315. Positions 552-730, 803-1068.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200866. 18 interactions.
DIPDIP-34312N.
IntActQ62315. 20 interactions.
MINTMINT-4792531.

PTM databases

PhosphoSiteQ62315.

Proteomic databases

PRIDEQ62315.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044608; ENSMUSP00000037774; ENSMUSG00000038518. [Q62315-1]
ENSMUST00000173246; ENSMUSP00000134205; ENSMUSG00000038518. [Q62315-1]
ENSMUST00000173704; ENSMUSP00000134675; ENSMUSG00000038518. [Q62315-1]
GeneID16468.
KEGGmmu:16468.
UCSCuc007qgr.2. mouse. [Q62315-1]
uc007qgv.1. mouse. [Q62315-2]

Organism-specific databases

CTD3720.
MGIMGI:104813. Jarid2.

Phylogenomic databases

eggNOGNOG327026.
GeneTreeENSGT00530000063118.
HOGENOMHOG000013203.
HOVERGENHBG052160.
InParanoidQ3TPU4.
KOK11478.
OMAWAAMDEI.
OrthoDBEOG76MK7F.
PhylomeDBQ62315.
TreeFamTF323264.

Gene expression databases

ArrayExpressQ62315.
BgeeQ62315.
CleanExMM_JARID2.
GenevestigatorQ62315.

Family and domain databases

Gene3D1.10.150.60. 1 hit.
InterProIPR001606. ARID/BRIGHT_DNA-bd.
IPR003347. JmjC_dom.
IPR003349. TF_JmjN.
IPR004198. Znf_C5HC2.
[Graphical view]
PfamPF01388. ARID. 1 hit.
PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view]
SMARTSM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
[Graphical view]
SUPFAMSSF46774. SSF46774. 1 hit.
PROSITEPS51011. ARID. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSJARID2. mouse.
EvolutionaryTraceQ62315.
NextBio289745.
PROQ62315.
SOURCESearch...

Entry information

Entry nameJARD2_MOUSE
AccessionPrimary (citable) accession number: Q62315
Secondary accession number(s): Q3TPU4, Q3UHS7, Q99LD1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot