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Protein

Protein Jumonji

Gene

JARID2

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

Functioni

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.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein, Repressor

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_264352. PRC2 methylates histones and DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Jumonji
Alternative name(s):
Jumonji/ARID domain-containing protein 2
Gene namesi
Name:JARID2
Synonyms:JMJ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:6196. JARID2.

Subcellular locationi

GO - Cellular componenti

  • ESC/E(Z) complex Source: Ensembl
  • histone methyltransferase complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29995.

Polymorphism and mutation databases

BioMutaiJARID2.
DMDMi61252601.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12461246Protein JumonjiPRO_0000200591Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781Phosphoserine1 Publication
Modified residuei378 – 3781N6-acetyllysine1 Publication
Modified residuei455 – 4551Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92833.
PaxDbiQ92833.
PRIDEiQ92833.

PTM databases

PhosphoSiteiQ92833.

Expressioni

Tissue specificityi

During embryogenesis, predominantly expressed in neurons and particularly in dorsal root ganglion cells.

Gene expression databases

BgeeiQ92833.
CleanExiHS_JARID2.
GenevisibleiQ92833. HS.

Organism-specific databases

HPAiCAB069890.

Interactioni

Subunit structurei

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 (By similarity). 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.By similarity

Protein-protein interaction databases

BioGridi109923. 16 interactions.
DIPiDIP-45494N.
IntActiQ92833. 3 interactions.
STRINGi9606.ENSP00000341280.

Structurei

3D structure databases

ProteinModelPortaliQ92833.
SMRiQ92833. Positions 617-732.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini557 – 59842JmjNPROSITE-ProRule annotationAdd
BLAST
Domaini621 – 71393ARIDPROSITE-ProRule annotationAdd
BLAST
Domaini884 – 1048165JmjCPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi104 – 1107Nuclear localization signalBy similarity
Motifi874 – 8785GSGFP motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1234 – 124613Poly-SerAdd
BLAST

Domaini

The ARID domain is required to target the PRC2 complex to its target genes.By similarity
The GSGFP motif is required for the interaction with SUZ12.By similarity

Sequence similaritiesi

Contains 1 ARID domain.PROSITE-ProRule annotation
Contains 1 JmjC domain.PROSITE-ProRule annotation
Contains 1 JmjN domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG327026.
GeneTreeiENSGT00530000063118.
HOGENOMiHOG000013203.
HOVERGENiHBG052160.
InParanoidiQ92833.
KOiK11478.
OMAiAGWAAMD.
OrthoDBiEOG76MK7F.
PhylomeDBiQ92833.
TreeFamiTF323264.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
InterProiIPR001606. ARID_dom.
IPR003347. JmjC_dom.
IPR003349. JmjN.
IPR004198. Znf_C5HC2.
[Graphical view]
PfamiPF01388. ARID. 1 hit.
PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view]
SMARTiSM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
PROSITEiPS51011. ARID. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q92833-1) [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

        10         20         30         40         50
MSKERPKRNI IQKKYDDSDG IPWSEERVVR KVLYLSLKEF KNSQKRQHAE
60 70 80 90 100
GIAGSLKTVN GLLGNDQSKG LGPASEQSEN EKDDASQVSS TSNDVSSSDF
110 120 130 140 150
EEGPSRKRPR LQAQRKFAQS QPNSPSTTPV KIVEPLLPPP ATQISDLSKR
160 170 180 190 200
KPKTEDFLTF LCLRGSPALP NSMVYFGSSQ DEEEVEEEDD ETEDVKTATN
210 220 230 240 250
NASSSCQSTP RKGKTHKHVH NGHVFNGSSR STREKEPVQK HKSKEATPAK
260 270 280 290 300
EKHSDHRADS RREQASANHP AAAPSTGSSA KGLAATHHHP PLHRSAQDLR
310 320 330 340 350
KQVSKVNGVT RMSSLGAGVT SAKKMREVRP SPSKTVKYTA TVTKGAVTYT
360 370 380 390 400
KAKRELVKDT KPNHHKPSSA VNHTISGKTE SSNAKTRKQV LSLGGASKST
410 420 430 440 450
GPAVNGLKVS GRLNPKSCTK EVGGRQLREG LQLREGLRNS KRRLEEAHQA
460 470 480 490 500
EKPQSPPKKM KGAAGPAEGP GKKAPAERGL LNGHVKKEVP ERSLERNRPK
510 520 530 540 550
RATAGKSTPG RQAHGKADSA SCENRSTSQP ESVHKPQDSG KAEKGGGKAG
560 570 580 590 600
WAAMDEIPVL RPSAKEFHDP LIYIESVRAQ VEKFGMCRVI PPPDWRPECK
610 620 630 640 650
LNDEMRFVTQ IQHIHKLGRR WGPNVQRLAC IKKHLKSQGI TMDELPLIGG
660 670 680 690 700
CELDLACFFR LINEMGGMQQ VTDLKKWNKL ADMLRIPRTA QDRLAKLQEA
710 720 730 740 750
YCQYLLSYDS LSPEEHRRLE KEVLMEKEIL EKRKGPLEGH TENDHHKFHP
760 770 780 790 800
LPRFEPKNGL IHGVAPRNGF RSKLKEVGQA QLKTGRRRLF AQEKEVVKEE
810 820 830 840 850
EEDKGVLNDF HKCIYKGRSV SLTTFYRTAR NIMSMCFSKE PAPAEIEQEY
860 870 880 890 900
WRLVEEKDCH VAVHCGKVDT NTHGSGFPVG KSEPFSRHGW NLTVLPNNTG
910 920 930 940 950
SILRHLGAVP GVTIPWLNIG MVFSTSCWSR DQNHLPYIDY LHTGADCIWY
960 970 980 990 1000
CIPAEEENKL EDVVHTLLQA NGTPGLQMLE SNVMISPEVL CKEGIKVHRT
1010 1020 1030 1040 1050
VQQSGQFVVC FPGSFVSKVC CGYSVSETVH FATTQWTSMG FETAKEMKRR
1060 1070 1080 1090 1100
HIAKPFSMEK LLYQIAQAEA KKENGPTLST ISALLDELRD TELRQRRQLF
1110 1120 1130 1140 1150
EAGLHSSARY GSHDGSSTVA DGKKKPRKWL QLETSERRCQ ICQHLCYLSM
1160 1170 1180 1190 1200
VVQENENVVF CLECALRHVE KQKSCRGLKL MYRYDEEQII SLVNQICGKV
1210 1220 1230 1240
SGKNGSIENC LSKPTPKRGP RKRATVDVPP SRLSASSSSK SASSSS
Length:1,246
Mass (Da):138,734
Last modified:March 15, 2005 - v2
Checksum:iE4929984259110DB
GO
Isoform 2 (identifier: Q92833-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: MSKERPKRNI...GIAGSLKTVN → MAAPRVCQVQFLVAYLEEPGIE
     949-1246: WYCIPAEEEN...SSSKSASSSS → CLSVEPVFPH...AWRGVLGPRL

Note: No experimental confirmation available.
Show »
Length:960
Mass (Da):106,139
Checksum:i985C77D3B34F699B
GO
Isoform 3 (identifier: Q92833-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-172: Missing.

Note: No experimental confirmation available.
Show »
Length:1,074
Mass (Da):119,689
Checksum:iA913DFCF25573C4A
GO

Sequence cautioni

The sequence AAC50822.1 differs from that shown. Reason: Frameshift at position 1233. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti250 – 2501K → E in BAH13011 (PubMed:14702039).Curated
Sequence conflicti599 – 5991C → S in BAH13011 (PubMed:14702039).Curated
Sequence conflicti673 – 6731D → E in AAC50822 (PubMed:8894700).Curated
Sequence conflicti681 – 6811A → S in AAC50822 (PubMed:8894700).Curated
Sequence conflicti688 – 6881R → K in AAC50822 (PubMed:8894700).Curated
Sequence conflicti692 – 6921D → E in AAC50822 (PubMed:8894700).Curated
Sequence conflicti705 – 7051L → I in AAC50822 (PubMed:8894700).Curated
Sequence conflicti754 – 7541F → L in AAC50822 (PubMed:8894700).Curated
Sequence conflicti1212 – 12121S → H in AAC50822 (PubMed:8894700).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 172172Missing in isoform 3. 1 PublicationVSP_045041Add
BLAST
Alternative sequencei1 – 6060MSKER…LKTVN → MAAPRVCQVQFLVAYLEEPG IE in isoform 2. 1 PublicationVSP_038756Add
BLAST
Alternative sequencei949 – 1246298WYCIP…ASSSS → CLSVEPVFPHLSVAVGSIVD LGISFLPCGDTRVMYPVESV AWRGVLGPRL in isoform 2. 1 PublicationVSP_038757Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57592 mRNA. Translation: AAC50822.1. Frameshift.
AK292861 mRNA. Translation: BAF85550.1.
AK299349 mRNA. Translation: BAH13011.1.
AK303610 mRNA. Translation: BAH13996.1.
AL136162, AL021938 Genomic DNA. Translation: CAI15719.1.
AL021938, AL136162 Genomic DNA. Translation: CAI19873.1.
CH471087 Genomic DNA. Translation: EAW55357.1.
BC046184 mRNA. Translation: AAH46184.1.
BC046246 mRNA. Translation: AAH46246.1.
CCDSiCCDS4533.1. [Q92833-1]
CCDS58996.1. [Q92833-3]
RefSeqiNP_001253969.1. NM_001267040.1. [Q92833-3]
NP_004964.2. NM_004973.3. [Q92833-1]
XP_005249146.1. XM_005249089.2. [Q92833-3]
UniGeneiHs.269059.

Genome annotation databases

EnsembliENST00000341776; ENSP00000341280; ENSG00000008083. [Q92833-1]
ENST00000397311; ENSP00000380478; ENSG00000008083. [Q92833-3]
GeneIDi3720.
KEGGihsa:3720.
UCSCiuc003nbj.4. human. [Q92833-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U57592 mRNA. Translation: AAC50822.1. Frameshift.
AK292861 mRNA. Translation: BAF85550.1.
AK299349 mRNA. Translation: BAH13011.1.
AK303610 mRNA. Translation: BAH13996.1.
AL136162, AL021938 Genomic DNA. Translation: CAI15719.1.
AL021938, AL136162 Genomic DNA. Translation: CAI19873.1.
CH471087 Genomic DNA. Translation: EAW55357.1.
BC046184 mRNA. Translation: AAH46184.1.
BC046246 mRNA. Translation: AAH46246.1.
CCDSiCCDS4533.1. [Q92833-1]
CCDS58996.1. [Q92833-3]
RefSeqiNP_001253969.1. NM_001267040.1. [Q92833-3]
NP_004964.2. NM_004973.3. [Q92833-1]
XP_005249146.1. XM_005249089.2. [Q92833-3]
UniGeneiHs.269059.

3D structure databases

ProteinModelPortaliQ92833.
SMRiQ92833. Positions 617-732.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109923. 16 interactions.
DIPiDIP-45494N.
IntActiQ92833. 3 interactions.
STRINGi9606.ENSP00000341280.

PTM databases

PhosphoSiteiQ92833.

Polymorphism and mutation databases

BioMutaiJARID2.
DMDMi61252601.

Proteomic databases

MaxQBiQ92833.
PaxDbiQ92833.
PRIDEiQ92833.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000341776; ENSP00000341280; ENSG00000008083. [Q92833-1]
ENST00000397311; ENSP00000380478; ENSG00000008083. [Q92833-3]
GeneIDi3720.
KEGGihsa:3720.
UCSCiuc003nbj.4. human. [Q92833-1]

Organism-specific databases

CTDi3720.
GeneCardsiGC06P015246.
HGNCiHGNC:6196. JARID2.
HPAiCAB069890.
MIMi601594. gene.
neXtProtiNX_Q92833.
PharmGKBiPA29995.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG327026.
GeneTreeiENSGT00530000063118.
HOGENOMiHOG000013203.
HOVERGENiHBG052160.
InParanoidiQ92833.
KOiK11478.
OMAiAGWAAMD.
OrthoDBiEOG76MK7F.
PhylomeDBiQ92833.
TreeFamiTF323264.

Enzyme and pathway databases

ReactomeiREACT_264352. PRC2 methylates histones and DNA.

Miscellaneous databases

ChiTaRSiJARID2. human.
GeneWikiiJARID2.
GenomeRNAii3720.
NextBioi14577.
PROiQ92833.
SOURCEiSearch...

Gene expression databases

BgeeiQ92833.
CleanExiHS_JARID2.
GenevisibleiQ92833. HS.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
InterProiIPR001606. ARID_dom.
IPR003347. JmjC_dom.
IPR003349. JmjN.
IPR004198. Znf_C5HC2.
[Graphical view]
PfamiPF01388. ARID. 1 hit.
PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view]
SMARTiSM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
PROSITEiPS51011. ARID. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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; 2 AND 3).
    Tissue: Thymus and Trachea.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Mammary gland and Testis.
  6. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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, SUBCELLULAR LOCATION, ASSOCIATION WITH THE PRC2 COMPLEX.
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiJARD2_HUMAN
AccessioniPrimary (citable) accession number: Q92833
Secondary accession number(s): A8K9Z6
, B7Z5S5, B7Z8L0, Q5U5L5, Q86X63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: March 15, 2005
Last modified: June 24, 2015
This is version 130 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.