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Q3UXZ9

- KDM5A_MOUSE

UniProt

Q3UXZ9 - KDM5A_MOUSE

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Protein

Lysine-specific demethylase 5A

Gene

Kdm5a

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

Functioni

Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and dimethylated but not monomethylated H3 'Lys-4'. May stimulate transcription mediated by nuclear receptors. Involved in transcriptional regulation of Hox proteins during cell differentiation. May participate in transcriptional repression of cytokines such as CXCL12. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. In a histone demethylase-independent manner, acts as a coactivator of the CLOCK-ARNTL/BMAL1-mediated transcriptional activation of PER1/2 and other clock-controlled genes and increases histone acetylation at PER1/2 promoters by inhibiting the activity of HDAC1.3 Publications

Cofactori

Binds 1 Fe2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi483 – 4831Iron; catalyticPROSITE-ProRule annotation
Metal bindingi486 – 4861Iron; catalyticPROSITE-ProRule annotation
Metal bindingi571 – 5711Iron; catalyticPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri293 – 34351PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1153 – 121058PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1599 – 165355PHD-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: UniProtKB
  2. DNA binding Source: InterPro
  3. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Source: InterPro
  4. transcription coactivator activity Source: UniProtKB
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. circadian regulation of gene expression Source: UniProtKB
  3. multicellular organismal development Source: UniProtKB-KW
  4. negative regulation of histone deacetylase activity Source: UniProtKB
  5. positive regulation of transcription, DNA-templated Source: Ensembl
  6. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Developmental protein, Dioxygenase, Oxidoreductase

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific demethylase 5A (EC:1.14.11.-)
Alternative name(s):
Histone demethylase JARID1A
Jumonji/ARID domain-containing protein 1A
Retinoblastoma-binding protein 2
Short name:
RBBP-2
Gene namesi
Name:Kdm5a
Synonyms:Jarid1a, Rbp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:2136980. Kdm5a.

Subcellular locationi

Nucleusnucleolus By similarity. Nucleus 1 PublicationPROSITE-ProRule annotation
Note: Occupies promoters of genes involved in RNA metabolism and mitochondrial function.1 Publication

GO - Cellular componenti

  1. cyclin-dependent protein kinase activating kinase holoenzyme complex Source: Ensembl
  2. cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice are grossly normal, except that they exhibit behavioral abnormalities when held upside down by the tail, and slight hematological defects.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16901690Lysine-specific demethylase 5APRO_0000292411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1111 – 11111Phosphoserine1 Publication
Modified residuei1331 – 13311PhosphoserineBy similarity
Modified residuei1598 – 15981PhosphoserineBy similarity
Modified residuei1603 – 16031PhosphoserineBy similarity
Modified residuei1666 – 16661PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3UXZ9.
PaxDbiQ3UXZ9.
PRIDEiQ3UXZ9.

PTM databases

PhosphoSiteiQ3UXZ9.

Expressioni

Gene expression databases

BgeeiQ3UXZ9.
CleanExiMM_RBP2.
ExpressionAtlasiQ3UXZ9. baseline and differential.
GenevestigatoriQ3UXZ9.

Interactioni

Subunit structurei

Interacts with RB1, ESR1, MYC, MYCN and LMO2 (By similarity). Interacts with SUZ12; the interaction is direct. Interacts with HDAC1, ARNTL/BMAL1 and CLOCK.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Suz12Q80U702EBI-2531441,EBI-2526494

Protein-protein interaction databases

BioGridi229572. 1 interaction.
IntActiQ3UXZ9. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ3UXZ9.
SMRiQ3UXZ9. Positions 18-81, 84-175, 260-585, 1162-1217, 1608-1659.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 6042JmjNPROSITE-ProRule annotationAdd
BLAST
Domaini84 – 17491ARIDPROSITE-ProRule annotationAdd
BLAST
Domaini437 – 603167JmjCPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1622 – 169069Interaction with LMO2By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi419 – 4235GSGFP motif1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1484 – 157996Lys-richAdd
BLAST

Domaini

The GSGFP motif is required for the interaction with SUZ12.1 Publication

Sequence similaritiesi

Belongs to the JARID1 histone demethylase family.Curated
Contains 1 ARID domain.PROSITE-ProRule annotation
Contains 1 JmjC domain.PROSITE-ProRule annotation
Contains 1 JmjN domain.PROSITE-ProRule annotation
Contains 3 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri293 – 34351PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1153 – 121058PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1599 – 165355PHD-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG327026.
GeneTreeiENSGT00530000063118.
HOGENOMiHOG000290719.
InParanoidiQ3UXZ9.
KOiK11446.
OMAiCVAHYRR.
PhylomeDBiQ3UXZ9.
TreeFamiTF106476.

Family and domain databases

Gene3Di1.10.150.60. 1 hit.
3.30.40.10. 3 hits.
InterProiIPR001606. ARID/BRIGHT_DNA-bd.
IPR003347. JmjC_dom.
IPR013637. Lys_sp_deMease_like_dom.
IPR003349. TF_JmjN.
IPR019786. Zinc_finger_PHD-type_CS.
IPR004198. Znf_C5HC2.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01388. ARID. 1 hit.
PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
PF00628. PHD. 2 hits.
PF08429. PLU-1. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view]
SMARTiSM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 3 hits.
[Graphical view]
SUPFAMiSSF46774. SSF46774. 1 hit.
SSF57903. SSF57903. 3 hits.
PROSITEiPS51011. ARID. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3UXZ9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PFAEKTGICK
60 70 80 90 100
IRPPKDWQPP FACEVKTFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL
110 120 130 140 150
QGSTLKIPVV ERKILDLYAL SKIVASKGGF EIVTKEKKWS KVGSRLGYLP
160 170 180 190 200
GKGTGSLLKS HYERILYPYE LFQSGVSLMG VQMPDLDLKE KVEAEVLSTD
210 220 230 240 250
IQPSPERGTR MNIPPKRTRR VKSQSDSGEV NRNTELKKLQ IFGAGPKVVG
260 270 280 290 300
LAVGAKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG
310 320 330 340 350
RGNNEDKLLL CDGCDDSYHT FCLLPPLPDV PKGDWRCPKC VAEECNKPRE
360 370 380 390 400
AFGFEQAVRE YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS
410 420 430 440 450
IEEDVIVEYG ADISSKDFGS GFPKKDGQRK MLPEEEEYAL SGWNLNNMPV
460 470 480 490 500
LEQSVLAHIN VDISGMKVPW LYVGMCFSSF CWHIEDHWSY SINYLHWGEP
510 520 530 540 550
KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM NPNVLMEHGV
560 570 580 590 600
PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN
610 620 630 640 650
HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR
660 670 680 690 700
ESVVQMGVVM SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL
710 720 730 740 750
YHPTDLCSCP MQNKCLRYRY PLEDLPSLLY GVKVRAQSYD TWVNRVTEAL
760 770 780 790 800
SASFNHKKDL IELRVMLEDA EDRKYPENDL FRKLRDAVKE AETCGSVAQL
810 820 830 840 850
LLSKKQKHRQ SSDSGKTRTK LTVEELKAFV QQLVSLPCVI SQTRQVKNLL
860 870 880 890 900
DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ
910 920 930 940 950
ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT
960 970 980 990 1000
VSERWEEKAK VCLQARPRHS MANLENIVNE AKNIPAFLPN VLSLKEALQK
1010 1020 1030 1040 1050
AREWTAKVEA IQSGNNYAYL EQLESLSAKG RPIPVRLDAL PQVESQVAAA
1060 1070 1080 1090 1100
RAWRERTGRT FLKKNSSHTL LQVLSPRTDI GVYGSGKNRR KKVKEIIEKE
1110 1120 1130 1140 1150
KEKDLDLEPL SDLEEGLEES RDTAMVVAVF KEREQKEIEA MHSLRAANLA
1160 1170 1180 1190 1200
KMTIVERIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG
1210 1220 1230 1240 1250
SSWQAKDVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT
1260 1270 1280 1290 1300
ERAMSWQDKA RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL
1310 1320 1330 1340 1350
QKAAANPDLQ GHLPSFQQSA FNRVVSSVSS SPHQTMDYDD EETDSDEDIR
1360 1370 1380 1390 1400
ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP IKSEEVVTHM WTAPSFCAEH
1410 1420 1430 1440 1450
AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG AKAQLEELMM
1460 1470 1480 1490 1500
VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSIE EKPLKMKGKD
1510 1520 1530 1540 1550
SSEKKRKRKL EKVEQLFGEG KQKTKELKKI DKPKKKKLKL NVDKSKELNK
1560 1570 1580 1590 1600
LAKKLAKEEE RKKKKEKAAA AKVELVKEST EKKRERKVLD IPSKYDWSGA
1610 1620 1630 1640 1650
EESDDENAVC AAQNCQRPCK DKVDWVQCDG GCDEWFHQVC VGVSAEMAEN
1660 1670 1680 1690
EDYICINCAK KQGPDSPGQA PPPPFLMSYK LPMEDLKETS
Length:1,690
Mass (Da):192,216
Last modified:June 26, 2007 - v2
Checksum:iEFCF56AAAA51F0FC
GO

Sequence cautioni

The sequence BAE22414.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101A → S in BAE38548. (PubMed:16141072)Curated
Sequence conflicti14 – 141V → R in BAE38548. (PubMed:16141072)Curated
Sequence conflicti17 – 171P → A in BAE38548. (PubMed:16141072)Curated
Sequence conflicti24 – 241P → A in BAE38548. (PubMed:16141072)Curated
Sequence conflicti544 – 5441V → A in BAE38548. (PubMed:16141072)Curated
Sequence conflicti1272 – 12721A → P in BAE22414. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC155720 Genomic DNA. No translation available.
AC078896 Genomic DNA. No translation available.
AK135085 mRNA. Translation: BAE22414.1. Different initiation.
AK144877 mRNA. Translation: BAE26113.1.
AK166055 mRNA. Translation: BAE38548.1.
BC080691 mRNA. Translation: AAH80691.1. Different termination.
CCDSiCCDS51889.1.
RefSeqiNP_666109.2. NM_145997.2.
UniGeneiMm.404761.
Mm.463658.

Genome annotation databases

EnsembliENSMUST00000100996; ENSMUSP00000098558; ENSMUSG00000030180.
GeneIDi214899.
KEGGimmu:214899.
UCSCiuc009dne.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC155720 Genomic DNA. No translation available.
AC078896 Genomic DNA. No translation available.
AK135085 mRNA. Translation: BAE22414.1 . Different initiation.
AK144877 mRNA. Translation: BAE26113.1 .
AK166055 mRNA. Translation: BAE38548.1 .
BC080691 mRNA. Translation: AAH80691.1 . Different termination.
CCDSi CCDS51889.1.
RefSeqi NP_666109.2. NM_145997.2.
UniGenei Mm.404761.
Mm.463658.

3D structure databases

ProteinModelPortali Q3UXZ9.
SMRi Q3UXZ9. Positions 18-81, 84-175, 260-585, 1162-1217, 1608-1659.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 229572. 1 interaction.
IntActi Q3UXZ9. 1 interaction.

PTM databases

PhosphoSitei Q3UXZ9.

Proteomic databases

MaxQBi Q3UXZ9.
PaxDbi Q3UXZ9.
PRIDEi Q3UXZ9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000100996 ; ENSMUSP00000098558 ; ENSMUSG00000030180 .
GeneIDi 214899.
KEGGi mmu:214899.
UCSCi uc009dne.2. mouse.

Organism-specific databases

CTDi 5927.
MGIi MGI:2136980. Kdm5a.

Phylogenomic databases

eggNOGi NOG327026.
GeneTreei ENSGT00530000063118.
HOGENOMi HOG000290719.
InParanoidi Q3UXZ9.
KOi K11446.
OMAi CVAHYRR.
PhylomeDBi Q3UXZ9.
TreeFami TF106476.

Miscellaneous databases

ChiTaRSi KDM5A. mouse.
NextBioi 374501.
PROi Q3UXZ9.
SOURCEi Search...

Gene expression databases

Bgeei Q3UXZ9.
CleanExi MM_RBP2.
ExpressionAtlasi Q3UXZ9. baseline and differential.
Genevestigatori Q3UXZ9.

Family and domain databases

Gene3Di 1.10.150.60. 1 hit.
3.30.40.10. 3 hits.
InterProi IPR001606. ARID/BRIGHT_DNA-bd.
IPR003347. JmjC_dom.
IPR013637. Lys_sp_deMease_like_dom.
IPR003349. TF_JmjN.
IPR019786. Zinc_finger_PHD-type_CS.
IPR004198. Znf_C5HC2.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view ]
Pfami PF01388. ARID. 1 hit.
PF02373. JmjC. 1 hit.
PF02375. JmjN. 1 hit.
PF00628. PHD. 2 hits.
PF08429. PLU-1. 1 hit.
PF02928. zf-C5HC2. 1 hit.
[Graphical view ]
SMARTi SM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 3 hits.
[Graphical view ]
SUPFAMi SSF46774. SSF46774. 1 hit.
SSF57903. SSF57903. 3 hits.
PROSITEi PS51011. ARID. 1 hit.
PS51184. JMJC. 1 hit.
PS51183. JMJN. 1 hit.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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.
    , 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] OF 1-1552.
    Strain: C57BL/6J.
    Tissue: Lung and Olfactory bulb.
  3. "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] OF 1-1099.
    Strain: C57BL/6J.
    Tissue: Germ cell.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1538-1546, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3."
    Christensen J., Agger K., Cloos P.A.C., Pasini D., Rose S., Sennels L., Rappsilber J., Hansen K.H., Salcini A.E., Helin K.
    Cell 128:1063-1076(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "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: SUBCELLULAR LOCATION, DOMAIN GSGFP MOTIF, INTERACTION WITH SUZ12.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and influences the circadian clock."
    DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J., Panda S.
    Science 333:1881-1885(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ARNTL; CLOCK AND HDAC1.

Entry informationi

Entry nameiKDM5A_MOUSE
AccessioniPrimary (citable) accession number: Q3UXZ9
Secondary accession number(s): Q3TM94, Q3UMI5, Q66JZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: October 29, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

External Data

Dasty 3