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Q80Y84

- KDM5B_MOUSE

UniProt

Q80Y84 - KDM5B_MOUSE

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Protein

Lysine-specific demethylase 5B

Gene

Kdm5b

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

Functioni

Histone demethylase that demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for FOXG1B and PAX9. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2.3 Publications

Cofactori

Fe2+By similarityNote: Binds 1 Fe(2+) ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi499 – 4991Iron; catalyticPROSITE-ProRule annotation
Metal bindingi502 – 5021Iron; catalyticPROSITE-ProRule annotation
Metal bindingi587 – 5871Iron; catalyticPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri309 – 35951PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1176 – 122449PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1484 – 153855PHD-type 3PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. histone demethylase activity (H3-dimethyl-K4 specific) Source: UniProtKB
  3. histone demethylase activity (H3-K4 specific) Source: MGI
  4. histone demethylase activity (H3-trimethyl-K4 specific) Source: UniProtKB
  5. 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
  6. transcription corepressor activity Source: Ensembl
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. histone H3-K4 demethylation Source: UniProtKB
  2. negative regulation of transcription, DNA-templated Source: UniProtKB
  3. regulation of circadian rhythm Source: UniProtKB
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Dioxygenase, Oxidoreductase, Repressor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

Iron, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_256030. HDMs demethylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific demethylase 5B (EC:1.14.11.-)
Alternative name(s):
Histone demethylase JARID1B
Jumonji/ARID domain-containing protein 1B
PLU-1
Gene namesi
Name:Kdm5b
Synonyms:Jarid1b, Kiaa4034, Plu1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:1922855. Kdm5b.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi499 – 4991H → A: Abolishes enzymatic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15441544Lysine-specific demethylase 5BPRO_0000292413Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei832 – 8321N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ80Y84.
PaxDbiQ80Y84.
PRIDEiQ80Y84.

PTM databases

PhosphoSiteiQ80Y84.

Expressioni

Tissue specificityi

Present at highest levels in testis, where it is enriched in spermatogonia and pachytene cells (at protein level).3 Publications

Developmental stagei

Expressed in developing brain, mammary bud, thymus, teeth, whisker follicle, intervertebral disks, olfactory epithelium, eye, stomach and limbs.1 Publication

Gene expression databases

BgeeiQ80Y84.
ExpressionAtlasiQ80Y84. baseline and differential.
GenevestigatoriQ80Y84.

Interactioni

Subunit structurei

Interacts with FOXG1B, PAX9, MYC, MYCN and RB1. Interacts with HDAC1, HDAC4, HDAC5 and HDAC7.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Morf4l1P607624EBI-1249551,EBI-2943018

Protein-protein interaction databases

BioGridi217610. 3 interactions.
IntActiQ80Y84. 4 interactions.

Structurei

Secondary structure

1
1544
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi97 – 11418Combined sources
Beta strandi122 – 1276Combined sources
Helixi130 – 14011Combined sources
Helixi143 – 1486Combined sources
Turni149 – 1513Combined sources
Helixi152 – 1587Combined sources
Beta strandi163 – 1653Combined sources
Helixi166 – 17712Combined sources
Helixi179 – 1879Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EQYNMR-A94-208[»]
DisProtiDP00711.
ProteinModelPortaliQ80Y84.
SMRiQ80Y84. Positions 31-208, 306-601, 1177-1223, 1486-1544.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ80Y84.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 7342JmjNPROSITE-ProRule annotationAdd
BLAST
Domaini97 – 18791ARIDPROSITE-ProRule annotationAdd
BLAST
Domaini453 – 619167JmjCPROSITE-ProRule annotationAdd
BLAST

Domaini

Both the JmjC domain and the JmjN domain are required for enzymatic activity.
The 2 first PHD-type zinc finger domains are required for transcription repression activity.By similarity

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 fingeri309 – 35951PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1176 – 122449PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1484 – 153855PHD-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG327026.
GeneTreeiENSGT00530000063118.
HOGENOMiHOG000290719.
InParanoidiQ80Y84.
KOiK11446.
OMAiPHSSVER.
OrthoDBiEOG7D85VK.
PhylomeDBiQ80Y84.
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. 3 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q80Y84-1) [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
MEPATTLPPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH
60 70 80 90 100
KIRPIAEQTG ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK
110 120 130 140 150
LNFLDQIAKY WELQGSTLKI PHVERKILDL FQLNKLVAEE GGFAVVCKDR
160 170 180 190 200
KWTKIATKMG FAPGKAVGSH IRGHYERILN PYNLFLSGDS LRCLQKPNLT
210 220 230 240 250
SDTKDKEYKP HDIPQRQSVQ PAETCPPARR AKRMRAEAMN IKIEPEEATE
260 270 280 290 300
ARTHNLRRRM GCTTPKWENE KEMKSTIKQE PTEKKDCELE SEKEKPKSRA
310 320 330 340 350
KKTATAVDLY VCLLCGSGND EDRLLLCDGC DDSYHTFCLV PPLHDVPKGD
360 370 380 390 400
WRCPKCLAQE CNKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM
410 420 430 440 450
VPTELVEKEF WRLVSTIEED VTVEYGADIA SKEFGSGFPV RDGKIKISPE
460 470 480 490 500
EEEYLDSGWN LNNMPVMEQS VLAHITADIC GMKLPWLYVG MCFSSFCWHI
510 520 530 540 550
EDHWSYSINY LHWGEPKTWY GVPGYAAEQL ENVMKKLAPE LFVSQPDLLH
560 570 580 590 600
QLVTIMNPNT LMTHEVPVYR TNQCAGEFVI TFPRAYHSGF NQGFNFAEAV
610 620 630 640 650
NFCTVDWLPL GRQCVEHYRL LHRYCVFSHD EMICKMASKA DVLDVVVAST
660 670 680 690 700
VQKDMAIMIE DEKALRETVR KLGVIDSERM DFELLPDDER QCIKCKTTCF
710 720 730 740 750
MSAISCSCKP GLLVCLHHVK ELCSCPPYKY NLRYRYTLDD LYPMMNALKL
760 770 780 790 800
RAESYNEWAL NVNEALEAKI NKKKSLVSFK ALIEESEMKK FPDNDLLRHL
810 820 830 840 850
RLVTQDAEKC ASVAQQLLNG KRQTRYRSGG GKSQNQLTVN ELRQFVTQLY
860 870 880 890 900
ALPCVLSQTP LLKDLLNRVE DFQQQSQKLL SEEMPSAAEL QELLDVSFEF
910 920 930 940 950
DVELPQLTEM RIRLEQARWL EEVQQACLDS SSLSLDDMRR LIDLGVGLAP
960 970 980 990 1000
YSAVEKAMAR LQELLTVSEH WDDKAKSLLR ARPRHSLSSL ATAVKEMEEI
1010 1020 1030 1040 1050
PAYLPNGTVL KDSVQRARDW VQDVDALQAG GRVPVLETLI ELVARGRSIP
1060 1070 1080 1090 1100
VHLNSLPRLE MLVAEVHAWK ECAAKTFLPE NSTYSLLEVL CPRCDIGLLG
1110 1120 1130 1140 1150
LKRKQRKLKE PLPSGKKRST KLESLSDLER ALMESKETAA AMATLGEARL
1160 1170 1180 1190 1200
REMEALQSLR FANEEKLLSP VQDLEMKVCL CQKTPATPMI QCELCRDAFH
1210 1220 1230 1240 1250
TSCVAAPSIS QSSRIWLCPH CRRSEKPPLE KILPLLASLQ RIRVRLPEGD
1260 1270 1280 1290 1300
ALRYMIERTV NWQHRAQQLL SSGNLKLVQD QVGSGLLSSR WPASAGQASA
1310 1320 1330 1340 1350
TDKVSQPPGT TSFSLPDDWD NRTSYLHSPF STGQSCLPLH GLSPEVNELL
1360 1370 1380 1390 1400
MEAQLLQVSL PEIQELYQTL LTKPSSVQQA DRSSPVRSSS EKNDCLRGKR
1410 1420 1430 1440 1450
DAINSPERKL KRRPEREGLP SERWDRVKHM RTPQKKKIKL SHPKDMDSFK
1460 1470 1480 1490 1500
LERERSYDLV RNAETHSLPS DTSYSEQEDS EDEDAICPAV SCLQPEGDEV
1510 1520 1530 1540
DWVQCDGSCN QWFHQVCVGV SPEMAEKEDY ICVRCTGKDA PSRK
Length:1,544
Mass (Da):175,555
Last modified:June 1, 2003 - v1
Checksum:iD83E2691C65DCB31
GO
Isoform 2 (identifier: Q80Y84-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1501-1544: DWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTGKDAPSRK → SEVWAIEDALSPNSETL

Note: No experimental confirmation available.

Show »
Length:1,517
Mass (Da):172,410
Checksum:i37772163EC76CDB2
GO

Sequence cautioni

The sequence BAD90482.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortenedCurated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281P → S in BAD90482. 1 PublicationCurated
Sequence conflicti139 – 1391E → Q in BAC30898. (PubMed:16141072)Curated
Sequence conflicti761 – 7611N → Y in AAL92848. (PubMed:14516692)Curated
Sequence conflicti761 – 7611N → Y in AAL92849. (PubMed:14516692)Curated
Sequence conflicti1428 – 14281K → R in AAL92848. (PubMed:14516692)Curated
Sequence conflicti1428 – 14281K → R in AAL92849. (PubMed:14516692)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1501 – 154444DWVQC…APSRK → SEVWAIEDALSPNSETL in isoform 2. 1 PublicationVSP_026409Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY082429 mRNA. Translation: AAL92848.1.
AY082430 mRNA. Translation: AAL92849.1.
AK220451 mRNA. Translation: BAD90482.1. Different initiation.
BC048180 mRNA. Translation: AAH48180.1.
BC057318 mRNA. Translation: AAH57318.1.
AK041304 mRNA. Translation: BAC30898.1.
CCDSiCCDS35716.1. [Q80Y84-1]
RefSeqiNP_690855.2. NM_152895.2. [Q80Y84-1]
UniGeneiMm.28995.
Mm.391994.

Genome annotation databases

EnsembliENSMUST00000047714; ENSMUSP00000038138; ENSMUSG00000042207. [Q80Y84-1]
ENSMUST00000112198; ENSMUSP00000107817; ENSMUSG00000042207. [Q80Y84-2]
GeneIDi75605.
KEGGimmu:75605.
UCSCiuc007csg.2. mouse. [Q80Y84-2]
uc011wsg.1. mouse. [Q80Y84-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY082429 mRNA. Translation: AAL92848.1 .
AY082430 mRNA. Translation: AAL92849.1 .
AK220451 mRNA. Translation: BAD90482.1 . Different initiation.
BC048180 mRNA. Translation: AAH48180.1 .
BC057318 mRNA. Translation: AAH57318.1 .
AK041304 mRNA. Translation: BAC30898.1 .
CCDSi CCDS35716.1. [Q80Y84-1 ]
RefSeqi NP_690855.2. NM_152895.2. [Q80Y84-1 ]
UniGenei Mm.28995.
Mm.391994.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EQY NMR - A 94-208 [» ]
DisProti DP00711.
ProteinModelPortali Q80Y84.
SMRi Q80Y84. Positions 31-208, 306-601, 1177-1223, 1486-1544.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 217610. 3 interactions.
IntActi Q80Y84. 4 interactions.

PTM databases

PhosphoSitei Q80Y84.

Proteomic databases

MaxQBi Q80Y84.
PaxDbi Q80Y84.
PRIDEi Q80Y84.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000047714 ; ENSMUSP00000038138 ; ENSMUSG00000042207 . [Q80Y84-1 ]
ENSMUST00000112198 ; ENSMUSP00000107817 ; ENSMUSG00000042207 . [Q80Y84-2 ]
GeneIDi 75605.
KEGGi mmu:75605.
UCSCi uc007csg.2. mouse. [Q80Y84-2 ]
uc011wsg.1. mouse. [Q80Y84-1 ]

Organism-specific databases

CTDi 10765.
MGIi MGI:1922855. Kdm5b.
Rougei Search...

Phylogenomic databases

eggNOGi NOG327026.
GeneTreei ENSGT00530000063118.
HOGENOMi HOG000290719.
InParanoidi Q80Y84.
KOi K11446.
OMAi PHSSVER.
OrthoDBi EOG7D85VK.
PhylomeDBi Q80Y84.
TreeFami TF106476.

Enzyme and pathway databases

Reactomei REACT_256030. HDMs demethylate histones.

Miscellaneous databases

EvolutionaryTracei Q80Y84.
NextBioi 343484.
PROi Q80Y84.
SOURCEi Search...

Gene expression databases

Bgeei Q80Y84.
ExpressionAtlasi Q80Y84. baseline and differential.
Genevestigatori Q80Y84.

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. 3 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. "Characterisation and developmental expression of mouse Plu-1, a homologue of a human nuclear protein (PLU-1) which is specifically up-regulated in breast cancer."
    Madsen B., Spencer-Dene B., Poulsom R., Hall D., Lu P.J., Scott K., Shaw A.T., Burchell J.M., Freemont P., Taylor-Papadimitriou J.
    Mech. Dev. 119:S239-S246(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: BALB/c.
    Tissue: Testis.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  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] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "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 1-1433.
    Strain: C57BL/6J.
    Tissue: Aorta.
  5. "PLU-1 nuclear protein, which is upregulated in breast cancer, shows restricted expression in normal human adult tissues: a new cancer/testis antigen?"
    Barrett A., Madsen B., Copier J., Lu P.J., Cooper L., Scibetta A.G., Burchell J., Taylor-Papadimitriou J.
    Int. J. Cancer 101:581-588(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "PLU-1, a transcriptional repressor and putative testis-cancer antigen, has a specific expression and localisation pattern during meiosis."
    Madsen B., Tarsounas M., Burchell J.M., Hall D., Poulsom R., Taylor-Papadimitriou J.
    Chromosoma 112:124-132(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  7. "The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases."
    Iwase S., Lan F., Bayliss P., de la Torre-Ubieta L., Huarte M., Qi H.H., Whetstine J.R., Bonni A., Roberts T.M., Shi Y.
    Cell 128:1077-1088(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins."
    Seward D.J., Cubberley G., Kim S., Schonewald M., Zhang L., Tripet B., Bentley D.L.
    Nat. Struct. Mol. Biol. 14:240-242(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF HIS-499.
  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.
  10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-832, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiKDM5B_MOUSE
AccessioniPrimary (citable) accession number: Q80Y84
Secondary accession number(s): Q5DTR9, Q8BLU1, Q8JZL8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 1, 2003
Last modified: November 26, 2014
This is version 99 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

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3