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Q9UGL1

- KDM5B_HUMAN

UniProt

Q9UGL1 - KDM5B_HUMAN

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Protein

Lysine-specific demethylase 5B

Gene

KDM5B

Organism
Homo sapiens (Human)
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. Favors the proliferation of breast cancer cells by repressing tumor suppressor genes such as BRCA1 and HOXA5. In contrast, may act as a tumor suppressor for melanoma. Represses the CLOCK-ARNTL/BMAL1 heterodimer-mediated transcriptional activation of the core clock component PER2 By similarity.By similarity4 Publications

Cofactori

Binds 1 Fe2+ 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: GDB
  2. histone demethylase activity (H3-dimethyl-K4 specific) Source: UniProtKB
  3. histone demethylase activity (H3-trimethyl-K4 specific) Source: UniProtKB
  4. 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
  5. sequence-specific DNA binding transcription factor activity Source: ProtInc
  6. transcription corepressor activity Source: UniProtKB
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. histone H3-K4 demethylation Source: UniProtKB
  2. histone H3-K4 demethylation, trimethyl-H3-K4-specific Source: GOC
  3. negative regulation of transcription, DNA-templated Source: GDB
  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

Names & Taxonomyi

Protein namesi
Recommended name:
Lysine-specific demethylase 5B (EC:1.14.11.-)
Alternative name(s):
Cancer/testis antigen 31
Short name:
CT31
Histone demethylase JARID1B
Jumonji/ARID domain-containing protein 1B
PLU-1
Retinoblastoma-binding protein 2 homolog 1
Short name:
RBP2-H1
Gene namesi
Name:KDM5B
Synonyms:JARID1B, PLU1, RBBP2H1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:18039. KDM5B.

Subcellular locationi

Nucleus 2 PublicationsPROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleus Source: GDB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi335 – 3351H → A: Slightly impairs transcription repression ability. 1 Publication
Mutagenesisi499 – 4991H → Y: Abolishes enzymatic activity. 1 Publication
Mutagenesisi1200 – 12001H → A: Impairs transcription repression ability and interaction with HDAC4. 1 Publication

Organism-specific databases

PharmGKBiPA164721626.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15441544Lysine-specific demethylase 5BPRO_0000292412Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei832 – 8321N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9UGL1.
PaxDbiQ9UGL1.
PRIDEiQ9UGL1.

PTM databases

PhosphoSiteiQ9UGL1.

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in testis. Down-regulated in melanoma and glioblastoma. Up-regulated in breast cancer (at protein level).5 Publications

Gene expression databases

BgeeiQ9UGL1.
CleanExiHS_JARID1B.
ExpressionAtlasiQ9UGL1. baseline and differential.
GenevestigatoriQ9UGL1.

Organism-specific databases

HPAiHPA027179.

Interactioni

Subunit structurei

Interacts with FOXG1B, PAX9, MYC, MYCN and RB1. Interacts with HDAC1, HDAC4, HDAC5 and HDAC7.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTCFP497118EBI-2514978,EBI-932887

Protein-protein interaction databases

BioGridi115984. 65 interactions.
DIPiDIP-53652N.
IntActiQ9UGL1. 3 interactions.
STRINGi9606.ENSP00000356234.

Structurei

Secondary structure

1
1544
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1495 – 15006Combined sources
Beta strandi1502 – 15054Combined sources
Turni1506 – 15094Combined sources
Beta strandi1511 – 15144Combined sources
Helixi1515 – 15184Combined sources
Helixi1522 – 15265Combined sources
Helixi1533 – 15375Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MA5NMR-A1487-1544[»]
2MNYNMR-A306-360[»]
2MNZNMR-A306-360[»]
DisProtiDP00712.
ProteinModelPortaliQ9UGL1.
SMRiQ9UGL1. Positions 31-208, 310-601, 1177-1223, 1486-1544.
ModBaseiSearch...
MobiDBiSearch...

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1434 – 14396Poly-Lys

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.

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.
InParanoidiQ9UGL1.
KOiK11446.
OMAiELMMEAQ.
OrthoDBiEOG7D85VK.
PhylomeDBiQ9UGL1.
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: Q9UGL1-1) [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
MEAATTLHPG 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
TDTKDKEYKP HDIPQRQSVQ PSETCPPARR AKRMRAEAMN IKIEPEETTE
260 270 280 290 300
ARTHNLRRRM GCPTPKCENE KEMKSSIKQE PIERKDYIVE NEKEKPKSRS
310 320 330 340 350
KKATNAVDLY VCLLCGSGND EDRLLLCDGC DDSYHTFCLI PPLHDVPKGD
360 370 380 390 400
WRCPKCLAQE CSKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM
410 420 430 440 450
VPTELVEKEF WRLVSTIEED VTVEYGADIA SKEFGSGFPV RDGKIKLSPE
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 QCVKCKTTCF
710 720 730 740 750
MSAISCSCKP GLLVCLHHVK ELCSCPPYKY KLRYRYTLDD 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 DFQQHSQKLL SEETPSAAEL QDLLDVSFEF
910 920 930 940 950
DVELPQLAEM RIRLEQARWL EEVQQACLDP SSLTLDDMRR LIDLGVGLAP
960 970 980 990 1000
YSAVEKAMAR LQELLTVSEH WDDKAKSLLK ARPRHSLNSL ATAVKEIEEI
1010 1020 1030 1040 1050
PAYLPNGAAL KDSVQRARDW LQDVEGLQAG GRVPVLDTLI ELVTRGRSIP
1060 1070 1080 1090 1100
VHLNSLPRLE TLVAEVQAWK ECAVNTFLTE NSPYSLLEVL CPRCDIGLLG
1110 1120 1130 1140 1150
LKRKQRKLKE PLPNGKKKST KLESLSDLER ALTESKETAS AMATLGEARL
1160 1170 1180 1190 1200
REMEALQSLR LANEGKLLSP LQDVDIKICL CQKAPAAPMI QCELCRDAFH
1210 1220 1230 1240 1250
TSCVAVPSIS QGLRIWLCPH CRRSEKPPLE KILPLLASLQ RIRVRLPEGD
1260 1270 1280 1290 1300
ALRYMIERTV NWQHRAQQLL SSGNLKFVQD RVGSGLLYSR WQASAGQVSD
1310 1320 1330 1340 1350
TNKVSQPPGT TSFSLPDDWD NRTSYLHSPF STGRSCIPLH GVSPEVNELL
1360 1370 1380 1390 1400
MEAQLLQVSL PEIQELYQTL LAKPSPAQQT DRSSPVRPSS EKNDCCRGKR
1410 1420 1430 1440 1450
DGINSLERKL KRRLEREGLS SERWERVKKM RTPKKKKIKL SHPKDMNNFK
1460 1470 1480 1490 1500
LERERSYELV RSAETHSLPS DTSYSEQEDS EDEDAICPAV SCLQPEGDEV
1510 1520 1530 1540
DWVQCDGSCN QWFHQVCVGV SPEMAEKEDY ICVRCTVKDA PSRK
Length:1,544
Mass (Da):175,658
Last modified:May 18, 2010 - v3
Checksum:i70A0738D9A709F61
GO
Isoform 2 (identifier: Q9UGL1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     237-237: E → ERQSLAVLPRLECSGAILAHCNLRLLDSSNSSASASQ

Show »
Length:1,580
Mass (Da):179,409
Checksum:i61B03B8A7EE16B3C
GO

Sequence cautioni

The sequence CAB63108.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti78 – 781V → G in CAB63108. (PubMed:10878660)Curated
Sequence conflicti585 – 5895AYHSG → VPQW in AAD16061. (PubMed:10616211)Curated
Sequence conflicti708 – 7081C → W in AAD16061. (PubMed:10616211)Curated
Sequence conflicti759 – 7591A → P in AAD16061. (PubMed:10616211)Curated
Sequence conflicti771 – 7711N → T in AAD16061. (PubMed:10616211)Curated
Sequence conflicti771 – 7711N → T in CAB63108. (PubMed:10878660)Curated
Sequence conflicti1182 – 11821Q → R in AAD16061. (PubMed:10616211)Curated
Sequence conflicti1293 – 12931A → P in AAD16061. (PubMed:10616211)Curated
Sequence conflicti1307 – 13071P → L in AAD16061. (PubMed:10616211)Curated
Sequence conflicti1331 – 13311S → ST in AAD16061. (PubMed:10616211)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei237 – 2371E → ERQSLAVLPRLECSGAILAH CNLRLLDSSNSSASASQ in isoform 2. 1 PublicationVSP_026408

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ132440 mRNA. Translation: CAB43532.1.
AF087481 mRNA. Translation: AAD16061.1.
AJ243706 mRNA. Translation: CAB63108.1. Different initiation.
AC098934 Genomic DNA. No translation available.
AC104463 Genomic DNA. No translation available.
CCDSiCCDS30974.1. [Q9UGL1-1]
RefSeqiNP_006609.3. NM_006618.3. [Q9UGL1-1]
UniGeneiHs.443650.

Genome annotation databases

EnsembliENST00000367264; ENSP00000356233; ENSG00000117139. [Q9UGL1-2]
ENST00000367265; ENSP00000356234; ENSG00000117139. [Q9UGL1-1]
GeneIDi10765.
KEGGihsa:10765.
UCSCiuc001gyf.3. human. [Q9UGL1-1]
uc009xag.3. human. [Q9UGL1-2]

Polymorphism databases

DMDMi296439317.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ132440 mRNA. Translation: CAB43532.1 .
AF087481 mRNA. Translation: AAD16061.1 .
AJ243706 mRNA. Translation: CAB63108.1 . Different initiation.
AC098934 Genomic DNA. No translation available.
AC104463 Genomic DNA. No translation available.
CCDSi CCDS30974.1. [Q9UGL1-1 ]
RefSeqi NP_006609.3. NM_006618.3. [Q9UGL1-1 ]
UniGenei Hs.443650.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2MA5 NMR - A 1487-1544 [» ]
2MNY NMR - A 306-360 [» ]
2MNZ NMR - A 306-360 [» ]
DisProti DP00712.
ProteinModelPortali Q9UGL1.
SMRi Q9UGL1. Positions 31-208, 310-601, 1177-1223, 1486-1544.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115984. 65 interactions.
DIPi DIP-53652N.
IntActi Q9UGL1. 3 interactions.
STRINGi 9606.ENSP00000356234.

Chemistry

GuidetoPHARMACOLOGYi 2681.

PTM databases

PhosphoSitei Q9UGL1.

Polymorphism databases

DMDMi 296439317.

Proteomic databases

MaxQBi Q9UGL1.
PaxDbi Q9UGL1.
PRIDEi Q9UGL1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367264 ; ENSP00000356233 ; ENSG00000117139 . [Q9UGL1-2 ]
ENST00000367265 ; ENSP00000356234 ; ENSG00000117139 . [Q9UGL1-1 ]
GeneIDi 10765.
KEGGi hsa:10765.
UCSCi uc001gyf.3. human. [Q9UGL1-1 ]
uc009xag.3. human. [Q9UGL1-2 ]

Organism-specific databases

CTDi 10765.
GeneCardsi GC01M202696.
H-InvDB HIX0001478.
HGNCi HGNC:18039. KDM5B.
HPAi HPA027179.
MIMi 605393. gene.
neXtProti NX_Q9UGL1.
PharmGKBi PA164721626.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG327026.
GeneTreei ENSGT00530000063118.
HOGENOMi HOG000290719.
InParanoidi Q9UGL1.
KOi K11446.
OMAi ELMMEAQ.
OrthoDBi EOG7D85VK.
PhylomeDBi Q9UGL1.
TreeFami TF106476.

Miscellaneous databases

ChiTaRSi KDM5B. human.
GeneWikii JARID1B.
GenomeRNAii 10765.
NextBioi 40877.
PROi Q9UGL1.
SOURCEi Search...

Gene expression databases

Bgeei Q9UGL1.
CleanExi HS_JARID1B.
ExpressionAtlasi Q9UGL1. baseline and differential.
Genevestigatori Q9UGL1.

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. "A novel gene (PLU-1) containing highly conserved putative DNA/chromatin binding motifs is specifically up-regulated in breast cancer."
    Lu P.J., Sundquist K., Baeckstrom D., Poulsom R., Hanby A., Meier-Ewert S., Jones T., Mitchell M., Pitha-Rowe P., Freemont P., Taylor-Papadimitriou J.
    J. Biol. Chem. 274:15633-15645(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Mammary cancer.
  2. "Deficiency of a novel retinoblastoma binding protein 2-homolog is a consistent feature of sporadic human melanoma skin cancer."
    Vogt T., Kroiss M., McClelland M., Gruss C., Becker B., Bosserhoff A.K., Rumpler G., Bogenrieder T., Landthaler M., Stolz W.
    Lab. Invest. 79:1615-1627(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Tissue: Teratocarcinoma.
  3. "Isolation and chromosomal localization of a new human retinoblastoma binding protein 2 homologue 1a (RBBP2H1A)."
    Kashuba V., Protopopov A., Podowski R., Gizatullin R., Li J., Klein G., Wahlestedt C., Zabarovsky E.
    Eur. J. Hum. Genet. 8:407-413(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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, SUBCELLULAR LOCATION.
  6. "Human PLU-1 has transcriptional repression properties and interacts with the developmental transcription factors BF-1 and PAX9."
    Tan K., Shaw A.L., Madsen B., Jensen K., Taylor-Papadimitriou J., Freemont P.S.
    J. Biol. Chem. 278:20507-20513(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FOXG1B AND PAX9.
  7. "Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding protein downregulated in malignant melanomas."
    Roesch A., Becker B., Meyer S., Wild P., Hafner C., Landthaler M., Vogt T.
    Mod. Pathol. 18:1249-1257(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INTERACTION WITH RB1.
  8. "Re-expression of the retinoblastoma-binding protein 2-homolog 1 reveals tumor-suppressive functions in highly metastatic melanoma cells."
    Roesch A., Becker B., Schneider-Brachert W., Hagen I., Landthaler M., Vogt T.
    J. Invest. Dermatol. 126:1850-1859(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RB1.
  9. "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.
  10. "The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth."
    Secombe J., Li L., Carlos L., Eisenman R.N.
    Genes Dev. 21:537-551(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYC AND MYCN.
  11. "Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases."
    Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K., Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P., Taylor-Papadimitriou J.
    Int. J. Cancer 121:265-275(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC1; HDAC4; HDAC5 AND HDAC7, MUTAGENESIS OF HIS-335 AND HIS-1200.
  12. "PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation."
    Yamane K., Tateishi K., Klose R.J., Fang J., Fabrizio L.A., Erdjument-Bromage H., Taylor-Papadimitriou J., Tempst P., Zhang Y.
    Mol. Cell 25:801-812(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF HIS-499.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiKDM5B_HUMAN
AccessioniPrimary (citable) accession number: Q9UGL1
Secondary accession number(s): O95811, Q15752, Q9Y3Q5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 109 of the entry and version 3 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3