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Q9UGL1 (KDM5B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:KDM5B
Synonyms:JARID1B, PLU1, RBBP2H1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1544 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.8 Ref.9 Ref.12

Cofactor

Binds 1 Fe2+ ion per subunit By similarity.

Subunit structure

Interacts with FOXG1B, PAX9, MYC, MYCN and RB1. Interacts with HDAC1, HDAC4, HDAC5 and HDAC7 By similarity. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11

Subcellular location

Nucleus Ref.1 Ref.5.

Tissue specificity

Ubiquitously expressed, with highest levels in testis. Down-regulated in melanoma and glioblastoma. Up-regulated in breast cancer (at protein level). Ref.1 Ref.2 Ref.3 Ref.5 Ref.7

Domain

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 similarities

Belongs to the JARID1 histone demethylase family.

Contains 1 ARID domain.

Contains 1 JmjC domain.

Contains 1 JmjN domain.

Contains 3 PHD-type zinc fingers.

Sequence caution

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

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandIron
Metal-binding
Zinc
   Molecular functionChromatin regulator
Dioxygenase
Oxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhistone H3-K4 demethylation

Inferred from direct assay PubMed 20228790. Source: UniProtKB

histone H3-K4 demethylation, trimethyl-H3-K4-specific

Inferred from direct assay PubMed 20228790. Source: GOC

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.6. Source: GDB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Traceable author statement Ref.6. Source: GDB

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15640446. Source: GDB

histone demethylase activity (H3-dimethyl-K4 specific)

Inferred from direct assay PubMed 20228790. Source: UniProtKB

histone demethylase activity (H3-trimethyl-K4 specific)

Inferred from direct assay PubMed 20228790. Source: UniProtKB

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

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

transcription corepressor activity

Inferred from direct assay Ref.6. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UGL1-1)

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: Q9UGL1-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15441544Lysine-specific demethylase 5B
PRO_0000292412

Regions

Domain32 – 7342JmjN
Domain97 – 18791ARID
Domain453 – 619167JmjC
Zinc finger309 – 35951PHD-type 1
Zinc finger1176 – 122449PHD-type 2
Zinc finger1484 – 153855PHD-type 3
Compositional bias1434 – 14396Poly-Lys

Sites

Metal binding4991Iron; catalytic By similarity
Metal binding5021Iron; catalytic By similarity
Metal binding5871Iron; catalytic By similarity

Amino acid modifications

Modified residue8321N6-acetyllysine By similarity

Natural variations

Alternative sequence2371E → ERQSLAVLPRLECSGAILAH CNLRLLDSSNSSASASQ in isoform 2.
VSP_026408

Experimental info

Mutagenesis3351H → A: Slightly impairs transcription repression ability. Ref.11
Mutagenesis4991H → Y: Abolishes enzymatic activity. Ref.12
Mutagenesis12001H → A: Impairs transcription repression ability and interaction with HDAC4. Ref.11
Sequence conflict781V → G in CAB63108. Ref.3
Sequence conflict585 – 5895AYHSG → VPQW in AAD16061. Ref.2
Sequence conflict7081C → W in AAD16061. Ref.2
Sequence conflict7591A → P in AAD16061. Ref.2
Sequence conflict7711N → T in AAD16061. Ref.2
Sequence conflict7711N → T in CAB63108. Ref.3
Sequence conflict11821Q → R in AAD16061. Ref.2
Sequence conflict12931A → P in AAD16061. Ref.2
Sequence conflict13071P → L in AAD16061. Ref.2
Sequence conflict13311S → ST in AAD16061. Ref.2

Secondary structure

............. 1544
Helix Strand Turn

Details...

Sequences

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

Last modified May 18, 2010. Version 3.
Checksum: 70A0738D9A709F61

FASTA1,544175,658
        10         20         30         40         50         60 
MEAATTLHPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH KIRPIAEQTG 

        70         80         90        100        110        120 
ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK LNFLDQIAKY WELQGSTLKI 

       130        140        150        160        170        180 
PHVERKILDL FQLNKLVAEE GGFAVVCKDR KWTKIATKMG FAPGKAVGSH IRGHYERILN 

       190        200        210        220        230        240 
PYNLFLSGDS LRCLQKPNLT TDTKDKEYKP HDIPQRQSVQ PSETCPPARR AKRMRAEAMN 

       250        260        270        280        290        300 
IKIEPEETTE ARTHNLRRRM GCPTPKCENE KEMKSSIKQE PIERKDYIVE NEKEKPKSRS 

       310        320        330        340        350        360 
KKATNAVDLY VCLLCGSGND EDRLLLCDGC DDSYHTFCLI PPLHDVPKGD WRCPKCLAQE 

       370        380        390        400        410        420 
CSKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM VPTELVEKEF WRLVSTIEED 

       430        440        450        460        470        480 
VTVEYGADIA SKEFGSGFPV RDGKIKLSPE EEEYLDSGWN LNNMPVMEQS VLAHITADIC 

       490        500        510        520        530        540 
GMKLPWLYVG MCFSSFCWHI EDHWSYSINY LHWGEPKTWY GVPGYAAEQL ENVMKKLAPE 

       550        560        570        580        590        600 
LFVSQPDLLH QLVTIMNPNT LMTHEVPVYR TNQCAGEFVI TFPRAYHSGF NQGFNFAEAV 

       610        620        630        640        650        660 
NFCTVDWLPL GRQCVEHYRL LHRYCVFSHD EMICKMASKA DVLDVVVAST VQKDMAIMIE 

       670        680        690        700        710        720 
DEKALRETVR KLGVIDSERM DFELLPDDER QCVKCKTTCF MSAISCSCKP GLLVCLHHVK 

       730        740        750        760        770        780 
ELCSCPPYKY KLRYRYTLDD LYPMMNALKL RAESYNEWAL NVNEALEAKI NKKKSLVSFK 

       790        800        810        820        830        840 
ALIEESEMKK FPDNDLLRHL RLVTQDAEKC ASVAQQLLNG KRQTRYRSGG GKSQNQLTVN 

       850        860        870        880        890        900 
ELRQFVTQLY ALPCVLSQTP LLKDLLNRVE DFQQHSQKLL SEETPSAAEL QDLLDVSFEF 

       910        920        930        940        950        960 
DVELPQLAEM RIRLEQARWL EEVQQACLDP SSLTLDDMRR LIDLGVGLAP YSAVEKAMAR 

       970        980        990       1000       1010       1020 
LQELLTVSEH WDDKAKSLLK ARPRHSLNSL ATAVKEIEEI PAYLPNGAAL KDSVQRARDW 

      1030       1040       1050       1060       1070       1080 
LQDVEGLQAG GRVPVLDTLI ELVTRGRSIP VHLNSLPRLE TLVAEVQAWK ECAVNTFLTE 

      1090       1100       1110       1120       1130       1140 
NSPYSLLEVL CPRCDIGLLG LKRKQRKLKE PLPNGKKKST KLESLSDLER ALTESKETAS 

      1150       1160       1170       1180       1190       1200 
AMATLGEARL REMEALQSLR LANEGKLLSP LQDVDIKICL CQKAPAAPMI QCELCRDAFH 

      1210       1220       1230       1240       1250       1260 
TSCVAVPSIS QGLRIWLCPH CRRSEKPPLE KILPLLASLQ RIRVRLPEGD ALRYMIERTV 

      1270       1280       1290       1300       1310       1320 
NWQHRAQQLL SSGNLKFVQD RVGSGLLYSR WQASAGQVSD TNKVSQPPGT TSFSLPDDWD 

      1330       1340       1350       1360       1370       1380 
NRTSYLHSPF STGRSCIPLH GVSPEVNELL MEAQLLQVSL PEIQELYQTL LAKPSPAQQT 

      1390       1400       1410       1420       1430       1440 
DRSSPVRPSS EKNDCCRGKR DGINSLERKL KRRLEREGLS SERWERVKKM RTPKKKKIKL 

      1450       1460       1470       1480       1490       1500 
SHPKDMNNFK LERERSYELV RSAETHSLPS DTSYSEQEDS EDEDAICPAV SCLQPEGDEV 

      1510       1520       1530       1540 
DWVQCDGSCN QWFHQVCVGV SPEMAEKEDY ICVRCTVKDA PSRK 

« Hide

Isoform 2 [UniParc].

Checksum: 61B03B8A7EE16B3C
Show »

FASTA1,580179,409

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_006609.3. NM_006618.3.
UniGeneHs.443650.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2MA5NMR-A1487-1544[»]
DisProtDP00712.
ProteinModelPortalQ9UGL1.
SMRQ9UGL1. Positions 31-208, 307-637, 1178-1223, 1486-1544.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115984. 64 interactions.
DIPDIP-53652N.
IntActQ9UGL1. 2 interactions.
STRING9606.ENSP00000356234.

PTM databases

PhosphoSiteQ9UGL1.

Polymorphism databases

DMDM296439317.

Proteomic databases

PaxDbQ9UGL1.
PRIDEQ9UGL1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367264; ENSP00000356233; ENSG00000117139. [Q9UGL1-2]
ENST00000367265; ENSP00000356234; ENSG00000117139. [Q9UGL1-1]
GeneID10765.
KEGGhsa:10765.
UCSCuc001gyf.3. human. [Q9UGL1-1]
uc009xag.3. human. [Q9UGL1-2]

Organism-specific databases

CTD10765.
GeneCardsGC01M202696.
H-InvDBHIX0001478.
HGNCHGNC:18039. KDM5B.
HPAHPA027179.
MIM605393. gene.
neXtProtNX_Q9UGL1.
PharmGKBPA164721626.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG327026.
HOGENOMHOG000290719.
InParanoidQ9UGL1.
KOK11446.
OMAELMMEAQ.
OrthoDBEOG7D85VK.
PhylomeDBQ9UGL1.
TreeFamTF106476.

Gene expression databases

ArrayExpressQ9UGL1.
BgeeQ9UGL1.
CleanExHS_JARID1B.
GenevestigatorQ9UGL1.

Family and domain databases

Gene3D1.10.150.60. 1 hit.
3.30.40.10. 3 hits.
InterProIPR001606. 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]
PfamPF01388. 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]
SMARTSM00501. BRIGHT. 1 hit.
SM00558. JmjC. 1 hit.
SM00545. JmjN. 1 hit.
SM00249. PHD. 3 hits.
[Graphical view]
SUPFAMSSF46774. SSF46774. 1 hit.
SSF57903. SSF57903. 3 hits.
PROSITEPS51011. 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]
ProtoNetSearch...

Other

ChiTaRSKDM5B. human.
GeneWikiJARID1B.
GenomeRNAi10765.
NextBio40877.
PROQ9UGL1.
SOURCESearch...

Entry information

Entry nameKDM5B_HUMAN
AccessionPrimary (citable) accession number: Q9UGL1
Secondary accession number(s): O95811, Q15752, Q9Y3Q5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM