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Reviewed, UniProtKB/Swiss-Prot Q8NHM5 (KDM2B_HUMAN)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lysine-specific demethylase 2B
    EC=1.14.11.27
Alternative name(s):
    JmjC domain-containing histone demethylation protein 1B
    [Histone-H3]-lysine-36 demethylase 1B
    F-box and leucine-rich repeat protein 10
    F-box/LRR-repeat protein 10
    F-box protein FBL10
    Jumonji domain-containing EMSY-interactor methyltransferase motif protein
      Short name=Protein JEMMA
    CXXC-type zinc finger protein 2
    Protein-containing CXXC domain 2
Gene names
Name: KDM2B
Synonyms: CXXC2, FBL10, FBXL10, JHDM1B, PCCX2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Histone demethylase that demethylates 'Lys-4' and 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation. May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.

Catalytic activity

Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2. Ref.7

Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2. Ref.7

Cofactor

Binds 1 Fe2+ ion per subunit By similarity.

Subunit structure

Directly interacts with SKP1A and CUL1 By similarity.

Subcellular location

Nucleusnucleolus.

Domain

The JmjC domain mediates demethylation activity By similarity. It is also required for repression of ribosomal RNA genes.

Sequence similarities

Belongs to the JHDM1 histone demethylase family.

Contains 1 CXXC-type zinc finger.

Contains 1 F-box domain.

Contains 1 JmjC domain.

Contains 4 LRR (leucine-rich) repeats.

Contains 1 PHD-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Leucine-rich repeat
Repeat
Zinc-finger
   LigandIron
Metal-binding
RNA-binding
Zinc
rRNA-binding
   Molecular functionChromatin regulator
Dioxygenase
Oxidoreductase
Repressor
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processchromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

modification-dependent protein catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Non-traceable author statement. Source: UniProtKB

   Molecular functionDNA binding

Non-traceable author statement. Source: UniProtKB

histone demethylase activity (H3-K36 specific)

Inferred from electronic annotation. Source: EC

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: UniProtKB

zinc ion binding

Non-traceable author statement. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8NHM5-1)

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: Q8NHM5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     730-730: K → KAYK
     1277-1336: DCNKVTDQCL...VEEKLLQKLS → ASLLGRVFGLQFWGICEPQARKNAGWA
Isoform 3 (identifier: Q8NHM5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     856-868: LKPGKEDKLFRKK → Q
     1204-1204: G → GPG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13361336Lysine-specific demethylase 2B
PRO_0000119853

Regions

Domain178 – 346169JmjC
Domain1059 – 110547F-box
Repeat1148 – 117124LRR 1
Repeat1217 – 124226LRR 2
Repeat1269 – 129325LRR 3
Repeat1294 – 133643LRR 4
Zinc finger606 – 65247CXXC-type
Zinc finger659 – 72567PHD-type
Coiled coil943 – 97129 Potential
Compositional bias409 – 43022Glu-rich
Compositional bias1014 – 105643Pro-rich

Sites

Metal binding2421Iron; catalytic By similarity
Metal binding2441Iron; catalytic By similarity
Metal binding3141Iron; catalytic By similarity
Binding site2391Substrate By similarity
Binding site2591Substrate By similarity

Amino acid modifications

Modified residue2231Phosphotyrosine Ref.9
Modified residue4741Phosphoserine Ref.6
Modified residue4971Phosphoserine Ref.6

Natural variations

Alternative sequence7301K → KAYK in isoform 2.
VSP_011340
Alternative sequence856 – 86813LKPGK…LFRKK → Q in isoform 3.
VSP_017475
Alternative sequence12041G → GPG in isoform 3.
VSP_017476
Alternative sequence1277 – 133660DCNKV…LQKLS → ASLLGRVFGLQFWGICEPQA RKNAGWA in isoform 2.
VSP_011341

Experimental info

Sequence conflict8641L → F in BAC11159. Ref.4
Sequence conflict12261T → R in BAC11159. Ref.4
Sequence conflict12951I → T in BAC11159. Ref.4
Sequence conflict13341K → R in BAC11159. Ref.4

Sequences

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

Last modified October 1, 2002. Version 1.
Checksum: 3A1A17B8EA9EA953

FASTA1,336152,615
        10         20         30         40         50         60 
MAGPQMGGSA EDHPPRKRHA AEKQKKKTVI YTKCFEFESA TQRPIDRQRY DENEDLSDVE 

        70         80         90        100        110        120 
EIVSVRGFSL EEKLRSQLYQ GDFVHAMEGK DFNYEYVQRE ALRVPLIFRE KDGLGIKMPD 

       130        140        150        160        170        180 
PDFTVRDVKL LVGSRRLVDV MDVNTQKGTE MSMSQFVRYY ETPEAQRDKL YNVISLEFSH 

       190        200        210        220        230        240 
TKLEHLVKRP TVVDLVDWVD NMWPQHLKEK QTEATNAIAE MKYPKVKKYC LMSVKGCFTD 

       250        260        270        280        290        300 
FHIDFGGTSV WYHVFRGGKI FWLIPPTLHN LALYEEWVLS GKQSDIFLGD RVERCQRIEL 

       310        320        330        340        350        360 
KQGYTFFIPS GWIHAVYTPV DSLVFGGNIL HSFNVPMQLR IYEIEDRTRV QPKFRYPFYY 

       370        380        390        400        410        420 
EMCWYVLERY VYCVTQRSHL TQEYQRESML IDAPRKPSID GFSSDSWLEM EEEACDQQPQ 

       430        440        450        460        470        480 
EEEEKDEEGE GRDRAPKPPT DGSTSPTSTP SEDQEALGKK PKAPALRFLK RTLSNESEES 

       490        500        510        520        530        540 
VKSTTLAVDY PKTPTGSPAT EVSAKWTHLT EFELKGLKAL VEKLESLPEN KKCVPEGIED 

       550        560        570        580        590        600 
PQALLEGVKN VLKEHADDDP SLAITGVPVV TWPKKTPKNR AVGRPKGKLG PASAVKLAAN 

       610        620        630        640        650        660 
RTTAGARRRR TRCRKCEACL RTECGECHFC KDMKKFGGPG RMKQSCIMRQ CIAPVLPHTA 

       670        680        690        700        710        720 
VCLVCGEAGK EDTVEEEEGK FNLMLMECSI CNEIIHPGCL KIKESEGVVN DELPNCWECP 

       730        740        750        760        770        780 
KCNHAGKTGK QKRGPGFKYA SNLPGSLLKE QKMNRDNKEG QEPAKRRSEC EEAPRRRSDE 

       790        800        810        820        830        840 
HSKKVPPDGL LRRKSDDVHL RKKRKYEKPQ ELSGRKRASS LQTSPGSSSH LSPRPPLGSS 

       850        860        870        880        890        900 
LSPWWRSSLT YFQQQLKPGK EDKLFRKKRR SWKNAEDRMA LANKPLRRFK QEPEDELPEA 

       910        920        930        940        950        960 
PPKTRESDHS RSSSPTAGPS TEGAEGPEEK KKVKMRRKRR LPNKELSREL SKELNHEIQR 

       970        980        990       1000       1010       1020 
TENSLANENQ QPIKSEPESE GEEPKRPPGI CERPHRFSKG LNGTPRELRH QLGPSLRSPP 

      1030       1040       1050       1060       1070       1080 
RVISRPPPSV SPPKCIQMER HVIRPPPISP PPDSLPLDDG AAHVMHREVW MAVFSYLSHQ 

      1090       1100       1110       1120       1130       1140 
DLCVCMRVCR TWNRWCCDKR LWTRIDLNHC KSITPLMLSG IIRRQPVSLD LSWTNISKKQ 

      1150       1160       1170       1180       1190       1200 
LSWLINRLPG LRDLVLSGCS WIAVSALCSS SCPLLRTLDV QWVEGLKDAQ MRDLLSPPTD 

      1210       1220       1230       1240       1250       1260 
NRPGQMDNRS KLRNIVELRL AGLDITDASL RLIIRHMPLL SKLHLSYCNH VTDQSINLLT 

      1270       1280       1290       1300       1310       1320 
AVGTTTRDSL TEINLSDCNK VTDQCLSFFK RCGNICHIDL RYCKQVTKEG CEQFIAEMSV 

      1330 
SVQFGQVEEK LLQKLS 

« Hide

Isoform 2.

Checksum: 3329D5375AD25930
Show »

FASTA1,306149,034
Isoform 3.

Checksum: BCBDAE3F675E017C
Show »

FASTA1,326151,328

References

« Hide 'large scale' references
[1]"JEMMA (Jumonji domain, EMSY-interactor, methyltransferase motif) is a novel protein which interacts with EMSY."
Hughes-Davies L.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-1336 (ISOFORM 3).
Tissue: Testis.
[3]Fujino T., Hasegawa M., Shibata S., Kishimoto T., Imai S., Takano T.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 480-1336 (ISOFORM 2).
Tissue: Fibroblast.
[4]"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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 504-1336 (ISOFORM 1).
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1336 (ISOFORM 1).
Tissue: Brain.
[6]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474 AND SER-497, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"Histone demethylation by a family of JmjC domain-containing proteins."
Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H., Tempst P., Zhang Y.
Nature 439:811-816(2006) [PubMed: 16362057] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY.
[8]"JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes."
Frescas D., Guardavaccaro D., Bassermann F., Koyama-Nasu R., Pagano M.
Nature 450:309-313(2007) [PubMed: 17994099] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, MASS SPECTROMETRY.
Tissue: Epithelium.
+Additional computationally mapped references.

Cross-references

Sequence databases

AJ459424 mRNA. Translation: CAD30700.1.
AL133572 mRNA. Translation: CAB63721.2.
AB031230 mRNA. Translation: BAA97672.1.
AK027440 mRNA. Translation: BAB55112.1. Different initiation.
AK027692 mRNA. Translation: BAB55301.1. Different initiation.
AK074718 mRNA. Translation: BAC11159.1. Different initiation.
BC008735 mRNA. Translation: AAH08735.2. Different initiation.
IPIIPI00185326.
IPI00737594.
IPI00747262.
PIRT43477.
RefSeqNP_115979.3.
UniGeneHs.524800

3D structure databases

SMRQ8NHM5. Positions 66-392.
ModBaseSearch...

PTM databases

PhosphoSiteQ8NHM5.

Proteomic databases

PRIDEQ8NHM5.

Genome annotation databases

EnsemblENSG00000089094. Homo sapiens. [Contig view]
GeneID84678.

Organism-specific databases

GeneCardsGC12M120329.
H-InvDBHIX0020867.
HGNCHGNC:13610. KDM2B.
MIM609078. gene.
PharmGKBPA134907116.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ8NHM5.
OMAQ8NHM5. QLKPGKE.

Enzyme and pathway databases

BRENDA1.14.11.27. 247.

Gene expression databases

ArrayExpressQ8NHM5.
BgeeQ8NHM5.
CleanExHS_FBXL10.
GermOnlineENSG00000089094. Homo sapiens.

Family and domain databases

InterProIPR001810. F-box.
IPR013129. TF_JmjC.
IPR003347. TF_JmjC_AAH.
IPR019786. Zinc_finger_PHD-type_CS.
IPR002857. Znf_CXXC.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
[Graphical view]
PfamPF00646. F-box. 1 hit.
PF02373. JmjC. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
SMARTSM00256. FBOX. 1 hit.
SM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
PROSITEPS50181. FBOX. False negative.
PS51184. JMJC. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS01359. ZF_PHD_1. False negative.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio74711.
SOURCESearch...

Entry information

Entry nameKDM2B_HUMAN
AccessionPrimary (citable) accession number: Q8NHM5
Secondary accession number(s): Q8NCI2 expand/collapse secondary AC list , Q96HC7, Q96SL0, Q96T03, Q9NS96, Q9UF75
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2002
Last modified: June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents