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Q8NHM5 (KDM2B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysine-specific demethylase 2B

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

Protein attributes

Sequence length1336 AA.
Sequence statusComplete.
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. Ref.7 Ref.8

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 SKP1 and CUL1 By similarity.

Subcellular location

Nucleusnucleolus Ref.8.

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 7 LRR (leucine-rich) repeats.

Contains 1 PHD-type zinc finger.

Sequence caution

The sequence AAH08735.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAB55112.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB55301.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC11159.1 differs from that shown. Reason: Erroneous initiation.

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
rRNA-binding
Zinc
   Molecular functionChromatin regulator
Dioxygenase
Oxidoreductase
Repressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processembryonic camera-type eye morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

forebrain development

Inferred from sequence or structural similarity. Source: BHF-UCL

fourth ventricle development

Inferred from sequence or structural similarity. Source: BHF-UCL

hindbrain development

Inferred from sequence or structural similarity. Source: BHF-UCL

histone H2A monoubiquitination

Inferred from direct assay PubMed 16943429. Source: UniProtKB

histone demethylation

Traceable author statement PubMed 21220025. Source: GOC

initiation of neural tube closure

Inferred from sequence or structural similarity. Source: BHF-UCL

lateral ventricle development

Inferred from sequence or structural similarity. Source: BHF-UCL

midbrain development

Inferred from sequence or structural similarity. Source: BHF-UCL

midbrain-hindbrain boundary morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of neural precursor cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of neuron apoptotic process

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

spermatogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

third ventricle development

Inferred from sequence or structural similarity. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Non-traceable author statement PubMed 10799292. Source: UniProtKB

   Molecular_functionDNA binding

Non-traceable author statement PubMed 10799292. Source: UniProtKB

histone demethylase activity

Traceable author statement PubMed 21220025. Source: BHF-UCL

histone demethylase activity (H3-K36 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

rRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

BCORQ6W2J92EBI-3955564,EBI-950027

Alternative products

This entry describes 4 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.
Isoform 4 (identifier: Q8NHM5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: MAGPQMGGSAEDHPPRKRHAAEKQKKKTVIYTKCFEFESATQ → MEAEKDSGRRL
     818-855: Missing.
     1320-1336: VSVQFGQVEEKLLQKLS → SFQGRSCSTTRLGDE
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
Repeat1093 – 112028LRR 1
Repeat1133 – 115422LRR 2
Repeat1156 – 118227LRR 3
Repeat1222 – 124726LRR 4
Repeat1248 – 127730LRR 5
Repeat1278 – 130225LRR 6
Repeat1303 – 133634LRR 7
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 residue4741Phosphoserine Ref.13
Modified residue4771Phosphoserine Ref.13
Modified residue4931Phosphothreonine Ref.11 Ref.13
Modified residue4971Phosphoserine Ref.13
Modified residue9751Phosphoserine Ref.11
Modified residue9791Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 4242MAGPQ…ESATQ → MEAEKDSGRRL in isoform 4.
VSP_043146
Alternative sequence7301K → KAYK in isoform 2.
VSP_011340
Alternative sequence818 – 85538Missing in isoform 4.
VSP_043147
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
Alternative sequence1320 – 133617VSVQF…LQKLS → SFQGRSCSTTRLGDE in isoform 4.
VSP_043148

Experimental info

Sequence conflict8641L → F in BAC11159. Ref.5
Sequence conflict12261T → R in BAC11159. Ref.5
Sequence conflict12951I → T in BAC11159. Ref.5
Sequence conflict13341K → R in BAC11159. Ref.5

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 [UniParc].

Checksum: 3329D5375AD25930
Show »

FASTA1,306149,034
Isoform 3 [UniParc].

Checksum: BCBDAE3F675E017C
Show »

FASTA1,326151,328
Isoform 4 [UniParc].

Checksum: 69C8C16EFDE3541C
Show »

FASTA1,265144,769

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]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 504-1336 (ISOFORM 1).
Tissue: Hippocampus.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-1336 (ISOFORM 3).
Tissue: Testis.
[5]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.
[6]"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 710-1336 (ISOFORM 1).
Tissue: Brain.
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[9]"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.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-493; SER-975 AND SER-979, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; SER-477; THR-493 AND SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ459424 mRNA. Translation: CAD30700.1.
AK027440 mRNA. Translation: BAB55112.1. Different initiation.
AK027692 mRNA. Translation: BAB55301.1. Different initiation.
AK074718 mRNA. Translation: BAC11159.1. Different initiation.
AK127328 mRNA. Translation: BAG54483.1.
AC048337 Genomic DNA. No translation available.
AC073650 Genomic DNA. No translation available.
AC145422 Genomic DNA. No translation available.
AL133572 mRNA. Translation: CAB63721.2.
AB031230 mRNA. Translation: BAA97672.1.
BC008735 mRNA. Translation: AAH08735.2. Different initiation.
PIRT43477.
RefSeqNP_001005366.1. NM_001005366.1.
NP_115979.3. NM_032590.4.
UniGeneHs.524800.

3D structure databases

ProteinModelPortalQ8NHM5.
SMRQ8NHM5. Positions 9-573, 609-722, 1063-1333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124197. 19 interactions.
IntActQ8NHM5. 3 interactions.
STRING9606.ENSP00000366271.

PTM databases

PhosphoSiteQ8NHM5.

Polymorphism databases

DMDM51316032.

Proteomic databases

PaxDbQ8NHM5.
PRIDEQ8NHM5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377069; ENSP00000366269; ENSG00000089094. [Q8NHM5-4]
ENST00000377071; ENSP00000366271; ENSG00000089094. [Q8NHM5-1]
ENST00000542973; ENSP00000437821; ENSG00000089094.
ENST00000606143; ENSP00000476018; ENSG00000272358. [Q8NHM5-1]
ENST00000606773; ENSP00000476251; ENSG00000272358. [Q8NHM5-4]
ENST00000607408; ENSP00000476072; ENSG00000272358.
GeneID84678.
KEGGhsa:84678.
UCSCuc001uaq.3. human. [Q8NHM5-1]
uc001uas.3. human. [Q8NHM5-4]

Organism-specific databases

CTD84678.
GeneCardsGC12M121866.
HGNCHGNC:13610. KDM2B.
MIM609078. gene.
neXtProtNX_Q8NHM5.
PharmGKBPA164721242.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG290496.
HOGENOMHOG000007396.
InParanoidQ8NHM5.
KOK10276.
OMANAEDRMA.
OrthoDBEOG78SQH0.
PhylomeDBQ8NHM5.
TreeFamTF106480.

Enzyme and pathway databases

SignaLinkQ8NHM5.

Gene expression databases

ArrayExpressQ8NHM5.
BgeeQ8NHM5.
CleanExHS_FBXL10.
GenevestigatorQ8NHM5.

Family and domain databases

InterProIPR001810. F-box_dom.
IPR003347. JmjC_dom.
IPR002857. Znf_CXXC.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
[Graphical view]
PfamPF00646. F-box. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
SMARTSM00256. FBOX. 1 hit.
SM00558. JmjC. 1 hit.
SM00249. PHD. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS51184. JMJC. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKDM2B. human.
GenomeRNAi84678.
NextBio74711.
PROQ8NHM5.
SOURCESearch...

Entry information

Entry nameKDM2B_HUMAN
AccessionPrimary (citable) accession number: Q8NHM5
Secondary accession number(s): A8MRS1 expand/collapse secondary AC list , Q8NCI2, Q96HC7, Q96SL0, Q96T03, Q9NS96, Q9UF75
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 116 of the entry and version 1 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

MIM cross-references

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

Human chromosome 12

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