ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8NHM5


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name JHD1B_HUMAN
Primary accession number Q8NHM5
Secondary accession numbers Q8NCI2 Q96HC7 Q96SL0 Q96T03 Q9NS96 Q9UF75
Integrated into Swiss-Prot on August 16, 2004
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 60)
Name and origin of the protein
Protein name JmjC domain-containing histone demethylation protein 1B
Synonyms EC 1.14.11.27
[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
Protein JEMMA
CXXC-type zinc finger protein 2
Protein-containing CXXC domain 2
Gene name
Name: FBXL10
Synonyms: CXXC2, FBL10, JHDM1B, PCCX2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Hughes-Davies L.;
"JEMMA (Jumonji domain, EMSY-interactor, methyltransferase motif) is a novel protein which interacts with EMSY.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-1336 (ISOFORM 3).
TISSUE=Testis;
The German cDNA consortium;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 480-1336 (ISOFORM 2).
TISSUE=Fibroblast;
Fujino T., Hasegawa M., Shibata S., Kishimoto T., Imai S., Takano T.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 504-1336 (ISOFORM 1).
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1336 (ISOFORM 1).
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474 AND SER-497, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[7]
FUNCTION, AND ENZYME ACTIVITY.
DOI=10.1038/nature04433; PubMed=16362057 [NCBI, ExPASy, EBI, Israel, Japan]
Tsukada Y., Fang J., Erdjument-Bromage H., Warren M.E., Borchers C.H., Tempst P., Zhang Y.;
"Histone demethylation by a family of JmjC domain-containing proteins.";
Nature 439:811-816(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"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.";
J. Proteome Res. 6:4150-4162(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ459424; CAD30700.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133572; CAB63721.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB031230; BAA97672.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK027440; BAB55112.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK027692; BAB55301.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK074718; BAC11159.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008735; AAH08735.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T43477; T43477.
RefSeq NP_115979.3; -.
UniGene Hs.524800
3D structure databases
SMR Q8NHM5; 66-392.
ModBase Q8NHM5.
PTM databases
PhosphoSite Q8NHM5; -.
Organism-specific databases
GeneCards GC12M120329; -.
H-InvDB HIX0020867; -.
HGNC HGNC:13610; FBXL10.
GenAtlas FBXL10.
MIM 609078; gene. [NCBI / EBI]
PharmGKB PA134907116; -.
GeneCards Q8NHM5.
Gene expression databases
ArrayExpress Q8NHM5; -.
CleanEx HS_FBXL10; -.
GermOnline ENSG00000089094; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (non-traceable author statement from UniProtKB).
GO:0003677; Molecular function: DNA binding (non-traceable author statement from UniProtKB).
GO:0051864; Molecular function: histone demethylase activity (H3-K36 specific) (inferred from electronic annotation from EC).
GO:0005506; Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016702; Molecular function: oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (non-traceable author statement from UniProtKB).
GO:0016568; Biological process: chromatin modification (inferred from electronic annotation from UniProtKB-KW).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006355; Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001810; F-box.
IPR013129; TF_JmjC.
IPR003347; TF_JmjC_AAH.
IPR002857; Znf_CXXC.
IPR001965; Znf_PHD.
IPR013083; Znf_RING/FYVE/PHD.
Graphical view of domain structure.
Gene3D G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
Pfam PF00646; F-box; 1.
PF02373; JmjC; 1.
PF02008; zf-CXXC; 1.
Pfam graphical view of domain structure.
SMART SM00256; FBOX; 1.
SM00558; JmjC; 1.
SM00249; PHD; 1.
SMART graphical view of domain structure.
PROSITE PS50181; FBOX; FALSE_NEG.
PS51184; JMJC; 1.
PS51058; ZF_CXXC; 1.
PS01359; ZF_PHD_1; FALSE_NEG.
PS50016; ZF_PHD_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q8NHM5; -.
Genome annotation databases
Ensembl ENSG00000089094; Homo sapiens. [Contig view]
GeneID 84678; -.
Phylogenomic databases
HOVERGEN Q8NHM5; -.
Other
NextBio 74711; -.
SOURCE FBXL10; Homo sapiens.
ProtoNet Q8NHM5.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Chromatin regulator; Coiled coil; Dioxygenase; Iron; Leucine-rich repeat; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Repeat; Transcription; Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1336  1336     JmjC domain-containing histone demethylation protein 1B. PRO_0000119853
DOMAIN   178    346  169     JmjC. 
DOMAIN   1059   1105  47     F-box. 
REPEAT   1148   1171  24     LRR 1. 
REPEAT   1217   1242  26     LRR 2. 
REPEAT   1269   1293  25     LRR 3. 
REPEAT   1294   1336  43     LRR 4. 
ZN_FING   606    652  47     CXXC-type. 
ZN_FING   659    725  67     PHD-type. 
COILED   943    971  29     Potential. 
COMPBIAS   409    430  22     Glu-rich. 
COMPBIAS   1014   1056  43     Pro-rich. 
METAL   242    242        Iron; catalytic (By similarity). 
METAL   244    244        Iron; catalytic (By similarity). 
METAL   314    314        Iron; catalytic (By similarity). 
BINDING   239    239        Substrate (By similarity). 
BINDING   259    259        Substrate (By similarity). 
MOD_RES   223    223        Phosphotyrosine. 
MOD_RES   474    474        Phosphoserine. 
MOD_RES   497    497        Phosphoserine. 
VAR_SEQ   730    730        K -> KAYK (in isoform 2). VSP_011340
VAR_SEQ   856    868        LKPGKEDKLFRKK -> Q (in isoform 3). VSP_017475
VAR_SEQ   1204   1204        G -> GPG (in isoform 3). VSP_017476
VAR_SEQ   1277   1336        DCNKVTDQCLSFFKRCGNICHIDLRYCKQVTKEGCEQFIA EMSVSVQFGQVEEKLLQKLS -> ASLLGRVFGLQFWGICEPQARKNAGWA (in isoform 2). VSP_011341
CONFLICT   864    864        L -> F (in Ref. 4; BAC11159). 
CONFLICT   1226   1226        T -> R (in Ref. 4; BAC11159). 
CONFLICT   1295   1295        I -> T (in Ref. 4; BAC11159). 
CONFLICT   1334   1334        K -> R (in Ref. 4; BAC11159). 
Sequence information
Length: 1336 AA [This is the length of the unprocessed precursor] Molecular weight: 152615 Da [This is the MW of the unprocessed precursor] CRC64: 3A1A17B8EA9EA953 [This is a checksum on the sequence]
        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 

Q8NHM5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ca flag CBR Canada Mirror sites: Australia  Brazil  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!