Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q9Y2K7 (JHD1A_HUMAN)

Last modified November 4, 2008. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    JmjC domain-containing histone demethylation protein 1A
    EC=1.14.11.27
Alternative name(s):
    [Histone-H3]-lysine-36 demethylase 1A
    F-box/LRR-repeat protein 11
    F-box and leucine-rich repeat protein 11
    F-box protein FBL7
    F-box protein Lilina
    CXXC-type zinc finger protein 8
Gene names
Name: FBXL11
Synonyms: CXXC8, FBL7, JHDM1A, KIAA1004
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1162 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylted H3 'Lys-36'. May also recognize and bind to some phosphorylated proteins and promotes their ubiquitination and degradation.

Catalytic activity

Protein N(6),N(6)-dimethyl-L-lysine + 2-oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO(2).

Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O(2) = protein L-lysine + succinate + formaldehyde + CO(2).

Cofactor

Binds 1 Fe(2+) ion per subunit.

Subunit structure

Part of a SCF (SKP1-cullin-F-box) protein ligase complex By similarity.

Subcellular location

NucleusProbable.

Tissue specificity

Widely expressed, with highest levels in brain, testis and ovary, followed by lung.

Domain

The JmjC domain mediates the demethylation activity.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR.

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 3 LRR (leucine-rich) repeats.

Contains 1 PHD-type zinc finger.

Sequence caution

The sequence BAB15795.1 differs from that shown. Reason: Frameshift at position 410.

Ontologies

Keywords

   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainLeucine-rich repeat
Repeat
Zinc-finger
   LigandIron
Metal-binding
Zinc
   Molecular functionChromatin regulator
Dioxygenase
Oxidoreductase
   PTMPhosphoprotein

Gene Ontology (GO)

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SKP1P632081EBI-765758,EBI-307486

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y2K7-1)

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: Q9Y2K7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-306: Missing.
Notes: No experimental confirmation available.
Isoform 3 (identifier: Q9Y2K7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     774-782: REKENNPSG → LRQETLDKN
     783-1162: Missing.
Notes: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11621162JmjC domain-containing histone demethylation protein 1A
PRO_0000119855

Regions

Domain148 – 316169JmjC
Domain889 – 93648F-box
Repeat1000 – 102526LRR 1
Repeat1063 – 109129LRR 2
Repeat1095 – 111824LRR 3
Zinc finger564 – 61047CXXC-type
Zinc finger617 – 67862PHD-type

Sites

Metal binding2121Iron; catalytic Probable
Metal binding2141Iron; catalytic By similarity
Metal binding2841Iron; catalytic By similarity
Binding site2091Substrate By similarity
Binding site2291Substrate By similarity

Amino acid modifications

Modified residue281Phosphoserine
Modified residue5341Phosphothreonine
Modified residue5501Phosphothreonine
Modified residue5581Phosphoserine
Modified residue6321Phosphothreonine
Modified residue7131Phosphothreonine
Modified residue7181Phosphoserine
Modified residue7201Phosphothreonine
Modified residue7311Phosphoserine
Modified residue7391Phosphoserine
Modified residue7401Phosphoserine

Natural variations

Alternative sequence1 – 306306Missing in isoform 2.
VSP_017468
Alternative sequence774 – 7829REKENNPSG → LRQETLDKN in isoform 3.
VSP_017469
Alternative sequence783 – 1162380Missing in isoform 3.
VSP_017470

Experimental info

Mutagenesis2121H → A: Abolishes histone demethylase activity
Sequence conflict5181K → I in AAH47371. Ref.5
Sequence conflict6571D → G in AAH47371. Ref.5
Sequence conflict11281Missing in AAH01203. Ref.5

Sequences

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

Last modified November 7, 2003. Version 3.
Checksum: 88620A363A5C5842

FASTA1,162132,793
        10         20         30         40         50         60 
MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLHTNKYN ANFVTFMEGK 

        70         80         90        100        110        120 
DFNVEYIQRG GLRDPLIFKN SDGLGIKMPD PDFTVNDVKM CVGSRRMVDV MDVNTQKGIE 

       130        140        150        160        170        180 
MTMAQWTRYY ETPEEEREKL YNVISLEFSH TRLENMVQRP STVDFIDWVD NMWPRHLKES 

       190        200        210        220        230        240 
QTESTNAILE MQYPKVQKYC LMSVRGCYTD FHVDFGGTSV WYHIHQGGKV FWLIPPTAHN 

       250        260        270        280        290        300 
LELYENWLLS GKQGDIFLGD RVSDCQRIEL KQGYTFVIPS GWIHAVYTPT DTLVFGGNFL 

       310        320        330        340        350        360 
HSFNIPMQLK IYNIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL TKEFQKESLS 

       370        380        390        400        410        420 
MDLELNGLES GNGDEEAVDR EPRRLSSRRS VLTSPVANGV NLDYDGLGKT CRSLPSLKKT 

       430        440        450        460        470        480 
LAGDSSSDCS RGSHNGQVWD PQCAPRKDRQ VHLTHFELEG LRCLVDKLES LPLHKKCVPT 

       490        500        510        520        530        540 
GIEDEDALIA DVKILLEELA NSDPKLALTG VPIVQWPKRD KLKFPTRPKV RVPTIPITKP 

       550        560        570        580        590        600 
HTMKPAPRLT PVRPAAASPI VSGARRRRVR CRKCKACVQG ECGVCHYCRD MKKFGGPGRM 

       610        620        630        640        650        660 
KQSCVLRQCL APRLPHSVTC SLCGEVDQNE ETQDFEKKLM ECCICNEIVH PGCLQMDGEG 

       670        680        690        700        710        720 
LLNEELPNCW ECPKCYQEDS SEKAQKRKME ESDEEAVQAK VLRPLRSCDE PLTPPPHSPT 

       730        740        750        760        770        780 
SMLQLIHDPV SPRGMVTRSS PGAGPSDHHS ASRDERFKRR QLLRLQATER TMVREKENNP 

       790        800        810        820        830        840 
SGKKELSEVE KAKIRGSYLT VTLQRPTKEL HGTSIVPKLQ AITASSANLR HSPRVLVQHC 

       850        860        870        880        890        900 
PARTPQRGDE EGLGGEEEEE EEEEEEDDSA EEGGAARLNG RGSWAQDGDE SWMQREVWMS 

       910        920        930        940        950        960 
VFRYLSRREL CECMRVCKTW YKWCCDKRLW TKIDLSRCKA IVPQALSGII KRQPVSLDLS 

       970        980        990       1000       1010       1020 
WTNISKKQLT WLVNRLPGLK DLLLAGCSWS AVSALSTSSC PLLRTLDLRW AVGIKDPQIR 

      1030       1040       1050       1060       1070       1080 
DLLTPPADKP GQDNRSKLRN MTDFRLAGLD ITDATLRLII RHMPLLSRLD LSHCSHLTDQ 

      1090       1100       1110       1120       1130       1140 
SSNLLTAVGS STRYSLTELN MAGCNKLTDQ TLIYLRRIAN VTLIDLRGCK QITRKACEHF 

      1150       1160 
ISDLSINSLY CLSDEKLIQK IS 

« Hide

Isoform 2 [UniParc].

Checksum: C1351A450B4482E0
Show »

85696,859
Isoform 3 [UniParc].

Checksum: 667E9A3E503C6550
Show »

78289,948

References

« Hide 'large scale' references
[1]"cDNA cloning and expression analysis of new members of the mammalian F-box protein family."
Ilyin G.P., Rialland M., Pigeon C., Guguen-Guillouzo C.
Genomics 67:40-47(2000) [PubMed: 10945468] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed: 10231032] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Brain.
[3]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed: 12168954] [Abstract]
Cited for: SEQUENCE REVISION.
[4]"Characterization of long cDNA clones from human adult spleen."
Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.
DNA Res. 7:357-366(2000) [PubMed: 11214971] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Spleen.
[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] (ISOFORMS 1; 2 AND 3).
Tissue: Eye, Testis and Uterus.
[6]Pagano M.
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 667-1162.
[7]The German cDNA consortium
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1134-1162.
Tissue: Testis.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, MUTAGENESIS OF HIS-212.
[10]"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 THR-534, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632, MASS SPECTROMETRY.
[12]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550; SER-558; THR-713; SER-718; THR-720; SER-731; SER-739 AND SER-740, MASS SPECTROMETRY.

Cross-references

Sequence databases

AB023221 mRNA. Translation: BAA76848.2. Different initiation.
AK024505 mRNA. Translation: BAB15795.1. Frameshift.
BC001203 mRNA. Translation: AAH01203.1.
BC047371 mRNA. Translation: AAH47371.1.
BC047486 mRNA. Translation: AAH47486.1.
BC064360 mRNA. Translation: AAH64360.1.
AF179221 mRNA. Translation: AAD56012.1. Different initiation.
AL117517 mRNA. Translation: CAH10721.1.
RefSeqNP_036440.1.
UniGeneHs.124147

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9Y2K7.

PTM databases

PhosphoSiteQ9Y2K7.

Genome annotation databases

EnsemblENSG00000173120. Homo sapiens. [Contig view]
GeneID22992.
KEGGhsa:22992.

Organism-specific databases

H-InvDBHIX0023005.
HGNCHGNC:13606. FBXL11.
HPACAB012272.
MIM605657. gene.
PharmGKBPA28020.
HUGESearch...
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOVERGENQ9Y2K7.

Gene expression databases

ArrayExpressQ9Y2K7.
CleanExHS_FBXL11.

Family and domain databases

InterProIPR001810. F-box.
IPR001611. LRR.
IPR013129. TF_JmjC.
IPR003347. TF_JmjC_AAH.
IPR002857. Znf_CXXC.
IPR001965. Znf_PHD.
[Graphical view]
PfamPF00646. F-box. 1 hit.
PF02373. JmjC. 1 hit.
PF00560. LRR_1. 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. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
BLOCKSSearch...
ProtoNetSearch...

Other Resources

NextBio43847.
SOURCESearch...

Entry information

Entry nameJHD1A_HUMAN
AccessionPrimary (citable) accession number: Q9Y2K7
Secondary accession number(s): Q49A21 expand/collapse secondary AC list , Q4G0M3, Q69YY8, Q9BVH5, Q9H7H5, Q9UK66
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 7, 2003
Last modified: November 4, 2008
This is version 67 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

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

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

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