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Reviewed, UniProtKB/Swiss-Prot P59997 (JHD1A_MOUSE)

Last modified November 25, 2008. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
    JmjC domain-containing histone demethylation protein 1A
    EC=1.14.11.27
Alternative name(s):
    [Histone-H3]-lysine-36 demethylase 1A
    F-box and leucine-rich repeat protein 11
    F-box/LRR-repeat protein 11
Gene names
Name: Fbxl11
Synonyms: Jhdm1a, Kiaa1004
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length1161 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 By similarity.

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 By similarity.

Subunit structure

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

Subcellular location

NucleusBy similarity.

Domain

The JmjC domain mediates the demethylation activity By similarity.

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 BC076576 differs from that shown. Reason: Frameshift at position 834.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P59997-1)

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: P59997-2)

The sequence of this isoform differs from the canonical sequence as follows:
     494-494: I → S
     495-1161: Missing.
Notes: No experimental confirmation available.
Isoform 3 (identifier: P59997-3)

The sequence of this isoform differs from the canonical sequence as follows:
     321-338: PNKFRYPFYYEMCWYVLE → SNVTIICVDVSPFKADVR
     339-1161: Missing.
Notes: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11611161JmjC domain-containing histone demethylation protein 1A
PRO_0000119856

Regions

Domain148 – 316169JmjC
Domain888 – 93548F-box
Repeat999 – 102426LRR 1
Repeat1062 – 109029LRR 2
Repeat1094 – 111724LRR 3
Zinc finger564 – 61047CXXC-type
Zinc finger617 – 67862PHD-type

Sites

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

Amino acid modifications

Modified residue281Phosphoserine By similarity
Modified residue3901Phosphoserine By similarity
Modified residue3941Phosphoserine By similarity
Modified residue5341Phosphothreonine By similarity
Modified residue5501Phosphothreonine By similarity
Modified residue5581Phosphoserine By similarity
Modified residue6321Phosphothreonine
Modified residue6921Phosphoserine By similarity
Modified residue7131Phosphothreonine By similarity
Modified residue7181Phosphoserine By similarity
Modified residue7201Phosphothreonine By similarity
Modified residue7211Phosphoserine By similarity
Modified residue7311Phosphoserine By similarity
Modified residue7391Phosphoserine By similarity
Modified residue7401Phosphoserine By similarity
Modified residue8681Phosphoserine By similarity

Natural variations

Alternative sequence321 – 33818PNKFR…WYVLE → SNVTIICVDVSPFKADVR in isoform 3.
VSP_017471
Alternative sequence339 – 1161823Missing in isoform 3.
VSP_017472
Alternative sequence4941I → S in isoform 2.
VSP_017473
Alternative sequence495 – 1161667Missing in isoform 2.
VSP_017474

Experimental info

Sequence conflict1591W → R in BAE20506. Ref.1
Sequence conflict1591W → R in BC076576. Ref.2
Sequence conflict2021I → M in BAE20506. Ref.1
Sequence conflict2021I → M in BC076576. Ref.2
Sequence conflict9131M → I in AAH57051. Ref.2

Sequences

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

Last modified March 7, 2006. Version 2.
Checksum: 210BD9F65BED0AE4

FASTA1,161132,680
        10         20         30         40         50         60 
MEPEEERIRY SQRLRGTMRR RYEDDGISDD EIEGKRTFDL EEKLQTNKYN ANFVTFMEGK 

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

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

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

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

       310        320        330        340        350        360 
HSFNIPMQLK IYSIEDRTRV PNKFRYPFYY EMCWYVLERY VYCITNRSHL TKDFQKESLS 

       370        380        390        400        410        420 
MDMELNELES GNGDEEGVDR EARRMNNKRS VLTSPVANGV NLDYDGLGKA CRSLPSLKKT 

       430        440        450        460        470        480 
LSGDSSSDST RGSHNGQVWD PQCSPKKDRQ VHLTHFELEG LRCLVDKLES LPLHKKCVPT 

       490        500        510        520        530        540 
GIEDEDALIA DVKILLEELA SSDPKLALTG 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 SDKAQKRKIE ESDEEAVQAK VLRPLRSCEE PLTPPPHSPT 

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

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

       850        860        870        880        890        900 
PARNPQHGDE EGLGGEEEEE EEEEEDDSAE EGGAARLNGR GSWAQDGDES WMQREVWMSV 

       910        920        930        940        950        960 
FRYLSRKELC ECMRVCKTWY KWCCDKRLWT KIDLSRCKAI VPQALSGIIK RQPVSLDLSW 

       970        980        990       1000       1010       1020 
TNISKKQLTW LVNRLPGLKD LLLAGCSWSA VSALSTSSCP LLRTLDLRWA VGIKDPQIRD 

      1030       1040       1050       1060       1070       1080 
LLTPPTDKPG QDNRSKLRNM TDFRLAGLDI TDATLRLIIR HMPLLSRLDL SHCSHLTDQS 

      1090       1100       1110       1120       1130       1140 
SNLLTAVGSS TRYSLTELNM AGCNKLTDQT LFFLRRIANV TLIDLRGCKQ ITRKACEHFI 

      1150       1160 
SDLSINSLYC LSDEKLIQKI S 

« Hide

Isoform 2 [UniParc].

Checksum: 00BAE63E96EC5E44
Show »

49457,492
Isoform 3 [UniParc].

Checksum: 73D648015209B855
Show »

33839,634

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 646-1161.
Strain: C57BL/6J.
Tissue: Skin.
[2]"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] (ISOFORM 1).
Strain: C57BL/6.
Tissue: Brain.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed: 15368895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 453-1161.
Tissue: Thymus.
[4]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

AK037157 mRNA. Translation: BAE20506.1.
AK141779 mRNA. Translation: BAE24832.1.
AK155866 mRNA. Translation: BAE33470.1.
BC057051 mRNA. Translation: AAH57051.1.
BC076576 mRNA. No translation available.
AK173084 mRNA. Translation: BAD32362.1.
RefSeqNP_001001984.2.
UniGeneMm.31941

3D structure databases

SMRP59997. Positions 36-364, 450-517.
ModBaseSearch...

PTM databases

PhosphoSiteP59997.

Genome annotation databases

EnsemblENSMUSG00000054611. Mus musculus. [Contig view]
GeneID225876.
KEGGmmu:225876.

Organism-specific databases

MGIMGI:1354736. Fbxl11.
RougeSearch...

Phylogenomic databases

HOGENOMP59997.
HOVERGENP59997.

Gene expression databases

ArrayExpressP59997.
CleanExMM_FBXL11.
GermOnlineENSMUSG00000054611. Mus musculus.

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.