Reviewed,
UniProtKB/Swiss-Prot P59997 (JHD1A_MOUSE)
Last modified
November 25, 2008.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 1161 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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. |
Ontologies
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1161 | 1161 | JmjC domain-containing histone demethylation protein 1A | PRO_0000119856 | |||||
Regions | |||||||||
| Domain | 148 – 316 | 169 | JmjC | ||||||
| Domain | 888 – 935 | 48 | F-box | ||||||
| Repeat | 999 – 1024 | 26 | LRR 1 | ||||||
| Repeat | 1062 – 1090 | 29 | LRR 2 | ||||||
| Repeat | 1094 – 1117 | 24 | LRR 3 | ||||||
| Zinc finger | 564 – 610 | 47 | CXXC-type | ||||||
| Zinc finger | 617 – 678 | 62 | PHD-type | ||||||
Sites | |||||||||
| Metal binding | 212 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 214 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 284 | 1 | Iron; catalytic By similarity | ||||||
| Binding site | 209 | 1 | Substrate By similarity | ||||||
| Binding site | 229 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 28 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 390 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 394 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 534 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 550 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 558 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 632 | 1 | Phosphothreonine | ||||||
| Modified residue | 692 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 713 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 718 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 720 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 721 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 731 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 739 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 740 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 868 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 321 – 338 | 18 | PNKFR…WYVLE → SNVTIICVDVSPFKADVR in isoform 3. | VSP_017471 | |||||
| Alternative sequence | 339 – 1161 | 823 | Missing in isoform 3. | VSP_017472 | |||||
| Alternative sequence | 494 | 1 | I → S in isoform 2. | VSP_017473 | |||||
| Alternative sequence | 495 – 1161 | 667 | Missing in isoform 2. | VSP_017474 | |||||
Experimental info | |||||||||
| Sequence conflict | 159 | 1 | W → R in BAE20506. Ref.1 | ||||||
| Sequence conflict | 159 | 1 | W → R in BC076576. Ref.2 | ||||||
| Sequence conflict | 202 | 1 | I → M in BAE20506. Ref.1 | ||||||
| Sequence conflict | 202 | 1 | I → M in BC076576. Ref.2 | ||||||
| Sequence conflict | 913 | 1 | M → I in AAH57051. Ref.2 | ||||||
Sequences
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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. 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. | |
| RefSeq | NP_001001984.2. |
| UniGene | Mm.31941 |
3D structure databases | |
| SMR | P59997. Positions 36-364, 450-517. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P59997. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000054611. Mus musculus. [Contig view] |
| GeneID | 225876. |
| KEGG | mmu:225876. |
Organism-specific databases | |
| MGI | MGI:1354736. Fbxl11. |
| Rouge | Search... |
Phylogenomic databases | |
| HOGENOM | P59997. |
| HOVERGEN | P59997. |
Gene expression databases | |
| ArrayExpress | P59997. |
| CleanEx | MM_FBXL11. |
| GermOnline | ENSMUSG00000054611. Mus musculus. |
Family and domain databases | |
| InterPro | IPR001810. F-box. IPR001611. LRR. IPR013129. TF_JmjC. IPR003347. TF_JmjC_AAH. IPR002857. Znf_CXXC. IPR001965. Znf_PHD. [Graphical view] |
| Pfam | PF00646. F-box. 1 hit. PF02373. JmjC. 1 hit. PF00560. LRR_1. 1 hit. PF02008. zf-CXXC. 1 hit. [Graphical view] |
| SMART | SM00256. FBOX. 1 hit. SM00558. JmjC. 1 hit. SM00249. PHD. 1 hit. [Graphical view] |
| PROSITE | PS50181. FBOX. False negative. PS51184. JMJC. 1 hit. PS51058. ZF_CXXC. 1 hit. PS01359. ZF_PHD_1. 1 hit. |

Clusters with