| Tag | Content |
|---|
| CPLM ID | CPLM-016800 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA |
Protein Synonyms/Alias | Histone lysine demethylase MINA; MYC-induced nuclear antigen |
Gene Name | Mina |
Gene Synonyms/Alias | Mina53 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 87 | LFSLSDLKRLCKKGV | ubiquitination | [1] | | 332 | LLSSDMKKDFVKHRL | ubiquitination | [1] | | 336 | DMKKDFVKHRLPPFF | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Is involved in the demethylation of trimethylated 'Lys-9' on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. Also catalyzes the hydroxylation of 60S ribosomal protein L27a on 'His-39' (By similarity). May play an important role in cell growth and survival. May be involved in ribosome biogenesis, most likely during the assembly process of pre-ribosomal particles. |
Sequence Annotation | DOMAIN 139 271 JmjC.
METAL 179 179 Iron; catalytic (By similarity).
METAL 181 181 Iron; catalytic (By similarity).
METAL 240 240 Iron; catalytic (By similarity).
MOD_RES 309 309 Phosphoserine (By similarity). |
Keyword | Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Ribosome biogenesis; Transcription; Transcription regulation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 465 AA |
Protein Sequence | MPKKVQPTGD ENEEASVPCK RVKEELPETL SVLNFDSPSS FFESLISPIK VETFFKEFWE 60
QKPLLIQRDD PVLAKYYQSL FSLSDLKRLC KKGVYYGRDV NVCRSISGKK KVLNKDGRAH 120
FLQLRKDFDQ KRATIQFHQP QRYKDELWRI QEKLECYFGS LVGSNVYMTP AGSQGLPPHY 180
DDVEVFILQL EGTKHWRLYS PTVPLAHEYS VESEDRIGTP THDFLLKPGD LLYFPRGTIH 240
QAETPSGLAY SIHLTISTYQ NNSWGDCLLD SISGFVFDIA KEDVALRSGM PRRMLLNVET 300
PADVTRKLSG FLRTLADQLE GREELLSSDM KKDFVKHRLP PFFEGNGTET MDPGKQLPRL 360
DNIIRLQFKD HIVLTVGPDK NPFDEAQQKV VYIYHSLKNV RQMHMIGEEE ESEIFGLRFP 420
LSHVDALKQI WCGSPIRVKD LKLDTDEEKE NLALSLWSES LIQVL 465 |
Gene Ontology | GO:0005829; C:cytosol; IDA:MGI. GO:0005730; C:nucleolus; ISO:MGI. GO:0005667; C:transcription factor complex; IPI:MGI. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW. GO:0001191; F:RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription; IGI:MGI. GO:0042127; P:regulation of cell proliferation; ISO:MGI. GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. |
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