CPLM-016950

Genbank Nucleotide ID

Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA

Protein Synonyms/Alias

60S ribosomal protein L27a histidine hydroxylase; Histone lysine demethylase MINA; MYC-induced nuclear antigen; Mineral dust-induced gene protein; Nucleolar protein 52; Ribosomal oxygenase MINA; ROX

Homo sapiens (Human)

Position	Peptide	Type	References
20	EEGPAPCKQMKLEAA	acetylation	[1]
62	FKEFWEQKPLLIQRD	ubiquitination	[2]
82	TYYGSLFKLTDLKSL	ubiquitination	[2]
87	LFKLTDLKSLCSRGM	ubiquitination	[2, 3]
118	KVLNKDGKAHFLQLR	ubiquitination	[2]
323	ADRLEGTKELLSSDM	ubiquitination	[2]
331	ELLSSDMKKDFIMHR	ubiquitination	[4]
332	LLSSDMKKDFIMHRL	ubiquitination	[2, 5]
356	ELSTPGGKLPRLDSV	acetylation	[5, 6]
356	ELSTPGGKLPRLDSV	ubiquitination	[2, 4, 5]
369	SVVRLQFKDHIVLTV	ubiquitination	[4]
428	LSHLDALKQIWNSPA	ubiquitination	[2]
439	NSPAISVKDLKLTTD	ubiquitination	[2, 4]
442	AISVKDLKLTTDEEK	ubiquitination	[4]

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]

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'. 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.

DOMAIN 139 271 JmjC.
METAL 179 179 Iron; catalytic (Probable).
METAL 181 181 Iron; catalytic (By similarity).
METAL 240 240 Iron; catalytic (By similarity).
MOD_RES 309 309 Phosphoserine.

3D-structure; Alternative splicing; Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Ribosome biogenesis; Transcription; Transcription regulation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HPA.
GO:0005829; C:cytosol; IEA:Compara.
GO:0005730; C:nucleolus; IDA:HPA.
GO:0005667; C:transcription factor complex; IEA:Compara.
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; IEA:Compara.
GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.

IPR003347; JmjC_dom.
IPR013109; NO66/MINA.