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Q8IUF8

- MINA_HUMAN

UniProt

Q8IUF8 - MINA_HUMAN

Protein

Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA

Gene

MINA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    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.8 Publications

    Catalytic activityi

    L-histidine-[60S ribosomal protein L27a] + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-histidine-[60S ribosomal protein L27a] + succinate + CO2.1 Publication

    Cofactori

    Binds 1 Fe2+ ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi179 – 1791Iron; catalyticCurated
    Metal bindingi181 – 1811Iron; catalyticPROSITE-ProRule annotation
    Metal bindingi240 – 2401Iron; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. dioxygenase activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. RNA polymerase II transcription factor binding transcription factor activity involved in negative regulation of transcription Source: Ensembl

    GO - Biological processi

    1. ribosome biogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Ribosome biogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA (EC:1.14.11.-)
    Alternative name(s):
    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
    Short name:
    ROX
    Gene namesi
    Name:MINAImported
    Synonyms:MDIGImported, MINA53Imported, NO52Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:19441. MINA.

    Subcellular locationi

    Nucleus 2 Publications. Nucleusnucleolus 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Ensembl
    3. nucleolus Source: HPA
    4. nucleus Source: HPA
    5. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi179 – 1791H → Y: Abolishes demethylase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134991047.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINAPRO_0000308377Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei309 – 3091Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8IUF8.
    PaxDbiQ8IUF8.
    PRIDEiQ8IUF8.

    PTM databases

    PhosphoSiteiQ8IUF8.

    Expressioni

    Tissue specificityi

    Expressed in liver, skeletal muscle, heart, pancreas, and placenta. Not detected in brain, lung or kidney. Expressed in several lung cancer tissues, but is barely detected in the adjacent non-cancerous tissues. Also highly expressed in several esophageal squamous cell carcinoma (ESCC), and colon cancer tissues, and in various cancer cell lines.4 Publications

    Inductioni

    Up-regulated in response to MYC, in alveolar macrophages from coal miners and in silica particle-treated A549 lung cancer cells.2 Publications

    Gene expression databases

    ArrayExpressiQ8IUF8.
    BgeeiQ8IUF8.
    CleanExiHS_MINA.
    GenevestigatoriQ8IUF8.

    Organism-specific databases

    HPAiCAB013458.
    HPA007603.
    HPA008080.

    Interactioni

    Protein-protein interaction databases

    BioGridi124309. 6 interactions.
    DIPiDIP-28141N.
    MINTiMINT-1454329.
    STRINGi9606.ENSP00000328251.

    Structurei

    Secondary structure

    1
    465
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi38 – 458
    Turni46 – 483
    Helixi51 – 577
    Turni58 – 614
    Beta strandi64 – 663
    Helixi71 – 8010
    Helixi85 – 906
    Beta strandi94 – 963
    Turni97 – 993
    Beta strandi100 – 1067
    Beta strandi109 – 1124
    Beta strandi116 – 1194
    Helixi121 – 1299
    Beta strandi134 – 1385
    Helixi140 – 1423
    Helixi145 – 15814
    Beta strandi162 – 1698
    Beta strandi178 – 1803
    Beta strandi182 – 19211
    Beta strandi194 – 1996
    Helixi214 – 2163
    Beta strandi221 – 2266
    Beta strandi231 – 2344
    Beta strandi239 – 2435
    Beta strandi246 – 2483
    Beta strandi251 – 2588
    Helixi264 – 27613
    Helixi284 – 2874
    Helixi294 – 2963
    Helixi302 – 32120
    Helixi329 – 3379
    Beta strandi344 – 3485
    Turni349 – 3513
    Beta strandi363 – 3664
    Helixi369 – 3713
    Beta strandi372 – 3754
    Beta strandi390 – 3956
    Turni402 – 4054
    Beta strandi417 – 4204
    Helixi421 – 4233
    Helixi424 – 4318
    Beta strandi434 – 4374
    Helixi438 – 4403
    Helixi446 – 45813
    Beta strandi462 – 4643

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XDVX-ray2.57A26-465[»]
    4BU2X-ray2.78A26-465[»]
    4BXFX-ray2.05A/B26-465[»]
    ProteinModelPortaliQ8IUF8.
    SMRiQ8IUF8. Positions 30-465.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IUF8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini139 – 271133JmjCPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MINA53/NO66 family.Curated
    Contains 1 JmjC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG83808.
    HOVERGENiHBG055265.
    InParanoidiQ8IUF8.
    OMAiSTYQNNS.
    OrthoDBiEOG7T1RBJ.
    PhylomeDBiQ8IUF8.
    TreeFamiTF318659.

    Family and domain databases

    InterProiIPR003347. JmjC_dom.
    [Graphical view]
    PfamiPF08007. Cupin_4. 1 hit.
    [Graphical view]
    SMARTiSM00558. JmjC. 1 hit.
    [Graphical view]
    PROSITEiPS51184. JMJC. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 16 Publications (identifier: Q8IUF8-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK    50
    TETFFKEFWE QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV 100
    NVCRCVNGKK KVLNKDGKAH FLQLRKDFDQ KRATIQFHQP QRFKDELWRI 150
    QEKLECYFGS LVGSNVYITP AGSQGLPPHY DDVEVFILQL EGEKHWRLYH 200
    PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH QADTPAGLAH 250
    STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES 300
    TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL 350
    STPGGKLPRL DSVVRLQFKD HIVLTVLPDQ DQSDEAQEKM VYIYHSLKNS 400
    RETHMMGNEE ETEFHGLRFP LSHLDALKQI WNSPAISVKD LKLTTDEEKE 450
    SLVLSLWTEC LIQVV 465
    Length:465
    Mass (Da):52,800
    Last modified:March 1, 2003 - v1
    Checksum:iB59F8AE9C802FEB0
    GO
    Isoform 21 Publication (identifier: Q8IUF8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         263-280: SWGDFLLDTISGLVFDTA → DAGARMRRCDLRAIAPQK
         281-465: Missing.

    Show »
    Length:280
    Mass (Da):31,818
    Checksum:i8B69C261ABC594EB
    GO
    Isoform 31 Publication (identifier: Q8IUF8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-254: Missing.
         255-261: TISTYQN → MLLQVPC

    Show »
    Length:211
    Mass (Da):23,909
    Checksum:iDA5AB0F080853151
    GO
    Isoform 4 (identifier: Q8IUF8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         297-297: Missing.

    Show »
    Length:464
    Mass (Da):52,672
    Checksum:i24902143244D1A79
    GO

    Sequence cautioni

    The sequence CAH10679.1 differs from that shown. Reason: Erroneous termination at position 431. Translated as Trp.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti87 – 871K → E in BAC16359. (PubMed:12091391)Curated
    Sequence conflicti107 – 1071N → S in BAC16359. (PubMed:12091391)Curated
    Sequence conflicti159 – 1591G → S in BAB55024. (PubMed:14702039)Curated
    Sequence conflicti221 – 2211V → A in BAC16359. (PubMed:12091391)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171A → P.
    Corresponds to variant rs35391656 [ dbSNP | Ensembl ].
    VAR_054079
    Natural varianti201 – 2011P → L.
    Corresponds to variant rs56183666 [ dbSNP | Ensembl ].
    VAR_062241
    Natural varianti386 – 3861A → T.4 Publications
    Corresponds to variant rs2172257 [ dbSNP | Ensembl ].
    VAR_036811

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 254254Missing in isoform 3. 1 PublicationVSP_052587Add
    BLAST
    Alternative sequencei255 – 2617TISTYQN → MLLQVPC in isoform 3. 1 PublicationVSP_052588
    Alternative sequencei263 – 28018SWGDF…VFDTA → DAGARMRRCDLRAIAPQK in isoform 2. 1 PublicationVSP_052589Add
    BLAST
    Alternative sequencei281 – 465185Missing in isoform 2. 1 PublicationVSP_052590Add
    BLAST
    Alternative sequencei297 – 2971Missing in isoform 4. 2 PublicationsVSP_038373

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB083189 mRNA. Translation: BAC16537.1.
    AB083190 mRNA. Translation: BAC16358.1.
    AB083191 mRNA. Translation: BAC16359.1.
    AB083192 mRNA. Translation: BAC16360.1.
    AB083193 mRNA. Translation: BAC16361.1.
    AY390536 mRNA. Translation: AAR27293.1.
    AY302110 mRNA. Translation: AAP59421.1.
    AY456380 mRNA. Translation: AAR21572.1.
    DQ453796 mRNA. Translation: ABE28016.1.
    AK027299 mRNA. Translation: BAB55024.1.
    AC026100 Genomic DNA. No translation available.
    AC110491 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79872.1.
    CH471052 Genomic DNA. Translation: EAW79873.1.
    BC014928 mRNA. Translation: AAH14928.1.
    CR627479 mRNA. Translation: CAH10679.1. Different termination.
    CCDSiCCDS2929.1. [Q8IUF8-4]
    CCDS43114.1. [Q8IUF8-1]
    RefSeqiNP_001035998.1. NM_001042533.2. [Q8IUF8-1]
    NP_001248758.1. NM_001261829.1. [Q8IUF8-4]
    NP_116167.3. NM_032778.5. [Q8IUF8-4]
    NP_694822.2. NM_153182.3. [Q8IUF8-1]
    XP_005247895.1. XM_005247838.2. [Q8IUF8-1]
    UniGeneiHs.570562.
    Hs.742206.

    Genome annotation databases

    EnsembliENST00000333396; ENSP00000328251; ENSG00000170854. [Q8IUF8-1]
    ENST00000360258; ENSP00000353395; ENSG00000170854. [Q8IUF8-4]
    ENST00000394198; ENSP00000377748; ENSG00000170854. [Q8IUF8-1]
    ENST00000514314; ENSP00000424955; ENSG00000170854. [Q8IUF8-2]
    GeneIDi84864.
    KEGGihsa:84864.
    UCSCiuc003drz.2. human. [Q8IUF8-1]
    uc003dsa.2. human. [Q8IUF8-4]

    Polymorphism databases

    DMDMi74750624.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB083189 mRNA. Translation: BAC16537.1 .
    AB083190 mRNA. Translation: BAC16358.1 .
    AB083191 mRNA. Translation: BAC16359.1 .
    AB083192 mRNA. Translation: BAC16360.1 .
    AB083193 mRNA. Translation: BAC16361.1 .
    AY390536 mRNA. Translation: AAR27293.1 .
    AY302110 mRNA. Translation: AAP59421.1 .
    AY456380 mRNA. Translation: AAR21572.1 .
    DQ453796 mRNA. Translation: ABE28016.1 .
    AK027299 mRNA. Translation: BAB55024.1 .
    AC026100 Genomic DNA. No translation available.
    AC110491 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW79872.1 .
    CH471052 Genomic DNA. Translation: EAW79873.1 .
    BC014928 mRNA. Translation: AAH14928.1 .
    CR627479 mRNA. Translation: CAH10679.1 . Different termination.
    CCDSi CCDS2929.1. [Q8IUF8-4 ]
    CCDS43114.1. [Q8IUF8-1 ]
    RefSeqi NP_001035998.1. NM_001042533.2. [Q8IUF8-1 ]
    NP_001248758.1. NM_001261829.1. [Q8IUF8-4 ]
    NP_116167.3. NM_032778.5. [Q8IUF8-4 ]
    NP_694822.2. NM_153182.3. [Q8IUF8-1 ]
    XP_005247895.1. XM_005247838.2. [Q8IUF8-1 ]
    UniGenei Hs.570562.
    Hs.742206.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XDV X-ray 2.57 A 26-465 [» ]
    4BU2 X-ray 2.78 A 26-465 [» ]
    4BXF X-ray 2.05 A/B 26-465 [» ]
    ProteinModelPortali Q8IUF8.
    SMRi Q8IUF8. Positions 30-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124309. 6 interactions.
    DIPi DIP-28141N.
    MINTi MINT-1454329.
    STRINGi 9606.ENSP00000328251.

    PTM databases

    PhosphoSitei Q8IUF8.

    Polymorphism databases

    DMDMi 74750624.

    Proteomic databases

    MaxQBi Q8IUF8.
    PaxDbi Q8IUF8.
    PRIDEi Q8IUF8.

    Protocols and materials databases

    DNASUi 84864.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000333396 ; ENSP00000328251 ; ENSG00000170854 . [Q8IUF8-1 ]
    ENST00000360258 ; ENSP00000353395 ; ENSG00000170854 . [Q8IUF8-4 ]
    ENST00000394198 ; ENSP00000377748 ; ENSG00000170854 . [Q8IUF8-1 ]
    ENST00000514314 ; ENSP00000424955 ; ENSG00000170854 . [Q8IUF8-2 ]
    GeneIDi 84864.
    KEGGi hsa:84864.
    UCSCi uc003drz.2. human. [Q8IUF8-1 ]
    uc003dsa.2. human. [Q8IUF8-4 ]

    Organism-specific databases

    CTDi 84864.
    GeneCardsi GC03M097660.
    HGNCi HGNC:19441. MINA.
    HPAi CAB013458.
    HPA007603.
    HPA008080.
    MIMi 612049. gene.
    neXtProti NX_Q8IUF8.
    PharmGKBi PA134991047.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG83808.
    HOVERGENi HBG055265.
    InParanoidi Q8IUF8.
    OMAi STYQNNS.
    OrthoDBi EOG7T1RBJ.
    PhylomeDBi Q8IUF8.
    TreeFami TF318659.

    Miscellaneous databases

    EvolutionaryTracei Q8IUF8.
    GeneWikii MINA.
    MYC-induced_nuclear_antigen.
    GenomeRNAii 84864.
    NextBioi 75123.
    PROi Q8IUF8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IUF8.
    Bgeei Q8IUF8.
    CleanExi HS_MINA.
    Genevestigatori Q8IUF8.

    Family and domain databases

    InterProi IPR003347. JmjC_dom.
    [Graphical view ]
    Pfami PF08007. Cupin_4. 1 hit.
    [Graphical view ]
    SMARTi SM00558. JmjC. 1 hit.
    [Graphical view ]
    PROSITEi PS51184. JMJC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel myc target gene, mina53, that is involved in cell proliferation."
      Tsuneoka M., Koda Y., Soejima M., Teye K., Kimura H.
      J. Biol. Chem. 277:35450-35459(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
      Tissue: ErythroleukemiaImported.
    2. "NO66, a highly conserved dual location protein in the nucleolus and in a special type of synchronously replicating chromatin."
      Eilbracht J., Reichenzeller M., Hergt M., Schnoelzer M., Heid H., Stoehr M., Franke W.W., Schmidt-Zachmann M.S.
      Mol. Biol. Cell 15:1816-1832(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-386.
    3. "The human mineral dust-induced gene, mdig, is a cell growth regulating gene associated with lung cancer."
      Zhang Y., Lu Y., Yuan B.-Z., Castranova V., Shi X., Stauffer J.L., Demers L.M., Chen F.
      Oncogene 24:4873-4882(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, TISSUE SPECIFICITY, INDUCTION.
      Tissue: Alveolar macrophageImported and Lung cancerImported.
    4. "MDIG gene, a potential biomarker for human lung cancer."
      Chang Q., Castranova V., Chen F.
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: LungImported.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), VARIANT THR-386.
      Tissue: EmbryoImported.
    6. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-386.
      Tissue: SkinImported.
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-465 (ISOFORM 1), VARIANT THR-386.
      Tissue: Melanoma.
    10. "Increased expression of a Myc target gene Mina53 in human colon cancer."
      Teye K., Tsuneoka M., Arima N., Koda Y., Nakamura Y., Ueta Y., Shirouzu K., Kimura H.
      Am. J. Pathol. 164:205-216(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    11. "Mina53 as a potential prognostic factor for esophageal squamous cell carcinoma."
      Tsuneoka M., Fujita H., Arima N., Teye K., Okamura T., Inutsuka H., Koda Y., Shirouzu K., Kimura H.
      Clin. Cancer Res. 10:7347-7356(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.
    12. "Protein NO52 -- a constitutive nucleolar component sharing high sequence homologies to protein NO66."
      Eilbracht J., Kneissel S., Hofmann A., Schmidt-Zachmann M.S.
      Eur. J. Cell Biol. 84:279-294(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Immunohistochemical expression of Mina53 and Ki67 proteins in human primary gingival squamous cell carcinoma."
      Kuratomi K., Yano H., Tsuneoka M., Sakamoto K., Kusukawa J., Kojiro M.
      Kurume Med. J. 53:71-78(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Lung cancer-associated JmjC domain protein mdig suppresses formation of tri-methyl lysine 9 of histone H3."
      Lu Y., Chang Q., Zhang Y., Beezhold K., Rojanasakul Y., Zhao H., Castranova V., Shi X., Chen F.
      Cell Cycle 8:2101-2109(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS HISTONE DEMETHYLASE, TISSUE SPECIFICITY, MUTAGENESIS OF HIS-179.
    15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: FUNCTION AS RPL27A HYDROXYLASE, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiMINA_HUMAN
    AccessioniPrimary (citable) accession number: Q8IUF8
    Secondary accession number(s): D3DN35
    , Q6AHW4, Q6SKS0, Q8IU69, Q8IUF6, Q8IUF7, Q96C17, Q96KB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 2007
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3