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Q8IUF8 (MINA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MINA
Synonyms:MDIG, MINA53, NO52
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.3 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18

Catalytic activity

L-histidine-[60S ribosomal protein L27a] + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-histidine-[60S ribosomal protein L27a] + succinate + CO2. Ref.18

Cofactor

Binds 1 Fe2+ ion per subunit By similarity.

Subcellular location

Nucleus. Nucleusnucleolus Ref.1 Ref.12.

Tissue specificity

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. Ref.3 Ref.10 Ref.11 Ref.14

Induction

Up-regulated in response to MYC, in alveolar macrophages from coal miners and in silica particle-treated A549 lung cancer cells. Ref.1 Ref.3

Sequence similarities

Belongs to the MINA53/NO66 family.

Contains 1 JmjC domain.

Sequence caution

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

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.7 Ref.8 (identifier: Q8IUF8-1)

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 Ref.1 (identifier: Q8IUF8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     263-280: SWGDFLLDTISGLVFDTA → DAGARMRRCDLRAIAPQK
     281-465: Missing.
Isoform 3 Ref.3 (identifier: Q8IUF8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-254: Missing.
     255-261: TISTYQN → MLLQVPC
Isoform 4 (identifier: Q8IUF8-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 465465Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA
PRO_0000308377

Regions

Domain139 – 271133JmjC

Sites

Metal binding1791Iron; catalytic Probable
Metal binding1811Iron; catalytic By similarity
Metal binding2401Iron; catalytic By similarity

Amino acid modifications

Modified residue3091Phosphoserine Ref.16

Natural variations

Alternative sequence1 – 254254Missing in isoform 3. Ref.3
VSP_052587
Alternative sequence255 – 2617TISTYQN → MLLQVPC in isoform 3. Ref.3
VSP_052588
Alternative sequence263 – 28018SWGDF…VFDTA → DAGARMRRCDLRAIAPQK in isoform 2. Ref.1
VSP_052589
Alternative sequence281 – 465185Missing in isoform 2. Ref.1
VSP_052590
Alternative sequence2971Missing in isoform 4.
VSP_038373
Natural variant171A → P.
Corresponds to variant rs35391656 [ dbSNP | Ensembl ].
VAR_054079
Natural variant2011P → L.
Corresponds to variant rs56183666 [ dbSNP | Ensembl ].
VAR_062241
Natural variant3861A → T. Ref.2 Ref.5 Ref.7 Ref.8 Ref.9
Corresponds to variant rs2172257 [ dbSNP | Ensembl ].
VAR_036811

Experimental info

Mutagenesis1791H → Y: Abolishes demethylase activity. Ref.14
Sequence conflict871K → E in BAC16359. Ref.1
Sequence conflict1071N → S in BAC16359. Ref.1
Sequence conflict1591G → S in BAB55024. Ref.5
Sequence conflict2211V → A in BAC16359. Ref.1

Secondary structure

....................................................................... 465
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2003. Version 1.
Checksum: B59F8AE9C802FEB0

FASTA46552,800
        10         20         30         40         50         60 
MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE 

        70         80         90        100        110        120 
QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH 

       130        140        150        160        170        180 
FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY 

       190        200        210        220        230        240 
DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH 

       250        260        270        280        290        300 
QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES 

       310        320        330        340        350        360 
TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL 

       370        380        390        400        410        420 
DSVVRLQFKD HIVLTVLPDQ DQSDEAQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP 

       430        440        450        460 
LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV 

« Hide

Isoform 2 [UniParc].

Checksum: 8B69C261ABC594EB
Show »

FASTA28031,818
Isoform 3 [UniParc].

Checksum: DA5AB0F080853151
Show »

FASTA21123,909
Isoform 4 [UniParc].

Checksum: 24902143244D1A79
Show »

FASTA46452,672

References

« Hide 'large scale' references
[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: Erythroleukemia.
[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 macrophage and Lung cancer.
[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: Lung.
[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. expand/collapse author list , 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: Embryo.
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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: Skin.
[9]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans."
Ge W., Wolf A., Feng T., Ho C.H., Sekirnik R., Zayer A., Granatino N., Cockman M.E., Loenarz C., Loik N.D., Hardy A.P., Claridge T.D., Hamed R.B., Chowdhury R., Gong L., Robinson C.V., Trudgian D.C., Jiang M. expand/collapse author list , Mackeen M.M., McCullagh J.S., Gordiyenko Y., Thalhammer A., Yamamoto A., Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M., Kessler B.M., Ratcliffe P.J., Preston G.M., Coleman M.L., Schofield C.J.
Nat. Chem. Biol. 8:960-962(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS RPL27A HYDROXYLASE, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2929.1. [Q8IUF8-4]
CCDS43114.1. [Q8IUF8-1]
RefSeqNP_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]
UniGeneHs.570562.
Hs.742206.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XDVX-ray2.57A26-465[»]
4BU2X-ray2.78A26-465[»]
4BXFX-ray2.05A/B26-465[»]
ProteinModelPortalQ8IUF8.
SMRQ8IUF8. Positions 30-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124309. 6 interactions.
MINTMINT-1454329.
STRING9606.ENSP00000328251.

PTM databases

PhosphoSiteQ8IUF8.

Polymorphism databases

DMDM74750624.

Proteomic databases

MaxQBQ8IUF8.
PaxDbQ8IUF8.
PRIDEQ8IUF8.

Protocols and materials databases

DNASU84864.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330299; ENSP00000327424; ENSG00000170854. [Q8IUF8-2]
ENST00000333396; ENSP00000328251; ENSG00000170854. [Q8IUF8-1]
ENST00000360258; ENSP00000353395; ENSG00000170854. [Q8IUF8-4]
ENST00000394198; ENSP00000377748; ENSG00000170854. [Q8IUF8-1]
ENST00000514314; ENSP00000424955; ENSG00000170854. [Q8IUF8-2]
GeneID84864.
KEGGhsa:84864.
UCSCuc003drz.2. human. [Q8IUF8-1]
uc003dsa.2. human. [Q8IUF8-4]

Organism-specific databases

CTD84864.
GeneCardsGC03M097660.
HGNCHGNC:19441. MINA.
HPACAB013458.
HPA007603.
HPA008080.
MIM612049. gene.
neXtProtNX_Q8IUF8.
PharmGKBPA134991047.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG83808.
HOVERGENHBG055265.
InParanoidQ8IUF8.
OMASTYQNNS.
OrthoDBEOG7T1RBJ.
PhylomeDBQ8IUF8.
TreeFamTF318659.

Gene expression databases

ArrayExpressQ8IUF8.
BgeeQ8IUF8.
CleanExHS_MINA.
GenevestigatorQ8IUF8.

Family and domain databases

InterProIPR003347. JmjC_dom.
[Graphical view]
PfamPF08007. Cupin_4. 1 hit.
[Graphical view]
SMARTSM00558. JmjC. 1 hit.
[Graphical view]
PROSITEPS51184. JMJC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8IUF8.
GeneWikiMINA.
MYC-induced_nuclear_antigen.
GenomeRNAi84864.
NextBio75123.
PROQ8IUF8.
SOURCESearch...

Entry information

Entry nameMINA_HUMAN
AccessionPrimary (citable) accession number: Q8IUF8
Secondary accession number(s): D3DN35 expand/collapse secondary AC list , Q6AHW4, Q6SKS0, Q8IU69, Q8IUF6, Q8IUF7, Q96C17, Q96KB0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM