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Q6NS38

- ALKB2_HUMAN

UniProt

Q6NS38 - ALKB2_HUMAN

Protein

Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2

Gene

ALKBH2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Dioxygenase that repairs alkylated DNA and RNA containing 1-methyladenine and 3-methylcytosine by oxidative demethylation. Can also repair alkylated DNA containing 1-ethenoadenine (in vitro). Has strong preference for double-stranded DNA. Has low efficiency with single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron.5 Publications

    Catalytic activityi

    DNA-base-CH3 + 2-oxoglutarate + O2 = DNA-base + formaldehyde + succinate + CO2.

    Cofactori

    Binds 1 Fe2+ ion per subunit.2 PublicationsPROSITE-ProRule annotation

    Enzyme regulationi

    Activated by ascorbate and magnesium ions.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi171 – 1711Iron; catalytic
    Metal bindingi173 – 1731Iron; catalytic
    Binding sitei174 – 1741Substrate
    Metal bindingi236 – 2361Iron; catalytic

    GO - Molecular functioni

    1. cytosine C-5 DNA demethylase activity Source: UniProtKB
    2. DNA-N1-methyladenine dioxygenase activity Source: UniProtKB
    3. ferrous iron binding Source: UniProtKB

    GO - Biological processi

    1. DNA dealkylation involved in DNA repair Source: UniProtKB
    2. DNA demethylation Source: BHF-UCL
    3. DNA repair Source: Reactome
    4. oxidative demethylation Source: BHF-UCL
    5. oxidative DNA demethylation Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    Iron, Magnesium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_526. ABH2 mediated Reversal of Alkylation Damage.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2 (EC:1.14.11.33)
    Alternative name(s):
    Alkylated DNA repair protein alkB homolog 2
    DNA oxidative demethylase ALKBH2
    Oxy DC1
    Gene namesi
    Name:ALKBH2
    Synonyms:ABH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:32487. ALKBH2.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Detected in replication foci during S-phase.

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi173 – 1731D → A: Loss of activity. 1 Publication
    Mutagenesisi236 – 2361H → A: Reduced activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA143485292.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261Alpha-ketoglutarate-dependent dioxygenase alkB homolog 2PRO_0000239275Add
    BLAST

    Proteomic databases

    MaxQBiQ6NS38.
    PaxDbiQ6NS38.
    PRIDEiQ6NS38.

    PTM databases

    PhosphoSiteiQ6NS38.

    Expressioni

    Tissue specificityi

    Detected in colon, small intestine, ovary, testis, prostate, skeletal muscle, heart, liver and urinary bladder.2 Publications

    Gene expression databases

    ArrayExpressiQ6NS38.
    BgeeiQ6NS38.
    CleanExiHS_ALKBH2.
    GenevestigatoriQ6NS38.

    Organism-specific databases

    HPAiCAB011198.

    Interactioni

    Protein-protein interaction databases

    BioGridi125741. 2 interactions.
    IntActiQ6NS38. 1 interaction.
    STRINGi9606.ENSP00000343021.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi58 – 625
    Beta strandi65 – 717
    Helixi75 – 8814
    Helixi94 – 974
    Beta strandi98 – 1014
    Beta strandi104 – 1074
    Beta strandi109 – 1168
    Beta strandi122 – 1243
    Beta strandi127 – 1293
    Helixi136 – 14914
    Beta strandi154 – 16310
    Beta strandi168 – 1714
    Beta strandi176 – 1783
    Beta strandi184 – 1918
    Beta strandi193 – 1997
    Helixi200 – 2023
    Beta strandi204 – 2063
    Beta strandi214 – 2185
    Beta strandi222 – 2276
    Helixi230 – 2334
    Beta strandi234 – 2385
    Beta strandi248 – 2547

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BTXX-ray2.00A56-258[»]
    3BTYX-ray2.35A56-258[»]
    3BTZX-ray3.00A57-258[»]
    3BU0X-ray2.50A56-258[»]
    3BUCX-ray2.59A56-258[»]
    3H8OX-ray2.50A56-261[»]
    3H8RX-ray1.77A56-261[»]
    3H8XX-ray2.50A56-261[»]
    3RZGX-ray1.62A56-261[»]
    3RZHX-ray2.25A56-261[»]
    3RZJX-ray2.50A56-261[»]
    3RZKX-ray2.78A56-261[»]
    3RZLX-ray2.60A/D56-261[»]
    3RZMX-ray3.06A56-260[»]
    3S57X-ray1.60A56-258[»]
    3S5AX-ray1.70A56-258[»]
    4MG2X-ray2.30A56-258[»]
    4MGTX-ray2.60A56-258[»]
    ProteinModelPortaliQ6NS38.
    SMRiQ6NS38. Positions 56-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6NS38.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini152 – 257106Fe2OG dioxygenasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni102 – 1043Substrate binding
    Regioni122 – 1243Substrate binding
    Regioni159 – 1613Alpha-ketoglutarate binding
    Regioni248 – 2547Alpha-ketoglutarate binding

    Sequence similaritiesi

    Belongs to the alkB family.Curated
    Contains 1 Fe2OG dioxygenase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG3145.
    HOGENOMiHOG000263606.
    HOVERGENiHBG080832.
    InParanoidiQ6NS38.
    KOiK10859.
    OMAiTGHTFNF.
    OrthoDBiEOG77T159.
    PhylomeDBiQ6NS38.
    TreeFamiTF331732.

    Family and domain databases

    Gene3Di2.60.120.590. 1 hit.
    InterProiIPR027450. AlkB-like.
    IPR005123. Oxoglu/Fe-dep_dioxygenase.
    [Graphical view]
    PfamiPF13532. 2OG-FeII_Oxy_2. 1 hit.
    [Graphical view]
    PROSITEiPS51471. FE2OG_OXY. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6NS38-1) [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

    MDRFLVKGAQ GGLLRKQEEQ EPTGEEPAVL GGDKESTRKR PRREAPGNGG    50
    HSAGPSWRHI RAEGLDCSYT VLFGKAEADE IFQELEKEVE YFTGALARVQ 100
    VFGKWHSVPR KQATYGDAGL TYTFSGLTLS PKPWIPVLER IRDHVSGVTG 150
    QTFNFVLINR YKDGCDHIGE HRDDERELAP GSPIASVSFG ACRDFVFRHK 200
    DSRGKSPSRR VAVVRLPLAH GSLLMMNHPT NTHWYHSLPV RKKVLAPRVN 250
    LTFRKILLTK K 261
    Length:261
    Mass (Da):29,322
    Last modified:July 5, 2004 - v1
    Checksum:iA376E13F92621A01
    GO
    Isoform 2 (identifier: Q6NS38-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         95-261: ALARVQVFGK...TFRKILLTKK → IKMAVTTSGS...SGCRWPTGAY

    Note: No experimental confirmation available.

    Show »
    Length:157
    Mass (Da):17,083
    Checksum:iCB86433F4323248A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431R → G in AAV28301. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti203 – 2031R → H.
    Corresponds to variant rs33962311 [ dbSNP | Ensembl ].
    VAR_048223

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei95 – 261167ALARV…LLTKK → IKMAVTTSGSTEMMKENWPL GAPLPLSPSVPAETLSSGIR IPVGKAPPGGWRWSGCRWPT GAY in isoform 2. 1 PublicationVSP_042923Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY754389 mRNA. Translation: AAV28301.1.
    AB277859 mRNA. Translation: BAF56576.1.
    AC011596 Genomic DNA. No translation available.
    BC070489 mRNA. Translation: AAH70489.1.
    CCDSiCCDS31897.1. [Q6NS38-1]
    CCDS55883.1. [Q6NS38-2]
    RefSeqiNP_001001655.1. NM_001001655.2. [Q6NS38-1]
    NP_001138846.1. NM_001145374.1. [Q6NS38-1]
    NP_001138847.1. NM_001145375.1. [Q6NS38-1]
    NP_001192108.1. NM_001205179.1. [Q6NS38-2]
    NP_001192109.1. NM_001205180.1. [Q6NS38-2]
    XP_005253892.1. XM_005253835.2. [Q6NS38-1]
    XP_005253893.1. XM_005253836.1. [Q6NS38-2]
    UniGeneiHs.374458.

    Genome annotation databases

    EnsembliENST00000343075; ENSP00000343021; ENSG00000189046. [Q6NS38-1]
    ENST00000429722; ENSP00000398181; ENSG00000189046. [Q6NS38-1]
    ENST00000440112; ENSP00000399820; ENSG00000189046. [Q6NS38-2]
    GeneIDi121642.
    KEGGihsa:121642.
    UCSCiuc001tnx.2. human. [Q6NS38-1]
    uc009zvd.2. human. [Q6NS38-2]

    Polymorphism databases

    DMDMi74736661.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY754389 mRNA. Translation: AAV28301.1 .
    AB277859 mRNA. Translation: BAF56576.1 .
    AC011596 Genomic DNA. No translation available.
    BC070489 mRNA. Translation: AAH70489.1 .
    CCDSi CCDS31897.1. [Q6NS38-1 ]
    CCDS55883.1. [Q6NS38-2 ]
    RefSeqi NP_001001655.1. NM_001001655.2. [Q6NS38-1 ]
    NP_001138846.1. NM_001145374.1. [Q6NS38-1 ]
    NP_001138847.1. NM_001145375.1. [Q6NS38-1 ]
    NP_001192108.1. NM_001205179.1. [Q6NS38-2 ]
    NP_001192109.1. NM_001205180.1. [Q6NS38-2 ]
    XP_005253892.1. XM_005253835.2. [Q6NS38-1 ]
    XP_005253893.1. XM_005253836.1. [Q6NS38-2 ]
    UniGenei Hs.374458.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BTX X-ray 2.00 A 56-258 [» ]
    3BTY X-ray 2.35 A 56-258 [» ]
    3BTZ X-ray 3.00 A 57-258 [» ]
    3BU0 X-ray 2.50 A 56-258 [» ]
    3BUC X-ray 2.59 A 56-258 [» ]
    3H8O X-ray 2.50 A 56-261 [» ]
    3H8R X-ray 1.77 A 56-261 [» ]
    3H8X X-ray 2.50 A 56-261 [» ]
    3RZG X-ray 1.62 A 56-261 [» ]
    3RZH X-ray 2.25 A 56-261 [» ]
    3RZJ X-ray 2.50 A 56-261 [» ]
    3RZK X-ray 2.78 A 56-261 [» ]
    3RZL X-ray 2.60 A/D 56-261 [» ]
    3RZM X-ray 3.06 A 56-260 [» ]
    3S57 X-ray 1.60 A 56-258 [» ]
    3S5A X-ray 1.70 A 56-258 [» ]
    4MG2 X-ray 2.30 A 56-258 [» ]
    4MGT X-ray 2.60 A 56-258 [» ]
    ProteinModelPortali Q6NS38.
    SMRi Q6NS38. Positions 56-258.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125741. 2 interactions.
    IntActi Q6NS38. 1 interaction.
    STRINGi 9606.ENSP00000343021.

    Chemistry

    DrugBanki DB00126. Vitamin C.

    PTM databases

    PhosphoSitei Q6NS38.

    Polymorphism databases

    DMDMi 74736661.

    Proteomic databases

    MaxQBi Q6NS38.
    PaxDbi Q6NS38.
    PRIDEi Q6NS38.

    Protocols and materials databases

    DNASUi 121642.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343075 ; ENSP00000343021 ; ENSG00000189046 . [Q6NS38-1 ]
    ENST00000429722 ; ENSP00000398181 ; ENSG00000189046 . [Q6NS38-1 ]
    ENST00000440112 ; ENSP00000399820 ; ENSG00000189046 . [Q6NS38-2 ]
    GeneIDi 121642.
    KEGGi hsa:121642.
    UCSCi uc001tnx.2. human. [Q6NS38-1 ]
    uc009zvd.2. human. [Q6NS38-2 ]

    Organism-specific databases

    CTDi 121642.
    GeneCardsi GC12M109525.
    HGNCi HGNC:32487. ALKBH2.
    HPAi CAB011198.
    MIMi 610602. gene.
    neXtProti NX_Q6NS38.
    PharmGKBi PA143485292.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3145.
    HOGENOMi HOG000263606.
    HOVERGENi HBG080832.
    InParanoidi Q6NS38.
    KOi K10859.
    OMAi TGHTFNF.
    OrthoDBi EOG77T159.
    PhylomeDBi Q6NS38.
    TreeFami TF331732.

    Enzyme and pathway databases

    Reactomei REACT_526. ABH2 mediated Reversal of Alkylation Damage.

    Miscellaneous databases

    EvolutionaryTracei Q6NS38.
    GenomeRNAii 121642.
    NextBioi 80790.
    PROi Q6NS38.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6NS38.
    Bgeei Q6NS38.
    CleanExi HS_ALKBH2.
    Genevestigatori Q6NS38.

    Family and domain databases

    Gene3Di 2.60.120.590. 1 hit.
    InterProi IPR027450. AlkB-like.
    IPR005123. Oxoglu/Fe-dep_dioxygenase.
    [Graphical view ]
    Pfami PF13532. 2OG-FeII_Oxy_2. 1 hit.
    [Graphical view ]
    PROSITEi PS51471. FE2OG_OXY. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of human 2OG-Fe(II) oxy DC1."
      Lin Y., Xie Y., Mao Y.
      Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Testis.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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).
      Tissue: Skin.
    5. Cited for: FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. "Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA."
      Aas P.A., Otterlei M., Falnes P.O., Vaagboe C.B., Skorpen F., Akbari M., Sundheim O., Bjoeraas M., Slupphaug G., Seeberg E., Krokan H.E.
      Nature 421:859-863(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    7. "Repair of methylation damage in DNA and RNA by mammalian AlkB homologues."
      Lee D.-H., Jin S.-G., Cai S., Chen Y., Pfeifer G.P., O'Connor T.R.
      J. Biol. Chem. 280:39448-39459(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-173 AND HIS-236, TISSUE SPECIFICITY.
    8. Cited for: FUNCTION, ENZYME REGULATION, COFACTOR.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA."
      Yang C.G., Yi C., Duguid E.M., Sullivan C.T., Jian X., Rice P.A., He C.
      Nature 452:961-965(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 56-258 IN COMPLEXES WITH DS-DNA; ALPHA-KETOGLUTARATE AND METAL IONS, FUNCTION, COFACTOR.
    11. "Structure determination of DNA methylation lesions N1-meA and N3-meC in duplex DNA using a cross-linked protein-DNA system."
      Lu L., Yi C., Jian X., Zheng G., He C.
      Nucleic Acids Res. 38:4415-4425(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 56-261 IN COMPLEXES WITH DOUBLE-STRANDED DNA CONTAINING 1-METHYLADENINE OR 3-METHYLCYTOSINE.

    Entry informationi

    Entry nameiALKB2_HUMAN
    AccessioniPrimary (citable) accession number: Q6NS38
    Secondary accession number(s): A4PET2, Q5XLE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 94 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 12
      Human chromosome 12: 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