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Q6P6C2

- ALKB5_HUMAN

UniProt

Q6P6C2 - ALKB5_HUMAN

Protein

RNA demethylase ALKBH5

Gene

ALKBH5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 2 (03 Oct 2012)
      Previous versions | rss
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    Functioni

    Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Requires molecular oxygen, alpha-ketoglutarate and iron. Demethylation of m6A mRNA affects mRNA processing and export and is required for spermatogenesis.2 Publications

    Cofactori

    Binds 1 Fe2+ ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi204 – 2041Iron; catalyticCurated
    Metal bindingi206 – 2061Iron; catalyticBy similarity
    Metal bindingi266 – 2661Iron; catalyticCurated

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. oxidative RNA demethylase activity Source: UniProtKB
    3. oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. mRNA export from nucleus Source: UniProtKB
    3. mRNA processing Source: UniProtKB
    4. oxidative single-stranded RNA demethylation Source: UniProtKB
    5. response to hypoxia Source: UniProtKB
    6. spermatogenesis Source: UniProtKB

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Differentiation, Spermatogenesis

    Keywords - Ligandi

    Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA demethylase ALKBH5 (EC:1.14.11.-)
    Alternative name(s):
    Alkylated DNA repair protein alkB homolog 5
    Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5
    Gene namesi
    Name:ALKBH5
    Synonyms:ABH5, OFOXD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:25996. ALKBH5.

    Subcellular locationi

    Nucleus speckle 2 Publications

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi204 – 2041H → A: Abolishes catalytic activity. 1 Publication
    Mutagenesisi266 – 2661H → A: Impaired catalytic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA142671230.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 394393RNA demethylase ALKBH5PRO_0000239283Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei64 – 641Phosphoserine2 Publications
    Modified residuei69 – 691Phosphoserine1 Publication
    Modified residuei71 – 711Phosphotyrosine1 Publication
    Modified residuei132 – 1321N6-acetyllysine1 Publication
    Modified residuei361 – 3611Phosphoserine1 Publication
    Modified residuei371 – 3711PhosphoserineBy similarity
    Modified residuei374 – 3741Phosphoserine1 Publication
    Modified residuei384 – 3841PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6P6C2.
    PaxDbiQ6P6C2.
    PRIDEiQ6P6C2.

    PTM databases

    PhosphoSiteiQ6P6C2.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest expression in lung, followed by testis, pancreas, spleen and ovary.1 Publication

    Inductioni

    By hypoxia, directly activated by HIF1A. Expression is regulated by PRMT7.2 Publications

    Gene expression databases

    ArrayExpressiQ6P6C2.
    BgeeiQ6P6C2.
    CleanExiHS_ALKBH5.
    GenevestigatoriQ6P6C2.

    Organism-specific databases

    HPAiHPA007196.

    Interactioni

    Protein-protein interaction databases

    BioGridi120237. 6 interactions.
    IntActiQ6P6C2. 1 interaction.
    STRINGi9606.ENSP00000382091.

    Structurei

    Secondary structure

    1
    394
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi75 – 8612
    Beta strandi89 – 935
    Helixi97 – 11519
    Helixi121 – 1233
    Beta strandi124 – 1274
    Beta strandi130 – 1378
    Beta strandi139 – 1413
    Beta strandi152 – 1554
    Beta strandi160 – 1623
    Helixi166 – 1716
    Helixi173 – 1786
    Beta strandi189 – 1957
    Beta strandi201 – 2044
    Turni208 – 2103
    Beta strandi215 – 2195
    Beta strandi224 – 2285
    Helixi231 – 2333
    Turni236 – 2383
    Beta strandi243 – 2486
    Beta strandi252 – 2565
    Helixi258 – 2625
    Beta strandi266 – 2683
    Helixi270 – 2723
    Beta strandi277 – 2837

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4NJ4X-ray2.02A/B66-292[»]
    4NRMX-ray2.17A66-292[»]
    4NROX-ray2.30A66-292[»]
    4NRPX-ray1.80A66-292[»]
    4NRQX-ray2.50A66-292[»]
    4O61X-ray1.90A/B74-294[»]
    4O7XX-ray1.78A66-292[»]
    4OCTX-ray2.28A/B74-294[»]
    ProteinModelPortaliQ6P6C2.
    SMRiQ6P6C2. Positions 70-292.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili67 – 11650Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi30 – 4819Ala-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the alkB family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG264303.
    HOGENOMiHOG000007505.
    HOVERGENiHBG080833.
    InParanoidiQ6P6C2.
    KOiK10767.
    OMAiGAKRKYQ.
    TreeFamiTF329212.

    Family and domain databases

    Gene3Di2.60.120.590. 1 hit.
    InterProiIPR027450. AlkB-like.
    [Graphical view]
    PfamiPF13532. 2OG-FeII_Oxy_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: Q6P6C2-2) [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

    MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP    50
    YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC 100
    AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP 150
    GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGGC 200
    IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR 250
    GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS 300
    VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS 350
    VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH 394
    Length:394
    Mass (Da):44,256
    Last modified:October 3, 2012 - v2
    Checksum:iDEB7BF8770BDB3A0
    GO
    Isoform 1 (identifier: Q6P6C2-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         386-394: ARKVKMRRH → GNSGSSLRSG...PPGWKGCWHQ

    Note: No experimental confirmation available.

    Show »
    Length:467
    Mass (Da):52,255
    Checksum:iCAB456568C428C85
    GO
    Isoform 3 (identifier: Q6P6C2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-32: MAAASGYTDLREKLKSMTSRDNYKAGSREAAA → MRRCWRPCPAGRGEGGGGRSP

    Show »
    Length:383
    Mass (Da):43,049
    Checksum:i45D8A30C0297A361
    GO

    Sequence cautioni

    The sequence BAA91078.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → L in BAA91078. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3232MAAAS…REAAA → MRRCWRPCPAGRGEGGGGRS P in isoform 3. 1 PublicationVSP_044226Add
    BLAST
    Alternative sequencei386 – 3949ARKVKMRRH → GNSGSSLRSGNSGSSLRSCP SFCFEGFVFVHWGVFVFCFL FFLILYIFPWFCCLLGLKNR IGQDLGSHILGIPPGWKGCW HQ in isoform 1. 1 PublicationVSP_019130

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000315 mRNA. Translation: BAA91078.1. Different initiation.
    AK301107 mRNA. Translation: BAG62706.1.
    AC087164 Genomic DNA. No translation available.
    AC109515 Genomic DNA. No translation available.
    CH471196 Genomic DNA. Translation: EAW55661.1.
    CH471196 Genomic DNA. Translation: EAW55662.1.
    BC062339 mRNA. Translation: AAH62339.1.
    CCDSiCCDS42272.1. [Q6P6C2-2]
    RefSeqiNP_060228.3. NM_017758.3. [Q6P6C2-2]
    UniGeneiHs.744130.

    Genome annotation databases

    EnsembliENST00000399138; ENSP00000382091; ENSG00000091542. [Q6P6C2-2]
    GeneIDi54890.
    KEGGihsa:54890.
    UCSCiuc010cpw.3. human. [Q6P6C2-2]

    Polymorphism databases

    DMDMi408359959.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000315 mRNA. Translation: BAA91078.1 . Different initiation.
    AK301107 mRNA. Translation: BAG62706.1 .
    AC087164 Genomic DNA. No translation available.
    AC109515 Genomic DNA. No translation available.
    CH471196 Genomic DNA. Translation: EAW55661.1 .
    CH471196 Genomic DNA. Translation: EAW55662.1 .
    BC062339 mRNA. Translation: AAH62339.1 .
    CCDSi CCDS42272.1. [Q6P6C2-2 ]
    RefSeqi NP_060228.3. NM_017758.3. [Q6P6C2-2 ]
    UniGenei Hs.744130.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4NJ4 X-ray 2.02 A/B 66-292 [» ]
    4NRM X-ray 2.17 A 66-292 [» ]
    4NRO X-ray 2.30 A 66-292 [» ]
    4NRP X-ray 1.80 A 66-292 [» ]
    4NRQ X-ray 2.50 A 66-292 [» ]
    4O61 X-ray 1.90 A/B 74-294 [» ]
    4O7X X-ray 1.78 A 66-292 [» ]
    4OCT X-ray 2.28 A/B 74-294 [» ]
    ProteinModelPortali Q6P6C2.
    SMRi Q6P6C2. Positions 70-292.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120237. 6 interactions.
    IntActi Q6P6C2. 1 interaction.
    STRINGi 9606.ENSP00000382091.

    PTM databases

    PhosphoSitei Q6P6C2.

    Polymorphism databases

    DMDMi 408359959.

    Proteomic databases

    MaxQBi Q6P6C2.
    PaxDbi Q6P6C2.
    PRIDEi Q6P6C2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000399138 ; ENSP00000382091 ; ENSG00000091542 . [Q6P6C2-2 ]
    GeneIDi 54890.
    KEGGi hsa:54890.
    UCSCi uc010cpw.3. human. [Q6P6C2-2 ]

    Organism-specific databases

    CTDi 54890.
    GeneCardsi GC17P018086.
    HGNCi HGNC:25996. ALKBH5.
    HPAi HPA007196.
    MIMi 613303. gene.
    neXtProti NX_Q6P6C2.
    PharmGKBi PA142671230.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264303.
    HOGENOMi HOG000007505.
    HOVERGENi HBG080833.
    InParanoidi Q6P6C2.
    KOi K10767.
    OMAi GAKRKYQ.
    TreeFami TF329212.

    Miscellaneous databases

    GenomeRNAii 54890.
    NextBioi 57883.
    PROi Q6P6C2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6P6C2.
    Bgeei Q6P6C2.
    CleanExi HS_ALKBH5.
    Genevestigatori Q6P6C2.

    Family and domain databases

    Gene3Di 2.60.120.590. 1 hit.
    InterProi IPR027450. AlkB-like.
    [Graphical view ]
    Pfami PF13532. 2OG-FeII_Oxy_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 2 AND 3).
      Tissue: Hepatoma and Spleen.
    2. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. 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: Brain.
    5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: TISSUE SPECIFICITY.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-69 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; TYR-71 AND SER-374, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Human AlkB homologue 5 is a nuclear 2-oxoglutarate dependent oxygenase and a direct target of hypoxia-inducible factor 1alpha (HIF-1alpha)."
      Thalhammer A., Bencokova Z., Poole R., Loenarz C., Adam J., O'Flaherty L., Schodel J., Mole D., Giaslakiotis K., Schofield C.J., Hammond E.M., Ratcliffe P.J., Pollard P.J.
      PLoS ONE 6:E16210-E16210(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
    13. "Protein arginine methyltransferase 7 regulates cellular response to DNA damage by methylating promoter histones H2A and H4 of the polymerase delta catalytic subunit gene, POLD1."
      Karkhanis V., Wang L., Tae S., Hu Y.J., Imbalzano A.N., Sif S.
      J. Biol. Chem. 287:29801-29814(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-204 AND HIS-266.

    Entry informationi

    Entry nameiALKB5_HUMAN
    AccessioniPrimary (citable) accession number: Q6P6C2
    Secondary accession number(s): B4DVJ4, D3DXC6, Q9NXD6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: October 3, 2012
    Last modified: October 1, 2014
    This is version 100 of the entry and version 2 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 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3