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Q9NXW9

- ALKB4_HUMAN

UniProt

Q9NXW9 - ALKB4_HUMAN

Protein

Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4

Gene

ALKBH4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Dioxygenase that mediates demethylation of actin monomethylated at 'Lys-84' (K84me1), thereby acting as a regulator of actomyosin-processes. Demethylation of actin K84me1 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration. May be involved in transcription regulation.2 Publications

    Cofactori

    Binds 1 Fe2+ ion per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi169 – 1691Iron; catalyticCurated
    Metal bindingi171 – 1711Iron; catalyticCurated
    Metal bindingi254 – 2541Iron; catalyticCurated
    Binding sitei265 – 26512-oxoglutarateSequence Analysis

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. demethylase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. 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

    GO - Biological processi

    1. actomyosin structure organization Source: UniProtKB
    2. cleavage furrow ingression Source: UniProtKB
    3. protein demethylation Source: UniProtKB
    4. regulation of transcription, DNA-templated Source: UniProtKB-KW
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Actin-binding, Iron, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4 (EC:1.14.11.-)
    Alternative name(s):
    Alkylated DNA repair protein alkB homolog 4
    Gene namesi
    Name:ALKBH4
    Synonyms:ABH4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:21900. ALKBH4.

    Subcellular locationi

    Cytoplasm. Nucleus. Midbody
    Note: Associates with the contractile ring and midbody.

    GO - Cellular componenti

    1. contractile ring Source: UniProtKB
    2. cytoplasm Source: UniProtKB-SubCell
    3. midbody Source: UniProtKB
    4. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi169 – 1691H → A: Loss of function mutant that acts as a dominant-negative mutant when overexpressed, leading to multinucleation and cleavage furrow disorganization; when associated with A-171 and A-254. 1 Publication
    Mutagenesisi171 – 1711D → A: Loss of function mutant that acts as a dominant-negative mutant when overexpressed, leading to multinucleation and cleavage furrow disorganization; when associated with A-169 and A-254. 1 Publication
    Mutagenesisi254 – 2541H → A: Loss of function mutant that acts as a dominant-negative mutant when overexpressed, leading to multinucleation and cleavage furrow disorganization; when associated with A-169 and A-171. 1 Publication

    Organism-specific databases

    PharmGKBiPA143485294.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 302301Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4PRO_0000239281Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NXW9.
    PaxDbiQ9NXW9.
    PRIDEiQ9NXW9.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest expression in pancreas, ovary and spleen.1 Publication

    Gene expression databases

    BgeeiQ9NXW9.
    CleanExiHS_ALKBH4.
    GenevestigatoriQ9NXW9.

    Organism-specific databases

    HPAiHPA051422.

    Interactioni

    Subunit structurei

    Interacts with ZFHX3, MLLT3, MLLT1, HSF4, EP300, TES, EIF3C, MTMR6 and PSMA6.1 Publication

    Protein-protein interaction databases

    BioGridi120148. 2 interactions.
    IntActiQ9NXW9. 1 interaction.
    STRINGi9606.ENSP00000292566.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NXW9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the alkB family.Curated

    Phylogenomic databases

    eggNOGiNOG255556.
    HOGENOMiHOG000015835.
    HOVERGENiHBG062006.
    InParanoidiQ9NXW9.
    KOiK10766.
    OMAiDRDPWKL.
    OrthoDBiEOG73Z2V0.
    PhylomeDBiQ9NXW9.
    TreeFamiTF314885.

    Family and domain databases

    Gene3Di2.60.120.590. 1 hit.
    InterProiIPR027450. AlkB-like.
    IPR005123. Oxoglu/Fe-dep_dioxygenase.
    [Graphical view]
    PfamiPF03171. 2OG-FeII_Oxy. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NXW9-1) [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

    MAAAAAETPE VLRECGCKGI RTCLICERQR GSDPPWELPP AKTYRFIYCS    50
    DTGWAVGTEE SDFEGWAFPF PGVMLIEDFV TREEEAELVR LMDRDPWKLS 100
    QSGRRKQDYG PKVNFRKQKL KTEGFCGLPS FSREVVRRMG LYPGLEGFRP 150
    VEQCNLDYCP ERGSAIDPHL DDAWLWGERL VSLNLLSPTV LSMCREAPGS 200
    LLLCSAPSAA PEALVDSVIA PSRSVLCQEV EVAIPLPARS LLVLTGAARH 250
    QWKHAIHRRH IEARRVCVTF RELSAEFGPG GRQQELGQEL LRIALSFQGR 300
    PV 302
    Length:302
    Mass (Da):33,838
    Last modified:October 1, 2000 - v1
    Checksum:i67C2DFE058962AF4
    GO
    Isoform 2 (identifier: Q9NXW9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         42-42: K → E
         43-302: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

    Show »
    Length:42
    Mass (Da):4,556
    Checksum:iD1438DF90A61CD02
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti210 – 2101A → V in BAD96409. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti247 – 2471A → V.
    Corresponds to variant rs41275227 [ dbSNP | Ensembl ].
    VAR_061004

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei42 – 421K → E in isoform 2. 1 PublicationVSP_019128
    Alternative sequencei43 – 302260Missing in isoform 2. 1 PublicationVSP_036841Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000020 mRNA. Translation: BAA90888.1.
    AK026097 mRNA. Translation: BAB15358.1. Sequence problems.
    AK222689 mRNA. Translation: BAD96409.1.
    AC093668 Genomic DNA. No translation available.
    BC002820 mRNA. Translation: AAH02820.1.
    BC017096 mRNA. Translation: AAH17096.1.
    CCDSiCCDS5723.1. [Q9NXW9-1]
    RefSeqiNP_060091.1. NM_017621.3. [Q9NXW9-1]
    XP_005250521.1. XM_005250464.1.
    UniGeneiHs.658598.

    Genome annotation databases

    EnsembliENST00000292566; ENSP00000292566; ENSG00000160993. [Q9NXW9-1]
    ENST00000490528; ENSP00000420362; ENSG00000160993. [Q9NXW9-2]
    GeneIDi54784.
    KEGGihsa:54784.
    UCSCiuc003uzl.3. human. [Q9NXW9-1]

    Polymorphism databases

    DMDMi74734701.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK000020 mRNA. Translation: BAA90888.1 .
    AK026097 mRNA. Translation: BAB15358.1 . Sequence problems.
    AK222689 mRNA. Translation: BAD96409.1 .
    AC093668 Genomic DNA. No translation available.
    BC002820 mRNA. Translation: AAH02820.1 .
    BC017096 mRNA. Translation: AAH17096.1 .
    CCDSi CCDS5723.1. [Q9NXW9-1 ]
    RefSeqi NP_060091.1. NM_017621.3. [Q9NXW9-1 ]
    XP_005250521.1. XM_005250464.1.
    UniGenei Hs.658598.

    3D structure databases

    ProteinModelPortali Q9NXW9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120148. 2 interactions.
    IntActi Q9NXW9. 1 interaction.
    STRINGi 9606.ENSP00000292566.

    Polymorphism databases

    DMDMi 74734701.

    Proteomic databases

    MaxQBi Q9NXW9.
    PaxDbi Q9NXW9.
    PRIDEi Q9NXW9.

    Protocols and materials databases

    DNASUi 54784.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000292566 ; ENSP00000292566 ; ENSG00000160993 . [Q9NXW9-1 ]
    ENST00000490528 ; ENSP00000420362 ; ENSG00000160993 . [Q9NXW9-2 ]
    GeneIDi 54784.
    KEGGi hsa:54784.
    UCSCi uc003uzl.3. human. [Q9NXW9-1 ]

    Organism-specific databases

    CTDi 54784.
    GeneCardsi GC07M102096.
    HGNCi HGNC:21900. ALKBH4.
    HPAi HPA051422.
    MIMi 613302. gene.
    neXtProti NX_Q9NXW9.
    PharmGKBi PA143485294.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255556.
    HOGENOMi HOG000015835.
    HOVERGENi HBG062006.
    InParanoidi Q9NXW9.
    KOi K10766.
    OMAi DRDPWKL.
    OrthoDBi EOG73Z2V0.
    PhylomeDBi Q9NXW9.
    TreeFami TF314885.

    Miscellaneous databases

    GenomeRNAii 54784.
    NextBioi 57445.
    PROi Q9NXW9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9NXW9.
    CleanExi HS_ALKBH4.
    Genevestigatori Q9NXW9.

    Family and domain databases

    Gene3Di 2.60.120.590. 1 hit.
    InterProi IPR027450. AlkB-like.
    IPR005123. Oxoglu/Fe-dep_dioxygenase.
    [Graphical view ]
    Pfami PF03171. 2OG-FeII_Oxy. 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 1 AND 2).
      Tissue: Adipose tissue and Epithelium.
    2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [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: Lung and Placenta.
    5. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Spectroscopic and magnetic studies of wild-type and mutant forms of the Fe(II)-and 2-oxoglutarate-dependent decarboxylase ALKBH4."
      Bjornstad L.G., Zoppellaro G., Tomter A.B., Falnes P.O., Andersson K.K.
      Biochem. J. 434:391-398(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COFACTOR.
    8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [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. "Human ALKBH4 interacts with proteins associated with transcription."
      Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A., Falnes P.O.
      PLoS ONE 7:E49045-E49045(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZFHX3; MLLT3; MLLT1; HSF4; EP300; TES; EIF3C; MTMR6 AND PSMA6, SUBCELLULAR LOCATION.
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: FUNCTION, SUBCELLULAR LOCATION, ACTIN-BINDING, MUTAGENESIS OF HIS-169; ASP-171 AND HIS-254.

    Entry informationi

    Entry nameiALKB4_HUMAN
    AccessioniPrimary (citable) accession number: Q9NXW9
    Secondary accession number(s): Q53H92, Q9H6A4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 95 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

    Miscellaneous

    Actin demethylase activity has not been directly confirmed in vitro; however a number of experiments strongly suggest that ALKBH4 acts as a protein demethylase.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3