ALKB4_HUMAN
ID ALKB4_HUMAN Reviewed; 302 AA.
AC Q9NXW9; Q53H92; Q9H6A4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4 {ECO:0000305};
DE AltName: Full=Alkylated DNA repair protein alkB homolog 4 {ECO:0000303|PubMed:21166655};
DE AltName: Full=DNA N6-methyl adenine demethylase ALKBH4 {ECO:0000305};
DE EC=1.14.11.51 {ECO:0000250|UniProtKB:Q9D8F1};
DE AltName: Full=Lysine-specific demethylase ALKBH4 {ECO:0000305};
DE EC=1.14.11.- {ECO:0000269|PubMed:22814378};
GN Name=ALKBH4 {ECO:0000303|PubMed:21166655, ECO:0000312|HGNC:HGNC:21900};
GN Synonyms=ABH4 {ECO:0000303|PubMed:17979886};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adipose tissue, and Epithelium;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17979886; DOI=10.1111/j.1582-4934.2007.00094.x;
RA Tsujikawa K., Koike K., Kitae K., Shinkawa A., Arima H., Suzuki T.,
RA Tsuchiya M., Makino Y., Furukawa T., Konishi N., Yamamoto H.;
RT "Expression and sub-cellular localization of human ABH family molecules.";
RL J. Cell. Mol. Med. 11:1105-1116(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP FUNCTION, AND COFACTOR.
RX PubMed=21166655; DOI=10.1042/bj20101667;
RA Bjornstad L.G., Zoppellaro G., Tomter A.B., Falnes P.O., Andersson K.K.;
RT "Spectroscopic and magnetic studies of wild-type and mutant forms of the
RT Fe(II)-and 2-oxoglutarate-dependent decarboxylase ALKBH4.";
RL Biochem. J. 434:391-398(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP INTERACTION WITH ZFHX3; MLLT3; MLLT1; HSF4; EP300; TES; EIF3C; MTMR6 AND
RP PSMA6, AND SUBCELLULAR LOCATION.
RX PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A.,
RA Falnes P.O.;
RT "Human ALKBH4 interacts with proteins associated with transcription.";
RL PLoS ONE 7:E49045-E49045(2012).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIN-BINDING, AND
RP MUTAGENESIS OF HIS-169; ASP-171 AND HIS-254.
RX PubMed=23673617; DOI=10.1038/ncomms2863;
RA Li M.M., Nilsen A., Shi Y., Fusser M., Ding Y.H., Fu Y., Liu B., Niu Y.,
RA Wu Y.S., Huang C.M., Olofsson M., Jin K.X., Lv Y., Xu X.Z., He C.,
RA Dong M.Q., Rendtlew Danielsen J.M., Klungland A., Yang Y.G.;
RT "ALKBH4-dependent demethylation of actin regulates actomyosin dynamics.";
RL Nat. Commun. 4:1832-1832(2013).
CC -!- FUNCTION: Dioxygenase that mediates demethylation of actin
CC monomethylated at 'Lys-84' (K84me1), thereby acting as a regulator of
CC actomyosin-processes (PubMed:23673617). Demethylation of actin K84me1
CC is required for maintaining actomyosin dynamics supporting normal
CC cleavage furrow ingression during cytokinesis and cell migration
CC (PubMed:23673617). In addition to proteins, also demethylates DNA:
CC specifically demethylates DNA methylated on the 6th position of adenine
CC (N(6)-methyladenosine) DNA, thereby regulating Polycomb silencing (By
CC similarity). {ECO:0000250|UniProtKB:Q9D8F1,
CC ECO:0000269|PubMed:23673617}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an N(6)-methyl-2'-deoxyadenosine in DNA + O2
CC = a 2'-deoxyadenosine in DNA + CO2 + formaldehyde + succinate;
CC Xref=Rhea:RHEA:49524, Rhea:RHEA-COMP:12418, Rhea:RHEA-COMP:12419,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:90615,
CC ChEBI:CHEBI:90616; EC=1.14.11.51;
CC Evidence={ECO:0000250|UniProtKB:Q9D8F1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49525;
CC Evidence={ECO:0000250|UniProtKB:Q9D8F1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + N(6)-methyl-L-lysyl-[protein] + O2 = CO2 +
CC formaldehyde + L-lysyl-[protein] + succinate; Xref=Rhea:RHEA:60924,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000269|PubMed:23673617};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60925;
CC Evidence={ECO:0000269|PubMed:23673617};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:21166655};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:21166655};
CC -!- SUBUNIT: Interacts with ZFHX3, MLLT3, MLLT1, HSF4, EP300, TES, EIF3C,
CC MTMR6 and PSMA6. {ECO:0000269|PubMed:23145062}.
CC -!- INTERACTION:
CC Q9NXW9; Q9NP55: BPIFA1; NbExp=3; IntAct=EBI-8637516, EBI-953896;
CC Q9NXW9; Q86UW9: DTX2; NbExp=11; IntAct=EBI-8637516, EBI-740376;
CC Q9NXW9; Q09472: EP300; NbExp=4; IntAct=EBI-8637516, EBI-447295;
CC Q9NXW9; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-8637516, EBI-11978259;
CC Q9NXW9; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-8637516, EBI-739467;
CC Q9NXW9; P80188: LCN2; NbExp=3; IntAct=EBI-8637516, EBI-11911016;
CC Q9NXW9; P42568: MLLT3; NbExp=5; IntAct=EBI-8637516, EBI-716132;
CC Q9NXW9; Q9GZT8: NIF3L1; NbExp=5; IntAct=EBI-8637516, EBI-740897;
CC Q9NXW9; P15884-3: TCF4; NbExp=3; IntAct=EBI-8637516, EBI-13636688;
CC Q9NXW9; Q9BUZ4: TRAF4; NbExp=4; IntAct=EBI-8637516, EBI-3650647;
CC Q9NXW9; Q9NX01: TXNL4B; NbExp=3; IntAct=EBI-8637516, EBI-10309345;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17979886}. Nucleus
CC {ECO:0000269|PubMed:17979886, ECO:0000269|PubMed:23145062}. Nucleus,
CC nucleolus {ECO:0000250|UniProtKB:Q9D8F1}. Midbody
CC {ECO:0000269|PubMed:23673617}. Note=Associates with the contractile
CC ring and midbody. {ECO:0000269|PubMed:23673617}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NXW9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NXW9-2; Sequence=VSP_019128, VSP_036841;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
CC pancreas, ovary and spleen. {ECO:0000269|PubMed:17979886}.
CC -!- MISCELLANEOUS: Actin demethylase activity has not been directly
CC confirmed in vitro; however a number of experiments strongly suggest
CC that ALKBH4 acts as a protein demethylase.
CC {ECO:0000305|PubMed:23673617}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15358.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AK000020; BAA90888.1; -; mRNA.
DR EMBL; AK026097; BAB15358.1; ALT_SEQ; mRNA.
DR EMBL; AK222689; BAD96409.1; -; mRNA.
DR EMBL; AC093668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002820; AAH02820.1; -; mRNA.
DR EMBL; BC017096; AAH17096.1; -; mRNA.
DR CCDS; CCDS5723.1; -. [Q9NXW9-1]
DR RefSeq; NP_060091.1; NM_017621.3. [Q9NXW9-1]
DR RefSeq; XP_005250521.1; XM_005250464.2.
DR AlphaFoldDB; Q9NXW9; -.
DR SMR; Q9NXW9; -.
DR BioGRID; 120148; 26.
DR IntAct; Q9NXW9; 18.
DR MINT; Q9NXW9; -.
DR STRING; 9606.ENSP00000292566; -.
DR iPTMnet; Q9NXW9; -.
DR PhosphoSitePlus; Q9NXW9; -.
DR BioMuta; ALKBH4; -.
DR DMDM; 74734701; -.
DR EPD; Q9NXW9; -.
DR jPOST; Q9NXW9; -.
DR MassIVE; Q9NXW9; -.
DR MaxQB; Q9NXW9; -.
DR PaxDb; Q9NXW9; -.
DR PeptideAtlas; Q9NXW9; -.
DR PRIDE; Q9NXW9; -.
DR ProteomicsDB; 83141; -. [Q9NXW9-1]
DR ProteomicsDB; 83142; -. [Q9NXW9-2]
DR Antibodypedia; 45707; 158 antibodies from 22 providers.
DR DNASU; 54784; -.
DR Ensembl; ENST00000292566.4; ENSP00000292566.3; ENSG00000160993.4. [Q9NXW9-1]
DR Ensembl; ENST00000490528.1; ENSP00000420362.1; ENSG00000160993.4. [Q9NXW9-2]
DR GeneID; 54784; -.
DR KEGG; hsa:54784; -.
DR MANE-Select; ENST00000292566.4; ENSP00000292566.3; NM_017621.4; NP_060091.1.
DR UCSC; uc003uzl.4; human. [Q9NXW9-1]
DR CTD; 54784; -.
DR GeneCards; ALKBH4; -.
DR HGNC; HGNC:21900; ALKBH4.
DR HPA; ENSG00000160993; Low tissue specificity.
DR MIM; 613302; gene.
DR neXtProt; NX_Q9NXW9; -.
DR OpenTargets; ENSG00000160993; -.
DR PharmGKB; PA143485294; -.
DR VEuPathDB; HostDB:ENSG00000160993; -.
DR eggNOG; KOG3959; Eukaryota.
DR GeneTree; ENSGT00390000006344; -.
DR HOGENOM; CLU_060545_0_0_1; -.
DR InParanoid; Q9NXW9; -.
DR OMA; VHHFLYD; -.
DR OrthoDB; 933314at2759; -.
DR PhylomeDB; Q9NXW9; -.
DR TreeFam; TF314885; -.
DR PathwayCommons; Q9NXW9; -.
DR SignaLink; Q9NXW9; -.
DR BioGRID-ORCS; 54784; 17 hits in 1082 CRISPR screens.
DR GenomeRNAi; 54784; -.
DR Pharos; Q9NXW9; Tbio.
DR PRO; PR:Q9NXW9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NXW9; protein.
DR Bgee; ENSG00000160993; Expressed in parotid gland and 175 other tissues.
DR Genevisible; Q9NXW9; HS.
DR GO; GO:0070938; C:contractile ring; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0032451; F:demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035516; F:oxidative DNA demethylase activity; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0031032; P:actomyosin structure organization; IMP:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0036090; P:cleavage furrow ingression; IMP:UniProtKB.
DR GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB.
DR GO; GO:0070989; P:oxidative demethylation; IBA:GO_Central.
DR GO; GO:0006482; P:protein demethylation; IDA:UniProtKB.
DR GO; GO:1902275; P:regulation of chromatin organization; ISS:UniProtKB.
DR Gene3D; 2.60.120.590; -; 1.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032857; ALKBH4.
DR PANTHER; PTHR12463; PTHR12463; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Chromatin regulator;
KW Cytoplasm; Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..302
FT /note="Alpha-ketoglutarate-dependent dioxygenase alkB
FT homolog 4"
FT /id="PRO_0000239281"
FT DOMAIN 150..274
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 171
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 254
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 265
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 42
FT /note="K -> E (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_019128"
FT VAR_SEQ 43..302
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_036841"
FT VARIANT 247
FT /note="A -> V (in dbSNP:rs41275227)"
FT /id="VAR_061004"
FT MUTAGEN 169
FT /note="H->A: Loss of function mutant that acts as a
FT dominant-negative mutant when overexpressed, leading to
FT multinucleation and cleavage furrow disorganization; when
FT associated with A-171 and A-254."
FT /evidence="ECO:0000269|PubMed:23673617"
FT MUTAGEN 171
FT /note="D->A: Loss of function mutant that acts as a
FT dominant-negative mutant when overexpressed, leading to
FT multinucleation and cleavage furrow disorganization; when
FT associated with A-169 and A-254."
FT /evidence="ECO:0000269|PubMed:23673617"
FT MUTAGEN 254
FT /note="H->A: Loss of function mutant that acts as a
FT dominant-negative mutant when overexpressed, leading to
FT multinucleation and cleavage furrow disorganization; when
FT associated with A-169 and A-171."
FT /evidence="ECO:0000269|PubMed:23673617"
FT CONFLICT 210
FT /note="A -> V (in Ref. 2; BAD96409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 33838 MW; 67C2DFE058962AF4 CRC64;
MAAAAAETPE VLRECGCKGI RTCLICERQR GSDPPWELPP AKTYRFIYCS DTGWAVGTEE
SDFEGWAFPF PGVMLIEDFV TREEEAELVR LMDRDPWKLS QSGRRKQDYG PKVNFRKQKL
KTEGFCGLPS FSREVVRRMG LYPGLEGFRP VEQCNLDYCP ERGSAIDPHL DDAWLWGERL
VSLNLLSPTV LSMCREAPGS LLLCSAPSAA PEALVDSVIA PSRSVLCQEV EVAIPLPARS
LLVLTGAARH QWKHAIHRRH IEARRVCVTF RELSAEFGPG GRQQELGQEL LRIALSFQGR
PV
