ALKB6_HUMAN
ID ALKB6_HUMAN Reviewed; 238 AA.
AC Q3KRA9; A5LGM8; A6NLP1; A8MU96;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 6;
DE EC=1.14.11.-;
DE AltName: Full=Alkylated DNA repair protein alkB homolog 6;
GN Name=ALKBH6; Synonyms=ABH6;
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 [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-238 (ISOFORM 2).
RC TISSUE=Urinary bladder;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP INTERACTION WITH VCPKMT.
RX PubMed=22948820; DOI=10.1038/ncomms2041;
RA Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S.,
RA Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.;
RT "Lysine methylation of VCP by a member of a novel human protein
RT methyltransferase family.";
RL Nat. Commun. 3:1038-1038(2012).
CC -!- FUNCTION: Probable dioxygenase that requires molecular oxygen, alpha-
CC ketoglutarate and iron. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- SUBUNIT: Interacts with VCPKMT. {ECO:0000269|PubMed:22948820}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17979886}. Nucleus
CC {ECO:0000269|PubMed:17979886}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3KRA9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3KRA9-2; Sequence=VSP_032056;
CC Name=3;
CC IsoId=Q3KRA9-3; Sequence=VSP_032056, VSP_032057;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in testis
CC and pancreas. {ECO:0000269|PubMed:17979886}.
CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI05802.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB273714; BAF63844.1; -; mRNA.
DR EMBL; AF038458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK310704; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC105801; AAI05802.1; ALT_INIT; mRNA.
DR CCDS; CCDS12485.2; -. [Q3KRA9-1]
DR CCDS; CCDS74342.1; -. [Q3KRA9-1]
DR RefSeq; NP_001284630.1; NM_001297701.1. [Q3KRA9-1]
DR RefSeq; NP_116267.3; NM_032878.3. [Q3KRA9-1]
DR RefSeq; XP_005259414.1; XM_005259357.4. [Q3KRA9-1]
DR PDB; 7VJS; X-ray; 1.79 A; A=1-238.
DR PDB; 7VJV; X-ray; 1.75 A; A=1-238.
DR PDBsum; 7VJS; -.
DR PDBsum; 7VJV; -.
DR AlphaFoldDB; Q3KRA9; -.
DR SMR; Q3KRA9; -.
DR STRING; 9606.ENSP00000368152; -.
DR iPTMnet; Q3KRA9; -.
DR PhosphoSitePlus; Q3KRA9; -.
DR BioMuta; ALKBH6; -.
DR DMDM; 172046713; -.
DR EPD; Q3KRA9; -.
DR jPOST; Q3KRA9; -.
DR MassIVE; Q3KRA9; -.
DR MaxQB; Q3KRA9; -.
DR PaxDb; Q3KRA9; -.
DR PeptideAtlas; Q3KRA9; -.
DR PRIDE; Q3KRA9; -.
DR ProteomicsDB; 61741; -. [Q3KRA9-1]
DR ProteomicsDB; 61742; -. [Q3KRA9-2]
DR ProteomicsDB; 61743; -. [Q3KRA9-3]
DR Antibodypedia; 68413; 77 antibodies from 17 providers.
DR DNASU; 84964; -.
DR Ensembl; ENST00000252984.11; ENSP00000252984.6; ENSG00000239382.11. [Q3KRA9-1]
DR Ensembl; ENST00000378875.8; ENSP00000368152.4; ENSG00000239382.11. [Q3KRA9-1]
DR GeneID; 84964; -.
DR KEGG; hsa:84964; -.
DR MANE-Select; ENST00000378875.8; ENSP00000368152.4; NM_032878.5; NP_116267.4.
DR UCSC; uc002ocv.2; human. [Q3KRA9-1]
DR CTD; 84964; -.
DR DisGeNET; 84964; -.
DR GeneCards; ALKBH6; -.
DR HGNC; HGNC:28243; ALKBH6.
DR HPA; ENSG00000239382; Low tissue specificity.
DR MIM; 613304; gene.
DR neXtProt; NX_Q3KRA9; -.
DR OpenTargets; ENSG00000239382; -.
DR PharmGKB; PA143485295; -.
DR VEuPathDB; HostDB:ENSG00000239382; -.
DR eggNOG; KOG3200; Eukaryota.
DR GeneTree; ENSGT00510000048626; -.
DR HOGENOM; CLU_059836_2_0_1; -.
DR InParanoid; Q3KRA9; -.
DR OrthoDB; 1573279at2759; -.
DR PhylomeDB; Q3KRA9; -.
DR TreeFam; TF314467; -.
DR PathwayCommons; Q3KRA9; -.
DR BioGRID-ORCS; 84964; 13 hits in 1086 CRISPR screens.
DR ChiTaRS; ALKBH6; human.
DR GenomeRNAi; 84964; -.
DR Pharos; Q3KRA9; Tdark.
DR PRO; PR:Q3KRA9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q3KRA9; protein.
DR Bgee; ENSG00000239382; Expressed in lateral nuclear group of thalamus and 170 other tissues.
DR ExpressionAtlas; Q3KRA9; baseline and differential.
DR Genevisible; Q3KRA9; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.590; -; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032862; ALKBH6.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR PANTHER; PTHR46030; PTHR46030; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Dioxygenase; Iron;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..238
FT /note="Alpha-ketoglutarate-dependent dioxygenase alkB
FT homolog 6"
FT /id="PRO_0000323716"
FT DOMAIN 96..227
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 138..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 103..105
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 116
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 218..224
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MAGRGMGMLNLEIGGDAGGRIGCKELVLM (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032056"
FT VAR_SEQ 64..238
FT /note="LPHPRGMVPERLPPWLQRYVDKVSNLSLFGGLPANHVLVNQYLPGEGIMPHE
FT DGPLYYPTVSTISLGSHTVLDFYEPRRPEDDDPTEQPRPPPRPTTSLLLEPRSLLVLRG
FT PAYTRLLHGIAAARVDALDAASSPPNAAACPSARPGACLVRGTRVSLTIRRVPRVLRAG
FT LLLGK -> PSGPHCLPQVGFLIPEGWFLSGCPHGSSATWTKCQTSASLEASQLTMSS
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032057"
SQ SEQUENCE 238 AA; 26483 MW; 2CA6EEDA8DB61388 CRC64;
MEEQDARVPA LEPFRVEQAP PVIYYVPDFI SKEEEEYLLR QVFNAPKPKW TQLSGRKLQN
WGGLPHPRGM VPERLPPWLQ RYVDKVSNLS LFGGLPANHV LVNQYLPGEG IMPHEDGPLY
YPTVSTISLG SHTVLDFYEP RRPEDDDPTE QPRPPPRPTT SLLLEPRSLL VLRGPAYTRL
LHGIAAARVD ALDAASSPPN AAACPSARPG ACLVRGTRVS LTIRRVPRVL RAGLLLGK
