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Protein

Alkylated DNA repair protein alkB homolog 8

Gene

ALKBH8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its methyltransferase domain (PubMed:20123966, PubMed:20308323). Catalyzes the last step in the formation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA (PubMed:20123966, PubMed:20308323). Has a preference for tRNA(Arg) and tRNA(Glu), and does not bind tRNA(Lys)(PubMed:20308323). Binds tRNA and catalyzes the iron and alpha-ketoglutarate dependent hydroxylation of 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in tRNA via its dioxygenase domain, giving rise to 5-(S)-methoxycarbonylhydroxymethyluridine; has a preference for tRNA(Gly) (PubMed:21285950). Required for normal survival after DNA damage (PubMed:20308323). May inhibit apoptosis and promote cell survival and angiogenesis (PubMed:19293182).4 Publications

Catalytic activityi

S-adenosyl-L-methionine + carboxymethyluridine(34) in tRNA = S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine(34) in tRNA.1 Publication

Cofactori

Fe2+1 Publication1 PublicationNote: Binds 1 Fe2+ ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi238 – 2381Iron; catalyticPROSITE-ProRule annotationCurated
Metal bindingi240 – 2401Iron; catalyticPROSITE-ProRule annotationCurated
Metal bindingi242 – 2421Zinc; via pros nitrogen1 Publication
Metal bindingi292 – 2921Iron; catalyticPROSITE-ProRule annotationCurated
Binding sitei328 – 3281Alpha-ketoglutarate1 Publication
Binding sitei334 – 3341Alpha-ketoglutarate1 Publication
Metal bindingi341 – 3411Zinc1 Publication
Metal bindingi343 – 3431Zinc1 Publication
Metal bindingi349 – 3491Zinc1 Publication

GO - Molecular functioni

  • iron ion binding Source: UniProtKB
  • 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
  • tRNA (uracil) methyltransferase activity Source: UniProtKB
  • tRNA binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • tRNA methylation Source: UniProtKB
  • tRNA wobble uridine modification Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Oxidoreductase, Transferase

Keywords - Ligandi

Iron, Metal-binding, RNA-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

BRENDAi2.1.1.229. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkylated DNA repair protein alkB homolog 8 (EC:1.14.11.-)
Alternative name(s):
Probable alpha-ketoglutarate-dependent dioxygenase ABH8
S-adenosyl-L-methionine-dependent tRNA methyltransferase ABH8
tRNA (carboxymethyluridine(34)-5-O)-methyltransferase ABH8 (EC:2.1.1.229)
Gene namesi
Name:ALKBH8
Synonyms:ABH8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:25189. ALKBH8.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • microtubule cytoskeleton Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA143485296.

Polymorphism and mutation databases

BioMutaiALKBH8.
DMDMi189027650.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 664664Alkylated DNA repair protein alkB homolog 8PRO_0000337125Add
BLAST

Proteomic databases

MaxQBiQ96BT7.
PaxDbiQ96BT7.
PRIDEiQ96BT7.

PTM databases

PhosphoSiteiQ96BT7.

Expressioni

Tissue specificityi

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

Inductioni

Up-regulated after DNA damage. Induction is mediated via ATM.1 Publication

Gene expression databases

BgeeiQ96BT7.
CleanExiHS_ALKBH8.
ExpressionAtlasiQ96BT7. baseline and differential.
GenevisibleiQ96BT7. HS.

Organism-specific databases

HPAiHPA038724.
HPA038725.
HPA061514.

Interactioni

Subunit structurei

Interacts with TRMT112.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TRMT112Q9UI302EBI-10825637,EBI-373326

Protein-protein interaction databases

IntActiQ96BT7. 1 interaction.
STRINGi9606.ENSP00000374219.

Structurei

Secondary structure

1
664
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 283Combined sources
Turni30 – 345Combined sources
Beta strandi38 – 403Combined sources
Beta strandi43 – 486Combined sources
Helixi52 – 543Combined sources
Helixi58 – 669Combined sources
Beta strandi71 – 755Combined sources
Beta strandi81 – 899Combined sources
Helixi90 – 9910Combined sources
Turni100 – 1023Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi116 – 1194Combined sources
Beta strandi121 – 1299Combined sources
Beta strandi137 – 1404Combined sources
Helixi146 – 1538Combined sources
Beta strandi175 – 1773Combined sources
Helixi202 – 21413Combined sources
Beta strandi222 – 2298Combined sources
Beta strandi235 – 2384Combined sources
Turni242 – 2443Combined sources
Beta strandi249 – 2568Combined sources
Beta strandi258 – 2636Combined sources
Beta strandi269 – 2746Combined sources
Beta strandi278 – 2825Combined sources
Helixi285 – 2884Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi298 – 3047Combined sources
Beta strandi307 – 3093Combined sources
Beta strandi315 – 3184Combined sources
Beta strandi320 – 3245Combined sources
Beta strandi328 – 3347Combined sources
Turni346 – 3483Combined sources
Turni350 – 3556Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQ2NMR-A25-125[»]
3THPX-ray3.20A25-355[»]
3THTX-ray3.01A/B/C/D25-355[»]
ProteinModelPortaliQ96BT7.
SMRiQ96BT7. Positions 25-355, 377-505.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96BT7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 12078RRMAdd
BLAST
Domaini220 – 337118Fe2OG dioxygenasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni227 – 2293Alpha-ketoglutarate binding1 Publication
Regioni411 – 664254Methyltransferase domainAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0500.
GeneTreeiENSGT00530000063536.
HOGENOMiHOG000007984.
HOVERGENiHBG067234.
InParanoidiQ96BT7.
KOiK10770.
OMAiPCNCSYP.
OrthoDBiEOG780RMC.
PhylomeDBiQ96BT7.
TreeFamiTF316056.

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
3.40.50.150. 2 hits.
InterProiIPR027450. AlkB-like.
IPR015095. AlkB_hom8_N.
IPR013216. Methyltransf_11.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF13532. 2OG-FeII_Oxy_2. 1 hit.
PF09004. DUF1891. 1 hit.
PF08241. Methyltransf_11. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51471. FE2OG_OXY. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96BT7-1) [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

        10         20         30         40         50
MDSNHQSNYK LSKTEKKFLR KQIKAKHTLL RHEGIETVSY ATQSLVVANG
60 70 80 90 100
GLGNGVSRNQ LLPVLEKCGL VDALLMPPNK PYSFARYRTT EESKRAYVTL
110 120 130 140 150
NGKEVVDDLG QKITLYLNFV EKVQWKELRP QALPPGLMVV EEIISSEEEK
160 170 180 190 200
MLLESVDWTE DTDNQNSQKS LKHRRVKHFG YEFHYENNNV DKDKPLSGGL
210 220 230 240 250
PDICESFLEK WLRKGYIKHK PDQMTINQYE PGQGIPAHID THSAFEDEIV
260 270 280 290 300
SLSLGSEIVM DFKHPDGIAV PVMLPRRSLL VMTGESRYLW THGITCRKFD
310 320 330 340 350
TVQASESLKS GIITSDVGDL TLSKRGLRTS FTFRKVRQTP CNCSYPLVCD
360 370 380 390 400
SQRKETPPSF PESDKEASRL EQEYVHQVYE EIAGHFSSTR HTPWPHIVEF
410 420 430 440 450
LKALPSGSIV ADIGCGNGKY LGINKELYMI GCDRSQNLVD ICRERQFQAF
460 470 480 490 500
VCDALAVPVR SGSCDACISI AVIHHFATAE RRVAALQEIV RLLRPGGKAL
510 520 530 540 550
IYVWAMEQEY NKQKSKYLRG NRNSQGKKEE MNSDTSVQRS LVEQMRDMGS
560 570 580 590 600
RDSASSVPRI NDSQEGGCNS RQVSNSKLPV HVNRTSFYSQ DVLVPWHLKG
610 620 630 640 650
NPDKGKPVEP FGPIGSQDPS PVFHRYYHVF REGELEGACR TVSDVRILQS
660
YYDQGNWCVI LQKA
Length:664
Mass (Da):75,208
Last modified:May 20, 2008 - v2
Checksum:i4BE595D6757C2A43
GO
Isoform 2 (identifier: Q96BT7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     234-238: GIPAH → DCHGF
     239-664: Missing.

Note: No experimental confirmation available. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Show »
Length:238
Mass (Da):27,440
Checksum:i24EF6A3A66DCC2F7
GO
Isoform 3 (identifier: Q96BT7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     215-224: GYIKHKPDQM → AEKNLEVGIH
     225-664: Missing.

Note: No experimental confirmation available.
Show »
Length:224
Mass (Da):25,742
Checksum:i6FD66E832509EE87
GO
Isoform 4 (identifier: Q96BT7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MFAM

Note: May be due to competing donor splice site. No experimental confirmation available.
Show »
Length:667
Mass (Da):75,558
Checksum:iBF6DB408A2B1B39C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101K → R in BAC04566 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MFAM in isoform 4. 1 PublicationVSP_039159
Alternative sequencei215 – 22410GYIKHKPDQM → AEKNLEVGIH in isoform 3. 1 PublicationVSP_033925
Alternative sequencei225 – 664440Missing in isoform 3. 1 PublicationVSP_033926Add
BLAST
Alternative sequencei234 – 2385GIPAH → DCHGF in isoform 2. 1 PublicationVSP_033927
Alternative sequencei239 – 664426Missing in isoform 2. 1 PublicationVSP_033928Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB218768 mRNA. Translation: BAG16270.1.
AK095523 mRNA. Translation: BAC04566.1.
AK293603 mRNA. Translation: BAG57067.1.
AK304413 mRNA. Translation: BAG65244.1.
AP001823 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67089.1.
CH471065 Genomic DNA. Translation: EAW67090.1.
BC015183 mRNA. Translation: AAH15183.1.
CCDSiCCDS73376.1. [Q96BT7-4]
CCDS8337.2. [Q96BT7-1]
RefSeqiNP_001287939.1. NM_001301010.1. [Q96BT7-4]
NP_620130.2. NM_138775.2. [Q96BT7-1]
UniGeneiHs.503763.

Genome annotation databases

EnsembliENST00000260318; ENSP00000260318; ENSG00000137760. [Q96BT7-2]
ENST00000389568; ENSP00000374219; ENSG00000137760.
ENST00000417449; ENSP00000397673; ENSG00000137760. [Q96BT7-4]
ENST00000428149; ENSP00000415885; ENSG00000137760.
ENST00000429370; ENSP00000391225; ENSG00000137760. [Q96BT7-3]
GeneIDi91801.
KEGGihsa:91801.
UCSCiuc001pjk.3. human. [Q96BT7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB218768 mRNA. Translation: BAG16270.1.
AK095523 mRNA. Translation: BAC04566.1.
AK293603 mRNA. Translation: BAG57067.1.
AK304413 mRNA. Translation: BAG65244.1.
AP001823 Genomic DNA. No translation available.
CH471065 Genomic DNA. Translation: EAW67089.1.
CH471065 Genomic DNA. Translation: EAW67090.1.
BC015183 mRNA. Translation: AAH15183.1.
CCDSiCCDS73376.1. [Q96BT7-4]
CCDS8337.2. [Q96BT7-1]
RefSeqiNP_001287939.1. NM_001301010.1. [Q96BT7-4]
NP_620130.2. NM_138775.2. [Q96BT7-1]
UniGeneiHs.503763.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQ2NMR-A25-125[»]
3THPX-ray3.20A25-355[»]
3THTX-ray3.01A/B/C/D25-355[»]
ProteinModelPortaliQ96BT7.
SMRiQ96BT7. Positions 25-355, 377-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ96BT7. 1 interaction.
STRINGi9606.ENSP00000374219.

PTM databases

PhosphoSiteiQ96BT7.

Polymorphism and mutation databases

BioMutaiALKBH8.
DMDMi189027650.

Proteomic databases

MaxQBiQ96BT7.
PaxDbiQ96BT7.
PRIDEiQ96BT7.

Protocols and materials databases

DNASUi91801.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260318; ENSP00000260318; ENSG00000137760. [Q96BT7-2]
ENST00000389568; ENSP00000374219; ENSG00000137760.
ENST00000417449; ENSP00000397673; ENSG00000137760. [Q96BT7-4]
ENST00000428149; ENSP00000415885; ENSG00000137760.
ENST00000429370; ENSP00000391225; ENSG00000137760. [Q96BT7-3]
GeneIDi91801.
KEGGihsa:91801.
UCSCiuc001pjk.3. human. [Q96BT7-1]

Organism-specific databases

CTDi91801.
GeneCardsiGC11M107373.
HGNCiHGNC:25189. ALKBH8.
HPAiHPA038724.
HPA038725.
HPA061514.
MIMi613306. gene.
neXtProtiNX_Q96BT7.
PharmGKBiPA143485296.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0500.
GeneTreeiENSGT00530000063536.
HOGENOMiHOG000007984.
HOVERGENiHBG067234.
InParanoidiQ96BT7.
KOiK10770.
OMAiPCNCSYP.
OrthoDBiEOG780RMC.
PhylomeDBiQ96BT7.
TreeFamiTF316056.

Enzyme and pathway databases

BRENDAi2.1.1.229. 2681.

Miscellaneous databases

ChiTaRSiALKBH8. human.
EvolutionaryTraceiQ96BT7.
GenomeRNAii91801.
NextBioi77461.
PROiQ96BT7.
SOURCEiSearch...

Gene expression databases

BgeeiQ96BT7.
CleanExiHS_ALKBH8.
ExpressionAtlasiQ96BT7. baseline and differential.
GenevisibleiQ96BT7. HS.

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
3.40.50.150. 2 hits.
InterProiIPR027450. AlkB-like.
IPR015095. AlkB_hom8_N.
IPR013216. Methyltransf_11.
IPR005123. Oxoglu/Fe-dep_dioxygenase.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF13532. 2OG-FeII_Oxy_2. 1 hit.
PF09004. DUF1891. 1 hit.
PF08241. Methyltransf_11. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51471. FE2OG_OXY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "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; 3 AND 4).
    Tissue: Brain and Trachea.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2).
    Tissue: Uterus.
  6. "A novel human AlkB homologue, ALKBH8, contributes to human bladder cancer progression."
    Shimada K., Nakamura M., Anai S., De Velasco M., Tanaka M., Tsujikawa K., Ouji Y., Konishi N.
    Cancer Res. 69:3157-3164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Mammalian ALKBH8 possesses tRNA methyltransferase activity required for the biogenesis of multiple wobble uridine modifications implicated in translational decoding."
    Songe-Moller L., van den Born E., Leihne V., Vagbo C.B., Kristoffersen T., Krokan H.E., Kirpekar F., Falnes P.O., Klungland A.
    Mol. Cell. Biol. 30:1814-1827(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TRMT112.
  8. "Human AlkB homolog ABH8 is a tRNA methyltransferase required for wobble uridine modification and DNA damage survival."
    Fu D., Brophy J.A., Chan C.T., Atmore K.A., Begley U., Paules R.S., Dedon P.C., Begley T.J., Samson L.D.
    Mol. Cell. Biol. 30:2449-2459(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH TRMT112, INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "ALKBH8-mediated formation of a novel diastereomeric pair of wobble nucleosides in mammalian tRNA."
    van den Born E., Vagbo C.B., Songe-Moller L., Leihne V., Lien G.F., Leszczynska G., Malkiewicz A., Krokan H.E., Kirpekar F., Klungland A., Falnes P.O.
    Nat. Commun. 2:172-172(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, INTERACTION WITH TRMT112.
  10. "Solution structure of RNA binding domain in hypothetical protein LOC91801."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 25-125.
  11. "Crystal structure and RNA binding properties of the RNA recognition motif (RRM) and AlkB domains in human AlkB homolog 8 (ABH8), an enzyme catalyzing tRNA hypermodification."
    Pastore C., Topalidou I., Forouhar F., Yan A.C., Levy M., Hunt J.F.
    J. Biol. Chem. 287:2130-2143(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 25-355 IN COMPLEX WITH ALPHA-KETOGLUTARATE; MANGANESE AND ZINC, COFACTOR, INTERACTION WITH TRMT112, RNA-BINDING.

Entry informationi

Entry nameiALKB8_HUMAN
AccessioniPrimary (citable) accession number: Q96BT7
Secondary accession number(s): B1Q2M0, B4DEF6, Q8N989
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: July 22, 2015
This is version 124 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, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.