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Protein

RNA demethylase ALKBH5

Gene

ALKBH5

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

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 (PubMed:23177736, PubMed:24778178, PubMed:24616105, PubMed:24489119). Can also demethylate N(6)-methyladenosine in single-stranded DNA (in vitro) (PubMed:24616105). Requires molecular oxygen, alpha-ketoglutarate and iron (PubMed:21264265, PubMed:23177736, PubMed:24778178, PubMed:24616105, PubMed:24489119). Demethylation of m6A mRNA affects mRNA processing and export (PubMed:23177736). Required for spermatogenesis (By similarity).By similarity5 Publications

Cofactori

Fe2+3 PublicationsNote: Binds 1 Fe2+ ion per subunit.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi204 – 2041Iron; catalyticCurated
Metal bindingi206 – 2061Iron; catalyticCurated
Metal bindingi266 – 2661Iron; catalyticCurated
Binding sitei277 – 2771Alpha-ketoglutarate1 Publication

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
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Biological processi

Differentiation, Spermatogenesis

Keywords - Ligandi

Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA demethylase ALKBH51 Publication (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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:25996. ALKBH5.

Subcellular locationi

  1. Nucleus speckle 2 Publications

GO - Cellular componenti

  1. nuclear speck Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi130 – 1301R → A: Abolishes catalytic activity. 2 Publications
Mutagenesisi132 – 1321K → A: No effect on catalytic activity with N(6)-methyladenosine in single-stranded DNA. 1 Publication
Mutagenesisi139 – 1391Y → A: Abolishes catalytic activity. 2 Publications
Mutagenesisi141 – 1411Y → A: Abolishes catalytic activity with N(6)-methyladenosine in single-stranded DNA. 1 Publication
Mutagenesisi153 – 1531E → A: No effect on catalytic activity. 1 Publication
Mutagenesisi195 – 1951Y → A: Abolishes catalytic activity. 1 Publication
Mutagenesisi204 – 2041H → A: Abolishes catalytic activity. 2 Publications
Mutagenesisi209 – 2102HI → AA: Abolishes catalytic activity. 1 Publication
Mutagenesisi232 – 2343FQF → DDE: Impaired catalytic activity. 1 Publication
Mutagenesisi266 – 2661H → A: Impaired catalytic activity. 1 Publication
Mutagenesisi277 – 2771R → A: Abolishes catalytic activity; when associated with A-283. 1 Publication
Mutagenesisi283 – 2831R → A: Abolishes catalytic activity; when associated with A-277. 1 Publication

Organism-specific databases

PharmGKBiPA142671230.

Polymorphism and mutation databases

BioMutaiALKBH5.
DMDMi408359959.

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 – 641Phosphoserine3 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

BgeeiQ6P6C2.
CleanExiHS_ALKBH5.
ExpressionAtlasiQ6P6C2. baseline and differential.
GenevestigatoriQ6P6C2.

Organism-specific databases

HPAiHPA007196.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi120237. 5 interactions.
IntActiQ6P6C2. 1 interaction.
STRINGi9606.ENSP00000382091.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni193 – 1953Alpha-ketoglutarate binding1 Publication

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.
GeneTreeiENSGT00390000009298.
HOGENOMiHOG000007505.
HOVERGENiHBG080833.
InParanoidiQ6P6C2.
KOiK10767.
OMAiWVHELVI.
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. AlignAdd to basket

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

        10         20         30         40         50
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP
60 70 80 90 100
YPVSGAKRKY QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC
110 120 130 140 150
AKIEARIDEV VSRAEKGLYN EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP
160 170 180 190 200
GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR VIPEGFVNSA VINDYQPGGC
210 220 230 240 250
IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS EPVLSLPVRR
260 270 280 290 300
GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS
310 320 330 340 350
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS
360 370 380 390
VLLPTHRRRG SFSSENYWRK SYESSEDCSE AAGSPARKVK MRRH
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.Curated

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:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiALKBH5.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi120237. 5 interactions.
IntActiQ6P6C2. 1 interaction.
STRINGi9606.ENSP00000382091.

PTM databases

PhosphoSiteiQ6P6C2.

Polymorphism and mutation databases

BioMutaiALKBH5.
DMDMi408359959.

Proteomic databases

MaxQBiQ6P6C2.
PaxDbiQ6P6C2.
PRIDEiQ6P6C2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi54890.
GeneCardsiGC17P018086.
HGNCiHGNC:25996. ALKBH5.
HPAiHPA007196.
MIMi613303. gene.
neXtProtiNX_Q6P6C2.
PharmGKBiPA142671230.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG264303.
GeneTreeiENSGT00390000009298.
HOGENOMiHOG000007505.
HOVERGENiHBG080833.
InParanoidiQ6P6C2.
KOiK10767.
OMAiWVHELVI.
TreeFamiTF329212.

Miscellaneous databases

ChiTaRSiALKBH5. human.
GenomeRNAii54890.
NextBioi57883.
PROiQ6P6C2.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P6C2.
CleanExiHS_ALKBH5.
ExpressionAtlasiQ6P6C2. baseline and differential.
GenevestigatoriQ6P6C2.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-204 AND HIS-266.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "Structures of human ALKBH5 demethylase reveal a unique binding mode for specific single-stranded N6-methyladenosine RNA demethylation."
    Xu C., Liu K., Tempel W., Demetriades M., Aik W., Schofield C.J., Min J.
    J. Biol. Chem. 289:17299-17311(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 74-294 IN COMPLEX WITH ALPHA-KETOGLUTARATE AND MANGANESE, COFACTOR, FUNCTION, SUBUNIT, MUTAGENESIS OF ARG-130; TYR-139 AND GLU-153.
  18. "Crystal structures of the human RNA demethylase Alkbh5 reveal basis for substrate recognition."
    Feng C., Liu Y., Wang G., Deng Z., Zhang Q., Wu W., Tong Y., Cheng C., Chen Z.
    J. Biol. Chem. 289:11571-11583(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 66-292 IN COMPLEX WITH ALPHA-KETOGLUTARATE AND MANGANESE, FUNCTION, COFACTOR, MUTAGENESIS OF ARG-130; LYS-132; TYR-139; TYR-141; TYR-195; HIS-204; 209-HIS-ILE-210; 232-PHE--PHE-234; ARG-277 AND ARG-283.
  19. "Structure of human RNA N?-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation."
    Aik W., Scotti J.S., Choi H., Gong L., Demetriades M., Schofield C.J., McDonough M.A.
    Nucleic Acids Res. 42:4741-4754(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 66-292 IN COMPLEX WITH MANGANESE AND INHIBITOR, FUNCTION, COFACTOR.

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: April 29, 2015
This is version 106 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

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.