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Q9NXW9

- ALKB4_HUMAN

UniProt

Q9NXW9 - ALKB4_HUMAN

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Protein

Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4

Gene
ALKBH4, ABH4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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; catalytic Inferred
Metal bindingi171 – 1711Iron; catalytic Inferred
Metal bindingi254 – 2541Iron; catalytic Inferred
Binding sitei265 – 26512-oxoglutarate Reviewed prediction

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
Complete GO annotation...

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.3 Publications

GO - Cellular componenti

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

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 – 11Removed1 Publication
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. 1 interaction.
IntActiQ9NXW9. 1 interaction.
STRINGi9606.ENSP00000292566.

Structurei

3D structure databases

ProteinModelPortaliQ9NXW9.

Family & Domainsi

Sequence similaritiesi

Belongs to the alkB family.

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

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. VSP_019128
Alternative sequencei43 – 302260Missing in isoform 2. VSP_036841Add
BLAST

Sequence conflict

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

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. 1 interaction.
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

« 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 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: July 9, 2014
This is version 94 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

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