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Protein

Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4

Gene

Alkbh4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Cofactori

Fe2+By similarityNote: Binds 1 Fe2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi167 – 1671Iron; catalyticBy similarity
Metal bindingi169 – 1691Iron; catalyticBy similarity
Metal bindingi252 – 2521Iron; catalyticBy similarity
Binding sitei263 – 26312-oxoglutarateSequence analysis

GO - Molecular functioni

GO - Biological processi

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1919291. Alkbh4.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Midbody By similarity

  • Note: Associates with the contractile ring and midbody.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic lethality.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 300299Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4PRO_0000239282Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9D8F1.
MaxQBiQ9D8F1.
PaxDbiQ9D8F1.
PRIDEiQ9D8F1.

Expressioni

Gene expression databases

BgeeiQ9D8F1.
CleanExiMM_ALKBH4.
ExpressionAtlasiQ9D8F1. baseline and differential.
GenevisibleiQ9D8F1. MM.

Interactioni

Subunit structurei

Interacts with ZFHX3, MLLT3, MLLT1, HSF4, EP300, TES, EIF3C, MTMR6 and PSMA6.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000098134.

Structurei

3D structure databases

ProteinModelPortaliQ9D8F1.
SMRiQ9D8F1. Positions 68-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the alkB family.Curated

Phylogenomic databases

eggNOGiKOG3959. Eukaryota.
ENOG4111IQR. LUCA.
GeneTreeiENSGT00390000006344.
HOGENOMiHOG000015835.
HOVERGENiHBG062006.
InParanoidiQ9D8F1.
KOiK10766.
OMAiDRDPWKL.
PhylomeDBiQ9D8F1.
TreeFamiTF314885.

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
InterProiIPR027450. AlkB-like.
IPR032857. ALKBH4.
[Graphical view]
PANTHERiPTHR12463. PTHR12463. 1 hit.

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. AlignAdd to basket

Isoform 1 (identifier: Q9D8F1-1) [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
MAAAAEVSLL QECGCKGIRT CLICERQRHR DPPWQICLQK KCCFLYCPDT
60 70 80 90 100
GWAAGAEGSD LEGWAFPFPG VTLIQDFVTP EEEAEMVRLM DCDPWKLSQS
110 120 130 140 150
GRKKQDYGPK VNFRKQKLKM AGFQGLPGFS QKVVQRMGLY PGLEDFQPVE
160 170 180 190 200
QCNLDYSPER GSAIDPHLDD AWLWGERLVS LNLLSATVVS MSPEAPGSLL
210 220 230 240 250
LCSAPSVRPD AFEDSLVAPS RSVPCQEVEV AITVPRRSLL VLTGAARHQW
260 270 280 290 300
THAIHRRHIK ARRVCATFRE LSSEFLPGGK QQELGQELLQ AALSFQGRPV
Length:300
Mass (Da):33,394
Last modified:June 1, 2001 - v1
Checksum:iC19FBBB89095B6ED
GO
Isoform 2 (identifier: Q9D8F1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: Missing.

Note: No experimental confirmation available.
Show »
Length:215
Mass (Da):23,976
Checksum:i1345834B207D258E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8585Missing in isoform 2. 1 PublicationVSP_019129Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008083 mRNA. Translation: BAB25449.1.
GL456122 Genomic DNA. No translation available.
BC022729 mRNA. Translation: AAH22729.1.
CCDSiCCDS19753.1. [Q9D8F1-2]
RefSeqiNP_082346.1. NM_028070.1. [Q9D8F1-2]
XP_006504565.1. XM_006504502.2. [Q9D8F1-1]
XP_006504566.1. XM_006504503.2. [Q9D8F1-2]
XP_006504567.1. XM_006504504.2. [Q9D8F1-2]
XP_006504568.1. XM_006504505.2. [Q9D8F1-2]
UniGeneiMm.486605.

Genome annotation databases

EnsembliENSMUST00000041100; ENSMUSP00000040403; ENSMUSG00000039754. [Q9D8F1-1]
ENSMUST00000100568; ENSMUSP00000098134; ENSMUSG00000039754. [Q9D8F1-2]
GeneIDi72041.
KEGGimmu:72041.
UCSCiuc009aaa.1. mouse. [Q9D8F1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008083 mRNA. Translation: BAB25449.1.
GL456122 Genomic DNA. No translation available.
BC022729 mRNA. Translation: AAH22729.1.
CCDSiCCDS19753.1. [Q9D8F1-2]
RefSeqiNP_082346.1. NM_028070.1. [Q9D8F1-2]
XP_006504565.1. XM_006504502.2. [Q9D8F1-1]
XP_006504566.1. XM_006504503.2. [Q9D8F1-2]
XP_006504567.1. XM_006504504.2. [Q9D8F1-2]
XP_006504568.1. XM_006504505.2. [Q9D8F1-2]
UniGeneiMm.486605.

3D structure databases

ProteinModelPortaliQ9D8F1.
SMRiQ9D8F1. Positions 68-273.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000098134.

Proteomic databases

EPDiQ9D8F1.
MaxQBiQ9D8F1.
PaxDbiQ9D8F1.
PRIDEiQ9D8F1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041100; ENSMUSP00000040403; ENSMUSG00000039754. [Q9D8F1-1]
ENSMUST00000100568; ENSMUSP00000098134; ENSMUSG00000039754. [Q9D8F1-2]
GeneIDi72041.
KEGGimmu:72041.
UCSCiuc009aaa.1. mouse. [Q9D8F1-1]

Organism-specific databases

CTDi54784.
MGIiMGI:1919291. Alkbh4.

Phylogenomic databases

eggNOGiKOG3959. Eukaryota.
ENOG4111IQR. LUCA.
GeneTreeiENSGT00390000006344.
HOGENOMiHOG000015835.
HOVERGENiHBG062006.
InParanoidiQ9D8F1.
KOiK10766.
OMAiDRDPWKL.
PhylomeDBiQ9D8F1.
TreeFamiTF314885.

Miscellaneous databases

NextBioi335284.
PROiQ9D8F1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D8F1.
CleanExiMM_ALKBH4.
ExpressionAtlasiQ9D8F1. baseline and differential.
GenevisibleiQ9D8F1. MM.

Family and domain databases

Gene3Di2.60.120.590. 1 hit.
InterProiIPR027450. AlkB-like.
IPR032857. ALKBH4.
[Graphical view]
PANTHERiPTHR12463. PTHR12463. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Small intestine.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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: Eye.
  4. Cited for: DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiALKB4_MOUSE
AccessioniPrimary (citable) accession number: Q9D8F1
Secondary accession number(s): Q8R1Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: June 1, 2001
Last modified: March 16, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.