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Q1L8L9 (KAD2_DANRE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Adenylate kinase 2, mitochondrial

Short name=AK 2
EC=2.7.4.3
Alternative name(s):
ATP-AMP transphosphorylase 2
Gene names
Name:ak2
ORF Names:si:ch211-197n10.1
OrganismDanio rerio (Zebrafish) (Brachydanio rerio)
Taxonomic identifier7955 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeDanio

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. This small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth. Plays a key role in hematopoiesis. Ref.3

Catalytic activity

ATP + AMP = 2 ADP.

Subunit structure

Monomer By similarity.

Subcellular location

Mitochondrion intermembrane space By similarity.

Disruption phenotype

Leads to aberrant leukocyte development. Ref.3

Sequence similarities

Belongs to the adenylate kinase family. AK2 subfamily.

Ontologies

Keywords
   Cellular componentMitochondrion
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processleukocyte differentiation

Inferred from mutant phenotype Ref.3. Source: ZFIN

   Cellular componentmitochondrial intermembrane space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 241241Adenylate kinase 2, mitochondrial
PRO_0000365695

Regions

Nucleotide binding24 – 329ATP By similarity
Nucleotide binding47 – 7630AMP By similarity

Sites

Binding site481AMP By similarity

Amino acid modifications

Disulfide bond44 ↔ 94 By similarity

Experimental info

Sequence conflict931A → S in AAH53160. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q1L8L9 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: D0AA5E0D3F374E4E

FASTA24126,616
        10         20         30         40         50         60 
MAPSTQEDDT VSGIRKGIRA ILLGPPGAGK GTQAPKLAEK YCVCHLATGD MLRAMVASGS 

        70         80         90        100        110        120 
ELGQRLKETM DAGKLVSDEM VVELIDNNLD TPACKNGFLL DGFPRTVKQA EMLDDLMEKR 

       130        140        150        160        170        180 
SEKLDSVIEF SVDDSLLVRR ICGRLIHQPS GRSYHEEFHP PKEHMKDDVT GEPLIRRSDD 

       190        200        210        220        230        240 
NETTLRSRLE SYHRQTSPLV QYYSARGLHT AIDASQSTDL VFASILAAFS AATCKDLVYF 


V 

« Hide

References

« Hide 'large scale' references
[1]The Danio rerio sequencing project at the Sanger Institute
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Tuebingen.
[2]NIH - Zebrafish Gene Collection (ZGC) project
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]"Reticular dysgenesis (aleukocytosis) is caused by mutations in the gene encoding mitochondrial adenylate kinase 2."
Pannicke U., Hoenig M., Hess I., Friesen C., Holzmann K., Rump E.-M., Barth T.F., Rojewski M.T., Schulz A., Boehm T., Friedrich W., Schwarz K.
Nat. Genet. 41:101-105(2009) [PubMed: 19043417] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX957241, CR753876 Genomic DNA. Translation: CAK04357.1.
CR753876, BX957241 Genomic DNA. Translation: CAK11314.1.
BC053160 mRNA. Translation: AAH53160.1.
IPIIPI00505523.
RefSeqNP_997761.1. NM_212596.1.
UniGeneDr.61277.

3D structure databases

ProteinModelPortalQ1L8L9.
SMRQ1L8L9. Positions 17-234.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1L8L9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSDART00000003167; ENSDARP00000010686; ENSDARG00000005926.
GeneID321793.
KEGGdre:321793.
NMPDRfig|7955.3.peg.10554.

Organism-specific databases

CTD204.
ZFINZDB-GENE-030131-512. ak2.

Phylogenomic databases

eggNOGfiNOG13543.
GeneTreeENSGT00600000084421.
HOGENOMHBG630208.
HOVERGENHBG000458.
InParanoidQ1L8L9.
OMAHEEFHPP.
OrthoDBEOG483D5C.
PhylomeDBQ1L8L9.

Gene expression databases

ArrayExpressQ1L8L9.
BgeeQ1L8L9.

Family and domain databases

InterProIPR006259. Adenyl_kin_sub.
IPR000850. Adenylate_kin.
IPR007862. Adenylate_kinase_lid-dom.
[Graphical view]
KOK00939.
PANTHERPTHR23359. Adenylate_kin. 1 hit.
PfamPF00406. ADK. 1 hit.
PF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
TIGRFAMsTIGR01351. Adk. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKAD2_DANRE
AccessionPrimary (citable) accession number: Q1L8L9
Secondary accession number(s): Q7T3D7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 3, 2009
Last sequence update: May 30, 2006
Last modified: November 16, 2011
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families