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P00568 (KAD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Names and origin

Protein namesRecommended name:
Adenylate kinase isoenzyme 1

Short name=AK 1
EC=2.7.4.3
Alternative name(s):
ATP-AMP transphosphorylase 1
Myokinase
Gene names
Name:AK1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Small ubiquitous enzyme involved in energy metabolism and nucleotide synthesis that is essential for maintenance and cell growth.

Catalytic activity

ATP + AMP = 2 ADP.

Subunit structure

Monomer.

Subcellular location

Cytoplasm.

Polymorphism

This enzyme represents the most common of at least five alleles.

Involvement in disease

Defects in AK1 are the cause of hemolytic anemia due to adenylate kinase deficiency [MIM:612631].

Sequence similarities

Belongs to the adenylate kinase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processATP metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate kinase activity

Traceable author statement. Source: ProtInc

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MLL3Q8NEZ41EBI-1044943,EBI-1042997

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Adenylate kinase isoenzyme 1
PRO_0000158910

Regions

Nucleotide binding15 – 239ATP
Nucleotide binding94 – 1018AMP By similarity

Sites

Binding site391AMP

Amino acid modifications

Modified residue11N-acetylmethionine Ref.1

Natural variations

Natural variant401G → R in hemolytic anemia. Ref.10
VAR_055337
Natural variant641G → R in hemolytic anemia. Ref.10
VAR_055338
Natural variant1231E → Q. [dbSNP:rs8192462]
VAR_034046
Natural variant1281R → W in hemolytic anemia. [dbSNP:rs28930974] Ref.2
VAR_004021
Natural variant1401Missing in hemolytic anemia.
VAR_055339
Natural variant1641Y → C in hemolytic anemia. Ref.9
VAR_055340

Experimental info

Sequence conflict91K → N in AAH01116. Ref.5
Sequence conflict1271Q → R AA sequence Ref.1
Sequence conflict1811S → E AA sequence Ref.1

Secondary structure

................................. 194
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00568-1 [UniParc].

Last modified April 16, 2002. Version 3.
Checksum: 95EC5AAA92D1F00F

FASTA19421,635
        10         20         30         40         50         60 
MEEKLKKTKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRSEVSSG SARGKKLSEI 

        70         80         90        100        110        120 
MEKGQLVPLE TVLDMLRDAM VAKVNTSKGF LIDGYPREVQ QGEEFERRIG QPTLLLYVDA 

       130        140        150        160        170        180 
GPETMTQRLL KRGETSGRVD DNEETIKKRL ETYYKATEPV IAFYEKRGIV RKVNAEGSVD 

       190 
SVFSQVCTHL DALK 

« Hide

References

« Hide 'large scale' references
[1]"Primary and tertiary structure of the principal human adenylate kinase."
von Zabern I., Wittmann-Liebold B., Untucht-Grau R., Schirmer R.H., Pai E.F.
Eur. J. Biochem. 68:281-290(1976) [PubMed: 183954] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Skeletal muscle.
[2]"Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase."
Matsuura S., Igarashi M., Tanizawa Y., Yamada M., Kishi F., Kajii T., Fujii H., Miwa S., Sakurai M., Nakazawa A.
J. Biol. Chem. 264:10148-10155(1989) [PubMed: 2542324] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HEMOLYTIC ANEMIA TRP-128.
[3]Noma T.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
[6]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 10-21; 32-44; 64-77; 89-97; 108-128; 156-166 AND 172-194, MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[7]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Crystal structure of human AK1A in complex with AP5A."
Structural genomics consortium (SGC)
Submitted (MAR-2007) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG.
[9]"Severe erythrocyte adenylate kinase deficiency due to homozygous A-->G substitution at codon 164 of human AK1 gene associated with chronic haemolytic anaemia."
Qualtieri A., Pedace V., Bisconte M.G., Bria M., Gulino B., Andreoli V., Brancati C.
Br. J. Haematol. 99:770-776(1997) [PubMed: 9432020] [Abstract]
Cited for: VARIANT HEMOLYTIC ANEMIA CYS-164.
[10]"Red cell adenylate kinase deficiency: molecular study of 3 new mutations (118G>A, 190G>A, and GAC deletion) associated with hereditary nonspherocytic hemolytic anemia."
Corrons J.-L., Garcia E., Tusell J.J., Varughese K.I., West C., Beutler E.
Blood 102:353-356(2003) [PubMed: 12649162] [Abstract]
Cited for: VARIANTS HEMOLYTIC ANEMIA ARG-40; ARG-64 AND ASP-140 DEL.
+Additional computationally mapped references.

Web resources

Wikipedia

Adenylate kinase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04809 Genomic DNA. Translation: AAA51686.1.
AB021871 mRNA. Translation: BAA78534.1.
BT019580 mRNA. Translation: AAV38387.1.
BC001116 mRNA. Translation: AAH01116.1.
IPIIPI00018342.
PIRKIHUA. A33508.
RefSeqNP_000467.1.
UniGeneHs.175473.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z83X-ray1.90A/B/C1-193[»]
2C95X-ray1.71A/B1-193[»]
ProteinModelPortalP00568.
ModBaseSearch...

Protein-protein interaction databases

IntActP00568. 2 interactions.
STRINGP00568.

2-D gel databases

OGPP00568.
REPRODUCTION-2DPAGEIPI00018342.
UCD-2DPAGEP00568.

Proteomic databases

PRIDEP00568.

Genome annotation databases

EnsemblENST00000373156; ENSP00000362249; ENSG00000106992; Homo sapiens. [Genome view]
ENST00000373176; ENSP00000362271; ENSG00000106992; Homo sapiens. [Genome view]
GeneID203.
KEGGhsa:203.
UCSCuc004bsm.2. human.

Organism-specific databases

CTD203.
GeneCardsGC09M130628.
H-InvDBHIX0008412.
HGNCHGNC:361. AK1.
HPACAB009893.
HPA006456.
MIM103000. gene.
612631. phenotype.
Orphanet86817. Hemolytic anemia due to adenylate kinase deficiency.
PharmGKBPA134990616.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06455.
HOVERGENHBG108060.
OrthoDBEOG96MF3T.
PhylomeDBP00568.

Enzyme and pathway databases

BRENDA2.7.4.3. 247.
ReactomeREACT_1698. Metabolism of nucleotides.

Gene expression databases

ArrayExpressP00568.
BgeeP00568.
CleanExHS_AK1.
GenevestigatorP00568.
GermOnlineENSG00000106992. Homo sapiens.

Family and domain databases

InterProIPR000850. Adenylate_kin.
IPR006267. Adenylate_kin1.
[Graphical view]
PANTHERPTHR23359. Adenylate_kin. 1 hit.
PfamPF00406. ADK. 1 hit.
[Graphical view]
PRINTSPR00094. ADENYLTKNASE.
TIGRFAMsTIGR01360. aden_kin_iso1. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio808.
SOURCESearch...

Entry information

Entry nameKAD1_HUMAN
AccessionPrimary (citable) accession number: P00568
Secondary accession number(s): Q9BVK9, Q9UQC7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 16, 2002
Last modified: August 10, 2010
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families