[1]	PROTEIN SEQUENCE. TISSUE=Skeletal muscle; PubMed=183954 [NCBI, ExPASy, EBI, Israel, Japan] von Zabern I., Wittmann-Liebold B., Untucht-Grau R., Schirmer R.H., Pai E.F.; "Primary and tertiary structure of the principal human adenylate kinase."; Eur. J. Biochem. 68:281-290(1976).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TRP-128. PubMed=2542324 [NCBI, ExPASy, EBI, Israel, Japan] Matsuura S., Igarashi M., Tanizawa Y., Yamada M., Kishi F., Kajii T., Fujii H., Miwa S., Sakurai M., Nakazawa A.; "Human adenylate kinase deficiency associated with hemolytic anemia. A single base substitution affecting solubility and catalytic activity of the cytosolic adenylate kinase."; J. Biol. Chem. 264:10148-10155(1989).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Retina; Noma T.; Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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.; "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Colon; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: This small ubiquitous enzyme is essential for maintenance and cell growth.
CATALYTIC ACTIVITY: ATP + AMP = 2 ADP.
SUBUNIT: Monomer.
INTERACTION:
Q8NEZ4:MLL3; NbExp=1; IntAct=EBI-1044943, EBI-1042997;
SUBCELLULAR LOCATION: Cytoplasm.
POLYMORPHISM: This enzyme represents the most common of at least five alleles.
DISEASE: Defects in AK1 are the cause of a form of hemolytic anemia [MIM:103000].
SIMILARITY: Belongs to the adenylate kinase family.
WEB RESOURCE: Name=Wikipedia; Note=Adenylate kinase entry; URL="http://en.wikipedia.org/wiki/Adenylate_kinase";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J04809; AAA51686.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB021871; BAA78534.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019580; AAV38387.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001116; AAH01116.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A33508; KIHUA.

NP_000467.1; -.

3D structure databases

PDB

1Z83; X-ray; 1.90 A; A/B/C=1-193.	[ExPASy / RCSB / EBI]
2C95; X-ray; 1.71 A; A/B=1-193.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1Z83; -.
2C95; -.

ModBase

P00568.

Protein-protein interaction databases

IntAct

P00568; -.

Enzyme and pathway databases

Reactome

REACT_1698; Nucleotide metabolism.

2D gel databases

OGP

P00568; -.

REPRODUCTION-2DPAGE

IPI00018342; -.

Organism-specific databases

HIX0008412; -.

HGNC:361; AK1.

AK1.

CAB009893; -.
HPA006456; -.

MIM

103000; gene+phenotype. [NCBI / EBI]

Orphanet

86817; Haemolytic anaemia due to adenylate kinase deficiency.

PharmGKB

PA134990616; -.

GeneCards

P00568.

Gene expression databases

ArrayExpress

P00568; -.

CleanEx

HS_AK1; -.

GermOnline

ENSG00000106992; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from HPA).
GO:0004017;	Molecular function: adenylate kinase activity (traceable author statement from ProtInc).
GO:0019206;	Molecular function: nucleoside kinase activity (inferred from experiment from Reactome).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR000850; Adenylate_kin.
IPR006267; Adenylate_kin1.
Graphical view of domain structure.

PANTHER

PTHR23359; Adenylate_kin; 1.

Pfam

PF00406; ADK; 1.
Pfam graphical view of domain structure.

PRINTS

PR00094; ADENYLTKNASE.

ProDom

PD000657; Adenylate_kin; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01360; aden_kin_iso1; 1.

PROSITE

PS00113; ADENYLATE_KINASE; 1.

Genome annotation databases

Ensembl

ENSG00000106992; Homo sapiens. [Contig view]

GeneID

203; -.

KEGG

hsa:203; -.

Phylogenomic databases

HOVERGEN

P00568; -.

Other

NextBio

808; -.

SOURCE

AK1; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Disease mutation; Kinase; Nucleotide-binding; Polymorphism; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 194`	`194`	`Adenylate kinase isoenzyme 1.`	`PRO_0000158910`
`NP_BIND`	`15 23`	`9`	`ATP (By similarity).`
`ACT_SITE`	`36 36`
`ACT_SITE`	`93 93`
`MOD_RES`	`1 1`		`N-acetylmethionine.`
`VARIANT`	`123 123`	`1`	`E -> Q (in dbSNP:rs8192462 [NCBI]).`	`VAR_034046 [3D]`
`VARIANT`	`128 128`	`1`	`R -> W (in hemolytic anemia).`	`VAR_004021 [3D]`
`CONFLICT`	`9 9`		`K -> N (in Ref. 5; AAH01116).`
`CONFLICT`	`127 127`		`Q -> R (in Ref. 1; AA sequence).`
`CONFLICT`	`181 181`		`S -> E (in Ref. 1; AA sequence).`
`HELIX`	`1 6`	`6`
`STRAND`	`10 15`	`6`
`HELIX`	`21 32`	`12`
`STRAND`	`35 38`	`4`
`HELIX`	`39 47`	`9`
`TURN`	`48 50`	`3`
`HELIX`	`52 61`	`10`
`TURN`	`62 64`	`3`
`HELIX`	`69 83`	`15`
`HELIX`	`84 86`	`3`
`STRAND`	`90 94`	`5`
`HELIX`	`99 108`	`10`
`STRAND`	`113 119`	`7`
`HELIX`	`122 135`	`14`
`HELIX`	`143 156`	`14`
`HELIX`	`158 165`	`8`
`TURN`	`166 168`	`3`
`STRAND`	`170 174`	`5`
`HELIX`	`179 191`	`13`

Sequence information

Length: 194 AA [This is the length of the unprocessed precursor]

Molecular weight: 21635 Da [This is the MW of the unprocessed precursor]

CRC64: 95EC5AAA92D1F00F [This is a checksum on the sequence]

        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

P00568 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools