Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00568

- KAD1_HUMAN

UniProt

P00568 - KAD1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Adenylate kinase isoenzyme 1

Gene

AK1

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

Functioni

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.1 PublicationUniRule annotation

Catalytic activityi

ATP + AMP = 2 ADP.1 PublicationUniRule annotation
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.1 PublicationUniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391AMP
Binding sitei44 – 441AMP
Binding sitei101 – 1011AMP
Binding sitei132 – 1321ATP
Binding sitei138 – 1381AMP
Binding sitei149 – 1491AMP
Binding sitei177 – 1771ATP; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 236ATP
Nucleotide bindingi65 – 673AMP
Nucleotide bindingi94 – 974AMP

GO - Molecular functioni

  1. adenylate kinase activity Source: ProtInc
  2. ATP binding Source: UniProtKB-KW
  3. nucleoside diphosphate kinase activity Source: UniProtKB

GO - Biological processi

  1. ADP biosynthetic process Source: UniProtKB-HAMAP
  2. AMP metabolic process Source: UniProtKB-HAMAP
  3. ATP metabolic process Source: UniProtKB-HAMAP
  4. cell cycle arrest Source: Ensembl
  5. nucleobase-containing small molecule interconversion Source: Reactome
  6. nucleobase-containing small molecule metabolic process Source: Reactome
  7. nucleoside diphosphate phosphorylation Source: UniProtKB
  8. nucleoside triphosphate biosynthetic process Source: UniProtKB
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.4.3. 2681.
ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKP00568.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinase isoenzyme 1UniRule annotation (EC:2.7.4.3UniRule annotation, EC:2.7.4.6UniRule annotation)
Short name:
AK 1UniRule annotation
Alternative name(s):
ATP-AMP transphosphorylase 1UniRule annotation
ATP:AMP phosphotransferaseUniRule annotation
Adenylate monophosphate kinaseUniRule annotation
MyokinaseUniRule annotation
Gene namesi
Name:AK1UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:361. AK1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. outer dense fiber Source: Ensembl
  5. plasma membrane Source: Ensembl
  6. sperm flagellum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Hemolytic anemia due to adenylate kinase deficiency (HAAKD) [MIM:612631]: A disease characterized by hemolytic anemia and undetectable erythrocyte adenylate kinase activity.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401G → R in HAAKD. 1 Publication
VAR_055337
Natural varianti64 – 641G → R in HAAKD. 1 Publication
VAR_055338
Natural varianti128 – 1281R → W in HAAKD. 1 Publication
Corresponds to variant rs28930974 [ dbSNP | Ensembl ].
VAR_004021
Natural varianti140 – 1401Missing in HAAKD. 1 Publication
VAR_055339
Natural varianti164 – 1641Y → C in HAAKD. 1 Publication
VAR_055340

Keywords - Diseasei

Disease mutation, Hereditary hemolytic anemia

Organism-specific databases

MIMi612631. phenotype.
Orphaneti86817. Hemolytic anemia due to adenylate kinase deficiency.
PharmGKBiPA24655.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194Adenylate kinase isoenzyme 1PRO_0000158910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 PublicationUniRule annotation

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP00568.
PaxDbiP00568.
PRIDEiP00568.

2D gel databases

OGPiP00568.
REPRODUCTION-2DPAGEIPI00018342.
UCD-2DPAGEP00568.

PTM databases

PhosphoSiteiP00568.

Expressioni

Gene expression databases

BgeeiP00568.
CleanExiHS_AK1.
ExpressionAtlasiP00568. baseline and differential.
GenevestigatoriP00568.

Organism-specific databases

HPAiCAB009893.
HPA006456.

Interactioni

Subunit structurei

Monomer.2 PublicationsUniRule annotation

Protein-protein interaction databases

BioGridi106706. 9 interactions.
IntActiP00568. 1 interaction.
STRINGi9606.ENSP00000362249.

Structurei

Secondary structure

194
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1 – 55Combined sources
Beta strandi10 – 156Combined sources
Helixi21 – 3212Combined sources
Beta strandi35 – 384Combined sources
Helixi39 – 4810Combined sources
Helixi52 – 6211Combined sources
Helixi69 – 8315Combined sources
Turni84 – 863Combined sources
Beta strandi90 – 945Combined sources
Helixi99 – 10810Combined sources
Beta strandi113 – 1197Combined sources
Helixi122 – 13312Combined sources
Beta strandi135 – 1373Combined sources
Helixi139 – 1413Combined sources
Helixi143 – 15614Combined sources
Helixi158 – 16710Combined sources
Beta strandi170 – 1745Combined sources
Helixi179 – 19315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z83X-ray1.90A/B/C1-193[»]
2C95X-ray1.71A/B1-193[»]
ProteinModelPortaliP00568.
SMRiP00568. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00568.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 6730NMPbindAdd
BLAST
Regioni131 – 14111LIDAdd
BLAST

Domaini

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.

Sequence similaritiesi

Belongs to the adenylate kinase family. AK1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0563.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
InParanoidiP00568.
KOiK00939.
OrthoDBiEOG7060S3.
PhylomeDBiP00568.
TreeFamiTF354283.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03171. Adenylate_kinase_AK1.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR028582. AK1.
IPR006267. AK1/5.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01360. aden_kin_iso1. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00568-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEEKLKKTKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRSEVSSG
60 70 80 90 100
SARGKKLSEI MEKGQLVPLE TVLDMLRDAM VAKVNTSKGF LIDGYPREVQ
110 120 130 140 150
QGEEFERRIG QPTLLLYVDA GPETMTQRLL KRGETSGRVD DNEETIKKRL
160 170 180 190
ETYYKATEPV IAFYEKRGIV RKVNAEGSVD SVFSQVCTHL DALK
Length:194
Mass (Da):21,635
Last modified:April 16, 2002 - v3
Checksum:i95EC5AAA92D1F00F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91K → N in AAH01116. (PubMed:15489334)Curated
Sequence conflicti127 – 1271Q → R AA sequence (PubMed:183954)Curated
Sequence conflicti181 – 1811S → E AA sequence (PubMed:183954)Curated

Polymorphismi

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401G → R in HAAKD. 1 Publication
VAR_055337
Natural varianti64 – 641G → R in HAAKD. 1 Publication
VAR_055338
Natural varianti123 – 1231E → Q.
Corresponds to variant rs8192462 [ dbSNP | Ensembl ].
VAR_034046
Natural varianti128 – 1281R → W in HAAKD. 1 Publication
Corresponds to variant rs28930974 [ dbSNP | Ensembl ].
VAR_004021
Natural varianti140 – 1401Missing in HAAKD. 1 Publication
VAR_055339
Natural varianti164 – 1641Y → C in HAAKD. 1 Publication
VAR_055340

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04809 Genomic DNA. Translation: AAA51686.1.
AB021871 mRNA. Translation: BAA78534.1.
BT019580 mRNA. Translation: AAV38387.1.
BC001116 mRNA. Translation: AAH01116.1.
CCDSiCCDS6881.1.
PIRiA33508. KIHUA.
RefSeqiNP_000467.1. NM_000476.2.
UniGeneiHs.175473.

Genome annotation databases

EnsembliENST00000373156; ENSP00000362249; ENSG00000106992.
ENST00000373176; ENSP00000362271; ENSG00000106992.
GeneIDi203.
KEGGihsa:203.
UCSCiuc004bsm.4. human.

Polymorphism databases

DMDMi20178288.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Adenylate kinase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04809 Genomic DNA. Translation: AAA51686.1 .
AB021871 mRNA. Translation: BAA78534.1 .
BT019580 mRNA. Translation: AAV38387.1 .
BC001116 mRNA. Translation: AAH01116.1 .
CCDSi CCDS6881.1.
PIRi A33508. KIHUA.
RefSeqi NP_000467.1. NM_000476.2.
UniGenei Hs.175473.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Z83 X-ray 1.90 A/B/C 1-193 [» ]
2C95 X-ray 1.71 A/B 1-193 [» ]
ProteinModelPortali P00568.
SMRi P00568. Positions 1-193.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106706. 9 interactions.
IntActi P00568. 1 interaction.
STRINGi 9606.ENSP00000362249.

PTM databases

PhosphoSitei P00568.

Polymorphism databases

DMDMi 20178288.

2D gel databases

OGPi P00568.
REPRODUCTION-2DPAGE IPI00018342.
UCD-2DPAGE P00568.

Proteomic databases

MaxQBi P00568.
PaxDbi P00568.
PRIDEi P00568.

Protocols and materials databases

DNASUi 203.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373156 ; ENSP00000362249 ; ENSG00000106992 .
ENST00000373176 ; ENSP00000362271 ; ENSG00000106992 .
GeneIDi 203.
KEGGi hsa:203.
UCSCi uc004bsm.4. human.

Organism-specific databases

CTDi 203.
GeneCardsi GC09M130628.
HGNCi HGNC:361. AK1.
HPAi CAB009893.
HPA006456.
MIMi 103000. gene.
612631. phenotype.
neXtProti NX_P00568.
Orphaneti 86817. Hemolytic anemia due to adenylate kinase deficiency.
PharmGKBi PA24655.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0563.
HOGENOMi HOG000238771.
HOVERGENi HBG108060.
InParanoidi P00568.
KOi K00939.
OrthoDBi EOG7060S3.
PhylomeDBi P00568.
TreeFami TF354283.

Enzyme and pathway databases

BRENDAi 2.7.4.3. 2681.
Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RK P00568.

Miscellaneous databases

EvolutionaryTracei P00568.
GenomeRNAii 203.
NextBioi 808.
PROi P00568.
SOURCEi Search...

Gene expression databases

Bgeei P00568.
CleanExi HS_AK1.
ExpressionAtlasi P00568. baseline and differential.
Genevestigatori P00568.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00235. Adenylate_kinase_Adk.
MF_03171. Adenylate_kinase_AK1.
InterProi IPR000850. Adenylat/UMP-CMP_kin.
IPR028582. AK1.
IPR006267. AK1/5.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR23359. PTHR23359. 1 hit.
PRINTSi PR00094. ADENYLTKNASE.
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01360. aden_kin_iso1. 1 hit.
PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, ACETYLATION AT MET-1.
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HAAKD 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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "The human adenylate kinase 9 is a nucleoside mono- and diphosphate kinase."
    Amiri M., Conserva F., Panayiotou C., Karlsson A., Solaroli N.
    Int. J. Biochem. Cell Biol. 45:925-931(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  9. "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 BI-SUBSTRATE ANALOG AP5A.
  10. "Structure of adenylate kinase 1 in complex with P1, P4-di(adenosine)tetraphosphate."
    Structural genomics consortium (SGC)
    Submitted (DEC-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG AP4A.
  11. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT HAAKD CYS-164.
  12. "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] [Europe PMC] [Abstract]
    Cited for: VARIANTS HAAKD ARG-40; ARG-64 AND ASP-140 DEL.

Entry informationi

Entry nameiKAD1_HUMAN
AccessioniPrimary (citable) accession number: P00568
Secondary accession number(s): Q9BVK9, Q9UQC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 16, 2002
Last modified: November 26, 2014
This is version 162 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3