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Q9Y6K8 (KAD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenylate kinase isoenzyme 5

Short name=AK 5
EC=2.7.4.3
EC=2.7.4.6
Alternative name(s):
ATP-AMP transphosphorylase 5
Gene names
Name:AK5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length562 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. Also displays broad nucleoside diphosphate kinase activity. Ref.6 Ref.7

Catalytic activity

ATP + AMP = 2 ADP. Ref.6 Ref.7

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. Ref.6 Ref.7

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00235

Subcellular location

Cytoplasm Ref.6.

Tissue specificity

Brain specific.

Sequence similarities

Belongs to the adenylate kinase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processADP biosynthetic process

Traceable author statement Ref.1. Source: ProtInc

ATP metabolic process

Inferred from electronic annotation. Source: InterPro

dADP biosynthetic process

Traceable author statement Ref.1. Source: ProtInc

nucleobase-containing small molecule interconversion

Traceable author statement. Source: Reactome

nucleobase-containing small molecule metabolic process

Traceable author statement. Source: Reactome

nucleoside diphosphate phosphorylation

Inferred from direct assay Ref.7. Source: UniProtKB

nucleoside triphosphate biosynthetic process

Inferred from direct assay Ref.7. Source: UniProtKB

pyrimidine ribonucleotide biosynthetic process

Traceable author statement Ref.1. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

microtubule organizing center

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

adenylate kinase activity

Traceable author statement Ref.1. Source: ProtInc

nucleoside diphosphate kinase activity

Inferred from direct assay Ref.7. Source: UniProtKB

nucleoside kinase activity

Inferred from experiment. Source: Reactome

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y6K8-1)

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.
Isoform 2 (identifier: Q9Y6K8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-365: Missing.
Note: It is unsure whether Met-1 or Met-5 is the initiator.
Isoform 3 (identifier: Q9Y6K8-3)

Also known as: Adenylate kinase 6;

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 562562Adenylate kinase isoenzyme 5 HAMAP-Rule MF_00235
PRO_0000158930

Regions

Nucleotide binding142 – 1476ATP 1 By similarity
Nucleotide binding191 – 1933AMP 1 By similarity
Nucleotide binding219 – 2224AMP 1 By similarity
Nucleotide binding386 – 3916ATP 2 By similarity
Nucleotide binding433 – 4353AMP 2 By similarity
Nucleotide binding462 – 4654AMP 2 By similarity
Region133 – 316184Adenylate kinase 1 HAMAP-Rule MF_00235
Region162 – 19332NMPbind 1 By similarity
Region256 – 26611LID 1 By similarity
Region377 – 559183Adenylate kinase 2 HAMAP-Rule MF_00235
Region406 – 43530NMPbind 2 By similarity
Region499 – 50911LID 2 By similarity

Sites

Binding site1681AMP 1 By similarity
Binding site2261AMP 1 By similarity
Binding site2571ATP 1 By similarity
Binding site2631AMP 1 By similarity
Binding site2741AMP 1 By similarity
Binding site4071AMP 2 By similarity
Binding site4121AMP 2 By similarity
Binding site4691AMP 2 By similarity
Binding site5001ATP 2 By similarity
Binding site5171AMP 2 By similarity
Binding site5451ATP 2; via carbonyl oxygen By similarity

Natural variations

Alternative sequence1 – 365365Missing in isoform 2.
VSP_037878
Alternative sequence1 – 2626Missing in isoform 3.
VSP_037879
Natural variant4651R → Q.
Corresponds to variant rs2803140 [ dbSNP | Ensembl ].
VAR_059435

Experimental info

Sequence conflict101L → M in AAH36666. Ref.5
Sequence conflict861E → G in AAH36666. Ref.5
Sequence conflict1821L → P in AAO16520. Ref.2
Sequence conflict1821L → P in AAH33896. Ref.5
Sequence conflict3211P → S in AAO16520. Ref.2
Sequence conflict3431I → T in AAO16520. Ref.2
Sequence conflict3481S → Y in AAH33896. Ref.5
Sequence conflict3851P → T in AAH33896. Ref.5
Sequence conflict5611Missing in AAP97322. Ref.2
Sequence conflict5611Missing in AAH33896. Ref.5
Sequence conflict5611Missing in AAH12467. Ref.5

Secondary structure

........................... 562
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 1, 2009. Version 2.
Checksum: CF7DB084924A782F

FASTA56263,333
        10         20         30         40         50         60 
MNTNDAKEYL ARREIPQLFE SLLNGLMCSK PEDPVEYLES CLQKVKELGG CDKVKWDTFV 

        70         80         90        100        110        120 
SQEKKTLPPL NGGQSRRSFL RNVMPENSNF PYRRYDRLPP IHQFSIESDT DLSETAELIE 

       130        140        150        160        170        180 
EYEVFDPTRP RPKIILVIGG PGSGKGTQSL KIAERYGFQY ISVGELLRKK IHSTSSNRKW 

       190        200        210        220        230        240 
SLIAKIITTG ELAPQETTIT EIKQKLMQIP DEEGIVIDGF PRDVAQALSF EDQICTPDLV 

       250        260        270        280        290        300 
VFLACANQRL KERLLKRAEQ QGRPDDNVKA TQRRLMNFKQ NAAPLVKYFQ EKGLIMTFDA 

       310        320        330        340        350        360 
DRDEDEVFYD ISMAVDNKLF PNKEAAAGSS DLDPSMILDT GEIIDTGSDY EDQGDDQLNV 

       370        380        390        400        410        420 
FGEDTMGGFM EDLRKCKIIF IIGGPGSGKG TQCEKLVEKY GFTHLSTGEL LREELASESE 

       430        440        450        460        470        480 
RSKLIRDIME RGDLVPSGIV LELLKEAMVA SLGDTRGFLI DGYPREVKQG EEFGRRIGDP 

       490        500        510        520        530        540 
QLVICMDCSA DTMTNRLLQR SRSSLPVDDT TKTIAKRLEA YYRASIPVIA YYETKTQLHK 

       550        560 
INAEGTPEDV FLQLCTAIDS IF 

« Hide

Isoform 2 [UniParc].

Checksum: B63514CB7C3B58AF
Show »

FASTA19721,974
Isoform 3 (Adenylate kinase 6) [UniParc].

Checksum: D263FD0BABB4B82A
Show »

FASTA53660,315

References

« Hide 'large scale' references
[1]"Identification of a novel human adenylate kinase. cDNA cloning, expression analysis, chromosome localization and characterization of the recombinant protein."
Van Rompay A.R., Johansson M., Karlsson A.
Eur. J. Biochem. 261:509-517(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Cloning and characterization of a novel human gene, adenylate kinase 6."
Li J., Ji C., Xie Y., Mao Y.
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]Guo J.H., Yu L., Li D.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[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] (ISOFORMS 1; 2 AND 3).
Tissue: Brain and Liver.
[6]"Identification of two active functional domains of human adenylate kinase 5."
Solaroli N., Panayiotou C., Johansson M., Karlsson A.
FEBS Lett. 583:2872-2876(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
[7]"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.
[8]"Crystal structure of adenylate kinase 5."
Structural genomics consortium (SGC)
Submitted (JUL-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 366-562 IN COMPLEX WITH AMP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF062595 mRNA. Translation: AAD27956.1.
AY171600 mRNA. Translation: AAO16520.2.
AF445193 mRNA. Translation: AAP97322.1.
CR541890 mRNA. Translation: CAG46688.1.
BC033896 mRNA. Translation: AAH33896.1.
BC036666 mRNA. Translation: AAH36666.1.
BC012467 mRNA. Translation: AAH12467.2.
CCDSCCDS675.1. [Q9Y6K8-1]
CCDS676.1. [Q9Y6K8-3]
RefSeqNP_036225.2. NM_012093.3. [Q9Y6K8-3]
NP_777283.1. NM_174858.2. [Q9Y6K8-1]
XP_006710635.1. XM_006710572.1. [Q9Y6K8-3]
UniGeneHs.559718.
Hs.597002.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BWJX-ray2.30A/B/C/D/E/F366-562[»]
ProteinModelPortalQ9Y6K8.
SMRQ9Y6K8. Positions 133-317, 368-562.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117670. 9 interactions.
IntActQ9Y6K8. 8 interactions.
STRING9606.ENSP00000346577.

PTM databases

PhosphoSiteQ9Y6K8.

Polymorphism databases

DMDM257051028.

Proteomic databases

MaxQBQ9Y6K8.
PaxDbQ9Y6K8.
PRIDEQ9Y6K8.

Protocols and materials databases

DNASU26289.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000344720; ENSP00000341430; ENSG00000154027. [Q9Y6K8-3]
ENST00000354567; ENSP00000346577; ENSG00000154027. [Q9Y6K8-1]
GeneID26289.
KEGGhsa:26289.
UCSCuc001dhn.3. human. [Q9Y6K8-1]

Organism-specific databases

CTD26289.
GeneCardsGC01P077747.
H-InvDBHIX0020812.
HGNCHGNC:365. AK5.
HPAHPA019128.
HPA057255.
MIM608009. gene.
neXtProtNX_Q9Y6K8.
PharmGKBPA24659.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0563.
HOVERGENHBG059001.
InParanoidQ9Y6K8.
KOK00939.
OMAVFGEDTM.
OrthoDBEOG7060S3.
PhylomeDBQ9Y6K8.
TreeFamTF313747.

Enzyme and pathway databases

BioCycMetaCyc:HS07943-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9Y6K8.
BgeeQ9Y6K8.
CleanExHS_AK5.
GenevestigatorQ9Y6K8.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
HAMAPMF_00235. Adenylate_kinase_Adk. 2 domains.
InterProIPR000850. Adenylat/UMP-CMP_kin.
IPR006267. AK1/5.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PRINTSPR00094. ADENYLTKNASE.
SUPFAMSSF47391. SSF47391. 1 hit.
SSF52540. SSF52540. 2 hits.
TIGRFAMsTIGR01360. aden_kin_iso1. 1 hit.
PROSITEPS00113. ADENYLATE_KINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y6K8.
GenomeRNAi26289.
NextBio48625.
PROQ9Y6K8.
SOURCESearch...

Entry information

Entry nameKAD5_HUMAN
AccessionPrimary (citable) accession number: Q9Y6K8
Secondary accession number(s): Q5U622 expand/collapse secondary AC list , Q6FH66, Q7Z4T5, Q86YS0, Q8N464, Q96EC9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: September 1, 2009
Last modified: July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM