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Q9Y6K8

- KAD5_HUMAN

UniProt

Q9Y6K8 - KAD5_HUMAN

Protein

Adenylate kinase isoenzyme 5

Gene

AK5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (01 Sep 2009)
      Previous versions | rss
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    Functioni

    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.2 Publications

    Catalytic activityi

    ATP + AMP = 2 ADP.
    ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei168 – 1681AMP 1By similarity
    Binding sitei226 – 2261AMP 1By similarity
    Binding sitei257 – 2571ATP 1By similarity
    Binding sitei263 – 2631AMP 1By similarity
    Binding sitei274 – 2741AMP 1By similarity
    Binding sitei407 – 4071AMP 2By similarity
    Binding sitei412 – 4121AMP 2By similarity
    Binding sitei469 – 4691AMP 2By similarity
    Binding sitei500 – 5001ATP 2By similarity
    Binding sitei517 – 5171AMP 2By similarity
    Binding sitei545 – 5451ATP 2; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi142 – 1476ATP 1By similarity
    Nucleotide bindingi191 – 1933AMP 1By similarity
    Nucleotide bindingi219 – 2224AMP 1By similarity
    Nucleotide bindingi386 – 3916ATP 2By similarity
    Nucleotide bindingi433 – 4353AMP 2By similarity
    Nucleotide bindingi462 – 4654AMP 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. ADP biosynthetic process Source: ProtInc
    2. ATP metabolic process Source: InterPro
    3. dADP biosynthetic process Source: ProtInc
    4. nucleobase-containing small molecule interconversion Source: Reactome
    5. nucleobase-containing small molecule metabolic process Source: Reactome
    6. nucleoside diphosphate phosphorylation Source: UniProtKB
    7. nucleoside triphosphate biosynthetic process Source: UniProtKB
    8. pyrimidine ribonucleotide biosynthetic process Source: ProtInc
    9. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07943-MONOMER.
    ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylate kinase isoenzyme 5 (EC:2.7.4.3, EC:2.7.4.6)
    Short name:
    AK 5
    Alternative name(s):
    ATP-AMP transphosphorylase 5
    Gene namesi
    Name:AK5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:365. AK5.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. microtubule organizing center Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24659.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 562562Adenylate kinase isoenzyme 5PRO_0000158930Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y6K8.
    PaxDbiQ9Y6K8.
    PRIDEiQ9Y6K8.

    PTM databases

    PhosphoSiteiQ9Y6K8.

    Expressioni

    Tissue specificityi

    Brain specific.

    Gene expression databases

    ArrayExpressiQ9Y6K8.
    BgeeiQ9Y6K8.
    CleanExiHS_AK5.
    GenevestigatoriQ9Y6K8.

    Organism-specific databases

    HPAiHPA019128.
    HPA057255.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi117670. 8 interactions.
    IntActiQ9Y6K8. 8 interactions.
    STRINGi9606.ENSP00000346577.

    Structurei

    Secondary structure

    1
    562
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi369 – 3757
    Beta strandi378 – 3836
    Helixi389 – 40012
    Beta strandi403 – 4064
    Helixi407 – 41711
    Helixi420 – 43011
    Helixi437 – 45115
    Beta strandi458 – 4614
    Helixi467 – 47610
    Beta strandi481 – 4877
    Helixi490 – 49910
    Helixi507 – 53529
    Beta strandi536 – 5427
    Helixi547 – 56115

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BWJX-ray2.30A/B/C/D/E/F366-562[»]
    ProteinModelPortaliQ9Y6K8.
    SMRiQ9Y6K8. Positions 133-317, 368-562.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y6K8.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni133 – 316184Adenylate kinase 1Add
    BLAST
    Regioni162 – 19332NMPbind 1By similarityAdd
    BLAST
    Regioni256 – 26611LID 1By similarityAdd
    BLAST
    Regioni377 – 559183Adenylate kinase 2Add
    BLAST
    Regioni406 – 43530NMPbind 2By similarityAdd
    BLAST
    Regioni499 – 50911LID 2By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the adenylate kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0563.
    HOVERGENiHBG059001.
    InParanoidiQ9Y6K8.
    KOiK00939.
    OMAiVFGEDTM.
    OrthoDBiEOG7060S3.
    PhylomeDBiQ9Y6K8.
    TreeFamiTF313747.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    HAMAPiMF_00235. Adenylate_kinase_Adk. 2 domains.
    InterProiIPR000850. Adenylat/UMP-CMP_kin.
    IPR006267. AK1/5.
    IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR23359. PTHR23359. 1 hit.
    PRINTSiPR00094. ADENYLTKNASE.
    SUPFAMiSSF47391. SSF47391. 1 hit.
    SSF52540. SSF52540. 2 hits.
    TIGRFAMsiTIGR01360. aden_kin_iso1. 1 hit.
    PROSITEiPS00113. ADENYLATE_KINASE. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y6K8-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MNTNDAKEYL ARREIPQLFE SLLNGLMCSK PEDPVEYLES CLQKVKELGG    50
    CDKVKWDTFV SQEKKTLPPL NGGQSRRSFL RNVMPENSNF PYRRYDRLPP 100
    IHQFSIESDT DLSETAELIE EYEVFDPTRP RPKIILVIGG PGSGKGTQSL 150
    KIAERYGFQY ISVGELLRKK IHSTSSNRKW SLIAKIITTG ELAPQETTIT 200
    EIKQKLMQIP DEEGIVIDGF PRDVAQALSF EDQICTPDLV VFLACANQRL 250
    KERLLKRAEQ QGRPDDNVKA TQRRLMNFKQ NAAPLVKYFQ EKGLIMTFDA 300
    DRDEDEVFYD ISMAVDNKLF PNKEAAAGSS DLDPSMILDT GEIIDTGSDY 350
    EDQGDDQLNV FGEDTMGGFM EDLRKCKIIF IIGGPGSGKG TQCEKLVEKY 400
    GFTHLSTGEL LREELASESE RSKLIRDIME RGDLVPSGIV LELLKEAMVA 450
    SLGDTRGFLI DGYPREVKQG EEFGRRIGDP QLVICMDCSA DTMTNRLLQR 500
    SRSSLPVDDT TKTIAKRLEA YYRASIPVIA YYETKTQLHK INAEGTPEDV 550
    FLQLCTAIDS IF 562
    Length:562
    Mass (Da):63,333
    Last modified:September 1, 2009 - v2
    Checksum:iCF7DB084924A782F
    GO
    Isoform 2 (identifier: Q9Y6K8-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:197
    Mass (Da):21,974
    Checksum:iB63514CB7C3B58AF
    GO
    Isoform 3 (identifier: Q9Y6K8-3) [UniParc]FASTAAdd to Basket

    Also known as: Adenylate kinase 6

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

    Show »
    Length:536
    Mass (Da):60,315
    Checksum:iD263FD0BABB4B82A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101L → M in AAH36666. (PubMed:15489334)Curated
    Sequence conflicti86 – 861E → G in AAH36666. (PubMed:15489334)Curated
    Sequence conflicti182 – 1821L → P in AAO16520. 1 PublicationCurated
    Sequence conflicti182 – 1821L → P in AAH33896. (PubMed:15489334)Curated
    Sequence conflicti321 – 3211P → S in AAO16520. 1 PublicationCurated
    Sequence conflicti343 – 3431I → T in AAO16520. 1 PublicationCurated
    Sequence conflicti348 – 3481S → Y in AAH33896. (PubMed:15489334)Curated
    Sequence conflicti385 – 3851P → T in AAH33896. (PubMed:15489334)Curated
    Sequence conflicti561 – 5611Missing in AAP97322. 1 PublicationCurated
    Sequence conflicti561 – 5611Missing in AAH33896. (PubMed:15489334)Curated
    Sequence conflicti561 – 5611Missing in AAH12467. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti465 – 4651R → Q.
    Corresponds to variant rs2803140 [ dbSNP | Ensembl ].
    VAR_059435

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 365365Missing in isoform 2. 3 PublicationsVSP_037878Add
    BLAST
    Alternative sequencei1 – 2626Missing in isoform 3. 2 PublicationsVSP_037879Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS675.1. [Q9Y6K8-1]
    CCDS676.1. [Q9Y6K8-3]
    RefSeqiNP_036225.2. NM_012093.3. [Q9Y6K8-3]
    NP_777283.1. NM_174858.2. [Q9Y6K8-1]
    XP_006710635.1. XM_006710572.1. [Q9Y6K8-3]
    UniGeneiHs.559718.
    Hs.597002.

    Genome annotation databases

    EnsembliENST00000344720; ENSP00000341430; ENSG00000154027. [Q9Y6K8-3]
    ENST00000354567; ENSP00000346577; ENSG00000154027. [Q9Y6K8-1]
    GeneIDi26289.
    KEGGihsa:26289.
    UCSCiuc001dhn.3. human. [Q9Y6K8-1]

    Polymorphism databases

    DMDMi257051028.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS675.1. [Q9Y6K8-1 ]
    CCDS676.1. [Q9Y6K8-3 ]
    RefSeqi NP_036225.2. NM_012093.3. [Q9Y6K8-3 ]
    NP_777283.1. NM_174858.2. [Q9Y6K8-1 ]
    XP_006710635.1. XM_006710572.1. [Q9Y6K8-3 ]
    UniGenei Hs.559718.
    Hs.597002.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BWJ X-ray 2.30 A/B/C/D/E/F 366-562 [» ]
    ProteinModelPortali Q9Y6K8.
    SMRi Q9Y6K8. Positions 133-317, 368-562.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117670. 8 interactions.
    IntActi Q9Y6K8. 8 interactions.
    STRINGi 9606.ENSP00000346577.

    PTM databases

    PhosphoSitei Q9Y6K8.

    Polymorphism databases

    DMDMi 257051028.

    Proteomic databases

    MaxQBi Q9Y6K8.
    PaxDbi Q9Y6K8.
    PRIDEi Q9Y6K8.

    Protocols and materials databases

    DNASUi 26289.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344720 ; ENSP00000341430 ; ENSG00000154027 . [Q9Y6K8-3 ]
    ENST00000354567 ; ENSP00000346577 ; ENSG00000154027 . [Q9Y6K8-1 ]
    GeneIDi 26289.
    KEGGi hsa:26289.
    UCSCi uc001dhn.3. human. [Q9Y6K8-1 ]

    Organism-specific databases

    CTDi 26289.
    GeneCardsi GC01P077747.
    H-InvDB HIX0020812.
    HGNCi HGNC:365. AK5.
    HPAi HPA019128.
    HPA057255.
    MIMi 608009. gene.
    neXtProti NX_Q9Y6K8.
    PharmGKBi PA24659.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0563.
    HOVERGENi HBG059001.
    InParanoidi Q9Y6K8.
    KOi K00939.
    OMAi VFGEDTM.
    OrthoDBi EOG7060S3.
    PhylomeDBi Q9Y6K8.
    TreeFami TF313747.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS07943-MONOMER.
    Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

    Miscellaneous databases

    EvolutionaryTracei Q9Y6K8.
    GenomeRNAii 26289.
    NextBioi 48625.
    PROi Q9Y6K8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y6K8.
    Bgeei Q9Y6K8.
    CleanExi HS_AK5.
    Genevestigatori Q9Y6K8.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    HAMAPi MF_00235. Adenylate_kinase_Adk. 2 domains.
    InterProi IPR000850. Adenylat/UMP-CMP_kin.
    IPR006267. AK1/5.
    IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR23359. PTHR23359. 1 hit.
    PRINTSi PR00094. ADENYLTKNASE.
    SUPFAMi SSF47391. SSF47391. 1 hit.
    SSF52540. SSF52540. 2 hits.
    TIGRFAMsi TIGR01360. aden_kin_iso1. 1 hit.
    PROSITEi PS00113. ADENYLATE_KINASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiKAD5_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6K8
    Secondary accession number(s): Q5U622
    , Q6FH66, Q7Z4T5, Q86YS0, Q8N464, Q96EC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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