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Q9Y3D8

- KAD6_HUMAN

UniProt

Q9Y3D8 - KAD6_HUMAN

Protein

Adenylate kinase isoenzyme 6

Gene

AK6

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

    Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. AMP and dAMP are the preferred substrates, but CMP and dCMP are also good substrates. IMP is phosphorylated to a much lesser extent. All nucleoside triphosphates ATP, GTP, UTP, CTP, dATP, dCTP, dGTP, and TTP are accepted as phosphate donors. CTP is the best phosphate donor, followed by UTP, ATP, GTP and dCTP. May have a role in nuclear energy homeostasis. Has also ATPase activity. May be involved in regulation of Cajal body (CB) formation.1 Publication

    Catalytic activityi

    ATP + AMP = 2 ADP.1 PublicationUniRule annotation

    Kineticsi

    kcat is 6.3 sec(-1) for adenylate kinase activity. kcat is 4.8 sec(-1) for ATPase activity.

    1. KM=192 µM for AMP3 Publications
    2. KM=45 µM for ATP (for adenylate kinase activity)3 Publications
    3. KM=332 µM for ATP (for ATPase activity)3 Publications

    Vmax=1.27 µmol/min/mg enzyme for ATPase activity3 Publications

    Vmax=982 nmol/min/mg enzyme for the forward adenylate kinase reaction3 Publications

    Vmax=955 nmol/min/mg enzyme for the reverse adenylate kinase reaction3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei39 – 391AMPCurated
    Binding sitei79 – 791ATP
    Binding sitei105 – 1051ATP
    Binding sitei109 – 1091ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 186ATP
    Nucleotide bindingi148 – 1492ATP

    GO - Molecular functioni

    1. adenylate kinase activity Source: UniProtKB
    2. ATPase activity Source: UniProtKB-HAMAP
    3. ATP binding Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. nucleotide phosphorylation Source: GOC

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylate kinase isoenzyme 6UniRule annotation (EC:2.7.4.3UniRule annotation)
    Short name:
    AK6UniRule annotation
    Alternative name(s):
    Adrenal gland protein AD-004
    Coilin-interacting nuclear ATPase proteinUniRule annotation
    Short name:
    hCINAP
    Dual activity adenylate kinase/ATPaseUniRule annotation
    Short name:
    AK/ATPaseUniRule annotation
    Gene namesi
    Name:AK6UniRule annotation
    Synonyms:CINAPUniRule annotation
    ORF Names:AD-004, CGI-137
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:49151. AK6.

    Subcellular locationi

    Nucleusnucleoplasm. NucleusCajal body
    Note: Displays widespread diffuse nucleoplasmic distribution but not detected in nucleoli. Detected in Cajal bodies but not in all cells.

    GO - Cellular componenti

    1. Cajal body Source: UniProtKB
    2. membrane Source: UniProtKB
    3. nucleoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi79 – 791H → G: Induces homodimerization. Reduces adenylate kinase activity by 72% and ATPase activity by 76%. Significantly changes Cajal body organization in the nucleus, resulting in enhanced apoptosis and reduced proliferation. 1 Publication

    Organism-specific databases

    PharmGKBiPA36317.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 172172Adenylate kinase isoenzyme 6PRO_0000153896Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y3D8.
    PaxDbiQ9Y3D8.
    PeptideAtlasiQ9Y3D8.
    PRIDEiQ9Y3D8.

    Expressioni

    Tissue specificityi

    Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, chorionic villi and the central nervous system.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y3D8.
    BgeeiQ9Y3D8.
    GenevestigatoriQ9Y3D8.

    Organism-specific databases

    HPAiCAB005361.

    Interactioni

    Subunit structurei

    Monomer and homodimer By similarity. Interacts with COIL (via C-terminus).3 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    COILP384325EBI-2896123,EBI-945751

    Protein-protein interaction databases

    BioGridi112743. 70 interactions.
    IntActiQ9Y3D8. 4 interactions.
    MINTiMINT-1389230.
    STRINGi9606.ENSP00000370201.

    Structurei

    Secondary structure

    1
    172
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 94
    Helixi16 – 2712
    Beta strandi30 – 334
    Helixi34 – 418
    Beta strandi44 – 485
    Turni49 – 524
    Beta strandi53 – 564
    Helixi58 – 7114
    Beta strandi74 – 774
    Helixi86 – 883
    Beta strandi90 – 967
    Helixi99 – 10810
    Helixi113 – 12412
    Helixi127 – 1359
    Helixi138 – 1403
    Beta strandi141 – 1455
    Helixi149 – 16921

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RKBX-ray2.00A1-172[»]
    3IIJX-ray1.76A1-172[»]
    3IIKX-ray1.95A1-172[»]
    3IILX-ray2.00A1-172[»]
    3IIMX-ray2.00A1-172[»]
    ProteinModelPortaliQ9Y3D8.
    SMRiQ9Y3D8. Positions 1-172.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y3D8.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni33 – 5624NMPbindAdd
    BLAST
    Regioni108 – 11811LIDAdd
    BLAST

    Sequence similaritiesi

    Belongs to the adenylate kinase family. AK6 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG1936.
    HOGENOMiHOG000224472.
    HOVERGENiHBG052207.
    InParanoidiQ9Y3D8.
    KOiK14535.
    OMAiDNVQCEI.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00039. Adenylate_kinase_AK6.
    InterProiIPR020618. Adenyl_kinase_AK6.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y3D8-1) [UniParc]FASTAAdd to Basket

    Also known as: AK6

    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

    MLLPNILLTG TPGVGKTTLG KELASKSGLK YINVGDLARE EQLYDGYDEE    50
    YDCPILDEDR VVDELDNQMR EGGVIVDYHG CDFFPERWFH IVFVLRTDTN 100
    VLYERLETRG YNEKKLTDNI QCEIFQVLYE EATASYKEEI VHQLPSNKPE 150
    ELENNVDQIL KWIEQWIKDH NS 172
    Length:172
    Mass (Da):20,061
    Last modified:November 1, 1999 - v1
    Checksum:i33F62318FB434301
    GO
    Isoform 2 (identifier: Q9Y3D8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-9: LLPNILLT → CHRKP

    Note: Gene prediction based on EST data.

    Show »
    Length:169
    Mass (Da):19,805
    Checksum:i3F341AE6C5898C66
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 98LLPNILLT → CHRKP in isoform 2. CuratedVSP_039714

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ878880 mRNA. Translation: CAI48030.1.
    AJ878881 mRNA. Translation: CAI48031.1.
    AF151895 mRNA. Translation: AAD34132.1.
    AF110777 mRNA. Translation: AAF14860.1.
    AC145132 Genomic DNA. No translation available.
    CH471137 Genomic DNA. Translation: EAW51290.1.
    CH471137 Genomic DNA. Translation: EAW51291.1.
    CH471137 Genomic DNA. Translation: EAW51292.1.
    CH471137 Genomic DNA. Translation: EAW51297.1.
    BC007349 mRNA. Translation: AAH07349.1.
    BC007426 mRNA. Translation: AAH07426.1.
    CCDSiCCDS4001.1. [Q9Y3D8-1]
    CCDS43324.1. [Q9Y3D8-2]
    RefSeqiNP_001015891.1. NM_001015891.1. [Q9Y3D8-2]
    NP_057367.1. NM_016283.4. [Q9Y3D8-1]
    UniGeneiHs.653163.

    Genome annotation databases

    GeneIDi102157402.
    KEGGihsa:102157402.
    UCSCiuc003jwa.3. human. [Q9Y3D8-1]
    uc003jwb.3. human. [Q9Y3D8-2]

    Polymorphism databases

    DMDMi6831735.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ878880 mRNA. Translation: CAI48030.1 .
    AJ878881 mRNA. Translation: CAI48031.1 .
    AF151895 mRNA. Translation: AAD34132.1 .
    AF110777 mRNA. Translation: AAF14860.1 .
    AC145132 Genomic DNA. No translation available.
    CH471137 Genomic DNA. Translation: EAW51290.1 .
    CH471137 Genomic DNA. Translation: EAW51291.1 .
    CH471137 Genomic DNA. Translation: EAW51292.1 .
    CH471137 Genomic DNA. Translation: EAW51297.1 .
    BC007349 mRNA. Translation: AAH07349.1 .
    BC007426 mRNA. Translation: AAH07426.1 .
    CCDSi CCDS4001.1. [Q9Y3D8-1 ]
    CCDS43324.1. [Q9Y3D8-2 ]
    RefSeqi NP_001015891.1. NM_001015891.1. [Q9Y3D8-2 ]
    NP_057367.1. NM_016283.4. [Q9Y3D8-1 ]
    UniGenei Hs.653163.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RKB X-ray 2.00 A 1-172 [» ]
    3IIJ X-ray 1.76 A 1-172 [» ]
    3IIK X-ray 1.95 A 1-172 [» ]
    3IIL X-ray 2.00 A 1-172 [» ]
    3IIM X-ray 2.00 A 1-172 [» ]
    ProteinModelPortali Q9Y3D8.
    SMRi Q9Y3D8. Positions 1-172.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112743. 70 interactions.
    IntActi Q9Y3D8. 4 interactions.
    MINTi MINT-1389230.
    STRINGi 9606.ENSP00000370201.

    Polymorphism databases

    DMDMi 6831735.

    Proteomic databases

    MaxQBi Q9Y3D8.
    PaxDbi Q9Y3D8.
    PeptideAtlasi Q9Y3D8.
    PRIDEi Q9Y3D8.

    Protocols and materials databases

    DNASUi 6880.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 102157402.
    KEGGi hsa:102157402.
    UCSCi uc003jwa.3. human. [Q9Y3D8-1 ]
    uc003jwb.3. human. [Q9Y3D8-2 ]

    Organism-specific databases

    CTDi 102157402.
    GeneCardsi GC05M068646.
    GC05M068647.
    HGNCi HGNC:49151. AK6.
    HPAi CAB005361.
    neXtProti NX_Q9Y3D8.
    PharmGKBi PA36317.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1936.
    HOGENOMi HOG000224472.
    HOVERGENi HBG052207.
    InParanoidi Q9Y3D8.
    KOi K14535.
    OMAi DNVQCEI.

    Miscellaneous databases

    ChiTaRSi TAF9. human.
    EvolutionaryTracei Q9Y3D8.
    GenomeRNAii 102157402.
    NextBioi 26873.

    Gene expression databases

    ArrayExpressi Q9Y3D8.
    Bgeei Q9Y3D8.
    Genevestigatori Q9Y3D8.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00039. Adenylate_kinase_AK6.
    InterProi IPR020618. Adenyl_kinase_AK6.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of hCINAP, a novel coilin-interacting protein encoded by a transcript from the transcription factor TAFIID32 locus."
      Santama N., Ogg S.C., Malekkou A., Zographos S.E., Weis K., Lamond A.I.
      J. Biol. Chem. 280:36429-36441(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH COIL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
      Tissue: Cervix carcinoma and Placenta.
    2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adrenal gland.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Lymph.
    7. "Protein preparation, crystallization and preliminary X-ray analysis of human adrenal gland protein AD-004."
      Ren H., Liang Y., Li R., Ding H., Qiu S., Lu S., An J., Li L., Luo M., Zheng X., Su X.D.
      Acta Crystallogr. D 60:1292-1294(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "The crystal structure of human adenylate kinase 6: an adenylate kinase localized to the cell nucleus."
      Ren H., Wang L., Bennett M., Liang Y., Zheng X., Lu F., Li L., Nan J., Luo M., Eriksson S., Zhang C., Su X.-D.
      Proc. Natl. Acad. Sci. U.S.A. 102:303-308(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    10. "hCINAP is an atypical mammalian nuclear adenylate kinase with an ATPase motif: structural and functional studies."
      Drakou C.E., Malekkou A., Hayes J.M., Lederer C.W., Leonidas D.D., Oikonomakos N.G., Lamond A.I., Santama N., Zographos S.E.
      Proteins 80:206-220(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH ADP AND DADP, MUTAGENESIS OF HIS-79, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiKAD6_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3D8
    Secondary accession number(s): A8MSZ6, Q5F2S9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 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 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Uncharacterized protein families (UPF)
      List of uncharacterized protein family (UPF) entries

    External Data

    Dasty 3