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P27144

- KAD4_HUMAN

UniProt

P27144 - KAD4_HUMAN

Protein

Adenylate kinase 4, mitochondrial

Gene

AK4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor. Also displays broad nucleoside diphosphate kinase activity.3 PublicationsUniRule annotation

    Catalytic activityi

    NTP + AMP = NDP + ADP.UniRule annotation
    ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation

    Kineticsi

    1. KM=5.3 µM for AMP with ATP as phosphate donor1 Publication
    2. KM=1.4 µM for AMP with GTP as phosphate donor1 Publication
    3. KM=507 µM for dAMP with ATP as phosphate donor1 Publication

    Vmax=90 pmol/min/µg enzyme with AMP as substrate and ATP as phosphate donor1 Publication

    Vmax=80 pmol/min/µg enzyme with AMP as substrate and GTP as phosphate donor1 Publication

    Vmax=88 pmol/min/µg enzyme with dAMP as substrate and ATP as phosphate donor1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei36 – 361AMP
    Binding sitei41 – 411AMPUniRule annotation
    Binding sitei96 – 961AMPUniRule annotation
    Binding sitei126 – 1261NTP
    Binding sitei170 – 1701AMP
    Binding sitei199 – 1991NTP; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi15 – 206NTP
    Nucleotide bindingi62 – 643AMP
    Nucleotide bindingi89 – 924AMP
    Nucleotide bindingi135 – 1362NTPUniRule annotation

    GO - Molecular functioni

    1. adenylate kinase activity Source: BHF-UCL
    2. ATP binding Source: UniProtKB-KW
    3. GTP binding Source: UniProtKB-KW
    4. nucleoside diphosphate kinase activity Source: UniProtKB
    5. nucleoside triphosphate adenylate kinase activity Source: BHF-UCL

    GO - Biological processi

    1. ADP biosynthetic process Source: UniProtKB-HAMAP
    2. AMP metabolic process Source: BHF-UCL
    3. ATP metabolic process Source: BHF-UCL
    4. brain development Source: Ensembl
    5. GTP metabolic process Source: BHF-UCL
    6. liver development Source: Ensembl
    7. nucleoside diphosphate phosphorylation Source: UniProtKB
    8. nucleoside triphosphate biosynthetic process Source: UniProtKB
    9. response to drug Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylate kinase 4, mitochondrialUniRule annotation (EC:2.7.4.10UniRule annotation, EC:2.7.4.6UniRule annotation)
    Short name:
    AK 4UniRule annotation
    Alternative name(s):
    Adenylate kinase 3-likeUniRule annotation
    GTP:AMP phosphotransferase AK4UniRule annotation
    Gene namesi
    Name:AK4UniRule annotation
    Synonyms:AK3, AK3L1UniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:363. AK4.

    Subcellular locationi

    Mitochondrion matrix 2 PublicationsUniRule annotation

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial matrix Source: BHF-UCL
    3. mitochondrion Source: BHF-UCL

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi4 – 41K → G: Abolishes mitochondrial import; when associated with G-7. 1 Publication
    Mutagenesisi7 – 71R → G: Abolishes mitochondrial import; when associated with G-4. 1 Publication

    Organism-specific databases

    PharmGKBiPA165750325.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 223223Adenylate kinase 4, mitochondrialPRO_0000158926Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei60 – 601N6-succinyllysineBy similarity
    Modified residuei175 – 1751N6-acetyllysineBy similarity
    Modified residuei179 – 1791N6-acetyllysine; alternateBy similarity
    Modified residuei179 – 1791N6-succinyllysine; alternateBy similarity
    Modified residuei186 – 1861N6-acetyllysine; alternateBy similarity
    Modified residuei186 – 1861N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP27144.
    PaxDbiP27144.
    PRIDEiP27144.

    2D gel databases

    UCD-2DPAGEP27144.

    PTM databases

    PhosphoSiteiP27144.

    Expressioni

    Tissue specificityi

    Highly expressed in kidney, moderately expressed in heart and liver and weakly expressed in brain.1 Publication

    Gene expression databases

    ArrayExpressiP27144.
    BgeeiP27144.
    CleanExiHS_AK3.
    HS_AK3L1.
    GenevestigatoriP27144.

    Organism-specific databases

    HPAiHPA042753.
    HPA049461.

    Interactioni

    Subunit structurei

    Monomer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    BioGridi106708. 8 interactions.
    IntActiP27144. 3 interactions.

    Structurei

    Secondary structure

    1
    223
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115
    Helixi18 – 2912
    Beta strandi32 – 343
    Helixi36 – 4510
    Helixi49 – 5911
    Helixi66 – 7813
    Turni79 – 824
    Beta strandi85 – 895
    Helixi94 – 1018
    Beta strandi108 – 1136
    Helixi116 – 1249
    Beta strandi126 – 1294
    Turni130 – 1334
    Beta strandi134 – 1374
    Turni138 – 1403
    Turni150 – 1523
    Helixi160 – 1623
    Helixi164 – 18724
    Beta strandi191 – 1955
    Helixi199 – 21113
    Helixi217 – 2193
    Helixi220 – 2223

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2AR7X-ray2.15A/B1-223[»]
    2BBWX-ray2.05A/B1-223[»]
    3NDPX-ray2.30A/B1-223[»]
    ProteinModelPortaliP27144.
    SMRiP27144. Positions 4-223.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27144.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 6430NMPbindAdd
    BLAST
    Regioni125 – 16238LIDAdd
    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 GTP/ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP/ATP hydrolysis.

    Sequence similaritiesi

    Belongs to the adenylate kinase family. AK3 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0563.
    HOGENOMiHOG000238772.
    HOVERGENiHBG000458.
    InParanoidiP27144.
    KOiK00939.
    OMAiGDVAKQY.
    PhylomeDBiP27144.
    TreeFamiTF312916.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00235. Adenylate_kinase_Adk.
    MF_03169. Adenylate_kinase_AK3.
    MF_03170. Adenylate_kinase_AK4.
    InterProiIPR006259. Adenyl_kin_sub.
    IPR000850. Adenylat/UMP-CMP_kin.
    IPR007862. Adenylate_kinase_lid-dom.
    IPR028586. AK3/Ak4_mitochondrial.
    IPR028585. AK4_mitochondrial.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR23359. PTHR23359. 1 hit.
    PfamiPF05191. ADK_lid. 1 hit.
    [Graphical view]
    PRINTSiPR00094. ADENYLTKNASE.
    SUPFAMiSSF52540. SSF52540. 2 hits.
    SSF57774. SSF57774. 1 hit.
    TIGRFAMsiTIGR01351. adk. 1 hit.
    PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P27144-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASKLLRAVI LGPPGSGKGT VCQRIAQNFG LQHLSSGHFL RENIKASTEV    50
    GEMAKQYIEK SLLVPDHVIT RLMMSELENR RGQHWLLDGF PRTLGQAEAL 100
    DKICEVDLVI SLNIPFETLK DRLSRRWIHP PSGRVYNLDF NPPHVHGIDD 150
    VTGEPLVQQE DDKPEAVAAR LRQYKDVAKP VIELYKSRGV LHQFSGTETN 200
    KIWPYVYTLF SNKITPIQSK EAY 223
    Length:223
    Mass (Da):25,268
    Last modified:August 1, 1992 - v1
    Checksum:i653341A8EB3BC723
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221C → S in AAH40224. (PubMed:15489334)Curated
    Sequence conflicti22 – 221C → S in AAI46654. (PubMed:15489334)Curated
    Sequence conflicti23 – 231Q → R in AAH66944. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60673 mRNA. Translation: CAA43088.1.
    CR456830 mRNA. Translation: CAG33111.1.
    AK313611 mRNA. Translation: BAG36374.1.
    AL356212, AC099680 Genomic DNA. Translation: CAI22412.1.
    CH471059 Genomic DNA. Translation: EAX06538.1.
    CH471059 Genomic DNA. Translation: EAX06540.1.
    CH471059 Genomic DNA. Translation: EAX06544.1.
    BC016180 mRNA. Translation: AAH16180.1.
    BC040224 mRNA. Translation: AAH40224.1.
    BC066944 mRNA. Translation: AAH66944.1.
    BC136886 mRNA. Translation: AAI36887.1.
    BC136887 mRNA. Translation: AAI36888.1.
    BC148270 mRNA. Translation: AAI48271.1.
    BC146653 mRNA. Translation: AAI46654.1.
    CCDSiCCDS629.1.
    PIRiA42820. KIHUA3.
    RefSeqiNP_001005353.1. NM_001005353.2.
    NP_037542.1. NM_013410.3.
    NP_982289.1. NM_203464.2.
    XP_003119578.1. XM_003119530.3.
    UniGeneiHs.10862.

    Genome annotation databases

    EnsembliENST00000327299; ENSP00000322175; ENSG00000162433.
    ENST00000395334; ENSP00000378743; ENSG00000162433.
    ENST00000545314; ENSP00000445912; ENSG00000162433.
    GeneIDi100507855.
    205.
    KEGGihsa:100507855.
    hsa:205.
    UCSCiuc001dby.3. human.

    Polymorphism databases

    DMDMi125157.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60673 mRNA. Translation: CAA43088.1 .
    CR456830 mRNA. Translation: CAG33111.1 .
    AK313611 mRNA. Translation: BAG36374.1 .
    AL356212 , AC099680 Genomic DNA. Translation: CAI22412.1 .
    CH471059 Genomic DNA. Translation: EAX06538.1 .
    CH471059 Genomic DNA. Translation: EAX06540.1 .
    CH471059 Genomic DNA. Translation: EAX06544.1 .
    BC016180 mRNA. Translation: AAH16180.1 .
    BC040224 mRNA. Translation: AAH40224.1 .
    BC066944 mRNA. Translation: AAH66944.1 .
    BC136886 mRNA. Translation: AAI36887.1 .
    BC136887 mRNA. Translation: AAI36888.1 .
    BC148270 mRNA. Translation: AAI48271.1 .
    BC146653 mRNA. Translation: AAI46654.1 .
    CCDSi CCDS629.1.
    PIRi A42820. KIHUA3.
    RefSeqi NP_001005353.1. NM_001005353.2.
    NP_037542.1. NM_013410.3.
    NP_982289.1. NM_203464.2.
    XP_003119578.1. XM_003119530.3.
    UniGenei Hs.10862.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AR7 X-ray 2.15 A/B 1-223 [» ]
    2BBW X-ray 2.05 A/B 1-223 [» ]
    3NDP X-ray 2.30 A/B 1-223 [» ]
    ProteinModelPortali P27144.
    SMRi P27144. Positions 4-223.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106708. 8 interactions.
    IntActi P27144. 3 interactions.

    Chemistry

    BindingDBi P27144.
    ChEMBLi CHEMBL4926.

    PTM databases

    PhosphoSitei P27144.

    Polymorphism databases

    DMDMi 125157.

    2D gel databases

    UCD-2DPAGE P27144.

    Proteomic databases

    MaxQBi P27144.
    PaxDbi P27144.
    PRIDEi P27144.

    Protocols and materials databases

    DNASUi 205.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000327299 ; ENSP00000322175 ; ENSG00000162433 .
    ENST00000395334 ; ENSP00000378743 ; ENSG00000162433 .
    ENST00000545314 ; ENSP00000445912 ; ENSG00000162433 .
    GeneIDi 100507855.
    205.
    KEGGi hsa:100507855.
    hsa:205.
    UCSCi uc001dby.3. human.

    Organism-specific databases

    CTDi 205.
    GeneCardsi GC01P065614.
    HGNCi HGNC:363. AK4.
    HPAi HPA042753.
    HPA049461.
    MIMi 103030. gene.
    neXtProti NX_P27144.
    PharmGKBi PA165750325.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0563.
    HOGENOMi HOG000238772.
    HOVERGENi HBG000458.
    InParanoidi P27144.
    KOi K00939.
    OMAi GDVAKQY.
    PhylomeDBi P27144.
    TreeFami TF312916.

    Miscellaneous databases

    EvolutionaryTracei P27144.
    GeneWikii AK3L1.
    NextBioi 818.
    PROi P27144.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27144.
    Bgeei P27144.
    CleanExi HS_AK3.
    HS_AK3L1.
    Genevestigatori P27144.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00235. Adenylate_kinase_Adk.
    MF_03169. Adenylate_kinase_AK3.
    MF_03170. Adenylate_kinase_AK4.
    InterProi IPR006259. Adenyl_kin_sub.
    IPR000850. Adenylat/UMP-CMP_kin.
    IPR007862. Adenylate_kinase_lid-dom.
    IPR028586. AK3/Ak4_mitochondrial.
    IPR028585. AK4_mitochondrial.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR23359. PTHR23359. 1 hit.
    Pfami PF05191. ADK_lid. 1 hit.
    [Graphical view ]
    PRINTSi PR00094. ADENYLTKNASE.
    SUPFAMi SSF52540. SSF52540. 2 hits.
    SSF57774. SSF57774. 1 hit.
    TIGRFAMsi TIGR01351. adk. 1 hit.
    PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of human adenylate kinase 3 (AK3) cDNA and mapping of the AK3 pseudogene to an intron of the NF1 gene."
      Xu G., O'Connell P., Stevens J., White R.
      Genomics 13:537-542(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [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].
      Tissue: Brain, Colon and Lung.
    7. "Structure and expression of human mitochondrial adenylate kinase targeted to the mitochondrial matrix."
      Noma T., Fujisawa K., Yamashiro Y., Shinohara M., Nakazawa A., Gondo T., Ishihara T., Yoshinobu K.
      Biochem. J. 358:225-232(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    8. "Evidence of an intact N-terminal translocation sequence of human mitochondrial adenylate kinase 4."
      Panayiotou C., Solaroli N., Johansson M., Karlsson A.
      Int. J. Biochem. Cell Biol. 42:62-69(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-4 AND ARG-7.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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.
    11. "Crystal structure of human adenylate kinase 4 (AK4) in complex with diguanosine pentaphosphate."
      Structural genomics consortium (SGC)
      Submitted (DEC-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH DIGUANOSINE PENTAPHOSPHATE.
    12. "Crystal structure of human adenylate kinase 4 (L171P) suggests the role of hinge region in protein domain motion."
      Liu R., Xu H., Wei Z., Wang Y., Lin Y., Gong W.
      Biochem. Biophys. Res. Commun. 379:92-97(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION.

    Entry informationi

    Entry nameiKAD4_HUMAN
    AccessioniPrimary (citable) accession number: P27144
    Secondary accession number(s): B2R927
    , D3DQ62, Q6IBH4, Q6NXQ5, Q8IUU9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 148 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 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3