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P54819

- KAD2_HUMAN

UniProt

P54819 - KAD2_HUMAN

Protein

Adenylate kinase 2, mitochondrial

Gene

AK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis.1 PublicationUniRule annotation

    Catalytic activityi

    ATP + AMP = 2 ADP.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei46 – 461AMPUniRule annotation
    Binding sitei51 – 511AMPUniRule annotation
    Binding sitei107 – 1071AMPUniRule annotation
    Binding sitei138 – 1381ATP
    Binding sitei142 – 1421ATPUniRule annotation
    Binding sitei175 – 1751AMP
    Binding sitei186 – 1861AMPUniRule annotation
    Binding sitei214 – 2141ATP; via carbonyl oxygen

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi25 – 306ATP
    Nucleotide bindingi72 – 743AMPUniRule annotation
    Nucleotide bindingi100 – 1034AMPUniRule annotation
    Nucleotide bindingi151 – 1522ATP

    GO - Molecular functioni

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

    GO - Biological processi

    1. ADP biosynthetic process Source: UniProtKB-HAMAP
    2. AMP metabolic process Source: UniProtKB-HAMAP
    3. brain development Source: Ensembl
    4. dATP metabolic process Source: Ensembl
    5. liver development Source: Ensembl
    6. nucleobase-containing small molecule interconversion Source: Reactome
    7. nucleobase-containing small molecule metabolic process Source: Reactome
    8. nucleotide phosphorylation Source: GOC
    9. oxidative phosphorylation Source: Ensembl
    10. response to thyroid hormone Source: Ensembl
    11. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Adenylate kinase 2, mitochondrialUniRule annotation (EC:2.7.4.3UniRule annotation)
    Short name:
    AK 2UniRule annotation
    Alternative name(s):
    ATP-AMP transphosphorylase 2UniRule annotation
    ATP:AMP phosphotransferaseUniRule annotation
    Adenylate monophosphate kinaseUniRule annotation
    Cleaved into the following chain:
    Adenylate kinase 2, mitochondrial, N-terminally processedUniRule annotation
    Gene namesi
    Name:AK2UniRule annotation
    Synonyms:ADK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:362. AK2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrial inner membrane Source: Ensembl
    4. mitochondrial intermembrane space Source: Reactome
    5. sperm mitochondrial sheath Source: Ensembl

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Reticular dysgenesis (RDYS) [MIM:267500]: Most severe form of inborn severe combined immunodeficiencies (SCID) and is characterized by absence of granulocytes and almost complete deficiency of lymphocytes in peripheral blood, hypoplasia of the thymus and secondary lymphoid organs, and lack of innate and adaptive humoral and cellular immune functions, leading to fatal septicemia within days after birth. In bone marrow of individuals with reticular dysgenesis, myeloid differentiation is blocked at the promyelocytic stage, whereas erythro- and megakaryocytic maturation is generally normal. In addition, affected newborns have bilateral sensorineural deafness. Defects may be due to its absence in leukocytes and inner ear, in which its absence can not be compensated by AK1.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti103 – 1031R → W in RDYS. 1 Publication
    VAR_054630
    Natural varianti165 – 1651D → G in RDYS. 1 Publication
    VAR_054631

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi267500. phenotype.
    Orphaneti33355. Reticular dysgenesis.
    PharmGKBiPA24656.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 239239Adenylate kinase 2, mitochondrialPRO_0000423212Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 PublicationUniRule annotation
    Chaini2 – 239238Adenylate kinase 2, mitochondrial, N-terminally processedPRO_0000158917Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications
    Disulfide bondi42 ↔ 921 PublicationUniRule annotation
    Modified residuei62 – 621N6-succinyllysineBy similarity
    Modified residuei93 – 931N6-succinyllysineBy similarity
    Modified residuei181 – 1811N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP54819.
    PaxDbiP54819.
    PRIDEiP54819.

    2D gel databases

    OGPiP54819.
    REPRODUCTION-2DPAGEIPI00218988.
    UCD-2DPAGEP54819.

    PTM databases

    PhosphoSiteiP54819.

    Expressioni

    Tissue specificityi

    Present in most tissues. Present at high level in heart, liver and kidney, and at low level in brain, skeletal muscle and skin. Present in thrombocytes but not in erythrocytes, which lack mitochondria. Present in all nucleated cell populations from blood, while AK1 is mostly absent. In spleen and lymph nodes, mononuclear cells lack AK1, whereas AK2 is readily detectable. These results indicate that leukocytes may be susceptible to defects caused by the lack of AK2, as they do not express AK1 in sufficient amounts to compensate for the AK2 functional deficits (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP54819.
    BgeeiP54819.
    CleanExiHS_AK2.
    GenevestigatoriP54819.

    Organism-specific databases

    HPAiHPA018479.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    BioGridi106707. 17 interactions.
    IntActiP54819. 4 interactions.

    Structurei

    Secondary structure

    1
    239
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 216
    Helixi28 – 3912
    Beta strandi42 – 454
    Helixi46 – 5611
    Helixi59 – 6911
    Helixi76 – 8712
    Helixi90 – 923
    Beta strandi95 – 1006
    Helixi105 – 11713
    Beta strandi124 – 1296
    Helixi132 – 1409
    Turni146 – 1483
    Beta strandi151 – 1533
    Turni154 – 1563
    Beta strandi166 – 1683
    Helixi180 – 20324
    Beta strandi207 – 2115
    Helixi216 – 23015

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C9YX-ray2.10A1-239[»]
    ProteinModelPortaliP54819.
    SMRiP54819. Positions 15-232.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54819.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 7430NMPbindAdd
    BLAST
    Regioni141 – 17838LIDAdd
    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. AK2 subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0563.
    HOVERGENiHBG000458.
    InParanoidiP54819.
    KOiK00939.
    OMAiLENNKAC.
    OrthoDBiEOG74TX0R.
    PhylomeDBiP54819.
    TreeFamiTF300896.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00235. Adenylate_kinase_Adk.
    MF_03168. Adenylate_kinase_AK2.
    InterProiIPR006259. Adenyl_kin_sub.
    IPR000850. Adenylat/UMP-CMP_kin.
    IPR007862. Adenylate_kinase_lid-dom.
    IPR028587. AK2.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR23359. PTHR23359. 1 hit.
    PfamiPF05191. ADK_lid. 1 hit.
    [Graphical view]
    PRINTSiPR00094. ADENYLTKNASE.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR01351. adk. 1 hit.
    PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P54819-1) [UniParc]FASTAAdd to Basket

    Also known as: AK2A, AK2isoA

    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

    MAPSVPAAEP EYPKGIRAVL LGPPGAGKGT QAPRLAENFC VCHLATGDML    50
    RAMVASGSEL GKKLKATMDA GKLVSDEMVV ELIEKNLETP LCKNGFLLDG 100
    FPRTVRQAEM LDDLMEKRKE KLDSVIEFSI PDSLLIRRIT GRLIHPKSGR 150
    SYHEEFNPPK EPMKDDITGE PLIRRSDDNE KALKIRLQAY HTQTTPLIEY 200
    YRKRGIHSAI DASQTPDVVF ASILAAFSKA TCKDLVMFI 239
    Length:239
    Mass (Da):26,478
    Last modified:January 23, 2007 - v2
    Checksum:i86FA94F9EE33629F
    GO
    Isoform 2 (identifier: P54819-2) [UniParc]FASTAAdd to Basket

    Also known as: AK2B, AK2isoB

    The sequence of this isoform differs from the canonical sequence as follows:
         232-239: CKDLVMFI → S

    Show »
    Length:232
    Mass (Da):25,615
    Checksum:i64AEE1A97D81D401
    GO
    Isoform 3 (identifier: P54819-3) [UniParc]FASTAAdd to Basket

    Also known as: AK2C

    The sequence of this isoform differs from the canonical sequence as follows:
         178-239: DNEKALKIRL...ATCKDLVMFI → IGQAKRSFLRLAKISFDVLIKKALA

    Show »
    Length:202
    Mass (Da):22,265
    Checksum:iAE7593A8ADBD00CF
    GO
    Isoform 4 (identifier: P54819-4) [UniParc]FASTAAdd to Basket

    Also known as: AK2D

    The sequence of this isoform differs from the canonical sequence as follows:
         2-48: Missing.
         177-178: DD → GL
         179-239: Missing.

    Show »
    Length:131
    Mass (Da):14,840
    Checksum:i99C780C24D0F7845
    GO
    Isoform 5 (identifier: P54819-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         135-142: Missing.
         232-239: CKDLVMFI → S

    Note: No experimental confirmation available.

    Show »
    Length:224
    Mass (Da):24,648
    Checksum:i1A769D71DDBB0B8A
    GO
    Isoform 6 (identifier: P54819-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-48: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:192
    Mass (Da):21,767
    Checksum:i599AC964FCA56E89
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti103 – 1031R → W in RDYS. 1 Publication
    VAR_054630
    Natural varianti165 – 1651D → G in RDYS. 1 Publication
    VAR_054631
    Natural varianti209 – 2091A → T.
    Corresponds to variant rs12116440 [ dbSNP | Ensembl ].
    VAR_050032

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 4847Missing in isoform 4 and isoform 6. 2 PublicationsVSP_002792Add
    BLAST
    Alternative sequencei135 – 1428Missing in isoform 5. 1 PublicationVSP_036503
    Alternative sequencei177 – 1782DD → GL in isoform 4. 1 PublicationVSP_002793
    Alternative sequencei178 – 23962DNEKA…LVMFI → IGQAKRSFLRLAKISFDVLI KKALA in isoform 3. 1 PublicationVSP_002791Add
    BLAST
    Alternative sequencei179 – 23961Missing in isoform 4. 1 PublicationVSP_002794Add
    BLAST
    Alternative sequencei232 – 2398CKDLVMFI → S in isoform 2 and isoform 5. 5 PublicationsVSP_002790

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39945 mRNA. Translation: AAC52061.1.
    U84371 mRNA. Translation: AAB41790.1.
    U54645 mRNA. Translation: AAC13881.1.
    AB005621 mRNA. Translation: BAC16747.1.
    AB005622 mRNA. Translation: BAC16748.1.
    AY080899 mRNA. Translation: AAL87027.1.
    AY080900 mRNA. Translation: AAL87028.1.
    AK291676 mRNA. Translation: BAF84365.1.
    AK295105 mRNA. Translation: BAG58139.1.
    AK296863 mRNA. Translation: BAG59426.1.
    AB451267 mRNA. Translation: BAG70081.1.
    AB451394 mRNA. Translation: BAG70208.1.
    AL020995 Genomic DNA. Translation: CAI19351.1.
    AL020995 Genomic DNA. Translation: CAI19352.1.
    CH471059 Genomic DNA. Translation: EAX07484.1.
    CH471059 Genomic DNA. Translation: EAX07486.1.
    BC009405 mRNA. Translation: AAH09405.1.
    BC070127 mRNA. Translation: AAH70127.1.
    BC090040 mRNA. Translation: AAH90040.1.
    CCDSiCCDS373.1. [P54819-2]
    CCDS374.1. [P54819-1]
    PIRiG02248.
    JC5893.
    RefSeqiNP_001186128.1. NM_001199199.1. [P54819-5]
    NP_001616.1. NM_001625.3. [P54819-1]
    NP_037543.1. NM_013411.4. [P54819-2]
    UniGeneiHs.470907.

    Genome annotation databases

    EnsembliENST00000354858; ENSP00000346921; ENSG00000004455. [P54819-1]
    ENST00000373449; ENSP00000362548; ENSG00000004455. [P54819-2]
    GeneIDi204.
    KEGGihsa:204.
    UCSCiuc001bwo.2. human. [P54819-2]
    uc001bwp.2. human. [P54819-1]
    uc010ohq.2. human. [P54819-5]

    Polymorphism databases

    DMDMi1708596.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U39945 mRNA. Translation: AAC52061.1 .
    U84371 mRNA. Translation: AAB41790.1 .
    U54645 mRNA. Translation: AAC13881.1 .
    AB005621 mRNA. Translation: BAC16747.1 .
    AB005622 mRNA. Translation: BAC16748.1 .
    AY080899 mRNA. Translation: AAL87027.1 .
    AY080900 mRNA. Translation: AAL87028.1 .
    AK291676 mRNA. Translation: BAF84365.1 .
    AK295105 mRNA. Translation: BAG58139.1 .
    AK296863 mRNA. Translation: BAG59426.1 .
    AB451267 mRNA. Translation: BAG70081.1 .
    AB451394 mRNA. Translation: BAG70208.1 .
    AL020995 Genomic DNA. Translation: CAI19351.1 .
    AL020995 Genomic DNA. Translation: CAI19352.1 .
    CH471059 Genomic DNA. Translation: EAX07484.1 .
    CH471059 Genomic DNA. Translation: EAX07486.1 .
    BC009405 mRNA. Translation: AAH09405.1 .
    BC070127 mRNA. Translation: AAH70127.1 .
    BC090040 mRNA. Translation: AAH90040.1 .
    CCDSi CCDS373.1. [P54819-2 ]
    CCDS374.1. [P54819-1 ]
    PIRi G02248.
    JC5893.
    RefSeqi NP_001186128.1. NM_001199199.1. [P54819-5 ]
    NP_001616.1. NM_001625.3. [P54819-1 ]
    NP_037543.1. NM_013411.4. [P54819-2 ]
    UniGenei Hs.470907.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C9Y X-ray 2.10 A 1-239 [» ]
    ProteinModelPortali P54819.
    SMRi P54819. Positions 15-232.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106707. 17 interactions.
    IntActi P54819. 4 interactions.

    Chemistry

    BindingDBi P54819.
    ChEMBLi CHEMBL4938.

    PTM databases

    PhosphoSitei P54819.

    Polymorphism databases

    DMDMi 1708596.

    2D gel databases

    OGPi P54819.
    REPRODUCTION-2DPAGE IPI00218988.
    UCD-2DPAGE P54819.

    Proteomic databases

    MaxQBi P54819.
    PaxDbi P54819.
    PRIDEi P54819.

    Protocols and materials databases

    DNASUi 204.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354858 ; ENSP00000346921 ; ENSG00000004455 . [P54819-1 ]
    ENST00000373449 ; ENSP00000362548 ; ENSG00000004455 . [P54819-2 ]
    GeneIDi 204.
    KEGGi hsa:204.
    UCSCi uc001bwo.2. human. [P54819-2 ]
    uc001bwp.2. human. [P54819-1 ]
    uc010ohq.2. human. [P54819-5 ]

    Organism-specific databases

    CTDi 204.
    GeneCardsi GC01M033476.
    HGNCi HGNC:362. AK2.
    HPAi HPA018479.
    MIMi 103020. gene.
    267500. phenotype.
    neXtProti NX_P54819.
    Orphaneti 33355. Reticular dysgenesis.
    PharmGKBi PA24656.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0563.
    HOVERGENi HBG000458.
    InParanoidi P54819.
    KOi K00939.
    OMAi LENNKAC.
    OrthoDBi EOG74TX0R.
    PhylomeDBi P54819.
    TreeFami TF300896.

    Enzyme and pathway databases

    Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

    Miscellaneous databases

    EvolutionaryTracei P54819.
    GeneWikii AK2.
    GenomeRNAii 204.
    NextBioi 812.
    PROi P54819.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P54819.
    Bgeei P54819.
    CleanExi HS_AK2.
    Genevestigatori P54819.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00235. Adenylate_kinase_Adk.
    MF_03168. Adenylate_kinase_AK2.
    InterProi IPR006259. Adenyl_kin_sub.
    IPR000850. Adenylat/UMP-CMP_kin.
    IPR007862. Adenylate_kinase_lid-dom.
    IPR028587. AK2.
    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. 1 hit.
    TIGRFAMsi TIGR01351. adk. 1 hit.
    PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of cDNA for human adenylate kinase 2A."
      Lee Y., Kim J.W., Lee I.A., Kang H.B., Choe Y.K., Lee H.G., Lim J.S., Kim H.J., Park C., Choe I.S.
      Biochem. Mol. Biol. Int. 39:833-842(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "Cloning and expression of human adenylate kinase 2 isozymes: differential expression of adenylate kinase 1 and 2 in human muscle tissues."
      Lee Y., Kim J.W., Lee S.M., Kim H.J., Lee K.S., Park C., Choe I.S.
      J. Biochem. 123:47-54(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Fetal liver.
    3. "cDNA cloning and tissue-specific expression of the gene encoding human adenylate kinase isozyme 2."
      Noma T., Song S., Yoon Y.-S., Tanaka S., Nakazawa A.
      Biochim. Biophys. Acta 1395:34-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    4. "Novel isoforms of human adenylate kinase 2."
      Guo J.
      Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
    5. "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] (ISOFORMS 1; 5 AND 6).
      Tissue: Brain, Placenta and Tongue.
    6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    7. "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].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 AND 2).
      Tissue: Placenta and Uterus.
    10. Bienvenut W.V., Heiserich L., Gottlieb E.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-14; 18-34; 73-85; 94-103; 107-117 AND 120-138, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG AP4A, DISULFIDE BOND.
    15. "Reticular dysgenesis (aleukocytosis) is caused by mutations in the gene encoding mitochondrial adenylate kinase 2."
      Pannicke U., Hoenig M., Hess I., Friesen C., Holzmann K., Rump E.-M., Barth T.F., Rojewski M.T., Schulz A., Boehm T., Friedrich W., Schwarz K.
      Nat. Genet. 41:101-105(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN RDYS, TISSUE SPECIFICITY.
    16. Cited for: VARIANTS RDYS TRP-103 AND GLY-165, FUNCTION.

    Entry informationi

    Entry nameiKAD2_HUMAN
    AccessioniPrimary (citable) accession number: P54819
    Secondary accession number(s): A8K6L1
    , B4DHH7, B4DL64, Q16856, Q5EB54, Q5TIF7, Q8TCY2, Q8TCY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 152 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, Direct protein sequencing, 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