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Q9UIJ7

- KAD3_HUMAN

UniProt

Q9UIJ7 - KAD3_HUMAN

Protein

GTP:AMP phosphotransferase AK3, mitochondrial

Gene

AK3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.1 PublicationUniRule annotation

    Catalytic activityi

    NTP + AMP = NDP + ADP.1 PublicationUniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei38 – 381AMPUniRule annotation
    Binding sitei43 – 431AMPUniRule annotation
    Binding sitei98 – 981AMPUniRule annotation
    Binding sitei128 – 1281GTPUniRule annotation
    Binding sitei161 – 1611AMPUniRule annotation
    Binding sitei172 – 1721AMPUniRule annotation
    Binding sitei201 – 2011GTP; via carbonyl oxygenUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi17 – 226GTPUniRule annotation
    Nucleotide bindingi64 – 663AMPUniRule annotation
    Nucleotide bindingi91 – 944AMPUniRule annotation
    Nucleotide bindingi137 – 1382GTPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: InterPro
    2. GTP binding Source: UniProtKB-KW
    3. 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. blood coagulation Source: Reactome
    4. GTP metabolic process Source: BHF-UCL
    5. ITP metabolic process Source: BHF-UCL
    6. UTP metabolic process Source: BHF-UCL

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    GTP:AMP phosphotransferase AK3, mitochondrialUniRule annotation (EC:2.7.4.10UniRule annotation)
    Alternative name(s):
    Adenylate kinase 3UniRule annotation
    Short name:
    AK 3UniRule annotation
    Adenylate kinase 3 alpha-like 1UniRule annotation
    Gene namesi
    Name:AK3UniRule annotation
    Synonyms:AK3L1, AK6, AKL3L
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:17376. AK3.

    Subcellular locationi

    Mitochondrion matrix 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. mitochondrial matrix Source: BHF-UCL
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164741184.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedUniRule annotation
    Chaini2 – 227226GTP:AMP phosphotransferase AK3, mitochondrialPRO_0000158922Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201N6-succinyllysineBy similarity
    Modified residuei34 – 341N6-acetyllysineBy similarity
    Modified residuei57 – 571N6-succinyllysineBy similarity
    Modified residuei64 – 641N6-acetyllysine; alternateBy similarity
    Modified residuei64 – 641N6-succinyllysine; alternateBy similarity
    Modified residuei80 – 801N6-acetyllysine; alternateBy similarity
    Modified residuei80 – 801N6-succinyllysine; alternateBy similarity
    Modified residuei174 – 1741N6-acetyllysine; alternateBy similarity
    Modified residuei174 – 1741N6-succinyllysine; alternateBy similarity
    Modified residuei189 – 1891N6-acetyllysine; alternateBy similarity
    Modified residuei189 – 1891N6-succinyllysine; alternateBy similarity
    Modified residuei203 – 2031N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9UIJ7.
    PaxDbiQ9UIJ7.
    PRIDEiQ9UIJ7.

    2D gel databases

    OGPiQ9UIJ7.
    REPRODUCTION-2DPAGEIPI00465256.
    UCD-2DPAGEQ9UIJ7.

    PTM databases

    PhosphoSiteiQ9UIJ7.

    Expressioni

    Tissue specificityi

    Highly expressed in heart, skeletal muscle and liver, moderately expressed in pancreas and kidney, and weakly expressed in placenta, brain and lung.1 Publication

    Gene expression databases

    BgeeiQ9UIJ7.
    CleanExiHS_AK3.
    HS_AK3L1.
    GenevestigatoriQ9UIJ7.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    BioGridi119127. 5 interactions.
    IntActiQ9UIJ7. 2 interactions.
    STRINGi9606.ENSP00000371230.

    Structurei

    Secondary structure

    1
    227
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi9 – 146
    Helixi20 – 3011
    Beta strandi31 – 377
    Helixi38 – 4811
    Helixi51 – 6010
    Turni61 – 633
    Helixi68 – 8013
    Beta strandi87 – 915
    Helixi96 – 1038
    Beta strandi110 – 1156
    Helixi118 – 1258
    Beta strandi128 – 1314
    Turni132 – 1354
    Beta strandi136 – 1394
    Turni140 – 1423
    Turni152 – 1543
    Helixi162 – 1643
    Helixi166 – 18924
    Beta strandi193 – 1975
    Helixi201 – 21212
    Turni213 – 2153

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZD8X-ray1.48A1-227[»]
    ProteinModelPortaliQ9UIJ7.
    SMRiQ9UIJ7. Positions 7-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UIJ7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni37 – 6630NMPbindAdd
    BLAST
    Regioni127 – 16438LIDAdd
    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 binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP hydrolysis.

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0563.
    HOGENOMiHOG000238772.
    HOVERGENiHBG000458.
    InParanoidiQ9UIJ7.
    KOiK00944.
    OMAiIAGRWVH.
    OrthoDBiEOG74TX0R.
    PhylomeDBiQ9UIJ7.
    TreeFamiTF312916.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    HAMAPiMF_00235. Adenylate_kinase_Adk.
    MF_03169. Adenylate_kinase_AK3.
    InterProiIPR006259. Adenyl_kin_sub.
    IPR000850. Adenylat/UMP-CMP_kin.
    IPR007862. Adenylate_kinase_lid-dom.
    IPR028586. AK3/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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UIJ7-1) [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

    MGASARLLRA VIMGAPGSGK GTVSSRITTH FELKHLSSGD LLRDNMLRGT    50
    EIGVLAKAFI DQGKLIPDDV MTRLALHELK NLTQYSWLLD GFPRTLPQAE 100
    ALDRAYQIDT VINLNVPFEV IKQRLTARWI HPASGRVYNI EFNPPKTVGI 150
    DDLTGEPLIQ REDDKPETVI KRLKAYEDQT KPVLEYYQKK GVLETFSGTE 200
    TNKIWPYVYA FLQTKVPQRS QKASVTP 227
    Length:227
    Mass (Da):25,565
    Last modified:January 23, 2007 - v4
    Checksum:i98A0EDF4FD9C9CEF
    GO
    Isoform 2 (identifier: Q9UIJ7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-70: Missing.

    Show »
    Length:158
    Mass (Da):18,323
    Checksum:iC7DA98633182FC79
    GO
    Isoform 3 (identifier: Q9UIJ7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         51-90: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:187
    Mass (Da):21,014
    Checksum:i107B098298461090
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51A → G in BAA87913. (PubMed:11485571)Curated
    Sequence conflicti38 – 381S → R in BAA87913. (PubMed:11485571)Curated
    Sequence conflicti57 – 571K → Q in BAA87913. (PubMed:11485571)Curated
    Sequence conflicti69 – 713DVM → YVT in BAA87913. (PubMed:11485571)Curated
    Sequence conflicti181 – 1811K → E in BAG60470. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 7069Missing in isoform 2. 2 PublicationsVSP_043090Add
    BLAST
    Alternative sequencei51 – 9040Missing in isoform 3. 1 PublicationVSP_044876Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021870 mRNA. Translation: BAA87913.1.
    AF183419 mRNA. Translation: AAG09688.1.
    AK001553 mRNA. Translation: BAA91753.1.
    AK001951 mRNA. Translation: BAA91996.1.
    AK027534 mRNA. Translation: BAB55183.1.
    AK098205 mRNA. Translation: BAG53592.1.
    AK298200 mRNA. Translation: BAG60470.1.
    AL136231, AL353151 Genomic DNA. Translation: CAI41262.1.
    AL353151, AL136231 Genomic DNA. Translation: CAH72282.1.
    AL136231, AL353151 Genomic DNA. Translation: CAI41260.1.
    AL353151, AL136231 Genomic DNA. Translation: CAH72283.1.
    CH471071 Genomic DNA. Translation: EAW58779.1.
    CH471071 Genomic DNA. Translation: EAW58780.1.
    CH471071 Genomic DNA. Translation: EAW58781.1.
    BC013771 mRNA. Translation: AAH13771.1.
    CCDSiCCDS56562.1. [Q9UIJ7-3]
    CCDS6455.1. [Q9UIJ7-1]
    RefSeqiNP_001186781.1. NM_001199852.1. [Q9UIJ7-3]
    NP_001186782.1. NM_001199853.1.
    NP_001186784.1. NM_001199855.1.
    NP_001186785.1. NM_001199856.1.
    NP_057366.2. NM_016282.3. [Q9UIJ7-1]
    UniGeneiHs.732022.

    Genome annotation databases

    EnsembliENST00000359883; ENSP00000352948; ENSG00000147853.
    ENST00000381809; ENSP00000371230; ENSG00000147853. [Q9UIJ7-1]
    ENST00000447596; ENSP00000413933; ENSG00000147853. [Q9UIJ7-3]
    GeneIDi50808.
    KEGGihsa:50808.
    UCSCiuc003ziq.2. human. [Q9UIJ7-1]

    Polymorphism databases

    DMDMi23831297.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021870 mRNA. Translation: BAA87913.1 .
    AF183419 mRNA. Translation: AAG09688.1 .
    AK001553 mRNA. Translation: BAA91753.1 .
    AK001951 mRNA. Translation: BAA91996.1 .
    AK027534 mRNA. Translation: BAB55183.1 .
    AK098205 mRNA. Translation: BAG53592.1 .
    AK298200 mRNA. Translation: BAG60470.1 .
    AL136231 , AL353151 Genomic DNA. Translation: CAI41262.1 .
    AL353151 , AL136231 Genomic DNA. Translation: CAH72282.1 .
    AL136231 , AL353151 Genomic DNA. Translation: CAI41260.1 .
    AL353151 , AL136231 Genomic DNA. Translation: CAH72283.1 .
    CH471071 Genomic DNA. Translation: EAW58779.1 .
    CH471071 Genomic DNA. Translation: EAW58780.1 .
    CH471071 Genomic DNA. Translation: EAW58781.1 .
    BC013771 mRNA. Translation: AAH13771.1 .
    CCDSi CCDS56562.1. [Q9UIJ7-3 ]
    CCDS6455.1. [Q9UIJ7-1 ]
    RefSeqi NP_001186781.1. NM_001199852.1. [Q9UIJ7-3 ]
    NP_001186782.1. NM_001199853.1.
    NP_001186784.1. NM_001199855.1.
    NP_001186785.1. NM_001199856.1.
    NP_057366.2. NM_016282.3. [Q9UIJ7-1 ]
    UniGenei Hs.732022.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZD8 X-ray 1.48 A 1-227 [» ]
    ProteinModelPortali Q9UIJ7.
    SMRi Q9UIJ7. Positions 7-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119127. 5 interactions.
    IntActi Q9UIJ7. 2 interactions.
    STRINGi 9606.ENSP00000371230.

    PTM databases

    PhosphoSitei Q9UIJ7.

    Polymorphism databases

    DMDMi 23831297.

    2D gel databases

    OGPi Q9UIJ7.
    REPRODUCTION-2DPAGE IPI00465256.
    UCD-2DPAGE Q9UIJ7.

    Proteomic databases

    MaxQBi Q9UIJ7.
    PaxDbi Q9UIJ7.
    PRIDEi Q9UIJ7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000359883 ; ENSP00000352948 ; ENSG00000147853 .
    ENST00000381809 ; ENSP00000371230 ; ENSG00000147853 . [Q9UIJ7-1 ]
    ENST00000447596 ; ENSP00000413933 ; ENSG00000147853 . [Q9UIJ7-3 ]
    GeneIDi 50808.
    KEGGi hsa:50808.
    UCSCi uc003ziq.2. human. [Q9UIJ7-1 ]

    Organism-specific databases

    CTDi 50808.
    GeneCardsi GC09M004703.
    HGNCi HGNC:17376. AK3.
    MIMi 609290. gene.
    neXtProti NX_Q9UIJ7.
    PharmGKBi PA164741184.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0563.
    HOGENOMi HOG000238772.
    HOVERGENi HBG000458.
    InParanoidi Q9UIJ7.
    KOi K00944.
    OMAi IAGRWVH.
    OrthoDBi EOG74TX0R.
    PhylomeDBi Q9UIJ7.
    TreeFami TF312916.

    Enzyme and pathway databases

    Reactomei REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    ChiTaRSi AK3. human.
    EvolutionaryTracei Q9UIJ7.
    GenomeRNAii 50808.
    NextBioi 53246.
    PROi Q9UIJ7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UIJ7.
    CleanExi HS_AK3.
    HS_AK3L1.
    Genevestigatori Q9UIJ7.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    HAMAPi MF_00235. Adenylate_kinase_Adk.
    MF_03169. Adenylate_kinase_AK3.
    InterProi IPR006259. Adenyl_kin_sub.
    IPR000850. Adenylat/UMP-CMP_kin.
    IPR007862. Adenylate_kinase_lid-dom.
    IPR028586. AK3/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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Liver.
    2. "A novel gene expressed in human pheochromocytoma."
      Li Y., Peng Y., Jiang Z., Gu W., Han Z., Chen Z.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Pheochromocytoma.
    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] (ISOFORMS 1; 2 AND 3).
      Tissue: Placenta.
    4. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Structure of human adenylate kinase 3-like 1."
      Structural genomics consortium (SGC)
      Submitted (MAY-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS).

    Entry informationi

    Entry nameiKAD3_HUMAN
    AccessioniPrimary (citable) accession number: Q9UIJ7
    Secondary accession number(s): B4DP58
    , D3DRI1, E7ET30, Q5VYW6, Q9H576, Q9HC01, Q9NPB4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 139 of the entry and version 4 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 9
      Human chromosome 9: 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