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Protein

Diphosphoinositol polyphosphate phosphohydrolase 3-alpha

Gene

NUDT10

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

Functioni

Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being the preferred substrates. The major reaction products are ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-phosphoribose 1-diphosphate.1 Publication

Catalytic activityi

Diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.3 Publications
P1,P(6)-bis(5'-adenosyl)hexaphosphate + H2O = adenosine 5'-pentaphosphate + AMP.3 Publications
P1,P(5)-bis(5'-adenosyl)pentaphosphate + H2O = adenosine 5'-tetraphosphate + AMP.3 Publications

Cofactori

Mg2+By similarity1 Publication, Mn2+By similarity1 PublicationNote: Binds 3 Mg2+ or Mn2+ ions per subunit. Mn2+ may be the true cofactor in vivo.By similarity1 Publication

Kineticsi

  1. KM=0.088 µM for PP-InsP52 Publications
  2. KM=19 µM for Ap6A2 Publications
  3. KM=50 µM for Ap5A2 Publications

    pH dependencei

    Optimum pH is 8.5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei9 – 91SubstrateBy similarity
    Binding sitei40 – 401SubstrateBy similarity
    Metal bindingi49 – 491Magnesium 1; via carbonyl oxygenBy similarity
    Metal bindingi65 – 651Magnesium 2By similarity
    Metal bindingi65 – 651Magnesium 3By similarity
    Active sitei68 – 681Proton acceptorBy similarity
    Metal bindingi69 – 691Magnesium 1By similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04604-MONOMER.
    BRENDAi3.6.1.60. 2681.
    ReactomeiR-HSA-1855167. Synthesis of pyrophosphates in the cytosol.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Diphosphoinositol polyphosphate phosphohydrolase 3-alpha1 Publication (EC:3.6.1.523 Publications)
    Short name:
    DIPP-3-alpha
    Short name:
    DIPP3-alpha1 Publication
    Short name:
    hDIPP3alpha1 Publication
    Alternative name(s):
    Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha
    Diadenosine hexaphosphate hydrolase (AMP-forming) (EC:3.6.1.603 Publications)
    Nucleoside diphosphate-linked moiety X motif 10
    Short name:
    Nudix motif 10
    hAps2
    Gene namesi
    Name:NUDT10
    Synonyms:APS2, DIPP3A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:17621. NUDT10.

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31831.

    Polymorphism and mutation databases

    BioMutaiNUDT10.
    DMDMi68565913.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 164164Diphosphoinositol polyphosphate phosphohydrolase 3-alphaPRO_0000057062Add
    BLAST

    Proteomic databases

    EPDiQ8NFP7.
    MaxQBiQ8NFP7.
    PaxDbiQ8NFP7.
    PRIDEiQ8NFP7.

    PTM databases

    iPTMnetiQ8NFP7.
    PhosphoSiteiQ8NFP7.

    Expressioni

    Tissue specificityi

    Mainly expressed in testis and, at lower level in brain. According to PubMed:12121577, it is widely expressed.2 Publications

    Gene expression databases

    BgeeiQ8NFP7.
    CleanExiHS_NUDT10.
    GenevisibleiQ8NFP7. HS.

    Organism-specific databases

    HPAiHPA047027.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MTUS2Q5JR593EBI-726826,EBI-742948
    SNAPC5O759713EBI-726826,EBI-749483
    TCF4P158843EBI-726826,EBI-533224

    Protein-protein interaction databases

    BioGridi128079. 3 interactions.
    IntActiQ8NFP7. 5 interactions.
    MINTiMINT-1383448.
    STRINGi9606.ENSP00000348831.

    Structurei

    Secondary structure

    1
    164
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 2710Combined sources
    Beta strandi32 – 376Combined sources
    Beta strandi39 – 413Combined sources
    Beta strandi44 – 463Combined sources
    Beta strandi49 – 513Combined sources
    Helixi58 – 7013Combined sources
    Beta strandi72 – 8312Combined sources
    Beta strandi92 – 10312Combined sources
    Helixi108 – 1136Combined sources
    Beta strandi117 – 1215Combined sources
    Helixi122 – 1309Combined sources
    Helixi134 – 14411Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MCFX-ray2.00A/B17-144[»]
    ProteinModelPortaliQ8NFP7.
    SMRiQ8NFP7. Positions 17-144.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8NFP7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 144128Nudix hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni17 – 193Substrate bindingBy similarity
    Regioni89 – 913Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi50 – 7122Nudix boxAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Nudix hydrolase family. DIPP subfamily.Curated
    Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiKOG2839. Eukaryota.
    COG0494. LUCA.
    GeneTreeiENSGT00390000012928.
    HOGENOMiHOG000237336.
    HOVERGENiHBG053341.
    InParanoidiQ8NFP7.
    KOiK07766.
    OMAiCKANQTR.
    OrthoDBiEOG7T7GVQ.
    PhylomeDBiQ8NFP7.
    TreeFamiTF106349.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiIPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PfamiPF00293. NUDIX. 1 hit.
    [Graphical view]
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiPS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8NFP7-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKCKPNQTRT YDPEGFKKRA ACLCFRSERE DEVLLVSSSR YPDRWIVPGG
    60 70 80 90 100
    GMEPEEEPGG AAVREVYEEA GVKGKLGRLL GVFEQNQDPK HRTYVYVLTV
    110 120 130 140 150
    TELLEDWEDS VSIGRKREWF KVEDAIKVLQ CHKPVHAEYL EKLKLGGSPT
    160
    NGNSMAPSSP DSDP
    Length:164
    Mass (Da):18,500
    Last modified:October 1, 2002 - v1
    Checksum:i589F342E02B285A7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901K → E in AAH50700 (PubMed:15489334).Curated
    Sequence conflicti135 – 1351V → M in AAH49383 (PubMed:15489334).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF469196 mRNA. Translation: AAM64113.1.
    AK291952 mRNA. Translation: BAF84641.1.
    AL158055 Genomic DNA. Translation: CAI40295.1.
    CH471180 Genomic DNA. Translation: EAW89910.1.
    CH471180 Genomic DNA. Translation: EAW89911.1.
    BC049383 mRNA. Translation: AAH49383.1.
    BC050700 mRNA. Translation: AAH50700.1.
    CCDSiCCDS35278.1.
    RefSeqiNP_001291892.1. NM_001304963.1.
    NP_694853.1. NM_153183.3.
    UniGeneiHs.375178.

    Genome annotation databases

    EnsembliENST00000356450; ENSP00000348831; ENSG00000122824.
    ENST00000376006; ENSP00000365174; ENSG00000122824.
    GeneIDi170685.
    KEGGihsa:170685.
    UCSCiuc004dph.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF469196 mRNA. Translation: AAM64113.1.
    AK291952 mRNA. Translation: BAF84641.1.
    AL158055 Genomic DNA. Translation: CAI40295.1.
    CH471180 Genomic DNA. Translation: EAW89910.1.
    CH471180 Genomic DNA. Translation: EAW89911.1.
    BC049383 mRNA. Translation: AAH49383.1.
    BC050700 mRNA. Translation: AAH50700.1.
    CCDSiCCDS35278.1.
    RefSeqiNP_001291892.1. NM_001304963.1.
    NP_694853.1. NM_153183.3.
    UniGeneiHs.375178.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MCFX-ray2.00A/B17-144[»]
    ProteinModelPortaliQ8NFP7.
    SMRiQ8NFP7. Positions 17-144.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi128079. 3 interactions.
    IntActiQ8NFP7. 5 interactions.
    MINTiMINT-1383448.
    STRINGi9606.ENSP00000348831.

    PTM databases

    iPTMnetiQ8NFP7.
    PhosphoSiteiQ8NFP7.

    Polymorphism and mutation databases

    BioMutaiNUDT10.
    DMDMi68565913.

    Proteomic databases

    EPDiQ8NFP7.
    MaxQBiQ8NFP7.
    PaxDbiQ8NFP7.
    PRIDEiQ8NFP7.

    Protocols and materials databases

    DNASUi170685.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000356450; ENSP00000348831; ENSG00000122824.
    ENST00000376006; ENSP00000365174; ENSG00000122824.
    GeneIDi170685.
    KEGGihsa:170685.
    UCSCiuc004dph.3. human.

    Organism-specific databases

    CTDi170685.
    GeneCardsiNUDT10.
    HGNCiHGNC:17621. NUDT10.
    HPAiHPA047027.
    MIMi300527. gene.
    neXtProtiNX_Q8NFP7.
    PharmGKBiPA31831.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG2839. Eukaryota.
    COG0494. LUCA.
    GeneTreeiENSGT00390000012928.
    HOGENOMiHOG000237336.
    HOVERGENiHBG053341.
    InParanoidiQ8NFP7.
    KOiK07766.
    OMAiCKANQTR.
    OrthoDBiEOG7T7GVQ.
    PhylomeDBiQ8NFP7.
    TreeFamiTF106349.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04604-MONOMER.
    BRENDAi3.6.1.60. 2681.
    ReactomeiR-HSA-1855167. Synthesis of pyrophosphates in the cytosol.

    Miscellaneous databases

    ChiTaRSiNUDT10. human.
    EvolutionaryTraceiQ8NFP7.
    GenomeRNAii170685.
    PROiQ8NFP7.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8NFP7.
    CleanExiHS_NUDT10.
    GenevisibleiQ8NFP7. HS.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiIPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PfamiPF00293. NUDIX. 1 hit.
    [Graphical view]
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiPS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "An adjacent pair of human NUDT genes on chromosome X are preferentially expressed in testis and encode two new isoforms of diphosphoinositol polyphosphate phosphohydrolase."
      Hidaka K., Caffrey J.J., Hua L., Zhang T., Falck J.R., Nickel G.C., Carrel L., Barnes L.D., Shears S.B.
      J. Biol. Chem. 277:32730-32738(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    2. "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].
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Ovary.
    6. "Cloning and characterisation of hAps1 and hAps2, human diadenosine polyphosphate-metabolising Nudix hydrolases."
      Leslie N.R., McLennan A.G., Safrany S.T.
      BMC Biochem. 3:20-20(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    7. "Nudix hydrolases that degrade dinucleoside and diphosphoinositol polyphosphates also have 5-phosphoribosyl 1-pyrophosphate (PRPP) pyrophosphatase activity that generates the glycolytic activator ribose 1,5-bisphosphate."
      Fisher D.I., Safrany S.T., Strike P., McLennan A.G., Cartwright J.L.
      J. Biol. Chem. 277:47313-47317(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Crystal structure of human diphosphoinositol polyphosphate phosphohydrolase 3-alpha."
      Structural genomics consortium (SGC)
      Submitted (APR-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 17-144 IN COMPLEX WITH CITRATE.

    Entry informationi

    Entry nameiNUD10_HUMAN
    AccessioniPrimary (citable) accession number: Q8NFP7
    Secondary accession number(s): A8K7D7
    , D3DX69, Q86VK1, Q86VR0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: October 1, 2002
    Last modified: June 8, 2016
    This is version 121 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 X
      Human chromosome X: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.