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Q9NZJ9

- NUDT4_HUMAN

UniProt

Q9NZJ9 - NUDT4_HUMAN

Protein

Diphosphoinositol polyphosphate phosphohydrolase 2

Gene

NUDT4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (05 Jul 2005)
      Previous versions | rss
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    Functioni

    Cleaves a beta-phosphate from the diphosphate groups in PP-InsP5 (diphosphoinositol pentakisphosphate), PP-InsP4 and [PP]2-InsP4 (bisdiphosphoinositol tetrakisphosphate), suggesting that it may play a role in signal transduction. Also able to catalyze the hydrolysis of dinucleoside oligophosphate Ap6A, but not Ap5A. The major reaction products are ADP and p4a from Ap6A. Also able to hydrolyze 5-phosphoribose 1-diphosphate. Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA.1 Publication

    Catalytic activityi

    Diphospho-myo-inositol polyphosphate + H2O = myo-inositol polyphosphate + phosphate.2 Publications

    Cofactori

    Binds 3 magnesium or manganese ions per subunit.By similarity

    Kineticsi

    1. KM=4.2 nM for PP-InsP51 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101SubstrateBy similarity
    Binding sitei41 – 411SubstrateBy similarity
    Metal bindingi50 – 501Magnesium 1; via carbonyl oxygenBy similarity
    Metal bindingi66 – 661Magnesium 2By similarity
    Metal bindingi66 – 661Magnesium 3By similarity
    Active sitei69 – 691Proton acceptorBy similarity
    Metal bindingi70 – 701Magnesium 1By similarity

    GO - Molecular functioni

    1. diphosphoinositol-polyphosphate diphosphatase activity Source: UniProtKB
    2. inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 1-diphosphatase activity Source: UniProtKB-EC
    3. inositol-1,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity Source: UniProtKB-EC
    4. inositol-1-diphosphate-2,3,4,5,6-pentakisphosphate diphosphatase activity Source: UniProtKB-EC
    5. inositol-3,5-bisdiphosphate-2,3,4,6-tetrakisphosphate 5-diphosphatase activity Source: UniProtKB-EC
    6. inositol-3-diphosphate-1,2,4,5,6-pentakisphosphate diphosphatase activity Source: UniProtKB-EC
    7. inositol-5-diphosphate-1,2,3,4,6-pentakisphosphate diphosphatase activity Source: UniProtKB-EC
    8. inositol diphosphate tetrakisphosphate diphosphatase activity Source: Reactome
    9. metal ion binding Source: UniProtKB-KW
    10. snoRNA binding Source: UniProtKB

    GO - Biological processi

    1. calcium-mediated signaling Source: UniProtKB
    2. cyclic-nucleotide-mediated signaling Source: UniProtKB
    3. cyclic nucleotide metabolic process Source: ProtInc
    4. inositol phosphate metabolic process Source: Reactome
    5. intracellular signal transduction Source: UniProtKB
    6. intracellular transport Source: UniProtKB
    7. regulation of RNA export from nucleus Source: UniProtKB
    8. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, RNA-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS10696-MONOMER.
    ReactomeiREACT_150188. Synthesis of pyrophosphates in the cytosol.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Diphosphoinositol polyphosphate phosphohydrolase 2 (EC:3.6.1.52)
    Short name:
    DIPP-2
    Alternative name(s):
    Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 2 (EC:3.6.1.-)
    Nucleoside diphosphate-linked moiety X motif 4
    Short name:
    Nudix motif 4
    Gene namesi
    Name:NUDT4
    Synonyms:DIPP2, KIAA0487
    ORF Names:HDCMB47P
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:8051. NUDT4.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. intracellular Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31835.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 180180Diphosphoinositol polyphosphate phosphohydrolase 2PRO_0000057058Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NZJ9.
    PRIDEiQ9NZJ9.

    PTM databases

    PhosphoSiteiQ9NZJ9.

    Expressioni

    Tissue specificityi

    Expressed in heart and, at lower level in skeletal muscle, pancreas and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ9NZJ9.
    BgeeiQ9NZJ9.
    CleanExiHS_NUDT4.
    GenevestigatoriQ9NZJ9.

    Organism-specific databases

    HPAiHPA017593.

    Interactioni

    Protein-protein interaction databases

    BioGridi116334. 1 interaction.
    MINTiMINT-2819936.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NZJ9.
    SMRiQ9NZJ9. Positions 9-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 144127Nudix hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni18 – 203Substrate bindingBy similarity
    Regioni89 – 913Substrate bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi51 – 7222Nudix boxAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    HOVERGENiHBG053341.
    InParanoidiQ9NZJ9.
    KOiK07766.
    OMAiLQTWEEN.
    OrthoDBiEOG7T7GVQ.
    PhylomeDBiQ9NZJ9.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NZJ9-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha, DIPP2alpha

    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

    MMKFKPNQTR TYDREGFKKR AACLCFRSEQ EDEVLLVSSS RYPDQWIVPG    50
    GGMEPEEEPG GAAVREVYEE AGVKGKLGRL LGIFENQDRK HRTYVYVLTV 100
    TEILEDWEDS VNIGRKREWF KVEDAIKVLQ CHKPVHAEYL EKLKLGCSPA 150
    NGNSTVPSLP DNNALFVTAA QTSGLPSSVR 180
    Length:180
    Mass (Da):20,306
    Last modified:July 5, 2005 - v2
    Checksum:i86D766F8F5B22D13
    GO
    Isoform 2 (identifier: Q9NZJ9-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta, DIPP2beta

    The sequence of this isoform differs from the canonical sequence as follows:
         85-85: E → EQ

    Show »
    Length:181
    Mass (Da):20,434
    Checksum:iCB3C131FAD21A4AA
    GO
    Isoform 3 (identifier: Q9NZJ9-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-52: Missing.
         85-85: E → EQ

    Show »
    Length:129
    Mass (Da):14,395
    Checksum:i2A8C483085B2D4D3
    GO

    Sequence cautioni

    The sequence BAE16985.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAF75563.1 differs from that shown. Reason: Erroneous termination at position 181. Translated as stop.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161G → D in AAF68857. (PubMed:10777568)Curated
    Sequence conflicti41 – 411R → Q in BAD97217. 1 PublicationCurated
    Sequence conflicti73 – 731V → D in AAF75563. 1 PublicationCurated
    Sequence conflicti164 – 1641A → V in AAF68857. (PubMed:10777568)Curated
    Sequence conflicti177 – 1771S → P in AAF68858. (PubMed:10777568)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5252Missing in isoform 3. 3 PublicationsVSP_014269Add
    BLAST
    Alternative sequencei85 – 851E → EQ in isoform 2 and isoform 3. 6 PublicationsVSP_014270

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191649 mRNA. Translation: AAF68855.1.
    AF191650 mRNA. Translation: AAF68856.1.
    AF191651 mRNA. Translation: AAF68857.1.
    AF191652 mRNA. Translation: AAF68858.2.
    AF191653 mRNA. Translation: AAF68859.1.
    AB007956 mRNA. Translation: BAE16985.1. Different initiation.
    AF067803 mRNA. Translation: AAF75563.1. Sequence problems.
    CR749445 mRNA. Translation: CAH18283.1.
    BT020109 mRNA. Translation: AAV38912.1.
    BT020110 mRNA. Translation: AAV38913.1.
    AK304296 mRNA. Translation: BAH14152.1.
    AK223497 mRNA. Translation: BAD97217.1.
    BC012069 mRNA. Translation: AAH12069.1.
    BC051310 mRNA. Translation: AAH51310.1.
    CCDSiCCDS44952.1. [Q9NZJ9-1]
    CCDS9044.1. [Q9NZJ9-2]
    RefSeqiNP_061967.3. NM_019094.4. [Q9NZJ9-1]
    NP_950241.1. NM_199040.2. [Q9NZJ9-2]
    XP_005268652.1. XM_005268595.2. [Q9NZJ9-3]
    UniGeneiHs.506325.

    Genome annotation databases

    EnsembliENST00000337179; ENSP00000338352; ENSG00000173598. [Q9NZJ9-2]
    ENST00000415493; ENSP00000406612; ENSG00000173598. [Q9NZJ9-1]
    ENST00000547014; ENSP00000448032; ENSG00000173598. [Q9NZJ9-3]
    ENST00000548662; ENSP00000449724; ENSG00000173598.
    ENST00000549992; ENSP00000449552; ENSG00000173598.
    GeneIDi11163.
    KEGGihsa:11163.
    UCSCiuc001tcm.3. human. [Q9NZJ9-1]
    uc010sup.2. human. [Q9NZJ9-2]
    uc010suq.2. human. [Q9NZJ9-3]

    Polymorphism databases

    DMDMi68565946.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191649 mRNA. Translation: AAF68855.1 .
    AF191650 mRNA. Translation: AAF68856.1 .
    AF191651 mRNA. Translation: AAF68857.1 .
    AF191652 mRNA. Translation: AAF68858.2 .
    AF191653 mRNA. Translation: AAF68859.1 .
    AB007956 mRNA. Translation: BAE16985.1 . Different initiation.
    AF067803 mRNA. Translation: AAF75563.1 . Sequence problems.
    CR749445 mRNA. Translation: CAH18283.1 .
    BT020109 mRNA. Translation: AAV38912.1 .
    BT020110 mRNA. Translation: AAV38913.1 .
    AK304296 mRNA. Translation: BAH14152.1 .
    AK223497 mRNA. Translation: BAD97217.1 .
    BC012069 mRNA. Translation: AAH12069.1 .
    BC051310 mRNA. Translation: AAH51310.1 .
    CCDSi CCDS44952.1. [Q9NZJ9-1 ]
    CCDS9044.1. [Q9NZJ9-2 ]
    RefSeqi NP_061967.3. NM_019094.4. [Q9NZJ9-1 ]
    NP_950241.1. NM_199040.2. [Q9NZJ9-2 ]
    XP_005268652.1. XM_005268595.2. [Q9NZJ9-3 ]
    UniGenei Hs.506325.

    3D structure databases

    ProteinModelPortali Q9NZJ9.
    SMRi Q9NZJ9. Positions 9-146.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116334. 1 interaction.
    MINTi MINT-2819936.

    PTM databases

    PhosphoSitei Q9NZJ9.

    Polymorphism databases

    DMDMi 68565946.

    Proteomic databases

    MaxQBi Q9NZJ9.
    PRIDEi Q9NZJ9.

    Protocols and materials databases

    DNASUi 11163.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337179 ; ENSP00000338352 ; ENSG00000173598 . [Q9NZJ9-2 ]
    ENST00000415493 ; ENSP00000406612 ; ENSG00000173598 . [Q9NZJ9-1 ]
    ENST00000547014 ; ENSP00000448032 ; ENSG00000173598 . [Q9NZJ9-3 ]
    ENST00000548662 ; ENSP00000449724 ; ENSG00000173598 .
    ENST00000549992 ; ENSP00000449552 ; ENSG00000173598 .
    GeneIDi 11163.
    KEGGi hsa:11163.
    UCSCi uc001tcm.3. human. [Q9NZJ9-1 ]
    uc010sup.2. human. [Q9NZJ9-2 ]
    uc010suq.2. human. [Q9NZJ9-3 ]

    Organism-specific databases

    CTDi 11163.
    GeneCardsi GC12P093771.
    HGNCi HGNC:8051. NUDT4.
    HPAi HPA017593.
    MIMi 609229. gene.
    neXtProti NX_Q9NZJ9.
    PharmGKBi PA31835.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    HOVERGENi HBG053341.
    InParanoidi Q9NZJ9.
    KOi K07766.
    OMAi LQTWEEN.
    OrthoDBi EOG7T7GVQ.
    PhylomeDBi Q9NZJ9.
    TreeFami TF106349.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS10696-MONOMER.
    Reactomei REACT_150188. Synthesis of pyrophosphates in the cytosol.

    Miscellaneous databases

    ChiTaRSi NUDT4. human.
    GeneWikii NUDT4.
    GenomeRNAii 11163.
    NextBioi 42469.
    PROi Q9NZJ9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NZJ9.
    Bgeei Q9NZJ9.
    CleanExi HS_NUDT4.
    Genevestigatori Q9NZJ9.

    Family and domain databases

    Gene3Di 3.90.79.10. 1 hit.
    InterProi IPR020084. NUDIX_hydrolase_CS.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view ]
    Pfami PF00293. NUDIX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55811. SSF55811. 1 hit.
    PROSITEi PS51462. NUDIX. 1 hit.
    PS00893. NUDIX_BOX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. The expanding NUDT family."
      Caffrey J.J., Safrany S.T., Yang X., Shears S.B.
      J. Biol. Chem. 275:12730-12736(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
      Tissue: Cerebellum.
    2. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
      Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
      DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "Novel gene identified from dendritic cells."
      Zhao Z., Huang X., Li N., Zhu X., Cao X.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Retina.
    5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    6. "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] (ISOFORM 3).
      Tissue: Trachea.
    7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    8. "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: Lymph and Placenta.
    9. "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: SUBCELLULAR LOCATION.
    10. "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: ENZYME ACTIVITY.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNUDT4_HUMAN
    AccessioniPrimary (citable) accession number: Q9NZJ9
    Secondary accession number(s): B7Z916
    , Q4AEJ6, Q53EZ2, Q68DD7, Q9NPC5, Q9NS30, Q9NZK0, Q9NZK1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 125 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3