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P16858

- G3P_MOUSE

UniProt

P16858 - G3P_MOUSE

Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

Gapdh

Organism
Mus musculus (Mouse)
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

    Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Modulates the organization and assembly of the cytoskeleton. Facilitates the CHP1-dependent microtubule and membrane associations through its ability to stimulate the binding of CHP1 to microtubules. Also participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC. Component of the GAIT (gamma interferon-activated inhibitor of translation) complex which mediates interferon-gamma-induced transcript-selective translation inhibition in inflammation processes. Upon interferon-gamma treatment assembles into the GAIT complex which binds to stem loop-containing GAIT elements in the 3'-UTR of diverse inflammatory mRNAs (such as ceruplasmin) and suppresses their translation.1 Publication

    Catalytic activityi

    D-glyceraldehyde 3-phosphate + phosphate + NAD+ = 3-phospho-D-glyceroyl phosphate + NADH.1 PublicationPROSITE-ProRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei33 – 331NADBy similarity
    Binding sitei78 – 781NAD; via carbonyl oxygenBy similarity
    Binding sitei120 – 1201NADBy similarity
    Active sitei150 – 1501NucleophilePROSITE-ProRule annotation
    Sitei177 – 1771Activates thiol group during catalysisBy similarity
    Binding sitei180 – 1801Glyceraldehyde 3-phosphateBy similarity
    Binding sitei232 – 2321Glyceraldehyde 3-phosphateBy similarity
    Binding sitei314 – 3141NADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi11 – 122NADBy similarity

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
    3. microtubule binding Source: UniProtKB
    4. NAD binding Source: InterPro
    5. NADP binding Source: InterPro
    6. peptidyl-cysteine S-nitrosylase activity Source: UniProtKB
    7. protein binding Source: IntAct

    GO - Biological processi

    1. glucose metabolic process Source: InterPro
    2. glycolytic process Source: UniProtKB-UniPathway
    3. microtubule cytoskeleton organization Source: UniProtKB
    4. negative regulation of translation Source: UniProtKB
    5. neuron apoptotic process Source: UniProtKB
    6. peptidyl-cysteine S-trans-nitrosylation Source: UniProtKB
    7. protein stabilization Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Keywords - Biological processi

    Apoptosis, Glycolysis, Translation regulation

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    SABIO-RKP16858.
    UniPathwayiUPA00109; UER00184.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glyceraldehyde-3-phosphate dehydrogenase (EC:1.2.1.12)
    Short name:
    GAPDH
    Alternative name(s):
    Peptidyl-cysteine S-nitrosylase GAPDH (EC:2.6.99.-)
    Gene namesi
    Name:Gapdh
    Synonyms:Gapd
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:95640. Gapdh.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Nucleus By similarity. Cytoplasmcytoskeleton By similarity
    Note: Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. GAIT complex Source: UniProtKB
    4. microtubule cytoskeleton Source: UniProtKB
    5. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi150 – 1501C → S: Abolishes sulfhydration and induces impaired enzyme activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 333332Glyceraldehyde-3-phosphate dehydrogenasePRO_0000145490Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N6,N6-dimethyllysineBy similarity
    Modified residuei7 – 71Deamidated asparagineBy similarity
    Modified residuei40 – 401PhosphotyrosineBy similarity
    Modified residuei59 – 591N6-acetyllysineBy similarity
    Modified residuei62 – 621Deamidated asparagineBy similarity
    Modified residuei64 – 641N6,N6-dimethyllysineBy similarity
    Modified residuei68 – 681Deamidated asparagineBy similarity
    Modified residuei73 – 731PhosphothreonineBy similarity
    Modified residuei120 – 1201PhosphoserineBy similarity
    Modified residuei146 – 1461PhosphoserineBy similarity
    Modified residuei147 – 1471Deamidated asparagineBy similarity
    Modified residuei149 – 1491PhosphoserineBy similarity
    Modified residuei150 – 1501ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited formBy similarity
    Modified residuei150 – 1501Cysteine persulfide1 Publication
    Modified residuei150 – 1501S-nitrosocysteine; in reversibly inhibited formBy similarity
    Modified residuei153 – 1531Deamidated asparagineBy similarity
    Modified residuei182 – 1821PhosphothreonineBy similarity
    Modified residuei192 – 1921N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei192 – 1921N6-acetyllysine; alternateBy similarity
    Modified residuei192 – 1921N6-malonyllysine; alternateBy similarity
    Modified residuei209 – 2091PhosphothreonineBy similarity
    Modified residuei213 – 2131N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei213 – 2131N6-malonyllysine; alternateBy similarity
    Modified residuei217 – 2171N6-acetyllysineBy similarity
    Modified residuei223 – 2231Deamidated asparagineBy similarity
    Modified residuei225 – 2251N6,N6-dimethyllysine; alternateBy similarity
    Modified residuei225 – 2251N6-acetyllysine; alternateBy similarity
    Modified residuei227 – 2271PhosphothreonineBy similarity
    Modified residuei235 – 2351PhosphothreonineBy similarity
    Modified residuei252 – 2521N6-acetyllysineBy similarity
    Modified residuei258 – 2581N6,N6-dimethyllysineBy similarity
    Modified residuei261 – 2611N6,N6-dimethyllysineBy similarity
    Modified residuei310 – 3101PhosphoserineBy similarity
    Modified residuei314 – 3141Deamidated asparagineBy similarity
    Modified residuei332 – 3321N6,N6-dimethyllysineBy similarity

    Post-translational modificationi

    ISGylated.By similarity
    S-nitrosylation of Cys-150 leads to interaction with SIAH1, followed by translocation to the nucleus.By similarity
    Sulfhydration at Cys-150 increases catalytic activity.

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Methylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    MaxQBiP16858.
    PaxDbiP16858.
    PRIDEiP16858.

    2D gel databases

    REPRODUCTION-2DPAGEP16858.
    Q5U410.
    SWISS-2DPAGEP16858.

    PTM databases

    PhosphoSiteiP16858.

    Expressioni

    Gene expression databases

    BgeeiP16858.
    CleanExiMM_GAPDH.
    GenevestigatoriP16858.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with EIF1AD, USP25, PRKCI and WARS. Interacts with TPPP; the interaction is direct. Interacts (when S-nitrosylated) with SIAH1; leading to nuclear translocation. Interacts with RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and SIAH1 and prevent nuclear translocation. Interacts with CHP1; the interaction increases the binding of CHP1 with microtubules. Associates with microtubules. Interacts with FKBP6; leading to inhibit GAPDH catalytic activity By similarity. Component of the GAIT complex.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Kcnma1Q084603EBI-444871,EBI-1633915

    Protein-protein interaction databases

    BioGridi199829. 6 interactions.
    785307. 1 interaction.
    IntActiP16858. 18 interactions.
    MINTiMINT-1869564.

    Structurei

    3D structure databases

    ProteinModelPortaliP16858.
    SMRiP16858. Positions 2-333.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 146145Interaction with WARSBy similarityAdd
    BLAST
    Regioni149 – 1513Glyceraldehyde 3-phosphate bindingBy similarity
    Regioni209 – 2102Glyceraldehyde 3-phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0057.
    GeneTreeiENSGT00720000108591.
    HOVERGENiHBG000227.
    InParanoidiA6H6A8.
    KOiK00134.
    OrthoDBiEOG7Q5HDF.
    PhylomeDBiP16858.
    TreeFamiTF300533.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR020831. GlycerAld/Erythrose_P_DH.
    IPR020830. GlycerAld_3-P_DH_AS.
    IPR020829. GlycerAld_3-P_DH_cat.
    IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
    IPR006424. Glyceraldehyde-3-P_DH_1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PANTHERiPTHR10836. PTHR10836. 1 hit.
    PfamiPF02800. Gp_dh_C. 1 hit.
    PF00044. Gp_dh_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000149. GAP_DH. 1 hit.
    PRINTSiPR00078. G3PDHDRGNASE.
    SMARTiSM00846. Gp_dh_N. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
    PROSITEiPS00071. GAPDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P16858-1 [UniParc]FASTAAdd to Basket

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    MVKVGVNGFG RIGRLVTRAA ICSGKVEIVA INDPFIDLNY MVYMFQYDST    50
    HGKFNGTVKA ENGKLVINGK PITIFQERDP TNIKWGEAGA EYVVESTGVF 100
    TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNHEKYDN SLKIVSNASC 150
    TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT ATQKTVDGPS GKLWRDGRGA 200
    AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTCRLEKP 250
    AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSNSHS STFDAGAGIA 300
    LNDNFVKLIS WYDNEYGYSN RVVDLMAYMA SKE 333
    Length:333
    Mass (Da):35,810
    Last modified:January 23, 2007 - v2
    Checksum:iF25131EFFA9F2BD6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31K → E in BAE40174. (PubMed:16141072)Curated
    Sequence conflicti30 – 301A → V in AAH92267. (PubMed:15489334)Curated
    Sequence conflicti82 – 821N → S in BAE35989. (PubMed:16141072)Curated
    Sequence conflicti84 – 841K → E in BAE40174. (PubMed:16141072)Curated
    Sequence conflicti89 – 891G → S in BAE26016. (PubMed:16141072)Curated
    Sequence conflicti91 – 911E → K in BAE35989. (PubMed:16141072)Curated
    Sequence conflicti134 – 1341N → D in AAH85315. (PubMed:15489334)Curated
    Sequence conflicti195 – 1951R → C in AAH85315. (PubMed:15489334)Curated
    Sequence conflicti300 – 3001A → S in AAH85315. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32599 mRNA. Translation: AAA37659.1.
    AK002273 mRNA. Translation: BAB21979.1.
    AK081405 mRNA. Translation: BAC38211.1.
    AK140794 mRNA. Translation: BAE24481.1.
    AK144690 mRNA. Translation: BAE26016.1.
    AK146435 mRNA. Translation: BAE27169.1.
    AK147738 mRNA. Translation: BAE28105.1.
    AK147891 mRNA. Translation: BAE28208.1.
    AK160399 mRNA. Translation: BAE35768.1.
    AK160753 mRNA. Translation: BAE35989.1.
    AK164415 mRNA. Translation: BAE37778.1.
    AK168217 mRNA. Translation: BAE40174.1.
    AL662926 Genomic DNA. Translation: CAI25599.1.
    BC082592 mRNA. Translation: AAH82592.1.
    BC083065 mRNA. Translation: AAH83065.1.
    BC083079 mRNA. Translation: AAH83079.1.
    BC083080 mRNA. Translation: AAH83080.1.
    BC083149 mRNA. Translation: AAH83149.1.
    BC085274 mRNA. Translation: AAH85274.1.
    BC085275 mRNA. Translation: AAH85275.1.
    BC085315 mRNA. Translation: AAH85315.1.
    BC091768 mRNA. Translation: AAH91768.1.
    BC092252 mRNA. Translation: AAH92252.1.
    BC092264 mRNA. Translation: AAH92264.1.
    BC092267 mRNA. Translation: AAH92267.1.
    BC092294 mRNA. Translation: AAH92294.1.
    BC093508 mRNA. Translation: AAH93508.1.
    BC094037 mRNA. Translation: AAH94037.1.
    BC095932 mRNA. Translation: AAH95932.1.
    BC096440 mRNA. Translation: AAH96440.1.
    BC096590 mRNA. Translation: AAH96590.1.
    BC110311 mRNA. Translation: AAI10312.1.
    BC145810 mRNA. Translation: AAI45811.1.
    BC145812 mRNA. Translation: AAI45813.1.
    DQ403054 mRNA. Translation: ABD77187.1.
    CCDSiCCDS51913.1.
    PIRiJT0553. DEMSG.
    RefSeqiNP_001276655.1. NM_001289726.1.
    NP_032110.1. NM_008084.3.
    XP_001476757.1. XM_001476707.4.
    UniGeneiMm.304088.
    Mm.309092.
    Mm.317779.
    Mm.343110.
    Mm.392463.
    Mm.458138.
    Mm.458416.

    Genome annotation databases

    EnsembliENSMUST00000073605; ENSMUSP00000073289; ENSMUSG00000057666.
    ENSMUST00000118875; ENSMUSP00000113213; ENSMUSG00000057666.
    GeneIDi100042025.
    14433.
    KEGGimmu:100042025.
    mmu:14433.
    UCSCiuc007igj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M32599 mRNA. Translation: AAA37659.1 .
    AK002273 mRNA. Translation: BAB21979.1 .
    AK081405 mRNA. Translation: BAC38211.1 .
    AK140794 mRNA. Translation: BAE24481.1 .
    AK144690 mRNA. Translation: BAE26016.1 .
    AK146435 mRNA. Translation: BAE27169.1 .
    AK147738 mRNA. Translation: BAE28105.1 .
    AK147891 mRNA. Translation: BAE28208.1 .
    AK160399 mRNA. Translation: BAE35768.1 .
    AK160753 mRNA. Translation: BAE35989.1 .
    AK164415 mRNA. Translation: BAE37778.1 .
    AK168217 mRNA. Translation: BAE40174.1 .
    AL662926 Genomic DNA. Translation: CAI25599.1 .
    BC082592 mRNA. Translation: AAH82592.1 .
    BC083065 mRNA. Translation: AAH83065.1 .
    BC083079 mRNA. Translation: AAH83079.1 .
    BC083080 mRNA. Translation: AAH83080.1 .
    BC083149 mRNA. Translation: AAH83149.1 .
    BC085274 mRNA. Translation: AAH85274.1 .
    BC085275 mRNA. Translation: AAH85275.1 .
    BC085315 mRNA. Translation: AAH85315.1 .
    BC091768 mRNA. Translation: AAH91768.1 .
    BC092252 mRNA. Translation: AAH92252.1 .
    BC092264 mRNA. Translation: AAH92264.1 .
    BC092267 mRNA. Translation: AAH92267.1 .
    BC092294 mRNA. Translation: AAH92294.1 .
    BC093508 mRNA. Translation: AAH93508.1 .
    BC094037 mRNA. Translation: AAH94037.1 .
    BC095932 mRNA. Translation: AAH95932.1 .
    BC096440 mRNA. Translation: AAH96440.1 .
    BC096590 mRNA. Translation: AAH96590.1 .
    BC110311 mRNA. Translation: AAI10312.1 .
    BC145810 mRNA. Translation: AAI45811.1 .
    BC145812 mRNA. Translation: AAI45813.1 .
    DQ403054 mRNA. Translation: ABD77187.1 .
    CCDSi CCDS51913.1.
    PIRi JT0553. DEMSG.
    RefSeqi NP_001276655.1. NM_001289726.1.
    NP_032110.1. NM_008084.3.
    XP_001476757.1. XM_001476707.4.
    UniGenei Mm.304088.
    Mm.309092.
    Mm.317779.
    Mm.343110.
    Mm.392463.
    Mm.458138.
    Mm.458416.

    3D structure databases

    ProteinModelPortali P16858.
    SMRi P16858. Positions 2-333.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199829. 6 interactions.
    785307. 1 interaction.
    IntActi P16858. 18 interactions.
    MINTi MINT-1869564.

    PTM databases

    PhosphoSitei P16858.

    2D gel databases

    REPRODUCTION-2DPAGE P16858.
    Q5U410.
    SWISS-2DPAGE P16858.

    Proteomic databases

    MaxQBi P16858.
    PaxDbi P16858.
    PRIDEi P16858.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000073605 ; ENSMUSP00000073289 ; ENSMUSG00000057666 .
    ENSMUST00000118875 ; ENSMUSP00000113213 ; ENSMUSG00000057666 .
    GeneIDi 100042025.
    14433.
    KEGGi mmu:100042025.
    mmu:14433.
    UCSCi uc007igj.1. mouse.

    Organism-specific databases

    CTDi 2597.
    MGIi MGI:95640. Gapdh.

    Phylogenomic databases

    eggNOGi COG0057.
    GeneTreei ENSGT00720000108591.
    HOVERGENi HBG000227.
    InParanoidi A6H6A8.
    KOi K00134.
    OrthoDBi EOG7Q5HDF.
    PhylomeDBi P16858.
    TreeFami TF300533.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00184 .
    SABIO-RK P16858.

    Miscellaneous databases

    NextBioi 286057.
    PROi P16858.
    SOURCEi Search...

    Gene expression databases

    Bgeei P16858.
    CleanExi MM_GAPDH.
    Genevestigatori P16858.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR020831. GlycerAld/Erythrose_P_DH.
    IPR020830. GlycerAld_3-P_DH_AS.
    IPR020829. GlycerAld_3-P_DH_cat.
    IPR020828. GlycerAld_3-P_DH_NAD(P)-bd.
    IPR006424. Glyceraldehyde-3-P_DH_1.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    PANTHERi PTHR10836. PTHR10836. 1 hit.
    Pfami PF02800. Gp_dh_C. 1 hit.
    PF00044. Gp_dh_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000149. GAP_DH. 1 hit.
    PRINTSi PR00078. G3PDHDRGNASE.
    SMARTi SM00846. Gp_dh_N. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01534. GAPDH-I. 1 hit.
    PROSITEi PS00071. GAPDH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Glyceraldehyde-3-phosphate dehydrogenase mRNA is a major interleukin 2-induced transcript in a cloned T-helper lymphocyte."
      Sabath D.E., Broome H.E., Prystowsky M.B.
      Gene 91:185-191(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BALB/c, C57BL/6J and DBA/2.
      Tissue: Cerebellum, Eye, Head, Kidney and Lung.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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].
      Strain: 129, C57BL/6, C57BL/6J, Czech II, FVB/N and FVB/N-3.
      Tissue: Brain, Colon, Embryo, Eye, Mammary gland and Mammary tumor.
    5. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 4-11; 27-50; 65-78; 85-105; 116-137; 144-189; 199-213; 218-246 AND 262-333, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    6. "Housekeeping genes for phylogenetic analysis of eutherian relationships."
      Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.
      Mol. Biol. Evol. 23:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-249.
    7. Cited for: CATALYTIC ACTIVITY, SULFHYDRATION AT CYS-150, MUTAGENESIS OF CYS-150.
    8. "Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages."
      Arif A., Chatterjee P., Moodt R.A., Fox P.L.
      Mol. Cell. Biol. 32:5046-5055(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, RECONSTITUTION OF THE GAIT COMPLEX.

    Entry informationi

    Entry nameiG3P_MOUSE
    AccessioniPrimary (citable) accession number: P16858
    Secondary accession number(s): A6H6A8
    , Q0QEU0, Q3THM2, Q3TUI2, Q3UMT2, Q4V783, Q569X2, Q569X5, Q5U410
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    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

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3