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P26443

- DHE3_MOUSE

UniProt

P26443 - DHE3_MOUSE

Protein

Glutamate dehydrogenase 1, mitochondrial

Gene

Glud1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Mitochondrial glutamate dehydrogenase that converts L-glutamate into alpha-ketoglutarate. Plays a key role in glutamine anaplerosis by producing alpha-ketoglutarate, an important intermediate in the tricarboxylic acid cycle. May be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate.1 Publication

    Catalytic activityi

    L-glutamate + H2O + NAD(P)+ = 2-oxoglutarate + NH3 + NAD(P)H.PROSITE-ProRule annotation

    Enzyme regulationi

    Subject to allosteric regulation. Activated by ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and activate the enzyme By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei147 – 1471SubstrateBy similarity
    Binding sitei171 – 1711SubstrateBy similarity
    Binding sitei176 – 1761NADBy similarity
    Active sitei183 – 1831PROSITE-ProRule annotation
    Binding sitei252 – 2521NADBy similarity
    Binding sitei266 – 2661GTPBy similarity
    Binding sitei270 – 2701GTPBy similarity
    Binding sitei319 – 3191GTPBy similarity
    Binding sitei322 – 3221GTPBy similarity
    Binding sitei438 – 4381SubstrateBy similarity
    Binding sitei444 – 4441NADBy similarity
    Binding sitei450 – 4501ADPBy similarity
    Binding sitei516 – 5161ADPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi141 – 1433NADBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glutamate dehydrogenase (NAD+) activity Source: Ensembl
    3. glutamate dehydrogenase [NAD(P)+] activity Source: UniProtKB
    4. GTP binding Source: UniProtKB-KW
    5. protein binding Source: MGI

    GO - Biological processi

    1. glutamine metabolic process Source: UniProtKB
    2. long-term memory Source: Ensembl
    3. positive regulation of insulin secretion Source: MGI
    4. response to aluminum ion Source: Ensembl
    5. tricarboxylic acid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    ATP-binding, GTP-binding, NADP, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate dehydrogenase 1, mitochondrial (EC:1.4.1.3)
    Short name:
    GDH 1
    Gene namesi
    Name:Glud1
    Synonyms:Glud
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:95753. Glud1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: MGI
    2. mitochondrial matrix Source: UniProtKB-SubCell
    3. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5353MitochondrionAdd
    BLAST
    Chaini54 – 558505Glutamate dehydrogenase 1, mitochondrialPRO_0000007212Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei68 – 681N6-succinyllysine1 Publication
    Modified residuei79 – 791Phosphoserine1 Publication
    Modified residuei84 – 841N6-acetyllysine; alternate2 Publications
    Modified residuei84 – 841N6-succinyllysine; alternate1 Publication
    Modified residuei90 – 901N6-acetyllysine1 Publication
    Modified residuei110 – 1101N6-acetyllysine; alternate1 Publication
    Modified residuei110 – 1101N6-succinyllysine; alternateBy similarity
    Modified residuei128 – 1281Phosphoserine1 Publication
    Modified residuei135 – 1351Phosphotyrosine1 Publication
    Modified residuei162 – 1621N6-acetyllysine; alternate1 Publication
    Modified residuei162 – 1621N6-succinyllysine; alternate1 Publication
    Modified residuei171 – 1711N6-acetyllysine1 Publication
    Modified residuei172 – 1721ADP-ribosylcysteineBy similarity
    Modified residuei183 – 1831N6-acetyllysine; alternateBy similarity
    Modified residuei183 – 1831N6-succinyllysine; alternate1 Publication
    Modified residuei187 – 1871N6-acetyllysine1 Publication
    Modified residuei191 – 1911N6-acetyllysine; alternate1 Publication
    Modified residuei191 – 1911N6-succinyllysine; alternate1 Publication
    Modified residuei200 – 2001N6-succinyllysine1 Publication
    Modified residuei211 – 2111N6-acetyllysine1 Publication
    Modified residuei326 – 3261N6-acetyllysine1 Publication
    Modified residuei346 – 3461N6-acetyllysine; alternate1 Publication
    Modified residuei346 – 3461N6-succinyllysine; alternate1 Publication
    Modified residuei352 – 3521N6-acetyllysine; alternate1 Publication
    Modified residuei352 – 3521N6-succinyllysine; alternate1 Publication
    Modified residuei363 – 3631N6-acetyllysine; alternate1 Publication
    Modified residuei363 – 3631N6-succinyllysine; alternate1 Publication
    Modified residuei365 – 3651N6-acetyllysine; alternate1 Publication
    Modified residuei365 – 3651N6-succinyllysine; alternate1 Publication
    Modified residuei386 – 3861N6-acetyllysineBy similarity
    Modified residuei390 – 3901N6-acetyllysine; alternate1 Publication
    Modified residuei390 – 3901N6-succinyllysine; alternate1 Publication
    Modified residuei399 – 3991N6-acetyllysine1 Publication
    Modified residuei415 – 4151N6-acetyllysine; alternate1 Publication
    Modified residuei415 – 4151N6-succinyllysine; alternateBy similarity
    Modified residuei457 – 4571N6-acetyllysine; alternate1 Publication
    Modified residuei457 – 4571N6-malonyllysine; alternateBy similarity
    Modified residuei457 – 4571N6-succinyllysine; alternateBy similarity
    Modified residuei477 – 4771N6-acetyllysine; alternate1 Publication
    Modified residuei477 – 4771N6-succinyllysine; alternate1 Publication
    Modified residuei480 – 4801N6-acetyllysine; alternate1 Publication
    Modified residuei480 – 4801N6-succinyllysine; alternate1 Publication
    Modified residuei503 – 5031N6-acetyllysine; alternate2 Publications
    Modified residuei503 – 5031N6-malonyllysine; alternateBy similarity
    Modified residuei503 – 5031N6-succinyllysine; alternate1 Publication
    Modified residuei527 – 5271N6-acetyllysine; alternate2 Publications
    Modified residuei527 – 5271N6-malonyllysine; alternateBy similarity
    Modified residuei527 – 5271N6-succinyllysine; alternate1 Publication
    Modified residuei545 – 5451N6-acetyllysine; alternate2 Publications
    Modified residuei545 – 5451N6-succinyllysine; alternate1 Publication
    Modified residuei548 – 5481N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylation of Lys-84 is observed in liver mitochondria from fasted mice but not from fed mice.2 Publications
    ADP-ribosylated by SIRT4, leading to inactivate glutamate dehydrogenase activity. Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer.

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Phosphoprotein

    Proteomic databases

    MaxQBiP26443.
    PaxDbiP26443.
    PRIDEiP26443.

    2D gel databases

    REPRODUCTION-2DPAGEP26443.
    SWISS-2DPAGEP26443.
    UCD-2DPAGEP26443.

    PTM databases

    PhosphoSiteiP26443.

    Expressioni

    Gene expression databases

    ArrayExpressiP26443.
    BgeeiP26443.
    GenevestigatoriP26443.

    Interactioni

    Subunit structurei

    Homohexamer.

    Protein-protein interaction databases

    BioGridi199956. 4 interactions.
    IntActiP26443. 9 interactions.
    MINTiMINT-1839447.

    Structurei

    3D structure databases

    ProteinModelPortaliP26443.
    SMRiP26443. Positions 63-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0334.
    GeneTreeiENSGT00390000000854.
    HOGENOMiHOG000243801.
    HOVERGENiHBG005479.
    InParanoidiP26443.
    KOiK00261.
    OMAiTCIGVIE.
    OrthoDBiEOG73NG50.
    PhylomeDBiP26443.
    TreeFamiTF313945.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR006095. Glu/Leu/Phe/Val_DH.
    IPR006096. Glu/Leu/Phe/Val_DH_C.
    IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view]
    PfamiPF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view]
    PRINTSiPR00082. GLFDHDRGNASE.
    SMARTiSM00839. ELFV_dehydrog. 1 hit.
    [Graphical view]
    PROSITEiPS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P26443-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYRRLGEALL LSRAGPAALG SAAADSAALL GWARGQPSAA PQPGLTPVAR    50
    RHYSEAAADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRESEEQKRN 100
    RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI 150
    RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK 200
    ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN 250
    AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG 300
    DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED 350
    FKLQHGSILG FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI 400
    IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS 450
    YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPVVPT AEFQDRISGA 500
    SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY 550
    NEAGVTFT 558
    Length:558
    Mass (Da):61,337
    Last modified:August 1, 1992 - v1
    Checksum:i92738AA5A133838A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti495 – 4951D → G in BAC40767. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57024 mRNA. Translation: CAA40341.1.
    AK089152 mRNA. Translation: BAC40767.1.
    BC052724 mRNA. Translation: AAH52724.1.
    BC057347 mRNA. Translation: AAH57347.1.
    CCDSiCCDS26935.1.
    PIRiS16239.
    RefSeqiNP_032159.1. NM_008133.4.
    UniGeneiMm.10600.

    Genome annotation databases

    EnsembliENSMUST00000022322; ENSMUSP00000022322; ENSMUSG00000021794.
    GeneIDi14661.
    KEGGimmu:14661.
    UCSCiuc007tas.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57024 mRNA. Translation: CAA40341.1 .
    AK089152 mRNA. Translation: BAC40767.1 .
    BC052724 mRNA. Translation: AAH52724.1 .
    BC057347 mRNA. Translation: AAH57347.1 .
    CCDSi CCDS26935.1.
    PIRi S16239.
    RefSeqi NP_032159.1. NM_008133.4.
    UniGenei Mm.10600.

    3D structure databases

    ProteinModelPortali P26443.
    SMRi P26443. Positions 63-558.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199956. 4 interactions.
    IntActi P26443. 9 interactions.
    MINTi MINT-1839447.

    PTM databases

    PhosphoSitei P26443.

    2D gel databases

    REPRODUCTION-2DPAGE P26443.
    SWISS-2DPAGE P26443.
    UCD-2DPAGE P26443.

    Proteomic databases

    MaxQBi P26443.
    PaxDbi P26443.
    PRIDEi P26443.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022322 ; ENSMUSP00000022322 ; ENSMUSG00000021794 .
    GeneIDi 14661.
    KEGGi mmu:14661.
    UCSCi uc007tas.2. mouse.

    Organism-specific databases

    CTDi 2746.
    MGIi MGI:95753. Glud1.

    Phylogenomic databases

    eggNOGi COG0334.
    GeneTreei ENSGT00390000000854.
    HOGENOMi HOG000243801.
    HOVERGENi HBG005479.
    InParanoidi P26443.
    KOi K00261.
    OMAi TCIGVIE.
    OrthoDBi EOG73NG50.
    PhylomeDBi P26443.
    TreeFami TF313945.

    Miscellaneous databases

    ChiTaRSi GLUD1. mouse.
    NextBioi 286534.
    PROi P26443.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P26443.
    Bgeei P26443.
    Genevestigatori P26443.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR006095. Glu/Leu/Phe/Val_DH.
    IPR006096. Glu/Leu/Phe/Val_DH_C.
    IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom.
    IPR016040. NAD(P)-bd_dom.
    [Graphical view ]
    Pfami PF00208. ELFV_dehydrog. 1 hit.
    PF02812. ELFV_dehydrog_N. 1 hit.
    [Graphical view ]
    PRINTSi PR00082. GLFDHDRGNASE.
    SMARTi SM00839. ELFV_dehydrog. 1 hit.
    [Graphical view ]
    PROSITEi PS00074. GLFV_DEHYDROGENASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, structure and expression analysis of a full-length mouse brain glutamate dehydrogenase cDNA."
      Tzimagiorgis G., Moschonas N.K.
      Biochim. Biophys. Acta 1089:250-253(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Brain.
    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: C57BL/6J.
      Tissue: Olfactory bulb.
    3. "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: C57BL/6.
      Tissue: Brain.
    4. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    5. "SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie restriction in pancreatic beta cells."
      Haigis M.C., Mostoslavsky R., Haigis K.M., Fahie K., Christodoulou D.C., Murphy A.J., Valenzuela D.M., Yancopoulos G.D., Karow M., Blander G., Wolberger C., Prolla T.A., Weindruch R., Alt F.W., Guarente L.
      Cell 126:941-954(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ADP-RIBOSYLATION.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-135, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    8. Cited for: FUNCTION, ADP-RIBOSYLATION.
    9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-503; LYS-527 AND LYS-545, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-84; LYS-162; LYS-183; LYS-191; LYS-200; LYS-346; LYS-352; LYS-363; LYS-365; LYS-390; LYS-477; LYS-480; LYS-503; LYS-527 AND LYS-545, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.
    10. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-90; LYS-110; LYS-162; LYS-171; LYS-187; LYS-191; LYS-211; LYS-326; LYS-346; LYS-352; LYS-363; LYS-365; LYS-390; LYS-399; LYS-415; LYS-457; LYS-477; LYS-480; LYS-503; LYS-527; LYS-545 AND LYS-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiDHE3_MOUSE
    AccessioniPrimary (citable) accession number: P26443
    Secondary accession number(s): Q8C273
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 134 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3