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P49448

- DHE4_HUMAN

UniProt

P49448 - DHE4_HUMAN

Protein

Glutamate dehydrogenase 2, mitochondrial

Gene

GLUD2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (27 Apr 2001)
      Previous versions | rss
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    Functioni

    Important for recycling the chief excitatory neurotransmitter, glutamate, during neurotransmission.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei84 – 841SubstrateBy similarity
    Active sitei183 – 1831PROSITE-ProRule annotation

    GO - Molecular functioni

    1. ADP binding Source: BHF-UCL
    2. glutamate dehydrogenase (NAD+) activity Source: UniProtKB
    3. glutamate dehydrogenase [NAD(P)+] activity Source: BHF-UCL
    4. GTP binding Source: BHF-UCL
    5. leucine binding Source: BHF-UCL

    GO - Biological processi

    1. glutamate biosynthetic process Source: BHF-UCL
    2. glutamate catabolic process Source: BHF-UCL
    3. glutamate metabolic process Source: UniProtKB
    4. oxidation-reduction process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NADP

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00018-MONOMER.
    BRENDAi1.4.1.3. 2681.
    SABIO-RKP49448.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate dehydrogenase 2, mitochondrial (EC:1.4.1.3)
    Short name:
    GDH 2
    Gene namesi
    Name:GLUD2
    Synonyms:GLUDP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:4336. GLUD2.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: BHF-UCL

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28738.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5353Mitochondrion1 PublicationAdd
    BLAST
    Chaini54 – 558505Glutamate dehydrogenase 2, mitochondrialPRO_0000007208Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei68 – 681N6-succinyllysineBy similarity
    Modified residuei79 – 791PhosphoserineBy similarity
    Modified residuei84 – 841N6-acetyllysine; alternateBy similarity
    Modified residuei84 – 841N6-succinyllysine; alternateBy similarity
    Modified residuei110 – 1101N6-acetyllysine; alternateBy similarity
    Modified residuei110 – 1101N6-succinyllysine; alternateBy similarity
    Modified residuei128 – 1281PhosphoserineBy similarity
    Modified residuei135 – 1351PhosphotyrosineBy similarity
    Modified residuei162 – 1621N6-acetyllysine; alternateBy similarity
    Modified residuei162 – 1621N6-succinyllysine; alternateBy similarity
    Modified residuei171 – 1711N6-acetyllysineBy similarity
    Modified residuei172 – 1721ADP-ribosylcysteine1 Publication
    Modified residuei183 – 1831N6-acetyllysine; alternateBy similarity
    Modified residuei183 – 1831N6-succinyllysine; alternateBy similarity
    Modified residuei187 – 1871N6-acetyllysineBy similarity
    Modified residuei191 – 1911N6-acetyllysine; alternateBy similarity
    Modified residuei191 – 1911N6-succinyllysine; alternateBy similarity
    Modified residuei200 – 2001N6-succinyllysineBy similarity
    Modified residuei211 – 2111N6-acetyllysineBy similarity
    Modified residuei326 – 3261N6-acetyllysineBy similarity
    Modified residuei346 – 3461N6-acetyllysine; alternateBy similarity
    Modified residuei346 – 3461N6-succinyllysine; alternateBy similarity
    Modified residuei352 – 3521N6-acetyllysine; alternateBy similarity
    Modified residuei352 – 3521N6-succinyllysine; alternateBy similarity
    Modified residuei363 – 3631N6-acetyllysine; alternateBy similarity
    Modified residuei363 – 3631N6-succinyllysine; alternateBy similarity
    Modified residuei365 – 3651N6-acetyllysine; alternateBy similarity
    Modified residuei365 – 3651N6-succinyllysine; alternateBy similarity
    Modified residuei386 – 3861N6-acetyllysineBy similarity
    Modified residuei390 – 3901N6-acetyllysine; alternateBy similarity
    Modified residuei390 – 3901N6-succinyllysine; alternateBy similarity
    Modified residuei399 – 3991N6-acetyllysineBy similarity
    Modified residuei415 – 4151N6-acetyllysine; alternateBy similarity
    Modified residuei415 – 4151N6-succinyllysine; alternateBy similarity
    Modified residuei457 – 4571N6-acetyllysine; alternateBy similarity
    Modified residuei457 – 4571N6-succinyllysine; alternateBy similarity
    Modified residuei477 – 4771N6-acetyllysine; alternateBy similarity
    Modified residuei477 – 4771N6-succinyllysine; alternateBy similarity
    Modified residuei480 – 4801N6-acetyllysine; alternateBy similarity
    Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
    Modified residuei503 – 5031N6-acetyllysine; alternateBy similarity
    Modified residuei503 – 5031N6-succinyllysine; alternateBy similarity
    Modified residuei527 – 5271N6-acetyllysine; alternateBy similarity
    Modified residuei527 – 5271N6-succinyllysine; alternateBy similarity
    Modified residuei545 – 5451N6-acetyllysine; alternateBy similarity
    Modified residuei545 – 5451N6-succinyllysine; alternateBy similarity
    Modified residuei548 – 5481N6-acetyllysineBy similarity

    Post-translational modificationi

    Stoichiometry shows that ADP-ribosylation occurs in one subunit per catalytically active homohexamer.

    Keywords - PTMi

    Acetylation, ADP-ribosylation, Phosphoprotein

    Proteomic databases

    MaxQBiP49448.
    PaxDbiP49448.
    PeptideAtlasiP49448.
    PRIDEiP49448.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00027146.

    PTM databases

    PhosphoSiteiP49448.

    Expressioni

    Tissue specificityi

    Expressed in retina, testis and, at a lower level, brain.

    Gene expression databases

    ArrayExpressiP49448.
    BgeeiP49448.
    GenevestigatoriP49448.

    Organism-specific databases

    HPAiHPA042492.
    HPA044839.

    Interactioni

    Subunit structurei

    Homohexamer.By similarity

    Protein-protein interaction databases

    BioGridi109009. 4 interactions.
    IntActiP49448. 4 interactions.
    MINTiMINT-1411373.
    STRINGi9606.ENSP00000327589.

    Structurei

    3D structure databases

    ProteinModelPortaliP49448.
    SMRiP49448. Positions 63-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0334.
    HOGENOMiHOG000243801.
    HOVERGENiHBG005479.
    InParanoidiP49448.
    KOiK00261.
    OMAiTMELCQK.
    OrthoDBiEOG73NG50.
    PhylomeDBiP49448.
    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.

    P49448-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYRYLAKALL PSRAGPAALG SAANHSAALL GRGRGQPAAA SQPGLALAAR    50
    RHYSELVADR EDDPNFFKMV EGFFDRGASI VEDKLVKDLR TQESEEQKRN 100
    RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI 150
    RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTENELEK 200
    ITRRFTMELA KKGFIGPGVD VPAPDMNTGE REMSWIADTY ASTIGHYDIN 250
    AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFR 300
    DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED 350
    FKLQHGSILG FPKAKPYEGS ILEVDCDILI PAATEKQLTK SNAPRVKAKI 400
    IAEGANGPTT PEADKIFLER NILVIPDLYL NAGGVTVSYF EWLKNLNHVS 450
    YGRLTFKYER DSNYHLLLSV QESLERKFGK HGGTIPIVPT AEFQDSISGA 500
    SEKDIVHSAL AYTMERSARQ IMHTAMKYNL GLDLRTAAYV NAIEKVFKVY 550
    SEAGVTFT 558
    Length:558
    Mass (Da):61,434
    Last modified:April 27, 2001 - v2
    Checksum:iF222B1B2CB74A6EA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti286 – 2861E → Q in CAA46995. (PubMed:8207021)Curated
    Sequence conflicti286 – 2861E → Q in AAA20969. (PubMed:8207021)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti498 – 4981S → A.
    Corresponds to variant rs9697983 [ dbSNP | Ensembl ].
    VAR_048867

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66310 Genomic DNA. Translation: CAA46995.1.
    U08997 Genomic DNA. Translation: AAA20969.1.
    AK313356 mRNA. Translation: BAG36157.1.
    AC006144 Genomic DNA. Translation: AAD05030.1.
    BC050732 mRNA. Translation: AAH50732.1.
    CCDSiCCDS14603.1.
    PIRiA53719.
    RefSeqiNP_036216.2. NM_012084.3.
    UniGeneiHs.368538.

    Genome annotation databases

    EnsembliENST00000328078; ENSP00000327589; ENSG00000182890.
    GeneIDi2747.
    KEGGihsa:2747.
    UCSCiuc004eto.3. human.

    Polymorphism databases

    DMDMi13432152.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66310 Genomic DNA. Translation: CAA46995.1 .
    U08997 Genomic DNA. Translation: AAA20969.1 .
    AK313356 mRNA. Translation: BAG36157.1 .
    AC006144 Genomic DNA. Translation: AAD05030.1 .
    BC050732 mRNA. Translation: AAH50732.1 .
    CCDSi CCDS14603.1.
    PIRi A53719.
    RefSeqi NP_036216.2. NM_012084.3.
    UniGenei Hs.368538.

    3D structure databases

    ProteinModelPortali P49448.
    SMRi P49448. Positions 63-558.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109009. 4 interactions.
    IntActi P49448. 4 interactions.
    MINTi MINT-1411373.
    STRINGi 9606.ENSP00000327589.

    Chemistry

    DrugBanki DB00142. L-Glutamic Acid.
    DB00157. NADH.

    PTM databases

    PhosphoSitei P49448.

    Polymorphism databases

    DMDMi 13432152.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00027146.

    Proteomic databases

    MaxQBi P49448.
    PaxDbi P49448.
    PeptideAtlasi P49448.
    PRIDEi P49448.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000328078 ; ENSP00000327589 ; ENSG00000182890 .
    GeneIDi 2747.
    KEGGi hsa:2747.
    UCSCi uc004eto.3. human.

    Organism-specific databases

    CTDi 2747.
    GeneCardsi GC0XP120181.
    HGNCi HGNC:4336. GLUD2.
    HPAi HPA042492.
    HPA044839.
    MIMi 300144. gene.
    neXtProti NX_P49448.
    PharmGKBi PA28738.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0334.
    HOGENOMi HOG000243801.
    HOVERGENi HBG005479.
    InParanoidi P49448.
    KOi K00261.
    OMAi TMELCQK.
    OrthoDBi EOG73NG50.
    PhylomeDBi P49448.
    TreeFami TF313945.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00018-MONOMER.
    BRENDAi 1.4.1.3. 2681.
    SABIO-RK P49448.

    Miscellaneous databases

    GeneWikii GLUD2.
    GenomeRNAii 2747.
    NextBioi 10828.
    PROi P49448.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49448.
    Bgeei P49448.
    Genevestigatori P49448.

    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. "Novel human glutamate dehydrogenase expressed in neural and testicular tissues and encoded by an X-linked intronless gene."
      Shashidharan P., Michaelidis T.M., Robakis N.K., Kresovali A., Papamatheakis J., Plaitakis A.
      J. Biol. Chem. 269:16971-16976(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Retina.
    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].
      Tissue: Testis.
    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. "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: Skin.
    5. "Identification of ADP-ribosylation site in human glutamate dehydrogenase isozymes."
      Choi M.M., Huh J.W., Yang S.J., Cho E.H., Choi S.Y., Cho S.W.
      FEBS Lett. 579:4125-4130(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ADP-RIBOSYLATION AT CYS-172.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Alpha helical structures in the leader sequence of human GLUD2 glutamate dehydrogenase responsible for mitochondrial import."
      Kotzamani D., Plaitakis A.
      Neurochem. Int. 61:463-469(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSIT PEPTIDE CLEAVAGE SITE, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiDHE4_HUMAN
    AccessioniPrimary (citable) accession number: P49448
    Secondary accession number(s): B2R8G0, Q9UDQ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: April 27, 2001
    Last modified: October 1, 2014
    This is version 129 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 X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3