Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P04406

- G3P_HUMAN

UniProt

P04406 - G3P_HUMAN

Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

GAPDH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 196 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. 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. 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 By similarity. 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. 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.By similarity3 Publications

    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 sitei35 – 351NAD2 Publications
    Binding sitei80 – 801NAD; via carbonyl oxygen2 Publications
    Binding sitei122 – 1221NAD2 Publications
    Active sitei152 – 1521Nucleophile
    Sitei179 – 1791Activates thiol group during catalysis
    Binding sitei182 – 1821Glyceraldehyde 3-phosphateBy similarity
    Binding sitei234 – 2341Glyceraldehyde 3-phosphateBy similarity
    Binding sitei316 – 3161NAD2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi13 – 142NAD2 Publications

    GO - Molecular functioni

    1. glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
    2. identical protein binding Source: IntAct
    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: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cellular response to interferon-gamma Source: UniProtKB
    3. gluconeogenesis Source: Reactome
    4. glucose metabolic process Source: Reactome
    5. glycolytic process Source: Reactome
    6. microtubule cytoskeleton organization Source: UniProtKB
    7. negative regulation of translation Source: UniProtKB
    8. neuron apoptotic process Source: UniProtKB
    9. peptidyl-cysteine S-trans-nitrosylation Source: UniProtKB
    10. protein stabilization Source: UniProtKB
    11. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase, Transferase

    Keywords - Biological processi

    Apoptosis, Glycolysis, Translation regulation

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03433-MONOMER.
    BRENDAi1.2.1.12. 2681.
    ReactomeiREACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    SABIO-RKP04406.
    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
    ORF Names:CDABP0047, OK/SW-cl.12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:4141. GAPDH.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Nucleus By similarity. Cytoplasmperinuclear region 1 Publication. Membrane 1 Publication. Cytoplasmcytoskeleton By similarity
    Note: Translocates to the nucleus following S-nitrosylation and interaction with SIAH1, which contains a nuclear localization signal By similarity. Postnuclear and Perinuclear regions.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProtKB
    4. GAIT complex Source: UniProtKB
    5. lipid particle Source: UniProtKB
    6. membrane Source: UniProtKB
    7. microtubule cytoskeleton Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    10. plasma membrane Source: HPA
    11. ribonucleoprotein complex Source: UniProtKB
    12. vesicle Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28554.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 335334Glyceraldehyde-3-phosphate dehydrogenasePRO_0000145486Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51N6,N6-dimethyllysine1 Publication
    Modified residuei9 – 91Deamidated asparagine1 Publication
    Modified residuei42 – 421Phosphotyrosine1 Publication
    Modified residuei61 – 611N6-acetyllysine1 Publication
    Modified residuei64 – 641Deamidated asparagine1 Publication
    Modified residuei66 – 661N6,N6-dimethyllysine1 Publication
    Modified residuei70 – 701Deamidated asparagine1 Publication
    Modified residuei75 – 751Phosphothreonine2 Publications
    Modified residuei83 – 831Phosphoserine4 Publications
    Modified residuei122 – 1221Phosphoserine1 Publication
    Modified residuei148 – 1481Phosphoserine1 Publication
    Modified residuei149 – 1491Deamidated asparagine1 Publication
    Modified residuei151 – 1511Phosphoserine1 Publication
    Modified residuei152 – 1521ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited formBy similarity
    Modified residuei152 – 1521Cysteine persulfideBy similarity
    Modified residuei152 – 1521S-nitrosocysteine; in reversibly inhibited formBy similarity
    Modified residuei155 – 1551Deamidated asparagine1 Publication
    Modified residuei184 – 1841Phosphothreonine3 Publications
    Modified residuei194 – 1941N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei194 – 1941N6-acetyllysine; alternate1 Publication
    Modified residuei194 – 1941N6-malonyllysine; alternate1 Publication
    Modified residuei211 – 2111Phosphothreonine1 Publication
    Modified residuei215 – 2151N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei215 – 2151N6-malonyllysine; alternate1 Publication
    Modified residuei219 – 2191N6-acetyllysine1 Publication
    Modified residuei225 – 2251Deamidated asparagine1 Publication
    Modified residuei227 – 2271N6,N6-dimethyllysine; alternate1 Publication
    Modified residuei227 – 2271N6-acetyllysine; alternate1 Publication
    Modified residuei229 – 2291Phosphothreonine1 Publication
    Modified residuei237 – 2371Phosphothreonine1 Publication
    Modified residuei254 – 2541N6-acetyllysine1 Publication
    Modified residuei260 – 2601N6,N6-dimethyllysine1 Publication
    Modified residuei263 – 2631N6,N6-dimethyllysine1 Publication
    Modified residuei312 – 3121Phosphoserine2 Publications
    Modified residuei316 – 3161Deamidated asparagine1 Publication
    Modified residuei334 – 3341N6,N6-dimethyllysine1 Publication

    Post-translational modificationi

    S-nitrosylation of Cys-152 leads to interaction with SIAH1, followed by translocation to the nucleus.By similarity
    ISGylated.1 Publication
    Sulfhydration at Cys-152 increases catalytic activity.By similarity

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiP04406.
    PaxDbiP04406.
    PRIDEiP04406.

    2D gel databases

    DOSAC-COBS-2DPAGEP04406.
    OGPiP04406.
    REPRODUCTION-2DPAGEIPI00219018.
    P04406.
    SWISS-2DPAGEP04406.
    UCD-2DPAGEP04406.

    PTM databases

    PhosphoSiteiP04406.

    Expressioni

    Gene expression databases

    ArrayExpressiP04406.
    BgeeiP04406.
    CleanExiHS_GAPDH.
    GenevestigatoriP04406.

    Organism-specific databases

    HPAiCAB005197.
    CAB016392.
    HPA040067.

    Interactioni

    Subunit structurei

    Homotetramer. 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 By similarity. Interacts with EIF1AD, USP25, PRKCI and WARS. Component of the GAIT complex. Interacts with FKBP6; leading to inhibit GAPDH catalytic activity.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-354056,EBI-354056
    EGFRP005334EBI-354056,EBI-297353
    PCNAP120043EBI-354056,EBI-358311
    PGK1P005582EBI-354056,EBI-709599
    PREPP481475EBI-354056,EBI-1049962
    RPA2P159272EBI-354056,EBI-621404

    Protein-protein interaction databases

    BioGridi108868. 153 interactions.
    DIPiDIP-32521N.
    IntActiP04406. 69 interactions.
    MINTiMINT-1150338.
    STRINGi9606.ENSP00000229239.

    Structurei

    Secondary structure

    1
    335
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Helixi13 – 2513
    Beta strandi27 – 348
    Beta strandi36 – 383
    Helixi40 – 489
    Turni51 – 533
    Beta strandi60 – 634
    Beta strandi66 – 694
    Beta strandi72 – 776
    Helixi82 – 843
    Turni87 – 915
    Beta strandi94 – 974
    Beta strandi99 – 1013
    Helixi105 – 1084
    Helixi109 – 1146
    Beta strandi117 – 1237
    Beta strandi126 – 1283
    Turni133 – 1353
    Helixi137 – 1393
    Beta strandi145 – 1484
    Helixi152 – 16817
    Beta strandi170 – 18011
    Beta strandi185 – 1895
    Helixi196 – 1994
    Turni202 – 2043
    Beta strandi207 – 2104
    Turni213 – 2164
    Helixi217 – 2204
    Helixi222 – 2243
    Beta strandi227 – 23610
    Beta strandi241 – 25111
    Helixi255 – 26713
    Turni268 – 2736
    Beta strandi274 – 2774
    Helixi283 – 2864
    Beta strandi292 – 2965
    Turni297 – 2993
    Beta strandi301 – 3044
    Beta strandi307 – 3148
    Helixi318 – 33316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U8FX-ray1.75O/P/Q/R1-335[»]
    1ZNQX-ray2.50O/P/Q/R1-335[»]
    2FEHmodel-O/P/Q/R1-335[»]
    3GPDX-ray3.50G/R2-335[»]
    ProteinModelPortaliP04406.
    SMRiP04406. Positions 3-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04406.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 148147Interaction with WARSAdd
    BLAST
    Regioni151 – 1533Glyceraldehyde 3-phosphate bindingBy similarity
    Regioni211 – 2122Glyceraldehyde 3-phosphate bindingBy similarity

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0057.
    HOGENOMiHOG000071678.
    HOVERGENiHBG000227.
    InParanoidiP04406.
    KOiK00134.
    OMAiKFASEGP.
    OrthoDBiEOG7Q5HDF.
    PhylomeDBiP04406.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P04406-1) [UniParc]FASTAAdd to Basket

    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

    MGKVKVGVNG FGRIGRLVTR AAFNSGKVDI VAINDPFIDL NYMVYMFQYD    50
    STHGKFHGTV KAENGKLVIN GNPITIFQER DPSKIKWGDA GAEYVVESTG 100
    VFTTMEKAGA HLQGGAKRVI ISAPSADAPM FVMGVNHEKY DNSLKIISNA 150
    SCTTNCLAPL AKVIHDNFGI VEGLMTTVHA ITATQKTVDG PSGKLWRDGR 200
    GALQNIIPAS TGAAKAVGKV IPELNGKLTG MAFRVPTANV SVVDLTCRLE 250
    KPAKYDDIKK VVKQASEGPL KGILGYTEHQ VVSSDFNSDT HSSTFDAGAG 300
    IALNDHFVKL ISWYDNEFGY SNRVVDLMAH MASKE 335
    Length:335
    Mass (Da):36,053
    Last modified:January 23, 2007 - v3
    Checksum:iC9C135E8AE3E8744
    GO
    Isoform 2 (identifier: P04406-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-42: Missing.

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:293
    Mass (Da):31,548
    Checksum:i6705C1F127BB6C09
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti225 – 2251N → D in CAA25833. (PubMed:6096821)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221A → G.1 Publication
    Corresponds to variant rs45541435 [ dbSNP | Ensembl ].
    VAR_018889
    Natural varianti251 – 2511K → N.
    Corresponds to variant rs1062429 [ dbSNP | Ensembl ].
    VAR_049218

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4242Missing in isoform 2. CuratedVSP_047289Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01677 mRNA. Translation: CAA25833.1.
    M17851 mRNA. Translation: AAA86283.1.
    M33197 mRNA. Translation: AAA52518.1.
    J02642 mRNA. Translation: AAA52496.1.
    J04038 Genomic DNA. Translation: AAA53191.1.
    X53778 mRNA. Translation: CAA37794.1.
    AF261085 mRNA. Translation: AAF99678.1.
    AY007133 mRNA. Translation: AAG01996.1.
    AB062273 mRNA. Translation: BAB93466.1.
    BT006893 mRNA. Translation: AAP35539.1.
    AY340484 Genomic DNA. Translation: AAP88932.1.
    CR407671 mRNA. Translation: CAG28599.1.
    AC006064 Genomic DNA. No translation available.
    CH471116 Genomic DNA. Translation: EAW88787.1.
    BC001601 mRNA. Translation: AAH01601.1.
    BC004109 mRNA. Translation: AAH04109.1.
    BC009081 mRNA. Translation: AAH09081.1.
    BC013310 mRNA. Translation: AAH13310.1.
    BC023632 mRNA. Translation: AAH23632.1.
    BC025925 mRNA. Translation: AAH25925.1.
    BC026907 mRNA. Translation: AAH26907.1.
    BC029618 mRNA. Translation: AAH29618.1.
    BC083511 mRNA. Translation: AAH83511.1.
    CCDSiCCDS58201.1. [P04406-2]
    CCDS8549.1. [P04406-1]
    PIRiA31988. DEHUG3.
    RefSeqiNP_001243728.1. NM_001256799.2. [P04406-2]
    NP_001276674.1. NM_001289745.1. [P04406-1]
    NP_001276675.1. NM_001289746.1. [P04406-1]
    NP_002037.2. NM_002046.5. [P04406-1]
    UniGeneiHs.544577.
    Hs.592355.
    Hs.598320.

    Genome annotation databases

    EnsembliENST00000229239; ENSP00000229239; ENSG00000111640. [P04406-1]
    ENST00000396858; ENSP00000380067; ENSG00000111640. [P04406-2]
    ENST00000396859; ENSP00000380068; ENSG00000111640. [P04406-1]
    ENST00000396861; ENSP00000380070; ENSG00000111640. [P04406-1]
    GeneIDi2597.
    KEGGihsa:2597.
    UCSCiuc001qop.2. human. [P04406-1]

    Polymorphism databases

    DMDMi120649.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Wikipedia

    Glyceraldehyde 3-phosphate dehydrogenase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X01677 mRNA. Translation: CAA25833.1 .
    M17851 mRNA. Translation: AAA86283.1 .
    M33197 mRNA. Translation: AAA52518.1 .
    J02642 mRNA. Translation: AAA52496.1 .
    J04038 Genomic DNA. Translation: AAA53191.1 .
    X53778 mRNA. Translation: CAA37794.1 .
    AF261085 mRNA. Translation: AAF99678.1 .
    AY007133 mRNA. Translation: AAG01996.1 .
    AB062273 mRNA. Translation: BAB93466.1 .
    BT006893 mRNA. Translation: AAP35539.1 .
    AY340484 Genomic DNA. Translation: AAP88932.1 .
    CR407671 mRNA. Translation: CAG28599.1 .
    AC006064 Genomic DNA. No translation available.
    CH471116 Genomic DNA. Translation: EAW88787.1 .
    BC001601 mRNA. Translation: AAH01601.1 .
    BC004109 mRNA. Translation: AAH04109.1 .
    BC009081 mRNA. Translation: AAH09081.1 .
    BC013310 mRNA. Translation: AAH13310.1 .
    BC023632 mRNA. Translation: AAH23632.1 .
    BC025925 mRNA. Translation: AAH25925.1 .
    BC026907 mRNA. Translation: AAH26907.1 .
    BC029618 mRNA. Translation: AAH29618.1 .
    BC083511 mRNA. Translation: AAH83511.1 .
    CCDSi CCDS58201.1. [P04406-2 ]
    CCDS8549.1. [P04406-1 ]
    PIRi A31988. DEHUG3.
    RefSeqi NP_001243728.1. NM_001256799.2. [P04406-2 ]
    NP_001276674.1. NM_001289745.1. [P04406-1 ]
    NP_001276675.1. NM_001289746.1. [P04406-1 ]
    NP_002037.2. NM_002046.5. [P04406-1 ]
    UniGenei Hs.544577.
    Hs.592355.
    Hs.598320.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1U8F X-ray 1.75 O/P/Q/R 1-335 [» ]
    1ZNQ X-ray 2.50 O/P/Q/R 1-335 [» ]
    2FEH model - O/P/Q/R 1-335 [» ]
    3GPD X-ray 3.50 G/R 2-335 [» ]
    ProteinModelPortali P04406.
    SMRi P04406. Positions 3-335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108868. 153 interactions.
    DIPi DIP-32521N.
    IntActi P04406. 69 interactions.
    MINTi MINT-1150338.
    STRINGi 9606.ENSP00000229239.

    Chemistry

    BindingDBi P04406.
    ChEMBLi CHEMBL2284.
    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P04406.

    Polymorphism databases

    DMDMi 120649.

    2D gel databases

    DOSAC-COBS-2DPAGE P04406.
    OGPi P04406.
    REPRODUCTION-2DPAGE IPI00219018.
    P04406.
    SWISS-2DPAGE P04406.
    UCD-2DPAGE P04406.

    Proteomic databases

    MaxQBi P04406.
    PaxDbi P04406.
    PRIDEi P04406.

    Protocols and materials databases

    DNASUi 2597.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000229239 ; ENSP00000229239 ; ENSG00000111640 . [P04406-1 ]
    ENST00000396858 ; ENSP00000380067 ; ENSG00000111640 . [P04406-2 ]
    ENST00000396859 ; ENSP00000380068 ; ENSG00000111640 . [P04406-1 ]
    ENST00000396861 ; ENSP00000380070 ; ENSG00000111640 . [P04406-1 ]
    GeneIDi 2597.
    KEGGi hsa:2597.
    UCSCi uc001qop.2. human. [P04406-1 ]

    Organism-specific databases

    CTDi 2597.
    GeneCardsi GC12P006643.
    H-InvDB HIX0000949.
    HIX0024996.
    HGNCi HGNC:4141. GAPDH.
    HPAi CAB005197.
    CAB016392.
    HPA040067.
    MIMi 138400. gene.
    neXtProti NX_P04406.
    PharmGKBi PA28554.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0057.
    HOGENOMi HOG000071678.
    HOVERGENi HBG000227.
    InParanoidi P04406.
    KOi K00134.
    OMAi KFASEGP.
    OrthoDBi EOG7Q5HDF.
    PhylomeDBi P04406.
    TreeFami TF300533.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00184 .
    BioCyci MetaCyc:HS03433-MONOMER.
    BRENDAi 1.2.1.12. 2681.
    Reactomei REACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    SABIO-RK P04406.

    Miscellaneous databases

    ChiTaRSi GAPDH. human.
    EvolutionaryTracei P04406.
    GeneWikii Glyceraldehyde_3-phosphate_dehydrogenase.
    GenomeRNAii 2597.
    NextBioi 10271.
    PROi P04406.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04406.
    Bgeei P04406.
    CleanExi HS_GAPDH.
    Genevestigatori P04406.

    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. "The glyceraldehyde 3 phosphate dehydrogenase gene family: structure of a human cDNA and of an X chromosome linked pseudogene; amazing complexity of the gene family in mouse."
      Hanauer A., Mandel J.-L.
      EMBO J. 3:2627-2633(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The complete sequence of a full length cDNA for human liver glyceraldehyde-3-phosphate dehydrogenase: evidence for multiple mRNA species."
      Arcari P., Martinelli R., Salvatore F.
      Nucleic Acids Res. 12:9179-9189(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene."
      Tso J.Y., Sun X.-H., Kao T.-H., Reece K.S., Wu R.
      Nucleic Acids Res. 13:2485-2502(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    4. "Enhanced expression of a glyceraldehyde-3-phosphate dehydrogenase gene in human lung cancers."
      Tokunaga K., Nakamura Y., Sakata K., Fujimori K., Ohkubo M., Sawada K., Sakiyama S.
      Cancer Res. 47:5616-5619(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    5. "Identification of the 37-kDa protein displaying a variable interaction with the erythroid cell membrane as glyceraldehyde-3-phosphate dehydrogenase."
      Allen R.W., Trach K.A., Hoch J.A.
      J. Biol. Chem. 262:649-653(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "Isolation and complete sequence of a functional human glyceraldehyde-3-phosphate dehydrogenase gene."
      Ercolani L., Florence B., Denaro M., Alexander M.
      J. Biol. Chem. 263:15335-15341(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY.
    7. "A human nuclear uracil DNA glycosylase is the 37-kDa subunit of glyceraldehyde-3-phosphate dehydrogenase."
      Meyer-Siegler K., Mauro D.J., Seal G., Wurzer J., Deriel J.K., Sirover M.A.
      Proc. Natl. Acad. Sci. U.S.A. 88:8460-8464(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    8. "cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs."
      Ye Z., Connor J.R.
      Biochem. Biophys. Res. Commun. 275:223-227(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Astrocytoma.
    9. "Pediatric leukemia cDNA sequencing project."
      Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
      Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Leukemia.
    10. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon adenocarcinoma.
    11. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    12. NIEHS SNPs program
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-22.
    13. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    14. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    15. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    16. "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: Eye, Kidney, Lung, Lymph and Placenta.
    17. "The complete amino acid sequence of human muscle glyceraldehyde 3-phosphate dehydrogenase."
      Nowak K., Wolny M., Banas T.
      FEBS Lett. 134:143-146(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 2-335.
      Tissue: Muscle.
    18. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Tissue: Platelet.
    19. Bienvenut W.V., Gao M., Leug H.
      Submitted (JUL-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13; 62-84; 118-139; 198-215; 220-227; 235-248 AND 310-335, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Prostatic carcinoma.
    20. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 67-80; 87-107; 119-139; 146-186; 201-215; 235-248 AND 310-334, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    21. "The major protein expression profile and two-dimensional protein database of human heart."
      Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A., Ershova E.S., Egorov T.A., Musalyamov A.K.
      Electrophoresis 16:1160-1169(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 220-226 AND 242-246.
      Tissue: Heart.
    22. "The covalent structure of glyceraldehyde-phosphate dehydrogenase from human muscles. Isolation and amino acid sequences of peptides from tryptic digest."
      Nowak K., Kuczek M., Ostropolska L., Malarska A., Wolny M., Branowski T.
      Hoppe-Seyler's Z. Physiol. Chem. 356:1181-1183(1975) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Muscle.
    23. "Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ciota /lambda and plays a role in microtubule dynamics in the early secretory pathway."
      Tisdale E.J.
      J. Biol. Chem. 277:3334-3341(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRKCI.
    24. "Subcellular localization of human glyceraldehyde-3-phosphate dehydrogenase is independent of its glycolytic function."
      Mazzola J.L., Sirover M.A.
      Biochim. Biophys. Acta 1622:50-56(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    25. "Noncanonical function of glutamyl-prolyl-tRNA synthetase: gene-specific silencing of translation."
      Sampath P., Mazumder B., Seshadri V., Gerber C.A., Chavatte L., Kinter M., Ting S.M., Dignam J.D., Kim S., Driscoll D.M., Fox P.L.
      Cell 119:195-208(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE GAIT COMPLEX.
    26. "Oxidative stress-responsive intracellular regulation specific for the angiostatic form of human tryptophanyl-tRNA synthetase."
      Wakasugi K., Nakano T., Morishima I.
      Biochemistry 44:225-232(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WARS.
    27. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. "The ubiquitin-specific protease USP25 interacts with three sarcomeric proteins."
      Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G., Marfany G.
      Cell. Mol. Life Sci. 63:723-734(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH USP25.
    30. "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
      Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
      Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: ISGYLATION.
    31. "Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase."
      Seo J., Jeong J., Kim Y.M., Hwang N., Paek E., Lee K.-J.
      J. Proteome Res. 7:587-602(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-75; SER-122; SER-148; THR-229; THR-237 AND SER-312, DEAMIDATION AT ASN-9; ASN-64; ASN-70; ASN-149; ASN-155; ASN-225 AND ASN-316, METHYLATION AT LYS-5; LYS-66; LYS-194; LYS-215; LYS-227; LYS-260; LYS-263 AND LYS-334.
    32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-151 AND THR-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "FKBP36 is an inherent multifunctional glyceraldehyde-3-phosphate dehydrogenase inhibitor."
      Jarczowski F., Jahreis G., Erdmann F., Schierhorn A., Fischer G., Edlich F.
      J. Biol. Chem. 284:766-773(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FKBP6.
    35. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-184; THR-211 AND SER-312, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    36. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61; LYS-194; LYS-219; LYS-227 AND LYS-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. "Haponin (eIF1AD) interacts with glyceraldehyde 3-phosphate dehydrogenase in the CHO-K1 cell line."
      Rakitina T.V., Bogatova O.V., Smirnova E.V., Pozdeev V.I., Kostanian I.A., Lipkin V.M.
      Bioorg. Khim. 36:312-318(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EIF1AD.
    38. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75; SER-83 AND THR-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    40. Cited for: MALONYLATION AT LYS-194 AND LYS-215.
    41. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    42. "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, RECONSTITUTION OF THE GAIT COMPLEX.
    43. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    44. "Twinning in crystals of human skeletal muscle D-glyceraldehyde-3-phosphate dehydrogenase."
      Mercer W.D., Winn S.I., Watson H.C.
      J. Mol. Biol. 104:277-283(1976) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
    45. "Structural analysis of human liver glyceraldehyde-3-phosphate dehydrogenase."
      Ismail S.A., Park H.W.
      Acta Crystallogr. D 61:1508-1513(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.
    46. "High-resolution structure of human D-glyceraldehyde-3-phosphate dehydrogenase."
      Jenkins J.L., Tanner J.J.
      Acta Crystallogr. D 62:290-301(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH NAD, SUBUNIT.

    Entry informationi

    Entry nameiG3P_HUMAN
    AccessioniPrimary (citable) accession number: P04406
    Secondary accession number(s): E7EUT4, P00354, Q53X65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 196 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3