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Protein

Glyceraldehyde-3-phosphate dehydrogenase

Gene

Gapdh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.PROSITE-ProRule annotation1 Publication

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Apoptosis, Glycolysis, Translation regulation

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.
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 Componenti: 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

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • GAIT complex Source: UniProtKB
  • microtubule cytoskeleton Source: UniProtKB
  • myelin sheath Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

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 residuei175 – 1751PhosphothreonineBy similarity
Modified residuei180 – 1801PhosphothreonineBy 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 residuei239 – 2391PhosphoserineBy similarity
Modified residuei245 – 2451S-nitrosocysteineBy 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 S-nitrosylation of Cys-245 is induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9 transnitrosylase complex and seems to prevent interaction with phosphorylated RPL13A and to interfere with GAIT complex activity (By similarity).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.
ExpressionAtlasiP16858. baseline and differential.
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). Interacts with phosphorylated RPL13A (By similarity). Component of the GAIT complex.By similarity1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi199829. 10 interactions.
785307. 1 interaction.
IntActiP16858. 20 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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi243 – 2486[IL]-x-C-x-x-[DE] motifBy similarity

Domaini

The [IL]-x-C-x-x-[DE] motif is a proposed target motif for cysteine S-nitrosylation mediated by the iNOS-S100A8/A9 transnitrosylase complex.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0057.
GeneTreeiENSGT00760000119172.
HOVERGENiHBG000227.
InParanoidiP16858.
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

« Hide

        10         20         30         40         50
MVKVGVNGFG RIGRLVTRAA ICSGKVEIVA INDPFIDLNY MVYMFQYDST
60 70 80 90 100
HGKFNGTVKA ENGKLVINGK PITIFQERDP TNIKWGEAGA EYVVESTGVF
110 120 130 140 150
TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNHEKYDN SLKIVSNASC
160 170 180 190 200
TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT ATQKTVDGPS GKLWRDGRGA
210 220 230 240 250
AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTCRLEKP
260 270 280 290 300
AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSNSHS STFDAGAGIA
310 320 330
LNDNFVKLIS WYDNEYGYSN RVVDLMAYMA SKE
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:
EMBLi
GenBanki
DDBJi
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_001476707.5.
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:
EMBLi
GenBanki
DDBJi
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_001476707.5.
UniGeneiMm.304088.
Mm.309092.
Mm.317779.
Mm.343110.
Mm.392463.
Mm.458138.
Mm.458416.

3D structure databases

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

Protein-protein interaction databases

BioGridi199829. 10 interactions.
785307. 1 interaction.
IntActiP16858. 20 interactions.
MINTiMINT-1869564.

PTM databases

PhosphoSiteiP16858.

2D gel databases

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

Proteomic databases

MaxQBiP16858.
PaxDbiP16858.
PRIDEiP16858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2597.
MGIiMGI:95640. Gapdh.

Phylogenomic databases

eggNOGiCOG0057.
GeneTreeiENSGT00760000119172.
HOVERGENiHBG000227.
InParanoidiP16858.
KOiK00134.
OrthoDBiEOG7Q5HDF.
PhylomeDBiP16858.
TreeFamiTF300533.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
ReactomeiREACT_308431. Gluconeogenesis.
REACT_314687. Glycolysis.
SABIO-RKP16858.

Miscellaneous databases

NextBioi286057.
PROiP16858.
SOURCEiSearch...

Gene expression databases

BgeeiP16858.
CleanExiMM_GAPDH.
ExpressionAtlasiP16858. baseline and differential.
GenevestigatoriP16858.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: May 27, 2015
This is version 160 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.