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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (38 kDa BFA-dependent ADP-ribosylation substrate) (BARS-38) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-)

 G3P_RAT                 Reviewed;         333 AA.
P04797; P09328; Q5M916; Q9QWU4;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 185.
RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
Short=GAPDH;
EC=1.2.1.12;
AltName: Full=38 kDa BFA-dependent ADP-ribosylation substrate;
AltName: Full=BARS-38;
AltName: Full=Peptidyl-cysteine S-nitrosylase GAPDH;
EC=2.6.99.-;
Name=Gapdh; Synonyms=Gapd;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Muscle;
PubMed=2987824; DOI=10.1093/nar/13.5.1431;
Fort P., Marty L., Piechaczyk M., el Sabrouty S., Dani C.,
Jeanteur P., Blanchard J.-M.;
"Various rat adult tissues express only one major mRNA species from
the glyceraldehyde-3-phosphate-dehydrogenase multigenic family.";
Nucleic Acids Res. 13:1431-1442(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2987855; DOI=10.1093/nar/13.7.2485;
Tso J.Y., Sun X.-H., Kao T.-H., Reece K.S., Wu R.;
"Isolation and characterization of rat and human glyceraldehyde-3-
phosphate dehydrogenase cDNAs: genomic complexity and molecular
evolution of the gene.";
Nucleic Acids Res. 13:2485-2502(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=Sprague-Dawley; TISSUE=Cerebellum;
PubMed=10424669; DOI=10.1097/00001756-199907130-00007;
Tajima H., Tsuchiya K., Yamada M., Kondo K., Katsube N., Ishitani R.;
"Over-expression of GAPDH induces apoptosis in COS-7 cells transfected
with cloned GAPDH cDNAs.";
NeuroReport 10:2029-2033(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
Zheng J., Ramirez V.D.;
"Isolation of a glyceraldehyde-3-phosphate dehydrogenase (GAPDH) cDNA
isoform from rat brain by a rapid PCR-based cloning method and its
expression by RT-PCR.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Pituitary anterior lobe;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 65-105; 116-137; 144-184; 233-246 AND 308-321, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 235-333.
TISSUE=Brain;
PubMed=3585333; DOI=10.1111/j.1471-4159.1987.tb03420.x;
Leung T.K.C., Hall C., Monfries C., Lim L.;
"Trifluoperazine activates and releases latent ATP-generating enzymes
associated with the synaptic plasma membrane.";
J. Neurochem. 49:232-238(1987).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 261-323, AND TISSUE SPECIFICITY.
TISSUE=Glial tumor;
PubMed=6548307; DOI=10.1093/nar/12.18.6951;
Piechaczyk M., Blanchard J.-M., Marty L., Dani C., Panabieres F.,
el Sabrouty S., Fort P., Jeanteur P.;
"Post-transcriptional regulation of glyceraldehyde-3-phosphate-
dehydrogenase gene expression in rat tissues.";
Nucleic Acids Res. 12:6951-6963(1984).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 267-333.
PubMed=2413848; DOI=10.1016/0006-291X(85)91310-5;
Maehara Y., Fujiyoshi T., Takahashi K., Yamamoto M., Endo H.;
"1.5 kb mRNA abundantly expressed in rat tumors encodes a 37
kilodalton protein in vitro.";
Biochem. Biophys. Res. Commun. 131:800-805(1985).
[10]
S-NITROSYLATION.
PubMed=1281150;
Molina y Vedia L., McDonald B., Reep B., Brune B., Di Silvio M.,
Billiar T.R., Lapetina E.G.;
"Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate
dehydrogenase inhibits enzymatic activity and increases endogenous
ADP-ribosylation.";
J. Biol. Chem. 267:24929-24932(1992).
[11]
S-NITROSYLATION AT CYS-150, ADP-RIBOSYLATION AT CYS-150, LACK OF
S-NITROSYLATION AT CYS-154, AND ACTIVE SITE.
PubMed=8626764; DOI=10.1074/jbc.271.8.4209;
Mohr S., Stamler J.S., Brune B.;
"Posttranslational modification of glyceraldehyde-3-phosphate
dehydrogenase by S-nitrosylation and subsequent NADH attachment.";
J. Biol. Chem. 271:4209-4214(1996).
[12]
FUNCTION, INTERACTION WITH CHP1, ASSOCIATION WITH MICROTUBULES, AND
SUBCELLULAR LOCATION.
PubMed=15312048; DOI=10.1042/BJ20040622;
Andrade J., Pearce S.T., Zhao H., Barroso M.;
"Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and
microtubules.";
Biochem. J. 384:327-336(2004).
[13]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SIAH1,
S-NITROSYLATION AT CYS-150, AND MUTAGENESIS OF CYS-150; LYS-225;
PRO-234 AND THR-235.
PubMed=15951807; DOI=10.1038/ncb1268;
Hara M.R., Agrawal N., Kim S.F., Cascio M.B., Fujimuro M., Ozeki Y.,
Takahashi M., Cheah J.H., Tankou S.K., Hester L.D., Ferris C.D.,
Hayward S.D., Snyder S.H., Sawa A.;
"S-nitrosylated GAPDH initiates apoptotic cell death by nuclear
translocation following Siah1 binding.";
Nat. Cell Biol. 7:665-674(2005).
[14]
SUBCELLULAR LOCATION, AND INTERACTION WITH RILPL1 AND SIAH1.
PubMed=19607794; DOI=10.1016/j.neuron.2009.05.024;
Sen N., Hara M.R., Ahmad A.S., Cascio M.B., Kamiya A., Ehmsen J.T.,
Agrawal N., Hester L., Dore S., Snyder S.H., Sawa A.;
"GOSPEL: a neuroprotective protein that binds to GAPDH upon S-
nitrosylation.";
Neuron 63:81-91(2009).
[15]
FUNCTION AS NITROSYLASE, SUBCELLULAR LOCATION, INTERACTION WITH SIRT1,
S-NITROSYLATION AT CYS-150, AND MUTAGENESIS OF SER-149; CYS-150;
THR-151 AND THR-152.
PubMed=20972425; DOI=10.1038/ncb2114;
Kornberg M.D., Sen N., Hara M.R., Juluri K.R., Nguyen J.V.,
Snowman A.M., Law L., Hester L.D., Snyder S.H.;
"GAPDH mediates nitrosylation of nuclear proteins.";
Nat. Cell Biol. 12:1094-1100(2010).
-!- FUNCTION: 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 (By similarity). {ECO:0000250,
ECO:0000269|PubMed:10424669, ECO:0000269|PubMed:15312048,
ECO:0000269|PubMed:15951807, ECO:0000269|PubMed:20972425}.
-!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
{ECO:0000255|PROSITE-ProRule:PRU10009}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 1/5.
-!- SUBUNIT: Homotetramer. Interacts with EIF1AD, USP25, PRKCI and
WARS. Interacts with TPPP; the interaction is direct (By
similarity). 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. Interacts with
phosphorylated RPL13A (By similarity). Associates with
microtubules. Component of the GAIT complex. Interacts with FKBP6;
leading to inhibit GAPDH catalytic activity (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P04406}.
-!- INTERACTION:
P47196:Akt1; NbExp=3; IntAct=EBI-349219, EBI-7204362;
P61023:Chp1; NbExp=3; IntAct=EBI-349219, EBI-917838;
Q80Z30:Ppm1e; NbExp=5; IntAct=EBI-349219, EBI-7473061;
P19357:Slc2a4; NbExp=2; IntAct=EBI-349219, EBI-915426;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton.
Nucleus. Note=Translocates to the nucleus following S-
nitrosylation and interaction with SIAH1, which contains a nuclear
localization signal. Colocalizes with CHP1 to small punctate
structures along the microtubules tracks.
-!- TISSUE SPECIFICITY: High levels in skeletal muscle and heart, low
levels in liver, brain, and kidney. {ECO:0000269|PubMed:6548307}.
-!- DOMAIN: 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. {ECO:0000250|UniProtKB:P04406}.
-!- PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1,
followed by translocation to the nucleus. The effect of S-
nitrosylation on enzymatic activity is unclear: according to some
authors, it inhibits enzymatic activity and increases endogenous
ADP-ribosylation, inhibiting the enzyme in a non-reversible manner
(PubMed:8626764). According to others, it does not affect
glycolysis (PubMed:15951807). ADP-ribosylation is likely to be a
pathophysiological event associated with inhibition of
gluconeogenesis. 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). {ECO:0000250|UniProtKB:P04406,
ECO:0000269|PubMed:1281150, ECO:0000269|PubMed:15951807,
ECO:0000269|PubMed:20972425, ECO:0000269|PubMed:8626764}.
-!- PTM: ISGylated. {ECO:0000250}.
-!- PTM: Sulfhydration at Cys-150 increases catalytic activity.
{ECO:0000250}.
-!- PTM: Oxidative stress can promote the formation of high molecular
weight disulfide-linked GAPDH aggregates, through a process called
nucleocytoplasmic coagulation. {ECO:0000250|UniProtKB:P04406}.
-!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
dehydrogenase family. {ECO:0000305}.
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EMBL; X02231; CAA26150.1; -; mRNA.
EMBL; M17701; AAA41193.1; -; mRNA.
EMBL; AB017801; BAB11748.1; -; mRNA.
EMBL; AF106860; AAD08929.2; -; mRNA.
EMBL; BC059110; AAH59110.1; -; mRNA.
EMBL; BC087743; AAH87743.1; -; mRNA.
EMBL; M29341; AAA40814.1; -; mRNA.
EMBL; M11561; AAA41795.1; -; mRNA.
PIR; A23013; DERTG.
RefSeq; NP_058704.1; NM_017008.4.
RefSeq; XP_017447924.1; XM_017592435.1.
RefSeq; XP_017458425.1; XM_017602936.1.
UniGene; Rn.129558; -.
UniGene; Rn.91450; -.
ProteinModelPortal; P04797; -.
SMR; P04797; -.
BioGrid; 246554; 8.
CORUM; P04797; -.
IntAct; P04797; 8.
MINT; P04797; -.
STRING; 10116.ENSRNOP00000040878; -.
ChEMBL; CHEMBL2176832; -.
MoonProt; P04797; -.
iPTMnet; P04797; -.
PhosphoSitePlus; P04797; -.
World-2DPAGE; 0004:P04797; -.
PaxDb; P04797; -.
PRIDE; P04797; -.
Ensembl; ENSRNOT00000050443; ENSRNOP00000040878; ENSRNOG00000018630.
GeneID; 108351137; -.
GeneID; 24383; -.
KEGG; rno:108351137; -.
KEGG; rno:24383; -.
UCSC; RGD:2661; rat.
CTD; 2597; -.
RGD; 2661; Gapdh.
eggNOG; KOG0657; Eukaryota.
eggNOG; COG0057; LUCA.
GeneTree; ENSGT00760000119172; -.
HOGENOM; HOG000071678; -.
HOVERGEN; HBG000227; -.
InParanoid; P04797; -.
KO; K00134; -.
OMA; FTLENMV; -.
OrthoDB; EOG091G0B1Y; -.
PhylomeDB; P04797; -.
TreeFam; TF300533; -.
BRENDA; 1.2.1.12; 5301.
SABIO-RK; P04797; -.
UniPathway; UPA00109; UER00184.
PRO; PR:P04797; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000018630; -.
Genevisible; P04797; RN.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0097452; C:GAIT complex; ISS:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0035605; F:peptidyl-cysteine S-nitrosylase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IMP:RGD.
GO; GO:0005975; P:carbohydrate metabolic process; IDA:RGD.
GO; GO:0006094; P:gluconeogenesis; IDA:RGD.
GO; GO:0006096; P:glycolytic process; IDA:RGD.
GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
GO; GO:0051402; P:neuron apoptotic process; IDA:UniProtKB.
GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
GO; GO:0060359; P:response to ammonium ion; IDA:RGD.
InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
InterPro; IPR020830; GlycerAld_3-P_DH_AS.
InterPro; IPR020829; GlycerAld_3-P_DH_cat.
InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
PANTHER; PTHR10836; PTHR10836; 1.
Pfam; PF02800; Gp_dh_C; 1.
Pfam; PF00044; Gp_dh_N; 1.
PIRSF; PIRSF000149; GAP_DH; 1.
PRINTS; PR00078; G3PDHDRGNASE.
SMART; SM00846; Gp_dh_N; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01534; GAPDH-I; 1.
PROSITE; PS00071; GAPDH; 1.
1: Evidence at protein level;
Acetylation; ADP-ribosylation; Apoptosis; Complete proteome;
Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycolysis;
Isopeptide bond; Methylation; NAD; Nucleus; Oxidoreductase;
Phosphoprotein; Reference proteome; S-nitrosylation; Transferase;
Translation regulation; Ubl conjugation.
CHAIN 1 333 Glyceraldehyde-3-phosphate dehydrogenase.
/FTId=PRO_0000145494.
NP_BIND 11 12 NAD. {ECO:0000250}.
REGION 1 146 Interaction with WARS. {ECO:0000250}.
REGION 149 151 Glyceraldehyde 3-phosphate binding.
{ECO:0000250}.
REGION 209 210 Glyceraldehyde 3-phosphate binding.
{ECO:0000250}.
MOTIF 243 248 [IL]-x-C-x-x-[DE] motif.
{ECO:0000250|UniProtKB:P04406}.
ACT_SITE 150 150 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU10009,
ECO:0000269|PubMed:8626764}.
BINDING 33 33 NAD. {ECO:0000250}.
BINDING 78 78 NAD; via carbonyl oxygen. {ECO:0000250}.
BINDING 120 120 NAD. {ECO:0000250}.
BINDING 180 180 Glyceraldehyde 3-phosphate.
{ECO:0000250}.
BINDING 232 232 Glyceraldehyde 3-phosphate.
{ECO:0000250}.
BINDING 314 314 NAD. {ECO:0000250}.
SITE 154 154 Not nitrosylated.
{ECO:0000269|PubMed:8626764}.
SITE 177 177 Activates thiol group during catalysis.
{ECO:0000250}.
MOD_RES 3 3 N6,N6-dimethyllysine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 7 7 Deamidated asparagine. {ECO:0000250}.
MOD_RES 40 40 Phosphotyrosine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 59 59 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 62 62 Deamidated asparagine. {ECO:0000250}.
MOD_RES 64 64 N6,N6-dimethyllysine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 68 68 Deamidated asparagine. {ECO:0000250}.
MOD_RES 73 73 Phosphothreonine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 146 146 Phosphoserine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 147 147 Deamidated asparagine. {ECO:0000250}.
MOD_RES 149 149 Phosphoserine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 150 150 ADP-ribosylcysteine; by autocatalysis; in
irreversibly inhibited form.
{ECO:0000269|PubMed:8626764}.
MOD_RES 150 150 Cysteine persulfide. {ECO:0000250}.
MOD_RES 150 150 S-nitrosocysteine; in reversibly
inhibited form.
{ECO:0000269|PubMed:15951807,
ECO:0000269|PubMed:20972425,
ECO:0000269|PubMed:8626764}.
MOD_RES 151 151 Phosphothreonine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 153 153 Deamidated asparagine. {ECO:0000250}.
MOD_RES 175 175 Phosphothreonine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 180 180 Phosphothreonine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 182 182 Phosphothreonine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 192 192 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 192 192 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 192 192 N6-malonyllysine; alternate.
{ECO:0000250}.
MOD_RES 209 209 Phosphothreonine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 213 213 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 213 213 N6-malonyllysine; alternate.
{ECO:0000250}.
MOD_RES 217 217 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 223 223 Deamidated asparagine. {ECO:0000250}.
MOD_RES 225 225 N6,N6-dimethyllysine; alternate.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 225 225 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 227 227 Phosphothreonine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 235 235 Phosphothreonine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 239 239 Phosphoserine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 245 245 S-nitrosocysteine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 252 252 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 258 258 N6,N6-dimethyllysine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 261 261 N6,N6-dimethyllysine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 314 314 Deamidated asparagine. {ECO:0000250}.
MOD_RES 331 331 Phosphoserine.
{ECO:0000250|UniProtKB:P04406}.
MOD_RES 332 332 N6,N6-dimethyllysine.
{ECO:0000250|UniProtKB:P04406}.
CROSSLNK 184 184 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P04406}.
MUTAGEN 149 149 S->A: Does not affect interaction with
SIRT1. {ECO:0000269|PubMed:20972425}.
MUTAGEN 150 150 C->S: Abolishes S-nitrosylation and
subsequent nuclear translocation.
{ECO:0000269|PubMed:15951807,
ECO:0000269|PubMed:20972425}.
MUTAGEN 151 151 T->A: Does not affect interaction with
SIRT1. {ECO:0000269|PubMed:20972425}.
MUTAGEN 152 152 T->A: Abolishes interaction and
subsequent nitrosylation of SIRT1.
{ECO:0000269|PubMed:20972425}.
MUTAGEN 225 225 K->A: Abolishes interaction with SIAH1.
{ECO:0000269|PubMed:15951807}.
MUTAGEN 234 234 P->A: Does not affect interaction with
SIAH1. {ECO:0000269|PubMed:15951807}.
MUTAGEN 235 235 T->A: Does not affect interaction with
SIAH1. {ECO:0000269|PubMed:15951807}.
CONFLICT 81 82 AN -> VK (in Ref. 1; AAA41193).
{ECO:0000305}.
CONFLICT 129 129 F -> L (in Ref. 5; AAH87743).
{ECO:0000305}.
CONFLICT 305 305 F -> I (in Ref. 1; AAA41193 and 8;
CAA26150). {ECO:0000305}.
SEQUENCE 333 AA; 35828 MW; D9E5ED4F38544C77 CRC64;
MVKVGVNGFG RIGRLVTRAA FSCDKVDIVA INDPFIDLNY MVYMFQYDST HGKFNGTVKA
ENGKLVINGK PITIFQERDP ANIKWGDAGA EYVVESTGVF TTMEKAGAHL KGGAKRVIIS
APSADAPMFV MGVNHEKYDN SLKIVSNASC TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT
ATQKTVDGPS GKLWRDGRGA AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV
VDLTCRLEKP AKYDDIKKVV KQAAEGPLKG ILGYTEDQVV SCDFNSNSHS STFDAGAGIA
LNDNFVKLIS WYDNEYGYSN RVVDLMAYMA SKE


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U1932r CLIA kit 38 kDa BFA-dependent ADP-ribosylation substrate,BARS-38,Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Rat,Rattus norvegicus 96T
E1932r ELISA kit 38 kDa BFA-dependent ADP-ribosylation substrate,BARS-38,Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Rat,Rattus norvegicus 96T
U1932r CLIA 38 kDa BFA-dependent ADP-ribosylation substrate,BARS-38,Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Rat,Rattus norvegicus 96T
E1932r ELISA 38 kDa BFA-dependent ADP-ribosylation substrate,BARS-38,Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Rat,Rattus norvegicus 96T
U1932p CLIA GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Pig,Sus scrofa 96T
U1932p CLIA kit GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Pig,Sus scrofa 96T
E1932p ELISA kit GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Pig,Sus scrofa 96T
E1932p ELISA GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH,Pig,Sus scrofa 96T
U1932m CLIA Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Mouse,Mus musculus,Peptidyl-cysteine S-nitrosylase GAPDH 96T
E1932b ELISA Bos taurus,Bovine,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH 96T
U1932m CLIA kit Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Mouse,Mus musculus,Peptidyl-cysteine S-nitrosylase GAPDH 96T
U1932b CLIA Bos taurus,Bovine,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH 96T
E1932m ELISA kit Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Mouse,Mus musculus,Peptidyl-cysteine S-nitrosylase GAPDH 96T
E1932b ELISA kit Bos taurus,Bovine,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH 96T
E1932m ELISA Gapd,GAPDH,Gapdh,Glyceraldehyde-3-phosphate dehydrogenase,Mouse,Mus musculus,Peptidyl-cysteine S-nitrosylase GAPDH 96T
U1932b CLIA kit Bos taurus,Bovine,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH 96T
E1932Rb ELISA kit GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Oryctolagus cuniculus,Peptidyl-cysteine S-nitrosylase GAPDH,Rabbit 96T
U1932Rb CLIA GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Oryctolagus cuniculus,Peptidyl-cysteine S-nitrosylase GAPDH,Rabbit 96T
U1932Rb CLIA kit GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Oryctolagus cuniculus,Peptidyl-cysteine S-nitrosylase GAPDH,Rabbit 96T
E1932Rb ELISA GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Oryctolagus cuniculus,Peptidyl-cysteine S-nitrosylase GAPDH,Rabbit 96T
E1932h ELISA kit CDABP0047,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Homo sapiens,Human,OK_SW-cl.12,Peptidyl-cysteine S-nitrosylase GAPDH 96T
U1932h CLIA CDABP0047,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Homo sapiens,Human,OK_SW-cl.12,Peptidyl-cysteine S-nitrosylase GAPDH 96T
E1932h ELISA CDABP0047,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Homo sapiens,Human,OK_SW-cl.12,Peptidyl-cysteine S-nitrosylase GAPDH 96T
U1932h CLIA kit CDABP0047,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Homo sapiens,Human,OK_SW-cl.12,Peptidyl-cysteine S-nitrosylase GAPDH 96T
E1932c ELISA Chicken,Gallus gallus,GAPD,GAPDH,GAPDH,Glyceraldehyde-3-phosphate dehydrogenase,Peptidyl-cysteine S-nitrosylase GAPDH 96T


 

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