G3P_PIG
ID G3P_PIG Reviewed; 333 AA.
AC P00355; O18816; P79299; P79317; Q29546;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE Short=GAPDH;
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P04406};
DE AltName: Full=Peptidyl-cysteine S-nitrosylase GAPDH {ECO:0000305};
DE EC=2.6.99.- {ECO:0000250|UniProtKB:P04797};
GN Name=GAPDH; Synonyms=GAPD;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Behdjani R., Silversides D.W.;
RT "Sus scrofa glyceraldehyde-3-phosphate dehydrogenase, genomic and cDNA
RT sequences.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-126.
RC TISSUE=Small intestine;
RA Winteroe A.K., Fredholm M.;
RT "Evaluation and characterization of a porcine small intestine cDNA
RT library.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-333.
RX PubMed=4299800; DOI=10.1038/2191025a0;
RA Harris J.I., Perham R.N.;
RT "Glyceraldehyde 3-phosphate dehydrogenase from pig muscle.";
RL Nature 219:1025-1028(1968).
RN [4]
RP SEQUENCE REVISION TO 46.
RA Harris J.I., Davidson B.E., Sajgo M., Noller H.F., Perham R.N.;
RL (In) Shugar D. (eds.);
RL Enzymes and isoenzymes: structure, properties and function, pp.1-15,
RL Academic Press, London and New York (1970).
RN [5]
RP PROTEIN SEQUENCE OF 2-23.
RC TISSUE=Liver;
RX PubMed=1201027; DOI=10.1016/0006-291x(75)90279-x;
RA Kulbe K.D., Jackson K.W., Tang J.;
RT "Structural evidence for a liver-specific glyceraldehyde-3-phosphate
RT dehydrogenase.";
RL Biochem. Biophys. Res. Commun. 67:35-42(1975).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 15-301.
RA Foss D.L., Murtaugh M.P.;
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 174-323.
RX PubMed=9241041; DOI=10.1095/biolreprod57.2.286;
RA Yelich J.V., Pomp D., Geisert R.D.;
RT "Detection of transcripts for retinoic acid receptors, retinol-binding
RT protein, and transforming growth factors during rapid trophoblastic
RT elongation in the porcine conceptus.";
RL Biol. Reprod. 57:286-294(1997).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 299-333.
RC TISSUE=Skeletal muscle;
RA Davoli R., Zambonelli P., Fontanesi L., Bigi D., Costosi E., Russo V.;
RT "Isolation and characterization of cDNA clones coding for porcine muscle
RT proteins.";
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and
CC nitrosylase activities, thereby playing a role in glycolysis and
CC nuclear functions, respectively. Glyceraldehyde-3-phosphate
CC dehydrogenase is a key enzyme in glycolysis that catalyzes the first
CC step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P)
CC into 3-phospho-D-glyceroyl phosphate (By similarity). Modulates the
CC organization and assembly of the cytoskeleton. Facilitates the CHP1-
CC dependent microtubule and membrane associations through its ability to
CC stimulate the binding of CHP1 to microtubules (By similarity).
CC Component of the GAIT (gamma interferon-activated inhibitor of
CC translation) complex which mediates interferon-gamma-induced
CC transcript-selective translation inhibition in inflammation processes.
CC Upon interferon-gamma treatment assembles into the GAIT complex which
CC binds to stem loop-containing GAIT elements in the 3'-UTR of diverse
CC inflammatory mRNAs (such as ceruplasmin) and suppresses their
CC translation. Also plays a role in innate immunity by promoting TNF-
CC induced NF-kappa-B activation and type I interferon production, via
CC interaction with TRAF2 and TRAF3, respectively (By similarity).
CC Participates in nuclear events including transcription, RNA transport,
CC DNA replication and apoptosis. Nuclear functions are probably due to
CC the nitrosylase activity that mediates cysteine S-nitrosylation of
CC nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity).
CC {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P04797}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC Evidence={ECO:0000250|UniProtKB:P04406, ECO:0000255|PROSITE-
CC ProRule:PRU10009};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L-
CC cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:66684, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:17089,
CC Rhea:RHEA-COMP:17090, Rhea:RHEA-COMP:17091, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:149494; Evidence={ECO:0000250|UniProtKB:P04797};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685;
CC Evidence={ECO:0000250|UniProtKB:P04797};
CC -!- ACTIVITY REGULATION: Glyceraldehyde-3-phosphate dehydrogenase activity
CC is inhibited by fumarate, via the formation of S-(2-succinyl)cysteine
CC residues. {ECO:0000250|UniProtKB:P04797}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5.
CC -!- SUBUNIT: Homotetramer (By similarity). Interacts with TPPP; the
CC interaction is direct (By similarity). Interacts (when S-nitrosylated)
CC with SIAH1; leading to nuclear translocation. Interacts with
CC RILPL1/GOSPEL, leading to prevent the interaction between GAPDH and
CC SIAH1 and prevent nuclear translocation. Interacts with CHP1; the
CC interaction increases the binding of CHP1 with microtubules. Associates
CC with microtubules (By similarity). Interacts with EIF1AD, USP25, PRKCI
CC and WARS1. Interacts with phosphorylated RPL13A; inhibited by
CC oxidatively-modified low-densitity lipoprotein (LDL(ox)). Component of
CC the GAIT complex. Interacts with FKBP6; leading to inhibit GAPDH
CC catalytic activity. Interacts with TRAF2, promoting TRAF2
CC ubiquitination. Interacts with TRAF3, promoting TRAF3 ubiquitination
CC (By similarity). {ECO:0000250|UniProtKB:P04406,
CC ECO:0000250|UniProtKB:P04797, ECO:0000250|UniProtKB:P10096}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}.
CC Note=Translocates to the nucleus following S-nitrosylation and
CC interaction with SIAH1, which contains a nuclear localization signal.
CC Colocalizes with CHP1 to small punctate structures along the
CC microtubules tracks. {ECO:0000250|UniProtKB:P04797}.
CC -!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
CC cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
CC transnitrosylase complex. {ECO:0000250|UniProtKB:P04406}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P04406}.
CC -!- PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1,
CC followed by translocation to the nucleus S-nitrosylation of Cys-245 is
CC induced by interferon-gamma and LDL(ox) implicating the iNOS-S100A8/9
CC transnitrosylase complex and seems to prevent interaction with
CC phosphorylated RPL13A and to interfere with GAIT complex activity (By
CC similarity). {ECO:0000250|UniProtKB:P04406,
CC ECO:0000250|UniProtKB:P04797}.
CC -!- PTM: Sulfhydration at Cys-150 increases catalytic activity.
CC {ECO:0000250|UniProtKB:P16858}.
CC -!- PTM: Oxidative stress can promote the formation of high molecular
CC weight disulfide-linked GAPDH aggregates, through a process called
CC nucleocytoplasmic coagulation. {ECO:0000250|UniProtKB:P04406}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AF017079; AAB94053.1; -; mRNA.
DR EMBL; Z84063; CAB06323.1; -; mRNA.
DR EMBL; U48832; AAA91804.1; -; mRNA.
DR EMBL; U82261; AAB40155.1; -; mRNA.
DR EMBL; X94251; CAA63935.1; -; mRNA.
DR PIR; B12055; B12055.
DR RefSeq; NP_001193288.1; NM_001206359.1.
DR PDB; 5DDI; X-ray; 2.40 A; P/R/S=2-333.
DR PDB; 5TSO; X-ray; 1.90 A; P/R/S=1-333.
DR PDBsum; 5DDI; -.
DR PDBsum; 5TSO; -.
DR AlphaFoldDB; P00355; -.
DR SMR; P00355; -.
DR IntAct; P00355; 1.
DR STRING; 9823.ENSSSCP00000000740; -.
DR Allergome; 12129; Sus s GAPDH.
DR PaxDb; P00355; -.
DR PeptideAtlas; P00355; -.
DR PRIDE; P00355; -.
DR Ensembl; ENSSSCT00005060912; ENSSSCP00005037648; ENSSSCG00005037806.
DR Ensembl; ENSSSCT00015092759; ENSSSCP00015037932; ENSSSCG00015069184.
DR Ensembl; ENSSSCT00035111381; ENSSSCP00035048787; ENSSSCG00035081064.
DR Ensembl; ENSSSCT00035111396; ENSSSCP00035048801; ENSSSCG00035081064.
DR Ensembl; ENSSSCT00040088131; ENSSSCP00040038735; ENSSSCG00040064450.
DR Ensembl; ENSSSCT00045030090; ENSSSCP00045020842; ENSSSCG00045017499.
DR Ensembl; ENSSSCT00055060969; ENSSSCP00055048878; ENSSSCG00055030580.
DR Ensembl; ENSSSCT00060058387; ENSSSCP00060024997; ENSSSCG00060043031.
DR Ensembl; ENSSSCT00065107183; ENSSSCP00065047768; ENSSSCG00065077443.
DR Ensembl; ENSSSCT00070038969; ENSSSCP00070032633; ENSSSCG00070019692.
DR Ensembl; ENSSSCT00070038975; ENSSSCP00070032639; ENSSSCG00070019692.
DR GeneID; 396823; -.
DR KEGG; ssc:396823; -.
DR CTD; 2597; -.
DR eggNOG; KOG0657; Eukaryota.
DR InParanoid; P00355; -.
DR OMA; NCVAPMA; -.
DR Reactome; R-SSC-70171; Glycolysis.
DR Reactome; R-SSC-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097452; C:GAIT complex; ISS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IEA:Ensembl.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0035605; F:peptidyl-cysteine S-nitrosylase activity; ISS:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IEA:Ensembl.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0050832; P:defense response to fungus; IEA:Ensembl.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0051873; P:killing by host of symbiont cells; IEA:Ensembl.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10836; PTHR10836; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ADP-ribosylation; Apoptosis; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Glycolysis; Immunity;
KW Innate immunity; Isopeptide bond; Methylation; NAD; Nucleus;
KW Oxidoreductase; Phosphoprotein; Reference proteome; S-nitrosylation;
KW Transferase; Translation regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1201027,
FT ECO:0000269|PubMed:4299800"
FT CHAIN 2..333
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000145491"
FT REGION 2..146
FT /note="Interaction with WARS1"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOTIF 243..248
FT /note="[IL]-x-C-x-x-[DE] motif"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 3
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 7
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 40
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 62
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 64
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 68
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 73
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 147
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 150
FT /note="ADP-ribosylcysteine; by autocatalysis; in
FT irreversibly inhibited form"
FT /evidence="ECO:0000250|UniProtKB:P04797"
FT MOD_RES 150
FT /note="Cysteine persulfide"
FT /evidence="ECO:0000250|UniProtKB:P16858"
FT MOD_RES 150
FT /note="S-(2-succinyl)cysteine"
FT /evidence="ECO:0000250|UniProtKB:P04797"
FT MOD_RES 150
FT /note="S-nitrosocysteine; in reversibly inhibited form"
FT /evidence="ECO:0000250|UniProtKB:P04797"
FT MOD_RES 151
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 153
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 175
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 192
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 192
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 192
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 209
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 213
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 213
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 217
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 223
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 225
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 225
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 227
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 245
FT /note="S-(2-succinyl)cysteine"
FT /evidence="ECO:0000250|UniProtKB:P04797"
FT MOD_RES 245
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 258
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 261
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 314
FT /note="Deamidated asparagine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 332
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT CROSSLNK 184
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT CONFLICT 7
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 70..71
FT /note="KA -> NP (in Ref. 1; AAB94053)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="N -> K (in Ref. 1; AAB94053)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..91
FT /note="AT -> TA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="T -> E (in Ref. 1; AAB94053)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="V -> M (in Ref. 1; AAB94053)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="V -> I (in Ref. 1; AAB94053)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="H -> N (in Ref. 1; AAB94053)"
FT /evidence="ECO:0000305"
FT CONFLICT 201
FT /note="A -> L (in Ref. 1; AAB94053)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="P -> A (in Ref. 1; AAB94053)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="D -> H (in Ref. 1; AAB94053)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="C -> S (in Ref. 1; AAB94053)"
FT /evidence="ECO:0000305"
FT CONFLICT 286..287
FT /note="SD -> DS (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="W -> S (in Ref. 1; AAB94053)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="R -> W (in Ref. 7; AAB40155)"
FT /evidence="ECO:0000305"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:5TSO"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:5TSO"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 150..166
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:5TSO"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5TSO"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 226..232
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 239..249
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 253..265
FT /evidence="ECO:0007829|PDB:5TSO"
FT TURN 266..271
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:5TSO"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:5TSO"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:5TSO"
FT HELIX 316..332
FT /evidence="ECO:0007829|PDB:5TSO"
SQ SEQUENCE 333 AA; 35836 MW; 5F29175285D897BB CRC64;
MVKVGVNGFG RIGRLVTRAA FNSGKVDIVA INDPFIDLHY MVYMFQYDST HGKFHGTVKA
ENGKLVINGK AITIFQERDP ANIKWGDAGA TYVVESTGVF TTMEKAGAHL KGGAKRVIIS
APSADAPMFV MGVNHEKYDN SLKIVSNASC TTNCLAPLAK VIHDHFGIVE GLMTTVHAIT
ATQKTVDGPS GKLWRDGRGA AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV
VDLTCRLEKP AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSDTHS STFDAGAGIA
LNDHFVKLIS WYDNEFGYSN RVVDLMVHMA SKE
