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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: glycolysis

This protein is involved in step 1 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (Gapdh), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm7293), Glyceraldehyde-3-phosphate dehydrogenase (Gapdhs), Glyceraldehyde-3-phosphate dehydrogenase (Gm3839)
  2. Phosphoglycerate kinase 2 (Pgk2), Phosphoglycerate kinase 1 (Pgk1)
  3. no protein annotated in this organism
  4. Gamma-enolase (Eno2), Alpha-enolase (Eno1), Beta-enolase (Eno3), Enolase 4 (Eno4)
  5. Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKLR (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase (Pklr), Pyruvate kinase PKM (Pkm)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei33NADBy similarity1
Binding sitei78NAD; via carbonyl oxygenBy similarity1
Binding sitei120NADBy similarity1
Active sitei150NucleophilePROSITE-ProRule annotation1
Sitei177Activates thiol group during catalysisBy similarity1
Binding sitei180Glyceraldehyde 3-phosphateBy similarity1
Binding sitei232Glyceraldehyde 3-phosphateBy similarity1
Binding sitei314NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi11 – 12NADBy similarity2

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

ReactomeiR-MMU-70171. Glycolysis.
R-MMU-70263. Gluconeogenesis.
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
Proteomesi
  • UP000000589 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

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi150C → S: Abolishes sulfhydration and induces impaired enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001454902 – 333Glyceraldehyde-3-phosphate dehydrogenaseAdd BLAST332

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N6,N6-dimethyllysineBy similarity1
Modified residuei7Deamidated asparagineBy similarity1
Modified residuei40PhosphotyrosineBy similarity1
Modified residuei59N6-acetyllysineBy similarity1
Modified residuei62Deamidated asparagineBy similarity1
Modified residuei64N6,N6-dimethyllysineBy similarity1
Modified residuei68Deamidated asparagineBy similarity1
Modified residuei73PhosphothreonineBy similarity1
Modified residuei120PhosphoserineBy similarity1
Modified residuei146PhosphoserineBy similarity1
Modified residuei147Deamidated asparagineBy similarity1
Modified residuei149PhosphoserineBy similarity1
Modified residuei150ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited formBy similarity1
Modified residuei150Cysteine persulfide1 Publication1
Modified residuei150S-nitrosocysteine; in reversibly inhibited formBy similarity1
Modified residuei151PhosphothreonineBy similarity1
Modified residuei153Deamidated asparagineBy similarity1
Modified residuei175PhosphothreonineBy similarity1
Modified residuei180PhosphothreonineBy similarity1
Modified residuei182PhosphothreonineBy similarity1
Modified residuei192N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei192N6-acetyllysine; alternateBy similarity1
Modified residuei192N6-malonyllysine; alternateBy similarity1
Modified residuei209PhosphothreonineBy similarity1
Modified residuei213N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei213N6-malonyllysine; alternateBy similarity1
Modified residuei217N6-acetyllysineBy similarity1
Modified residuei223Deamidated asparagineBy similarity1
Modified residuei225N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei225N6-acetyllysine; alternateBy similarity1
Modified residuei227PhosphothreonineBy similarity1
Modified residuei235PhosphothreonineBy similarity1
Modified residuei239PhosphoserineBy similarity1
Modified residuei245S-nitrosocysteineBy similarity1
Modified residuei252N6-acetyllysineBy similarity1
Modified residuei258N6,N6-dimethyllysineBy similarity1
Modified residuei261N6,N6-dimethyllysineBy similarity1
Modified residuei310PhosphoserineBy similarity1
Modified residuei314Deamidated asparagineBy similarity1
Modified residuei331PhosphoserineBy similarity1
Modified residuei332N6,N6-dimethyllysineBy similarity1

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.
Oxidative stress can promote the formation of high molecular weight disulfide-linked GAPDH aggregates, through a process called nucleocytoplasmic coagulation.By similarity

Keywords - PTMi

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

Proteomic databases

EPDiP16858.
MaxQBiP16858.
PaxDbiP16858.
PRIDEiP16858.
TopDownProteomicsiP16858.

2D gel databases

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

PTM databases

iPTMnetiP16858.
PhosphoSitePlusiP16858.
SwissPalmiP16858.

Expressioni

Gene expression databases

BgeeiENSMUSG00000057666.
CleanExiMM_GAPDH.
ExpressionAtlasiP16858. baseline and differential.
GenevisibleiP16858. MM.

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

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • microtubule binding Source: UniProtKB

Protein-protein interaction databases

BioGridi199829. 11 interactors.
785307. 1 interactor.
DIPiDIP-31404N.
IntActiP16858. 23 interactors.
MINTiMINT-1869564.
STRINGi10090.ENSMUSP00000113213.

Structurei

3D structure databases

ProteinModelPortaliP16858.
SMRiP16858.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 146Interaction with WARSBy similarityAdd BLAST145
Regioni149 – 151Glyceraldehyde 3-phosphate bindingBy similarity3
Regioni209 – 210Glyceraldehyde 3-phosphate bindingBy similarity2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi243 – 248[IL]-x-C-x-x-[DE] motifBy similarity6

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

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
GeneTreeiENSGT00760000119172.
HOVERGENiHBG000227.
InParanoidiP16858.
KOiK00134.
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]
SUPFAMiSSF51735. SSF51735. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti3K → E in BAE40174 (PubMed:16141072).Curated1
Sequence conflicti30A → V in AAH92267 (PubMed:15489334).Curated1
Sequence conflicti82N → S in BAE35989 (PubMed:16141072).Curated1
Sequence conflicti84K → E in BAE40174 (PubMed:16141072).Curated1
Sequence conflicti89G → S in BAE26016 (PubMed:16141072).Curated1
Sequence conflicti91E → K in BAE35989 (PubMed:16141072).Curated1
Sequence conflicti134N → D in AAH85315 (PubMed:15489334).Curated1
Sequence conflicti195R → C in AAH85315 (PubMed:15489334).Curated1
Sequence conflicti300A → S in AAH85315 (PubMed:15489334).Curated1

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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199829. 11 interactors.
785307. 1 interactor.
DIPiDIP-31404N.
IntActiP16858. 23 interactors.
MINTiMINT-1869564.
STRINGi10090.ENSMUSP00000113213.

PTM databases

iPTMnetiP16858.
PhosphoSitePlusiP16858.
SwissPalmiP16858.

2D gel databases

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

Proteomic databases

EPDiP16858.
MaxQBiP16858.
PaxDbiP16858.
PRIDEiP16858.
TopDownProteomicsiP16858.

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

CTDi100042025.
2597.
MGIiMGI:95640. Gapdh.

Phylogenomic databases

eggNOGiKOG0657. Eukaryota.
COG0057. LUCA.
GeneTreeiENSGT00760000119172.
HOVERGENiHBG000227.
InParanoidiP16858.
KOiK00134.
PhylomeDBiP16858.
TreeFamiTF300533.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00184.
ReactomeiR-MMU-70171. Glycolysis.
R-MMU-70263. Gluconeogenesis.
SABIO-RKP16858.

Miscellaneous databases

PROiP16858.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000057666.
CleanExiMM_GAPDH.
ExpressionAtlasiP16858. baseline and differential.
GenevisibleiP16858. MM.

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]
SUPFAMiSSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR01534. GAPDH-I. 1 hit.
PROSITEiPS00071. GAPDH. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 177 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

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 one 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.