GAPDH

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 (By similarity).By similarity

Catalytic activityⁱ

D-glyceraldehyde 3-phosphate + phosphate + NAD⁺ = 3-phospho-D-glyceroyl phosphate + NADH.PROSITE-ProRule annotation

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:

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase (GAPDHS), Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (GAPDHS)
Phosphoglycerate kinase (LOC100348124), Phosphoglycerate kinase (PGK1), Phosphoglycerate kinase (PGK2)
no protein annotated in this organism
Beta-enolase (ENO3)
Pyruvate kinase PKM (PKM), Pyruvate kinase (pklr), Pyruvate kinase (PKM), Pyruvate kinase (PKLR), Pyruvate kinase (PKLR)

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 key	Position(s)	DescriptionActions	Length
Binding siteⁱ	33	NAD1 Publication	1
Binding siteⁱ	78	NAD; via carbonyl oxygen1 Publication	1
Binding siteⁱ	120	NADBy similarity	1
Active siteⁱ	150	Nucleophile	1
Siteⁱ	177	Activates thiol group during catalysis	1
Binding siteⁱ	180	Glyceraldehyde 3-phosphateBy similarity	1
Binding siteⁱ	232	Glyceraldehyde 3-phosphateBy similarity	1
Binding siteⁱ	314	NAD1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Nucleotide bindingⁱ	11 – 12	NAD1 Publication		2

GO - Molecular functionⁱ

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity Source: UniProtKB
microtubule binding Source: UniProtKB
NAD binding Source: InterPro
NADP binding Source: InterPro
peptidyl-cysteine S-nitrosylase activity Source: UniProtKB

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

glucose metabolic process Source: InterPro
glycolytic process Source: UniProtKB-UniPathway
microtubule cytoskeleton organization Source: UniProtKB
neuron apoptotic process Source: UniProtKB
peptidyl-cysteine S-trans-nitrosylation Source: UniProtKB
protein stabilization Source: UniProtKB
regulation of translation Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase, Transferase
Biological process	Apoptosis, Glycolysis, Translation regulation
Ligand	NAD

Enzyme and pathway databases

SABIO-RKⁱ	P46406
UniPathwayⁱ	UPA00109;UER00184

Protein family/group databases

MoonProtⁱ	P46406

MoonProtⁱ

P46406

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
Organismⁱ	Oryctolagus cuniculus (Rabbit)
Taxonomic identifierⁱ	9986 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus
Proteomesⁱ	UP000001811 Componentⁱ: Unplaced

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechⁱ

Protein family/group databases

Allergomeⁱ

12131 Ory c GAPDH

Chemistry databases

ChEMBLⁱ	CHEMBL1075199

ChEMBLⁱ

CHEMBL1075199

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000145493	1 – 333	Glyceraldehyde-3-phosphate dehydrogenaseAdd BLAST		333

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	3	N6,N6-dimethyllysineBy similarity	1
Modified residueⁱ	7	Deamidated asparagineBy similarity	1
Modified residueⁱ	40	PhosphotyrosineBy similarity	1
Modified residueⁱ	59	N6-acetyllysineBy similarity	1
Modified residueⁱ	62	Deamidated asparagineBy similarity	1
Modified residueⁱ	64	N6,N6-dimethyllysineBy similarity	1
Modified residueⁱ	68	Deamidated asparagineBy similarity	1
Modified residueⁱ	73	PhosphothreonineBy similarity	1
Modified residueⁱ	120	PhosphoserineBy similarity	1
Modified residueⁱ	146	PhosphoserineBy similarity	1
Modified residueⁱ	147	Deamidated asparagineBy similarity	1
Modified residueⁱ	149	PhosphoserineBy similarity	1
Modified residueⁱ	150	ADP-ribosylcysteine; by autocatalysis; in irreversibly inhibited formBy similarity	1
Modified residueⁱ	150	Cysteine persulfideBy similarity	1
Modified residueⁱ	150	S-nitrosocysteine; in reversibly inhibited formBy similarity	1
Modified residueⁱ	151	PhosphothreonineBy similarity	1
Modified residueⁱ	153	Deamidated asparagineBy similarity	1
Modified residueⁱ	175	PhosphothreonineBy similarity	1
Modified residueⁱ	180	PhosphothreonineBy similarity	1
Modified residueⁱ	182	PhosphothreonineBy similarity	1
Cross-linkⁱ	184	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residueⁱ	192	N6,N6-dimethyllysine; alternateBy similarity	1
Modified residueⁱ	192	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	192	N6-malonyllysine; alternateBy similarity	1
Modified residueⁱ	209	PhosphothreonineBy similarity	1
Modified residueⁱ	213	N6,N6-dimethyllysine; alternateBy similarity	1
Modified residueⁱ	213	N6-malonyllysine; alternateBy similarity	1
Modified residueⁱ	217	N6-acetyllysineBy similarity	1
Modified residueⁱ	223	Deamidated asparagineBy similarity	1
Modified residueⁱ	225	N6,N6-dimethyllysine; alternateBy similarity	1
Modified residueⁱ	225	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	227	PhosphothreonineBy similarity	1
Modified residueⁱ	235	PhosphothreonineBy similarity	1
Modified residueⁱ	239	PhosphoserineBy similarity	1
Modified residueⁱ	245	S-nitrosocysteineBy similarity	1
Modified residueⁱ	252	N6-acetyllysineBy similarity	1
Modified residueⁱ	258	N6,N6-dimethyllysineBy similarity	1
Modified residueⁱ	261	N6,N6-dimethyllysineBy similarity	1
Modified residueⁱ	310	PhosphoserineBy similarity	1
Modified residueⁱ	314	Deamidated asparagineBy similarity	1
Modified residueⁱ	331	PhosphoserineBy similarity	1
Modified residueⁱ	332	N6,N6-dimethyllysineBy similarity	1

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.By similarity

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, Isopeptide bond, Methylation, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

PRIDEⁱ	P46406

PRIDEⁱ

P46406

PTM databases

CarbonylDBⁱ	P46406
SwissPalmⁱ	P46406

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 phosphorylated RPL13A (By similarity). Component of the GAIT complex. Interacts with FKBP6; leading to inhibit GAPDH catalytic activity (By similarity).By similarity

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
Chp1	P61023	2	EBI-2750726,EBI-917838	From Rattus norvegicus.

With

Entry

#Exp.

IntAct

Notes

Chp1

P61023

2

EBI-2750726,EBI-917838

From Rattus norvegicus.

GO - Molecular functionⁱ

microtubule binding Source: UniProtKB

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	1172097, 1 interactor
Database of interacting proteins More...DIPⁱ	DIP-6005N
IntActⁱ	P46406, 3 interactors
Molecular INTeraction database More...MINTⁱ	P46406
STRINGⁱ	9986.ENSOCUP00000017094

Chemistry databases

BindingDBⁱ

P46406

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	3 – 7	Combined sources	5
Helixⁱ	11 – 23	Combined sources	13
Beta strandⁱ	25 – 32	Combined sources	8
Beta strandⁱ	34 – 36	Combined sources	3
Helixⁱ	38 – 46	Combined sources	9
Turnⁱ	49 – 51	Combined sources	3
Beta strandⁱ	58 – 61	Combined sources	4
Beta strandⁱ	64 – 67	Combined sources	4
Beta strandⁱ	70 – 75	Combined sources	6
Helixⁱ	80 – 82	Combined sources	3
Helixⁱ	85 – 88	Combined sources	4
Beta strandⁱ	91 – 95	Combined sources	5
Beta strandⁱ	97 – 99	Combined sources	3
Helixⁱ	103 – 107	Combined sources	5
Helixⁱ	108 – 112	Combined sources	5
Beta strandⁱ	115 – 121	Combined sources	7
Beta strandⁱ	124 – 126	Combined sources	3
Turnⁱ	131 – 133	Combined sources	3
Helixⁱ	135 – 137	Combined sources	3
Beta strandⁱ	143 – 146	Combined sources	4
Helixⁱ	150 – 166	Combined sources	17
Beta strandⁱ	168 – 178	Combined sources	11
Beta strandⁱ	183 – 187	Combined sources	5
Helixⁱ	194 – 197	Combined sources	4
Turnⁱ	200 – 202	Combined sources	3
Beta strandⁱ	205 – 208	Combined sources	4
Helixⁱ	211 – 218	Combined sources	8
Helixⁱ	220 – 222	Combined sources	3
Beta strandⁱ	225 – 234	Combined sources	10
Beta strandⁱ	239 – 249	Combined sources	11
Helixⁱ	253 – 265	Combined sources	13
Turnⁱ	266 – 271	Combined sources	6
Beta strandⁱ	272 – 275	Combined sources	4
Helixⁱ	281 – 284	Combined sources	4
Beta strandⁱ	290 – 294	Combined sources	5
Turnⁱ	295 – 297	Combined sources	3
Beta strandⁱ	299 – 302	Combined sources	4
Beta strandⁱ	305 – 312	Combined sources	8
Helixⁱ	316 – 330	Combined sources	15

Show more details

3D structure databases

ProteinModelPortalⁱ	P46406
SMRⁱ	P46406
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P46406

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 146	Interaction with WARSBy similarityAdd BLAST	146
Regionⁱ	149 – 151	Glyceraldehyde 3-phosphate bindingBy similarity	3
Regionⁱ	209 – 210	Glyceraldehyde 3-phosphate bindingBy similarity	2

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	243 – 248	[IL]-x-C-x-x-[DE] motifBy similarity		6

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

Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.Curated

Phylogenomic databases

eggNOGⁱ	KOG0657 Eukaryota COG0057 LUCA
HOGENOMⁱ	HOG000071678
HOVERGENⁱ	HBG000227
InParanoidⁱ	P46406
KEGG Orthology (KO) More...KOⁱ	K00134

Family and domain databases

InterProⁱ	View protein in InterPro 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 IPR036291 NAD(P)-bd_dom_sf
PANTHERⁱ	PTHR10836 PTHR10836, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02800 Gp_dh_C, 1 hit PF00044 Gp_dh_N, 1 hit
PIRSFⁱ	PIRSF000149 GAP_DH, 1 hit
PRINTSⁱ	PR00078 G3PDHDRGNASE
SMARTⁱ	View protein in SMART SM00846 Gp_dh_N, 1 hit
SUPFAMⁱ	SSF51735 SSF51735, 1 hit
TIGRFAMsⁱ	TIGR01534 GAPDH-I, 1 hit
PROSITEⁱ	View protein in PROSITE PS00071 GAPDH, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.ⁱShow all

P46406-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MVKVGVNGFG RIGRLVTRAA FNSGKVDVVA INDPFIDLHY MVYMFQYDST 
        60         70         80         90        100
HGKFHGTVKA ENGKLVINGK AITIFQERDP ANIKWGDAGA EYVVESTGVF 
       110        120        130        140        150
TTMEKAGAHL KGGAKRVIIS APSADAPMFV MGVNHEKYDN SLKIVSNASC 
       160        170        180        190        200
TTNCLAPLAK VIHDHFGIVE GLMTTVHAIT ATQKTVDGPS GKLWRDGRGA 
       210        220        230        240        250
AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV VDLTCRLEKA 
       260        270        280        290        300
AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSATHS STFDAGAGIA 
       310        320        330 
LNDHFVKLIS WYDNEFGYSN RVVDLMVHMA SKE

Length:333

Mass (Da):35,780

Last modified:November 13, 2007 - v3

Checksum:ⁱ346DB9B59DF3C1DF

GO

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation
	G1TYG1	G1TYG1_RABIT		Glyceraldehyde-3-phosphate dehydrog... Glyceraldehyde-3-phosphate dehydrogenase, EC 1.2.1.12	GAPDH	333	Annotation score:

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L23961 mRNA Translation: AAA85218.1 V00884 mRNA Translation: CAA24253.1 AB231852 mRNA Translation: BAE19661.1
PIRⁱ	JC4309
NCBI Reference Sequences More...RefSeqⁱ	NP_001075722.1, NM_001082253.1
UniGeneⁱ	Ocu.87

Genome annotation databases

GeneIDⁱ	100009074
KEGGⁱ	ocu:100009074

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P46406	Glyceraldehyde-3-phosphate dehydrogenase (Fragment)		LEPEU		228	UniRef100_P46406

Protein	Similar proteins		Species	Score	Length	Source
P46406	Glyceraldehyde-3-phosphate dehydrogenase		MUSPF		333	UniRef90_P46406
Glyceraldehyde-3-phosphate dehydrogenase		PELSI		333
Glyceraldehyde-3-phosphate dehydrogenase		FELCA		333
Glyceraldehyde-3-phosphate dehydrogenase		CRIGR		333
Glyceraldehyde-3-phosphate dehydrogenase		COTJA		333
+198

Protein	Similar proteins		Species	Score	Length	Source
P46406	Glyceraldehyde-3-phosphate dehydrogenase		SPECI		333	UniRef50_P46406
Glyceraldehyde-3-phosphate dehydrogenase		MUSPF		333
Glyceraldehyde-3-phosphate dehydrogenase		CANLF		333
Glyceraldehyde-3-phosphate dehydrogenase		COTJA		333
Glyceraldehyde-3-phosphate dehydrogenase		CRIGR		333
+2181

Cross-referencesⁱ

Web resourcesⁱ

Worthington enzyme manual

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	L23961 mRNA Translation: AAA85218.1 V00884 mRNA Translation: CAA24253.1 AB231852 mRNA Translation: BAE19661.1
PIRⁱ	JC4309
RefSeqⁱ	NP_001075722.1, NM_001082253.1
UniGeneⁱ	Ocu.87

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1J0X	X-ray	2.40	O/P/Q/R	2-333	[»]
ProteinModelPortalⁱ	P46406
SMRⁱ	P46406
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	1172097, 1 interactor
DIPⁱ	DIP-6005N
IntActⁱ	P46406, 3 interactors
MINTⁱ	P46406
STRINGⁱ	9986.ENSOCUP00000017094

Chemistry databases

BindingDBⁱ	P46406
ChEMBLⁱ	CHEMBL1075199

Protein family/group databases

Allergomeⁱ	12131 Ory c GAPDH
MoonProtⁱ	P46406

PTM databases

CarbonylDBⁱ	P46406
SwissPalmⁱ	P46406

Proteomic databases

PRIDEⁱ	P46406

PRIDEⁱ

P46406

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	100009074
KEGGⁱ	ocu:100009074

Organism-specific databases

CTDⁱ	2597

CTDⁱ

2597

Phylogenomic databases

eggNOGⁱ	KOG0657 Eukaryota COG0057 LUCA
HOGENOMⁱ	HOG000071678
HOVERGENⁱ	HBG000227
InParanoidⁱ	P46406
KOⁱ	K00134

Enzyme and pathway databases

UniPathwayⁱ	UPA00109;UER00184
SABIO-RKⁱ	P46406

Miscellaneous databases

EvolutionaryTraceⁱ	P46406
Protein Ontology More...PROⁱ	PR:P46406

Family and domain databases

InterProⁱ	View protein in InterPro 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 IPR036291 NAD(P)-bd_dom_sf
PANTHERⁱ	PTHR10836 PTHR10836, 1 hit
Pfamⁱ	View protein in Pfam PF02800 Gp_dh_C, 1 hit PF00044 Gp_dh_N, 1 hit
PIRSFⁱ	PIRSF000149 GAP_DH, 1 hit
PRINTSⁱ	PR00078 G3PDHDRGNASE
SMARTⁱ	View protein in SMART SM00846 Gp_dh_N, 1 hit
SUPFAMⁱ	SSF51735 SSF51735, 1 hit
TIGRFAMsⁱ	TIGR01534 GAPDH-I, 1 hit
PROSITEⁱ	View protein in PROSITE PS00071 GAPDH, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	G3P_RABIT
Accessionⁱ	P46406Primary (citable) accession number: P46406 Secondary accession number(s): Q4AC92
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
	Last sequence update:	November 13, 2007
	Last modified:	June 20, 2018
	This is version 143 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P46406 (G3P_RABIT)

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Glyceraldehyde-3-phosphate dehydrogenase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: glycolysis

Sites

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Cytosol

Cytoskeleton

Cytoskeleton

Cytosol

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Protein family/group databases

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Motif

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Computationally mapped potential isoform sequencesi

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

UniProt is an ELIXIR core data resource

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Functionⁱ

Pathwayⁱ: glycolysis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Computationally mapped potential isoform sequencesⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ