UniProtKB - P80147 (GABT_PIG)

BLAST

>sp|P80147|GABT_PIG 4-aminobutyrate aminotransferase, mitochondrial OS=Sus scrofa OX=9823 GN=ABAT PE=1 SV=2
MASVLLTRRLACSFRHNHRLLVPGWRHISQAAAKVDVEFDYDGPLMKTEVPGPRSRELMK
QLNIIQNAEAVHFFCNYEESRGNYLVDVDGNRMLDLYSQISSIPIGYSHPALVKLVQQPQ
NVSTFINRPALGILPPENFVEKLRESLLSVAPKGMSQLITMACGSCSNENAFKTIFMWYR
SKERGQSAFSKEELETCMINQAPGCPDYSILSFMGAFHGRTMGCLATTHSKAIHKIDIPS
FDWPIAPFPRLKYPLEEFVKENQQEEARCLEEVEDLIVKYRKKKKTVAGIIVEPIQSEGG
DNHASDDFFRKLRDISRKHGCAFLVDEVQTGGGSTGKFWAHEHWGLDDPADVMTFSKKMM
TGGFFHKEEFRPNAPYRIFNTWLGDPSKNLLLAEVINIIKREDLLSNAAHAGKVLLTGLL
DLQARYPQFISRVRGRGTFCSFDTPDESIRNKLISIARNKGVMLGGCGDKSIRFRPTLVF
RDHHAHLFLNIFSDILADFK

Align
Format
Add to basket Added to basket
History
Entry version 146 (07 Nov 2018)
Sequence version 2 (01 Dec 1992)
Previous versions | rss
Other tutorials and videos
Help video
Feedback

Protein

4-aminobutyrate aminotransferase, mitochondrial

Gene

ABAT

Organism

Sus scrofa (Pig)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine.

Catalytic activityⁱ

4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.

(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.

Cofactorⁱ

pyridoxal 5'-phosphate2 Publications, [2Fe-2S] cluster1 PublicationNote: Binds 1 [2Fe-2S] cluster per homodimer.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	163	Iron-sulfur (2Fe-2S); shared with dimeric partner1 Publication	1
Metal bindingⁱ	166	Iron-sulfur (2Fe-2S); shared with dimeric partner1 Publication	1
Binding siteⁱ	220	Substrate1 Publication1 Publication	1
Binding siteⁱ	381	Pyridoxal phosphate; shared with dimeric partner2 Publications	1

GO - Molecular functionⁱ

(S)-3-amino-2-methylpropionate transaminase activity Source: UniProtKB-EC
2 iron, 2 sulfur cluster binding Source: UniProtKB-KW
4-aminobutyrate:2-oxoglutarate transaminase activity Source: UniProtKB-EC
4-aminobutyrate transaminase activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
metal ion binding Source: UniProtKB-KW
protein homodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 648527
pyridoxal phosphate binding
Source: UniProtKB
Inferred from direct assayⁱ
- 6470007
succinate-semialdehyde dehydrogenase binding
Source: UniProtKB
Inferred from direct assayⁱ
- 6470007

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

behavioral response to cocaine Source: UniProtKB
gamma-aminobutyric acid catabolic process
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
neurotransmitter catabolic process
Source: UniProtKB
Inferred by curatorⁱ
- 11561735

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Aminotransferase, Transferase
Biological process	Neurotransmitter degradation
Ligand	2Fe-2S, Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BRENDAⁱ	2.6.1.19 6170
Reactomeⁱ	R-SSC-916853 Degradation of GABA
SABIO-RKⁱ	P80147

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 4-aminobutyrate aminotransferase, mitochondrial (EC:2.6.1.19) Alternative name(s): (S)-3-amino-2-methylpropionate transaminase (EC:2.6.1.22) GABA aminotransferase Short name: GABA-AT Gamma-amino-N-butyrate transaminase Short name: GABA transaminase Short name: GABA-T L-AIBAT
Gene namesⁱ	Name:ABAT Synonyms:GABAT
Organismⁱ	Sus scrofa (Pig)
Taxonomic identifierⁱ	9823 [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 › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus
Proteomesⁱ	UP000008227 Componentⁱ: Chromosome 3

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Chemistry databases

ChEMBLⁱ	CHEMBL2266

ChEMBLⁱ

CHEMBL2266

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 28	Mitochondrion1 PublicationAdd BLAST		28
ChainⁱPRO_0000001251	29 – 500	4-aminobutyrate aminotransferase, mitochondrialAdd BLAST		472

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	231	N6-succinyllysineBy similarity	1
Modified residueⁱ	252	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	252	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	279	N6-acetyllysineBy similarity	1
Modified residueⁱ	318	N6-acetyllysineBy similarity	1
Disulfide bondⁱ	321	InterchainBy similarity
Modified residueⁱ	357	N6-(pyridoxal phosphate)lysine1 Publication	1
Modified residueⁱ	413	N6-acetyllysine; alternateBy similarity	1
Modified residueⁱ	413	N6-succinyllysine; alternateBy similarity	1
Modified residueⁱ	452	N6-acetyllysineBy similarity	1
Modified residueⁱ	470	N6-acetyllysineBy similarity	1

Keywords - PTMⁱ

Acetylation, Disulfide bond

Proteomic databases

PaxDbⁱ	P80147
PeptideAtlas More...PeptideAtlasⁱ	P80147
PRIDEⁱ	P80147

Expressionⁱ

Gene expression databases

ExpressionAtlasⁱ	P80147 baseline and differential
Genevisibleⁱ	P80147 SS

Interactionⁱ

Subunit structureⁱ

Homodimer; disulfide-linked.

GO - Molecular functionⁱ

protein homodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 648527
succinate-semialdehyde dehydrogenase binding
Source: UniProtKB
Inferred from direct assayⁱ
- 6470007

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	1149627, 1 interactor
STRINGⁱ	9823.ENSSSCP00000008445

Chemistry databases

BindingDBⁱ

P80147

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	53 – 65	Combined sources	13
Helixⁱ	77 – 79	Combined sources	3
Beta strandⁱ	84 – 87	Combined sources	4
Beta strandⁱ	92 – 97	Combined sources	6
Helixⁱ	98 – 101	Combined sources	4
Helixⁱ	110 – 117	Combined sources	8
Helixⁱ	119 – 121	Combined sources	3
Helixⁱ	122 – 126	Combined sources	5
Turnⁱ	131 – 133	Combined sources	3
Helixⁱ	139 – 145	Combined sources	7
Helixⁱ	147 – 150	Combined sources	4
Beta strandⁱ	157 – 163	Combined sources	7
Helixⁱ	164 – 184	Combined sources	21
Helixⁱ	191 – 197	Combined sources	7
Turnⁱ	198 – 200	Combined sources	3
Turnⁱ	202 – 204	Combined sources	3
Beta strandⁱ	209 – 213	Combined sources	5
Helixⁱ	222 – 227	Combined sources	6
Helixⁱ	232 – 235	Combined sources	4
Helixⁱ	255 – 257	Combined sources	3
Helixⁱ	259 – 282	Combined sources	24
Beta strandⁱ	287 – 292	Combined sources	6
Beta strandⁱ	294 – 296	Combined sources	3
Turnⁱ	298 – 300	Combined sources	3
Helixⁱ	306 – 318	Combined sources	13
Beta strandⁱ	322 – 326	Combined sources	5
Turnⁱ	328 – 335	Combined sources	8
Beta strandⁱ	336 – 339	Combined sources	4
Helixⁱ	340 – 344	Combined sources	5
Beta strandⁱ	351 – 355	Combined sources	5
Helixⁱ	357 – 359	Combined sources	3
Beta strandⁱ	360 – 366	Combined sources	7
Helixⁱ	368 – 370	Combined sources	3
Beta strandⁱ	373 – 378	Combined sources	6
Beta strandⁱ	381 – 384	Combined sources	4
Helixⁱ	386 – 401	Combined sources	16
Helixⁱ	404 – 425	Combined sources	22
Turnⁱ	427 – 429	Combined sources	3
Beta strandⁱ	431 – 436	Combined sources	6
Beta strandⁱ	439 – 443	Combined sources	5
Helixⁱ	447 – 459	Combined sources	13
Beta strandⁱ	465 – 467	Combined sources	3
Turnⁱ	468 – 470	Combined sources	3
Beta strandⁱ	471 – 473	Combined sources	3
Helixⁱ	482 – 498	Combined sources	17

Show more details

3D structure databases

ProteinModelPortalⁱ	P80147
SMRⁱ	P80147
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P80147

EvolutionaryTraceⁱ

P80147

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	164 – 165	Pyridoxal phosphate binding1 Publication		2

Sequence similaritiesⁱ

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG1405 Eukaryota COG0160 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000074885
HOGENOMⁱ	HOG000020208
HOVERGENⁱ	HBG000634
InParanoidⁱ	P80147
KEGG Orthology (KO) More...KOⁱ	K13524
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G08T5

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00610 OAT_like, 1 hit
Gene3Dⁱ	3.40.640.10, 1 hit 3.90.1150.10, 1 hit
InterProⁱ	View protein in InterPro IPR004631 4NH2But_aminotransferase_euk IPR005814 Aminotrans_3 IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00202 Aminotran_3, 1 hit
PIRSFⁱ	PIRSF000521 Transaminase_4ab_Lys_Orn, 1 hit
SUPFAMⁱ	SSF53383 SSF53383, 1 hit
TIGRFAMsⁱ	TIGR00699 GABAtrns_euk, 1 hit
PROSITEⁱ	View protein in PROSITE PS00600 AA_TRANSFER_CLASS_3, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show all Align All

P80147-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MASVLLTRRL ACSFRHNHRL LVPGWRHISQ AAAKVDVEFD YDGPLMKTEV 
        60         70         80         90        100
PGPRSRELMK QLNIIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI 
       110        120        130        140        150
SSIPIGYSHP ALVKLVQQPQ NVSTFINRPA LGILPPENFV EKLRESLLSV 
       160        170        180        190        200
APKGMSQLIT MACGSCSNEN AFKTIFMWYR SKERGQSAFS KEELETCMIN 
       210        220        230        240        250
QAPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS FDWPIAPFPR 
       260        270        280        290        300
LKYPLEEFVK ENQQEEARCL EEVEDLIVKY RKKKKTVAGI IVEPIQSEGG 
       310        320        330        340        350
DNHASDDFFR KLRDISRKHG CAFLVDEVQT GGGSTGKFWA HEHWGLDDPA 
       360        370        380        390        400
DVMTFSKKMM TGGFFHKEEF RPNAPYRIFN TWLGDPSKNL LLAEVINIIK 
       410        420        430        440        450
REDLLSNAAH AGKVLLTGLL DLQARYPQFI SRVRGRGTFC SFDTPDESIR 
       460        470        480        490        500
NKLISIARNK GVMLGGCGDK SIRFRPTLVF RDHHAHLFLN IFSDILADFK

Length:500

Mass (Da):56,620

Last modified:December 1, 1992 - v2

Checksum:ⁱBFD0B80846CEF5B7

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

	A0A286ZMM3	A0A286ZMM3_PIG		4-aminobutyrate aminotransferase, m... 4-aminobutyrate aminotransferase, mitochondrial	ABAT	444	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	454	I → N in AAA96981 (PubMed:1559966).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M84802 mRNA Translation: AAA96981.1
NCBI Reference Sequences More...RefSeqⁱ	NP_999428.1, NM_214263.1
UniGeneⁱ	Ssc.16251

Genome annotation databases

Ensemblⁱ	ENSSSCT00000008668; ENSSSCP00000008445; ENSSSCG00000007909 ENSSSCT00000039445; ENSSSCP00000045366; ENSSSCG00000007909 ENSSSCT00000048101; ENSSSCP00000032632; ENSSSCG00000007909 ENSSSCT00000064948; ENSSSCP00000035621; ENSSSCG00000007909
GeneIDⁱ	397500
KEGGⁱ	ssc:397500

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P80147	4-aminobutyrate aminotransferase, mitochondrial		BOVIN		500	UniRef90_P80147
4-aminobutyrate aminotransferase		CANLF		500
4-aminobutyrate aminotransferase, mitochondrial		CALJA		500
Uncharacterized protein		SHEEP		500
Uncharacterized protein		FELCA		500
+30

Protein	Similar proteins		Species	Score	Length	Source
P80147	4-aminobutyrate aminotransferase, mitochondrial		RAT		500	UniRef50_P50554
4-aminobutyrate aminotransferase, mitochondrial		MOUSE		500
4-aminobutyrate aminotransferase, mitochondrial		HUMAN		500
4-aminobutyrate aminotransferase, mitochondrial		BOVIN		500
ABAT isoform 7		PANTR		589
+304

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M84802 mRNA Translation: AAA96981.1
RefSeqⁱ	NP_999428.1, NM_214263.1
UniGeneⁱ	Ssc.16251

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
	1OHV	X-ray	2.30	A/B/C/D	29-500	[»]
	1OHW	X-ray	2.30	A/B/C/D	29-500	[»]
	1OHY	X-ray	2.80	A/B/C/D	29-500	[»]
	4Y0D	X-ray	2.19	A/B/C/D	39-500	[»]
	4Y0H	X-ray	1.63	A/B/C/D	39-500	[»]
	4Y0I	X-ray	1.66	A/B/C/D	39-499	[»]
	4ZSW	X-ray	1.70	A/B/C/D	39-499	[»]
	4ZSY	X-ray	1.70	A/B/C/D	39-499	[»]
	6B6G	X-ray	1.95	A/B/C/D	39-500	[»]
ProteinModelPortalⁱ	P80147
SMRⁱ	P80147
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	1149627, 1 interactor
STRINGⁱ	9823.ENSSSCP00000008445

Chemistry databases

BindingDBⁱ	P80147
ChEMBLⁱ	CHEMBL2266

Proteomic databases

PaxDbⁱ	P80147
PeptideAtlasⁱ	P80147
PRIDEⁱ	P80147

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENSSSCT00000008668; ENSSSCP00000008445; ENSSSCG00000007909 ENSSSCT00000039445; ENSSSCP00000045366; ENSSSCG00000007909 ENSSSCT00000048101; ENSSSCP00000032632; ENSSSCG00000007909 ENSSSCT00000064948; ENSSSCP00000035621; ENSSSCG00000007909
GeneIDⁱ	397500
KEGGⁱ	ssc:397500

Organism-specific databases

CTDⁱ	18

CTDⁱ

Phylogenomic databases

eggNOGⁱ	KOG1405 Eukaryota COG0160 LUCA
GeneTreeⁱ	ENSGT00550000074885
HOGENOMⁱ	HOG000020208
HOVERGENⁱ	HBG000634
InParanoidⁱ	P80147
KOⁱ	K13524
OrthoDBⁱ	EOG091G08T5

Enzyme and pathway databases

BRENDAⁱ	2.6.1.19 6170
Reactomeⁱ	R-SSC-916853 Degradation of GABA
SABIO-RKⁱ	P80147

Miscellaneous databases

ChiTaRSⁱ	ABAT pig
EvolutionaryTraceⁱ	P80147
Protein Ontology More...PROⁱ	PR:P80147

Gene expression databases

ExpressionAtlasⁱ	P80147 baseline and differential
Genevisibleⁱ	P80147 SS

Family and domain databases

CDDⁱ	cd00610 OAT_like, 1 hit
Gene3Dⁱ	3.40.640.10, 1 hit 3.90.1150.10, 1 hit
InterProⁱ	View protein in InterPro IPR004631 4NH2But_aminotransferase_euk IPR005814 Aminotrans_3 IPR015424 PyrdxlP-dep_Trfase IPR015422 PyrdxlP-dep_Trfase_dom1 IPR015421 PyrdxlP-dep_Trfase_major
Pfamⁱ	View protein in Pfam PF00202 Aminotran_3, 1 hit
PIRSFⁱ	PIRSF000521 Transaminase_4ab_Lys_Orn, 1 hit
SUPFAMⁱ	SSF53383 SSF53383, 1 hit
TIGRFAMsⁱ	TIGR00699 GABAtrns_euk, 1 hit
PROSITEⁱ	View protein in PROSITE PS00600 AA_TRANSFER_CLASS_3, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GABT_PIG
Accessionⁱ	P80147Primary (citable) accession number: P80147 Secondary accession number(s): P27820
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
	Last sequence update:	December 1, 1992
	Last modified:	November 7, 2018
	This is version 146 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P80147 (GABT_PIG)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

4-aminobutyrate aminotransferase, mitochondrial

ABAT

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

Sites

<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

<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

Mitochondrion

Cytosol

Mitochondrion

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

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

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression 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

<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

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression 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

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ