APOBEC3A

Functionⁱ

DNA deaminase (cytidine deaminase) with restriction activity against viruses, foreign DNA and mobility of retrotransposons. Exhibits antiviral activity against adeno-associated virus (AAV) and human T-cell leukemia virus type 1 (HTLV-1) and may inhibit the mobility of LTR and non-LTR retrotransposons. Selectively targets single-stranded DNA and can deaminate both methylcytosine and cytosine in foreign DNA. Can induce somatic hypermutation in the nuclear and mitochondrial DNA. May also play a role in the epigenetic regulation of gene expression through the process of active DNA demethylation.12 Publications

Miscellaneous

It is one of seven related genes or pseudogenes found in a cluster, thought to result from gene duplication, on chromosome 22.

Catalytic activityⁱ

Cytidine + H₂O = uridine + NH₃.4 Publications

Cofactorⁱ

Zn²⁺By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	70	Zinc; catalyticBy similarity	1
Active siteⁱ	72	Proton donorBy similarity	1
Metal bindingⁱ	101	Zinc; catalyticBy similarity	1
Metal bindingⁱ	106	Zinc; catalyticBy similarity	1

GO - Molecular functionⁱ

cytidine deaminase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 16527742
- 21123384
deoxycytidine deaminase activity
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 22457529
zinc ion binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase
Biological process	Antiviral defense, Immunity, Innate immunity
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

Reactomeⁱ	R-HSA-72200 mRNA Editing: C to U Conversion R-HSA-75094 Formation of the Editosome

Reactomeⁱ

R-HSA-72200 mRNA Editing: C to U Conversion
R-HSA-75094 Formation of the Editosome

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: DNA dC->dU-editing enzyme APOBEC-3A (EC:3.5.4.-) Short name: A3A Alternative name(s): Phorbolin-1
Gene namesⁱ	Name:APOBEC3A
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [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 › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 22

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000128383.12
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:17343 APOBEC3A
MIMⁱ	607109 gene
neXtProtⁱ	NX_P31941

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	28	R → E: No effect on deaminase activity despite an altered restriction activity towards genetic invaders. 1 Publication	1
Mutagenesisⁱ	29	H → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication	1
Mutagenesisⁱ	30	K → F: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication	1
Mutagenesisⁱ	57	N → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication	1
Mutagenesisⁱ	60	K → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication	1
Mutagenesisⁱ	69	R → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication	1
Mutagenesisⁱ	70	H → R: Altered deaminase activity. 1 Publication	1
Mutagenesisⁱ	72	E → Q: Altered deaminase activity and restriction activity towards genetic invaders. 2 Publications	1
Mutagenesisⁱ	98	W → L: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication	1
Mutagenesisⁱ	106	C → S: Altered deaminase activity. 1 Publication	1
Mutagenesisⁱ	128	R → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication	1
Mutagenesisⁱ	130	Y → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication	1
Mutagenesisⁱ	131	D → N: No effect on deaminase activity despite an altered restriction activity towards genetic invaders. 1 Publication	1
Mutagenesisⁱ	133	D → N: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication	1
Mutagenesisⁱ	136	Y → A: Altered deaminase activity and restriction activity towards genetic invaders. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	100913187 200315
Open Targets More...OpenTargetsⁱ	ENSG00000128383
PharmGKBⁱ	PA24891

Chemistry databases

ChEMBLⁱ	CHEMBL1741179

ChEMBLⁱ

CHEMBL1741179

Polymorphism and mutation databases

BioMutaⁱ	APOBEC3A
DMDMⁱ	12644206

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000171752	1 – 199	DNA dC->dU-editing enzyme APOBEC-3AAdd BLAST		199

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P31941
PaxDbⁱ	P31941
PeptideAtlas More...PeptideAtlasⁱ	P31941
PRIDEⁱ	P31941
ProteomicsDBⁱ	54806 54807 [P31941-2]

PTM databases

iPTMnetⁱ	P31941
PhosphoSitePlusⁱ	P31941

Expressionⁱ

Tissue specificityⁱ

Expressed in peripheral leukocytes with higher expression in CD14-positive phagocytic cells. Highly expressed in keratinocytes and in periphery blood monocytes. Also detected in non-lymphoid tissues including lung and adipose tissues. Found at high levels in colorectal adenocarcinoma, Burkitt's lymphoma and chronic myelogenous leukemia.4 Publications

Inductionⁱ

Up-regulated by interferon and CpG single-stranded DNA (at protein level).2 Publications

Gene expression databases

Bgeeⁱ	ENSG00000128383
CleanExⁱ	HS_APOBEC3A
ExpressionAtlasⁱ	P31941 baseline and differential
Genevisibleⁱ	P31941 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA043237 HPA056980 HPA066719

HPAⁱ

HPA043237
HPA056980
HPA066719

Interactionⁱ

Subunit structureⁱ

Interacts with AGO2. Interacts with TRIB3 (via N-terminus).2 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
C	Q784Z8	4	EBI-13050366,EBI-11666471	From Hepatitis B virus.
STAMBP	O95630	4	EBI-13050366,EBI-396676

Show more details

Protein-protein interaction databases

BioGridⁱ	128318, 2 interactors
Database of interacting proteins More...DIPⁱ	DIP-61365N
IntActⁱ	P31941, 2 interactors
STRINGⁱ	9606.ENSP00000249116

Chemistry databases

BindingDBⁱ

P31941

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Show more details

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	15 – 21	Combined sources	7
Beta strandⁱ	24 – 26	Combined sources	3
Beta strandⁱ	27 – 29	Combined sources	3
Beta strandⁱ	32 – 41	Combined sources	10
Beta strandⁱ	44 – 47	Combined sources	4
Helixⁱ	49 – 51	Combined sources	3
Beta strandⁱ	53 – 56	Combined sources	4
Turnⁱ	62 – 65	Combined sources	4
Helixⁱ	71 – 82	Combined sources	12
Beta strandⁱ	88 – 98	Combined sources	11
Turnⁱ	103 – 105	Combined sources	3
Helixⁱ	106 – 116	Combined sources	11
Beta strandⁱ	120 – 128	Combined sources	9
Helixⁱ	136 – 145	Combined sources	10
Beta strandⁱ	149 – 152	Combined sources	4
Helixⁱ	155 – 165	Combined sources	11
Helixⁱ	179 – 195	Combined sources	17

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
	2M65	NMR	-	A	1-199	[»]
	4XXO	X-ray	2.84	A/B	1-199	[»]
	5KEG	X-ray	2.20	A	1-199	[»]
	5SWW	X-ray	3.15	A/B/C/D	1-196	[»]
ProteinModelPortalⁱ	P31941
SMRⁱ	P31941
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	27 – 143	CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd BLAST		117

Sequence similaritiesⁱ

Belongs to the cytidine and deoxycytidylate deaminase family.Curated

Phylogenomic databases

eggNOGⁱ	ENOG410JNPI Eukaryota ENOG4111DZ4 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000062933
HOGENOMⁱ	HOG000033754
HOVERGENⁱ	HBG050434
KEGG Orthology (KO) More...KOⁱ	K18750
OMAⁱ	SGPRHLM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G07EI
PhylomeDBⁱ	P31941
TreeFamⁱ	TF331356

Family and domain databases

InterProⁱ	View protein in InterPro IPR016192 APOBEC/CMP_deaminase_Zn-bd IPR013158 APOBEC_N IPR002125 CMP_dCMP_dom IPR016193 Cytidine_deaminase-like
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08210 APOBEC_N, 1 hit
SUPFAMⁱ	SSF53927 SSF53927, 1 hit
PROSITEⁱ	View protein in PROSITE PS00903 CYT_DCMP_DEAMINASES_1, 1 hit PS51747 CYT_DCMP_DEAMINASES_2, 1 hit

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative initiation. Align Add to basket Added to basket

Isoform 1 (identifier: P31941-1) [UniParc]FASTA Add to basket

Also known as: Phorbolin-1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEASPASGPR HLMDPHIFTS NFNNGIGRHK TYLCYEVERL DNGTSVKMDQ 
        60         70         80         90        100
HRGFLHNQAK NLLCGFYGRH AELRFLDLVP SLQLDPAQIY RVTWFISWSP 
       110        120        130        140        150
CFSWGCAGEV RAFLQENTHV RLRIFAARIY DYDPLYKEAL QMLRDAGAQV 
       160        170        180        190 
SIMTYDEFKH CWDTFVDHQG CPFQPWDGLD EHSQALSGRL RAILQNQGN

Note: Enzymatically active.

Length:199

Mass (Da):23,012

Last modified:January 11, 2001 - v3

Checksum:ⁱ42E99E0D7DF7AA14

GO

Isoform 2 (identifier: P31941-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-12: Missing.

« Hide

        10         20         30         40         50
MDPHIFTSNF NNGIGRHKTY LCYEVERLDN GTSVKMDQHR GFLHNQAKNL 
        60         70         80         90        100
LCGFYGRHAE LRFLDLVPSL QLDPAQIYRV TWFISWSPCF SWGCAGEVRA 
       110        120        130        140        150
FLQENTHVRL RIFAARIYDY DPLYKEALQM LRDAGAQVSI MTYDEFKHCW 
       160        170        180 
DTFVDHQGCP FQPWDGLDEH SQALSGRLRA ILQNQGN

Note: Enzymatically active.

Show »

Length:187

Mass (Da):21,778

Checksum:ⁱC7901DFD6A693D9D

GO

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_048721	19	T → A. Corresponds to variant dbSNP:rs17000556Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_041723	1 – 12	Missing in isoform 2. CuratedAdd BLAST		12

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U03891 mRNA Translation: AAA03706.2 CR456393 mRNA Translation: CAG30279.1 AL022318 Genomic DNA Translation: CAI17897.1 BC126416 mRNA Translation: AAI26417.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS13981.1 [P31941-1]
PIRⁱ	G01233
NCBI Reference Sequences More...RefSeqⁱ	NP_001180218.1, NM_001193289.1 [P31941-1] NP_663745.1, NM_145699.3 [P31941-1]
UniGeneⁱ	Hs.226307

Genome annotation databases

Ensemblⁱ	ENST00000249116; ENSP00000249116; ENSG00000128383 [P31941-1] ENST00000402255; ENSP00000384359; ENSG00000128383 [P31941-1] ENST00000570508; ENSP00000461288; ENSG00000262156 [P31941-1] ENST00000618553; ENSP00000481904; ENSG00000128383 [P31941-1] ENST00000623492; ENSP00000485234; ENSG00000262156 [P31941-1]
GeneIDⁱ	100913187 200315
KEGGⁱ	hsa:100913187 hsa:200315
UCSC genome browser More...UCSCⁱ	uc003awn.2 human [P31941-1]

Keywords - Coding sequence diversityⁱ

Alternative initiation, Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length
P31941	APOBEC3A		HUMAN		199
APOBEC3A isoform 1 (Fragment)		PANTR		199
Apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3A (Fragment)		Pan troglodytes troglodytes		199
Apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3A (Fragment)		PANPA		199
Apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3A (Fragment)		western gorilla		199
+12

Protein	Similar proteins		Species	Score	Length
P31941	APOBEC3A		HUMAN		199
Apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3A (Fragment)		Pan troglodytes troglodytes		199
Apolipoprotein B mRNA editing enzyme catalytic polypeptide-like 3A (Fragment)		western gorilla		199
Uncharacterized protein		NOMLE		199
APOBEC3A isoform 1 (Fragment)		PANTR		199
+28

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U03891 mRNA Translation: AAA03706.2 CR456393 mRNA Translation: CAG30279.1 AL022318 Genomic DNA Translation: CAI17897.1 BC126416 mRNA Translation: AAI26417.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS13981.1 [P31941-1]
PIRⁱ	G01233
NCBI Reference Sequences More...RefSeqⁱ	NP_001180218.1, NM_001193289.1 [P31941-1] NP_663745.1, NM_145699.3 [P31941-1]
UniGeneⁱ	Hs.226307

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
	2M65	NMR	-	A	1-199	[»]
	4XXO	X-ray	2.84	A/B	1-199	[»]
	5KEG	X-ray	2.20	A	1-199	[»]
	5SWW	X-ray	3.15	A/B/C/D	1-196	[»]
ProteinModelPortalⁱ	P31941
SMRⁱ	P31941
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	128318, 2 interactors
Database of interacting proteins More...DIPⁱ	DIP-61365N
IntActⁱ	P31941, 2 interactors
STRINGⁱ	9606.ENSP00000249116

Chemistry databases

BindingDBⁱ	P31941
ChEMBLⁱ	CHEMBL1741179

PTM databases

iPTMnetⁱ	P31941
PhosphoSitePlusⁱ	P31941

Polymorphism and mutation databases

BioMutaⁱ	APOBEC3A
DMDMⁱ	12644206

Proteomic databases

MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P31941
PaxDbⁱ	P31941
PeptideAtlas More...PeptideAtlasⁱ	P31941
PRIDEⁱ	P31941
ProteomicsDBⁱ	54806 54807 [P31941-2]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	200315
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000249116; ENSP00000249116; ENSG00000128383 [P31941-1] ENST00000402255; ENSP00000384359; ENSG00000128383 [P31941-1] ENST00000570508; ENSP00000461288; ENSG00000262156 [P31941-1] ENST00000618553; ENSP00000481904; ENSG00000128383 [P31941-1] ENST00000623492; ENSP00000485234; ENSG00000262156 [P31941-1]
GeneIDⁱ	100913187 200315
KEGGⁱ	hsa:100913187 hsa:200315
UCSC genome browser More...UCSCⁱ	uc003awn.2 human [P31941-1]

Organism-specific databases

CTDⁱ	100913187 200315
DisGeNET More...DisGeNETⁱ	100913187 200315
EuPathDBⁱ	HostDB:ENSG00000128383.12
GeneCardsⁱ	APOBEC3A
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:17343 APOBEC3A
Human Protein Atlas More...HPAⁱ	HPA043237 HPA056980 HPA066719
MIMⁱ	607109 gene
neXtProtⁱ	NX_P31941
Open Targets More...OpenTargetsⁱ	ENSG00000128383
PharmGKBⁱ	PA24891
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410JNPI Eukaryota ENOG4111DZ4 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000062933
HOGENOMⁱ	HOG000033754
HOVERGENⁱ	HBG050434
KEGG Orthology (KO) More...KOⁱ	K18750
OMAⁱ	SGPRHLM
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G07EI
PhylomeDBⁱ	P31941
TreeFamⁱ	TF331356

Enzyme and pathway databases

Reactomeⁱ	R-HSA-72200 mRNA Editing: C to U Conversion R-HSA-75094 Formation of the Editosome

Reactomeⁱ

R-HSA-72200 mRNA Editing: C to U Conversion
R-HSA-75094 Formation of the Editosome

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P31941
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000128383
CleanExⁱ	HS_APOBEC3A
ExpressionAtlasⁱ	P31941 baseline and differential
Genevisibleⁱ	P31941 HS

Family and domain databases

InterProⁱ	View protein in InterPro IPR016192 APOBEC/CMP_deaminase_Zn-bd IPR013158 APOBEC_N IPR002125 CMP_dCMP_dom IPR016193 Cytidine_deaminase-like
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08210 APOBEC_N, 1 hit
SUPFAMⁱ	SSF53927 SSF53927, 1 hit
PROSITEⁱ	View protein in PROSITE PS00903 CYT_DCMP_DEAMINASES_1, 1 hit PS51747 CYT_DCMP_DEAMINASES_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ABC3A_HUMAN
Accessionⁱ	P31941Primary (citable) accession number: P31941 Secondary accession number(s): A0AVM1 , Q12807, Q5JZ93, Q9UH18
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
	Last sequence update:	January 11, 2001
	Last modified:	June 20, 2018
	This is version 158 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

Human chromosome 22
Human chromosome 22: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families

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UniProtKB - P31941 (ABC3A_HUMAN)

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DNA dC->dU-editing enzyme APOBEC-3A

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<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

Miscellaneous

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<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

<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 - 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

Organism-specific databases

<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

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Nucleus

Other locations

<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

Mutagenesis

Organism-specific databases

Chemistry databases

Polymorphism and mutation 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

Proteomic databases

PTM 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

Organism-specific 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

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

<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

Domains and Repeats

<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

Natural variant

Alternative sequence

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

PTM databases

Polymorphism and mutation 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

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ