RARA

Functionⁱ

Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RXR/RAR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. RARA plays an essential role in the regulation of retinoic acid-induced germ cell development during spermatogenesis. Has a role in the survival of early spermatocytes at the beginning prophase of meiosis. In Sertoli cells, may promote the survival and development of early meiotic prophase spermatocytes. In concert with RARG, required for skeletal growth, matrix homeostasis and growth plate function (By similarity).By similarity3 Publications

Caution

Regions

Feature key	Position(s)	DescriptionActions	Length
DNA bindingⁱ	88 – 153	Nuclear receptorPROSITE-ProRule annotationAdd BLAST	66
Zinc fingerⁱ	88 – 108	NR C4-typePROSITE-ProRule annotationAdd BLAST	21
Zinc fingerⁱ	124 – 148	NR C4-typePROSITE-ProRule annotationAdd BLAST	25

GO - Molecular functionⁱ

alpha-actinin binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 22351778
chromatin DNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19917671
DNA-binding transcription factor activity
Source: UniProtKB
Inferred from direct assayⁱ
- 18922886
- 20413580
drug binding Source: Ensembl
enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 12039952
- 9628876
histone deacetylase binding Source: Ensembl
mRNA 5'-UTR binding Source: Ensembl
protein domain specific binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 20413580
protein heterodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 19917671
protein kinase A binding
Source: UniProtKB
Inferred from direct assayⁱ
- 20215566
protein kinase B binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 16417524
retinoic acid binding
Source: BHF-UCL
Inferred from direct assayⁱ
- 2825025
retinoic acid receptor activity
Source: BHF-UCL
Inferred from direct assayⁱ
- 2825025
retinoic acid-responsive element binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19917671
RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
signaling receptor binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19628791
steroid hormone receptor activity Source: InterPro
transcription coactivator activity
Source: UniProtKB
Inferred from direct assayⁱ
- 20080953
transcription corepressor activity
Source: UniProtKB
Inferred from direct assayⁱ
- 20080953
transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17641689
translation repressor activity, mRNA regulatory element binding Source: Ensembl
zinc ion binding Source: InterPro

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

apoptotic cell clearance
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 19628791
cellular response to estrogen stimulus
Source: UniProtKB
Inferred from direct assayⁱ
- 20080953
cellular response to lipopolysaccharide Source: Ensembl
cellular response to retinoic acid
Source: UniProtKB
Inferred from direct assayⁱ
- 19917671
chondroblast differentiation Source: Ensembl
embryonic camera-type eye development Source: Ensembl
face development Source: Ensembl
female pregnancy Source: Ensembl
germ cell development Source: Ensembl
glandular epithelial cell development Source: Ensembl
growth plate cartilage development Source: Ensembl
hippocampus development Source: Ensembl
limb development Source: Ensembl
liver development Source: Ensembl
multicellular organism growth Source: Ensembl
negative regulation of apoptotic process Source: Ensembl
negative regulation of cartilage development Source: Ensembl
negative regulation of cell proliferation Source: Ensembl
negative regulation of granulocyte differentiation
Source: UniProtKB
Inferred from direct assayⁱ
- 19917671
negative regulation of interferon-gamma production
Source: BHF-UCL
Inferred from direct assayⁱ
- 18416830
negative regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
- 20080953
negative regulation of transcription by RNA polymerase II Source: Ensembl
negative regulation of translational initiation Source: Ensembl
negative regulation of tumor necrosis factor production
Source: BHF-UCL
Inferred from direct assayⁱ
- 18416830
neural tube closure Source: Ensembl
outflow tract septum morphogenesis Source: Ensembl
positive regulation of binding
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20080953
positive regulation of cell cycle
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20080953
positive regulation of cell proliferation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 20080953
positive regulation of interleukin-13 production
Source: BHF-UCL
Inferred from direct assayⁱ
- 18416830
positive regulation of interleukin-4 production
Source: BHF-UCL
Inferred from direct assayⁱ
- 18416830
positive regulation of interleukin-5 production
Source: BHF-UCL
Inferred from direct assayⁱ
- 18416830
positive regulation of neuron differentiation Source: Ensembl
positive regulation of T-helper 2 cell differentiation
Source: BHF-UCL
Inferred from direct assayⁱ
- 18416830
positive regulation of transcription, DNA-templated
Source: UniProtKB
Inferred from direct assayⁱ
positive regulation of transcription by RNA polymerase II
Source: UniProtKB
Inferred from direct assayⁱ
- 19850744
prostate gland development Source: Ensembl
protein phosphorylation
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 16456540
regulation of myelination Source: Ensembl
regulation of synaptic plasticity Source: Ensembl
response to cytokine Source: Ensembl
response to estradiol Source: Ensembl
response to ethanol Source: Ensembl
response to retinoic acid
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 17538076
response to vitamin A Source: Ensembl
retinoic acid receptor signaling pathway
Source: BHF-UCL
Inferred from mutant phenotypeⁱ
- 17538076
Sertoli cell fate commitment Source: Ensembl
signal transduction
Source: BHF-UCL
Inferred from direct assayⁱ
- 2825025
spermatogenesis Source: Ensembl
trachea cartilage development Source: Ensembl
transcription initiation from RNA polymerase II promoter Source: Reactome
ureteric bud development Source: Ensembl
ventricular cardiac muscle cell differentiation Source: Ensembl

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	DNA-binding, Receptor
Biological process	Transcription, Transcription regulation
Ligand	Metal-binding, Zinc

Enzyme and pathway databases

Reactomeⁱ	R-HSA-383280 Nuclear Receptor transcription pathway R-HSA-4090294 SUMOylation of intracellular receptors R-HSA-5362517 Signaling by Retinoic Acid R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
SignaLinkⁱ	P10276
SIGNORⁱ	P10276

Protein family/group databases

MoonDBⁱ	P10276 Predicted

MoonDBⁱ

P10276 Predicted

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Retinoic acid receptor alpha Short name: RAR-alpha Alternative name(s): Nuclear receptor subfamily 1 group B member 1
Gene namesⁱ	Name:RARA Synonyms:NR1B1
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 17

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000131759.17
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:9864 RARA
MIMⁱ	180240 gene
neXtProtⁱ	NX_P10276

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Chromosomal aberrations involving RARA are commonly found in acute promyelocytic leukemia. Translocation t(11;17)(q32;q21) with ZBTB16/PLZF; translocation t(15;17)(q21;q21) with PML; translocation t(5;17)(q32;q11) with NPM. The PML-RARA oncoprotein requires both the PML ring structure and coiled-coil domain for both interaction with UBE2I, nuclear microspeckle location and sumoylation. In addition, the coiled-coil domain functions in blocking RA-mediated transactivation and cell differentiation.3 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	95	S → A: No effect on PKB/AKT1-mediated phosphorylation. Repressed transactivation. 1 Publication	1
Mutagenesisⁱ	96	S → A: Abolishes PKB/AKT1-mediated phosphorylation. Repressed transactivation. 1 Publication	1
Mutagenesisⁱ	147	K → R: Abrogates sumoylation in the presence or absence of ATRA and primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-166; R-171 and R-399. 1 Publication	1
Mutagenesisⁱ	154	S → A: No effect on PKB/AKT1-mediated phosphorylation. No repression of transactivation. 1 Publication	1
Mutagenesisⁱ	157	S → A: No effect on PKB/AKT1-mediated phosphorylation. Repressed transactivation. 1 Publication	1
Mutagenesisⁱ	166	K → R: Cytoplasmic in the absence of ATRA and reduced transcriptional activity in the presence of ATRA. Low sumoylation levels in the presence of ATRA; when associated with R-399. Nuclear localization and enhanced transcriptional activity; when associated with R-171 and R-399. Primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-147; R-171 and R-399. 1 Publication	1
Mutagenesisⁱ	171	K → R: Cytoplasmic in the absence of ATRA and reduced transcriptional activity in the presence of ATRA. Low sumoylation levels in the presence of ATRA; when associated with R-399. Nuclear localization and enhanced transcriptional activity; when associated with R-166 and R-399. Primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-147; R-166 and R-399. 1 Publication	1
Mutagenesisⁱ	219	S → A: No effect on heterodimerization with RARA. On ATRA treatment, localizes to the nucleus, and increased protein levels; when associated with A-369. 1 Publication	1
Mutagenesisⁱ	219	S → E: No effect on heterodimerization with RARA. On ATRA treatment, localizes to both nucleus and cytoplasm, no increase in protein levels, and decrease in RARA-mediated transcriptional activity; when associated with E-369. 1 Publication	1
Mutagenesisⁱ	369	S → A: No effect on heterodimerization with RARA. On ATRA treatment, localizes to the nucleus, and increased protein levels; when associated with A-219. 1 Publication	1
Mutagenesisⁱ	369	S → E: Some inhibition of heterodimerization with RARA. On ATRA treatment, localizes to both nucleus and cytoplasm, increase in protein levels, and decrease in RARA-mediated transcriptional activity; when associated with E-219. 1 Publication	1
Mutagenesisⁱ	396	I → E: Abrogates interaction with NCOR1 or NCOR2. Increased affinity for NCOR1 and NCOR2 in the presence of BMS493. Increased transcriptional activity in the presence of agonist and decreased activity in the presence of neutral antagonist. 1 Publication	1
Mutagenesisⁱ	399	K → R in the absence of ATRA, abolishes sumoylation and is mainly nuclear. In the presence of ATRA, some sumoylation, cytoplasmic location, reduced transcriptional activity and no SENP6 binding. Low sumoylation levels in the presence of ATRA and nuclear location in the absence of ATRA; when associated with R-166 or with R-171. Primarily nuclear localization and enhanced ATRA-mediated transcriptional activity; when associated with R-147; R-166 and R-171. 1 Publication	1
Mutagenesisⁱ	409 – 410	LI → AA: Abolishes interaction with ASXL1 and NCOA1. 1 Publication	2
Mutagenesisⁱ	412	E → Q: Impairs interaction with ASXL1 and NCOA1; when associated with Q-415. 1 Publication	1
Mutagenesisⁱ	413 – 414	ML → AA: Abolishes interaction with ASXL1 and NCOA1. 1 Publication	2
Mutagenesisⁱ	415	E → Q: Impairs interaction with ASXL1 and NCOA1; when associated with Q-412. 1 Publication	1

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	60 – 61	Breakpoint for translocation to form PLZF-RAR-alpha, RAR-alpha1-PLZF and PML-RAR-alpha oncogenes		2

Keywords - Diseaseⁱ

Proto-oncogene

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5914
MalaCards human disease database More...MalaCardsⁱ	RARA
MIMⁱ	612376 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000131759
Orphanetⁱ	520 Acute promyelocytic leukemia
PharmGKBⁱ	PA34225

Chemistry databases

ChEMBLⁱ	CHEMBL2055
Drug and drug target database More...DrugBankⁱ	DB00459 Acitretin DB00210 Adapalene DB00523 Alitretinoin DB00926 Etretinate DB00982 Isotretinoin DB05785 LGD-1550 DB04942 Tamibarotene DB00799 Tazarotene
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYⁱ	590

Polymorphism and mutation databases

BioMutaⁱ	RARA
DMDMⁱ	133483

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000053461	1 – 462	Retinoic acid receptor alphaAdd BLAST		462

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	77	Phosphoserine; by CDK7By similarity	1
Modified residueⁱ	96	Phosphoserine; by PKB/AKT11 Publication	1
Cross-linkⁱ	166	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Cross-linkⁱ	171	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residueⁱ	219	Phosphoserine; by PKA1 Publication	1
Modified residueⁱ	369	Phosphoserine; by PKA1 Publication	1
Cross-linkⁱ	399	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationⁱ

Phosphorylated on serine and threonine residues. Phosphorylation does not change during cell cycle. Phosphorylation on Ser-77 is crucial for transcriptional activity (By similarity). Phosphorylation by AKT1 is required for the repressor activity but has no effect on DNA binding, protein stability nor subcellular localization. Phosphorylated by PKA in vitro. This phosphorylation on Ser-219 and Ser-369 is critical for ligand binding, nuclear localization and transcriptional activity in response to FSH signaling.By similarity2 Publications

Sumoylated with SUMO2, mainly on Lys-399 which is also required for SENP6 binding. On all-trans retinoic acid (ATRA) binding, a confromational change may occur that allows sumoylation on two additional site, Lys-166 and Lys-171. Probably desumoylated by SENP6. Sumoylation levels determine nuclear localization and regulate ATRA-mediated transcriptional activity.2 Publications

Trimethylation enhances heterodimerization with RXRA and positively modulates the transcriptional activation.

Ubiquitinated.

Keywords - PTMⁱ

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P10276
PaxDbⁱ	P10276
PeptideAtlas More...PeptideAtlasⁱ	P10276
PRIDEⁱ	P10276
ProteomicsDBⁱ	52592 52593 [P10276-2] 52594 [P10276-3]

PTM databases

iPTMnetⁱ	P10276
PhosphoSitePlusⁱ	P10276

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000131759 Expressed in 217 organ(s), highest expression level in nasal cavity epithelium
CleanExⁱ	HS_RARA
ExpressionAtlasⁱ	P10276 baseline and differential
Genevisibleⁱ	P10276 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA058282

HPAⁱ

HPA058282

Interactionⁱ

Subunit structureⁱ

Heterodimer; with RXRA. Binds DNA preferentially as a heterodimer. Interacts with CDK7 (By similarity). Interacts with coactivators NCOA3 and NCOA6. Interacts with NCOA7; the interaction requires ligand-binding. Interacts (via the ligand-binding domain) with PRAME; the interaction is ligand (retinoic acid)-dependent. Interacts with AKT1; the interaction phosphorylates RARA and represses transactivation. Interacts with PRKAR1A; the interaction negatively regulates RARA transcriptional activity. Interacts with NCOR1 and NCOR2. Interacts with PRMT2. Interacts with LRIF1. Interacts with ASXL1 and NCOA1. Interacts with ACTN4.By similarity14 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
ACTN4	O43707-1	2	EBI-413374,EBI-15971664
Ajuba	Q91XC0	7	EBI-413374,EBI-1565930	From Mus musculus.
Asxl1	P59598	4	EBI-413374,EBI-5743705	From Mus musculus.
CCNH	P51946	2	EBI-413374,EBI-741406
EZH2	Q15910	2	EBI-413374,EBI-530054
GNAQ	P50148	4	EBI-413374,EBI-3909604
ITGB1BP2	Q9UKP3	2	EBI-413374,EBI-5659717
MED1	Q15648	6	EBI-413374,EBI-394459
MED25	Q71SY5	10	EBI-413374,EBI-394558
NCOA1	Q15788	7	EBI-413374,EBI-455189
NCOA3	Q9Y6Q9	2	EBI-413374,EBI-81196
NCOR1	O75376	6	EBI-413374,EBI-347233
NCOR2	Q9Y618	4	EBI-413374,EBI-80830
NFE2L2	Q16236	2	EBI-413374,EBI-2007911
NRIP1	P48552	4	EBI-413374,EBI-746484
PHF8	Q9UPP1-2	2	EBI-413374,EBI-6601215
PRKDC	P78527	3	EBI-413374,EBI-352053
RXRA	P19793	14	EBI-413374,EBI-78598
RXRB	P28702	11	EBI-413374,EBI-748576
RXRB	P28702-3	3	EBI-413374,EBI-16429492
RXRG	P48443	14	EBI-413374,EBI-712405
SIRT1	Q96EB6	3	EBI-413374,EBI-1802965
SUMO1	P63165	5	EBI-413374,EBI-80140
TEKT4	Q8WW24	3	EBI-413374,EBI-750487
ZNF423	Q2M1K9	2	EBI-413374,EBI-950016

GO - Molecular functionⁱ

alpha-actinin binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 22351778
enzyme binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 12039952
- 9628876
histone deacetylase binding Source: Ensembl
protein domain specific binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 20413580
protein heterodimerization activity
Source: UniProtKB
Inferred from direct assayⁱ
- 19917671
protein kinase A binding
Source: UniProtKB
Inferred from direct assayⁱ
- 20215566
protein kinase B binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 16417524
signaling receptor binding
Source: UniProtKB
Inferred from direct assayⁱ
- 19628791
transcription factor binding
Source: UniProtKB
Inferred from physical interactionⁱ
- 17641689

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	111849, 116 interactors
ComplexPortalⁱ	CPX-508 RXRalpha-RARalpha retinoic acid receptor complex CPX-816 RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex
CORUMⁱ	P10276
Database of interacting proteins More...DIPⁱ	DIP-34N
IntActⁱ	P10276, 68 interactors
Molecular INTeraction database More...MINTⁱ	P10276
STRINGⁱ	9606.ENSP00000254066

Chemistry databases

BindingDBⁱ

P10276

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	89 – 91	Combined sources	3
Beta strandⁱ	97 – 99	Combined sources	3
Helixⁱ	106 – 117	Combined sources	12
Turnⁱ	134 – 136	Combined sources	3
Helixⁱ	137 – 139	Combined sources	3
Helixⁱ	141 – 150	Combined sources	10
Helixⁱ	155 – 157	Combined sources	3
Helixⁱ	183 – 196	Combined sources	14
Helixⁱ	202 – 204	Combined sources	3
Beta strandⁱ	214 – 216	Combined sources	3
Helixⁱ	222 – 244	Combined sources	23
Helixⁱ	249 – 251	Combined sources	3
Helixⁱ	254 – 275	Combined sources	22
Turnⁱ	279 – 282	Combined sources	4
Beta strandⁱ	283 – 285	Combined sources	3
Beta strandⁱ	289 – 293	Combined sources	5
Helixⁱ	294 – 300	Combined sources	7
Helixⁱ	303 – 305	Combined sources	3
Helixⁱ	306 – 316	Combined sources	11
Helixⁱ	317 – 319	Combined sources	3
Helixⁱ	323 – 334	Combined sources	12
Helixⁱ	345 – 366	Combined sources	22
Helixⁱ	373 – 401	Combined sources	29
Beta strandⁱ	402 – 404	Combined sources	3
Helixⁱ	408 – 414	Combined sources	7

Show more details

3D structure databases

ProteinModelPortalⁱ	P10276
SMRⁱ	P10276
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P10276

EvolutionaryTraceⁱ

P10276

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	183 – 417	NR LBDPROSITE-ProRule annotationAdd BLAST		235

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 87	ModulatingAdd BLAST	87
Regionⁱ	154 – 182	HingeAdd BLAST	29
Regionⁱ	404 – 419	Required for binding corepressor NCOR1Add BLAST	16

Domainⁱ

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

Sequence similaritiesⁱ

Belongs to the nuclear hormone receptor family. NR1 subfamily.Curated

Zinc finger

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Zinc fingerⁱ	88 – 108	NR C4-typePROSITE-ProRule annotationAdd BLAST		21
Zinc fingerⁱ	124 – 148	NR C4-typePROSITE-ProRule annotationAdd BLAST		25

Keywords - Domainⁱ

Zinc-finger

Phylogenomic databases

eggNOGⁱ	KOG3575 Eukaryota ENOG410XRZC LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00870000136372
HOGENOMⁱ	HOG000010312
HOVERGENⁱ	HBG005606
InParanoidⁱ	P10276
KEGG Orthology (KO) More...KOⁱ	K08527
OMAⁱ	QECSESY
PhylomeDBⁱ	P10276
TreeFamⁱ	TF328382

Family and domain databases

Gene3Dⁱ	3.30.50.10, 1 hit
InterProⁱ	View protein in InterPro IPR035500 NHR_like_dom_sf IPR000536 Nucl_hrmn_rcpt_lig-bd IPR001723 Nuclear_hrmn_rcpt IPR003078 Retinoic_acid_rcpt IPR001628 Znf_hrmn_rcpt IPR013088 Znf_NHR/GATA
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00104 Hormone_recep, 1 hit PF00105 zf-C4, 1 hit
PRINTSⁱ	PR01292 RETNOICACIDR PR00398 STRDHORMONER PR00047 STROIDFINGER
SMARTⁱ	View protein in SMART SM00430 HOLI, 1 hit SM00399 ZnF_C4, 1 hit
SUPFAMⁱ	SSF48508 SSF48508, 1 hit
PROSITEⁱ	View protein in PROSITE PS51843 NR_LBD, 1 hit PS00031 NUCLEAR_REC_DBD_1, 1 hit PS51030 NUCLEAR_REC_DBD_2, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.ⁱShow all

Isoform Alpha-1 (identifier: P10276-1) [UniParc]FASTA Add to basket

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
MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTTLQHQLPV 
        60         70         80         90        100
SGYSTPSPAT IETQSSSSEE IVPSPPSPPP LPRIYKPCFV CQDKSSGYHY 
       110        120        130        140        150
GVSACEGCKG FFRRSIQKNM VYTCHRDKNC IINKVTRNRC QYCRLQKCFE 
       160        170        180        190        200
VGMSKESVRN DRNKKKKEVP KPECSESYTL TPEVGELIEK VRKAHQETFP 
       210        220        230        240        250
ALCQLGKYTT NNSSEQRVSL DIDLWDKFSE LSTKCIIKTV EFAKQLPGFT 
       260        270        280        290        300
TLTIADQITL LKAACLDILI LRICTRYTPE QDTMTFSDGL TLNRTQMHNA 
       310        320        330        340        350
GFGPLTDLVF AFANQLLPLE MDDAETGLLS AICLICGDRQ DLEQPDRVDM 
       360        370        380        390        400
LQEPLLEALK VYVRKRRPSR PHMFPKMLMK ITDLRSISAK GAERVITLKM 
       410        420        430        440        450
EIPGSMPPLI QEMLENSEGL DTLSGQPGGG GRDGGGLAPP PGSCSPSLSP 
       460 
SSNRSSPATH SP

Length:462

Mass (Da):50,771

Last modified:October 1, 1989 - v2

Checksum:ⁱE8D1CF9A1E57CB99

GO

Isoform Alpha-2 (identifier: P10276-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-60: MASNSSSCPT...SGYSTPSPAT → MYESVEVGGP...TPLWNGSNHS

« Hide

        10         20         30         40         50
MYESVEVGGP TPNPFLVVDF YNQNRACLLP EKGLPAPGPY STPLRTPLWN 
        60         70         80         90        100
GSNHSIETQS SSSEEIVPSP PSPPPLPRIY KPCFVCQDKS SGYHYGVSAC 
       110        120        130        140        150
EGCKGFFRRS IQKNMVYTCH RDKNCIINKV TRNRCQYCRL QKCFEVGMSK 
       160        170        180        190        200
ESVRNDRNKK KKEVPKPECS ESYTLTPEVG ELIEKVRKAH QETFPALCQL 
       210        220        230        240        250
GKYTTNNSSE QRVSLDIDLW DKFSELSTKC IIKTVEFAKQ LPGFTTLTIA 
       260        270        280        290        300
DQITLLKAAC LDILILRICT RYTPEQDTMT FSDGLTLNRT QMHNAGFGPL 
       310        320        330        340        350
TDLVFAFANQ LLPLEMDDAE TGLLSAICLI CGDRQDLEQP DRVDMLQEPL 
       360        370        380        390        400
LEALKVYVRK RRPSRPHMFP KMLMKITDLR SISAKGAERV ITLKMEIPGS 
       410        420        430        440        450
MPPLIQEMLE NSEGLDTLSG QPGGGGRDGG GLAPPPGSCS PSLSPSSNRS 

SPATHSP

Show »

Length:457

Mass (Da):50,742

Checksum:ⁱ1E328ED7945D1F95

GO

Isoform Alpha-1-deltaBC (identifier: P10276-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
61-157: Missing.

« Hide

        10         20         30         40         50
MASNSSSCPT PGGGHLNGYP VPPYAFFFPP MLGGLSPPGA LTTLQHQLPV 
        60         70         80         90        100
SGYSTPSPAT VRNDRNKKKK EVPKPECSES YTLTPEVGEL IEKVRKAHQE 
       110        120        130        140        150
TFPALCQLGK YTTNNSSEQR VSLDIDLWDK FSELSTKCII KTVEFAKQLP 
       160        170        180        190        200
GFTTLTIADQ ITLLKAACLD ILILRICTRY TPEQDTMTFS DGLTLNRTQM 
       210        220        230        240        250
HNAGFGPLTD LVFAFANQLL PLEMDDAETG LLSAICLICG DRQDLEQPDR 
       260        270        280        290        300
VDMLQEPLLE ALKVYVRKRR PSRPHMFPKM LMKITDLRSI SAKGAERVIT 
       310        320        330        340        350
LKMEIPGSMP PLIQEMLENS EGLDTLSGQP GGGGRDGGGL APPPGSCSPS 
       360 
LSPSSNRSSP ATHSP

Note: Does not bind nor transactivate RARE on its own but may do so as a heterodimer with Alpha-1.

Show »

Length:365

Mass (Da):39,700

Checksum:ⁱD24F282D50E9953E

GO

Computationally mapped potential isoform sequencesⁱ

There are 3 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation
A8MUP8	A8MUP8_HUMAN	Retinoic acid receptor alpha Retinoic acid receptor alpha (Retinoic acid receptor, alpha, isoform CRA_e)	RARA hCG_2007196	478	Annotation score:
J3KSJ4	J3KSJ4_HUMAN	Retinoic acid receptor alpha Retinoic acid receptor alpha	RARA	186	Annotation score:
J3QRM2	J3QRM2_HUMAN	Retinoic acid receptor alpha Retinoic acid receptor alpha	RARA	66	Annotation score:

Sequence cautionⁱ

The sequence AAB00112 differs from that shown. Reason: Erroneous initiation.Curated

The sequence AAB00113 differs from that shown. Reason: Erroneous initiation.Curated

The sequence BAB62809 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	241	E → D in AAD05222 (PubMed:10337631).Curated		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_003629	1 – 60	MASNS…PSPAT → MYESVEVGGPTPNPFLVVDF YNQNRACLLPEKGLPAPGPY STPLRTPLWNGSNHS in isoform Alpha-2. 1 PublicationAdd BLAST		60
Alternative sequenceⁱVSP_043143	61 – 157	Missing in isoform Alpha-1-deltaBC. 1 PublicationAdd BLAST		97

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X06614 mRNA Translation: CAA29829.1 X06538 mRNA Translation: CAA29787.1 AF088895 AF088894 Genomic DNA Translation: AAD05222.1 FJ487576 mRNA Translation: ACK86665.1 AC080112 Genomic DNA No translation available. BC008727 mRNA Translation: AAH08727.1 BC071733 mRNA Translation: AAH71733.1 X56058, X58685 mRNA Translation: CAA39533.1 X58685 mRNA Translation: CAA41532.1 U41742 mRNA Translation: AAB00112.1 Different initiation. U41743 mRNA Translation: AAB00113.1 Different initiation. AF283809 Genomic DNA Translation: AAF87249.1 AB067754 mRNA Translation: BAB62809.1 Different initiation.
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS11366.1 [P10276-1] CCDS42317.1 [P10276-2] CCDS45671.1 [P10276-3]
PIRⁱ	A29491
NCBI Reference Sequences More...RefSeqⁱ	NP_000955.1, NM_000964.3 [P10276-1] NP_001019980.1, NM_001024809.3 [P10276-2] NP_001138773.1, NM_001145301.2 NP_001138774.1, NM_001145302.2 [P10276-3] XP_005257610.1, XM_005257553.1 [P10276-1] XP_005257611.1, XM_005257554.1 [P10276-1] XP_011523397.1, XM_011525095.1 [P10276-1]
UniGeneⁱ	Hs.654583

Genome annotation databases

Ensemblⁱ	ENST00000254066; ENSP00000254066; ENSG00000131759 [P10276-1] ENST00000394081; ENSP00000377643; ENSG00000131759 [P10276-2] ENST00000394089; ENSP00000377649; ENSG00000131759 [P10276-1] ENST00000425707; ENSP00000389993; ENSG00000131759 [P10276-3]
GeneIDⁱ	5914
KEGGⁱ	hsa:5914
UCSC genome browser More...UCSCⁱ	uc002hun.3 human [P10276-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Chromosomal rearrangement

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P10276	RARA protein		HUMAN		462	UniRef100_P10276
RARA isoform 2		PANTR		462
Retinoic acid receptor alpha isoform 1		MACMU		462
Retinoic acid receptor alpha		RHIBE		462
Retinoic acid receptor alpha		MACNE		462
+10
P10276-2	Retinoic acid nuclear receptor alpha variant 2		HUMAN		457	UniRef100_F1D8N9
Retinoic acid receptor alpha isoform 2		MACMU		457
RARA isoform 4		PANTR		457
Retinoic acid receptor alpha		CERAT		457
Retinoic acid receptor alpha		RHIRO		457
+6
P10276-3	RARA isoform 1		PANTR		365	UniRef100_P10276-3
Retinoic acid receptor alpha		MACMU		365
RARA isoform 4		PONAB		365
Retinoic acid receptor alpha		CERAT		365
Retinoic acid receptor alpha		RHIRO		365
+8

Protein	Similar proteins		Species	Score	Length	Source
P10276	RARA protein		HUMAN		462	UniRef90_P10276
RARA isoform 2		PANTR		462
Retinoic acid receptor alpha isoform 1		MACMU		462
Retinoic acid receptor alpha		RHIBE		462
Retinoic acid receptor alpha		MACNE		462
+35
P10276-3	RARA isoform 1		PANTR		365	UniRef90_P10276-3
Retinoic acid receptor alpha		MACMU		365
RARA isoform 4		PONAB		365
Retinoic acid receptor alpha		CERAT		365
Retinoic acid receptor alpha		RHIRO		365
+30

Protein	Similar proteins		Species	Score	Length	Source
P10276	Retinoic acid receptor alpha-A		DANRE		444	UniRef50_P10276
Retinoic acid receptor alpha		MOUSE		462
Retinoic acid receptor alpha		CANLF		462
RARA protein		HUMAN		462
RARA isoform 2		PANTR		462
+553
P10276-3	RARA isoform 1		PANTR		365	UniRef50_P10276-3
Retinoic acid receptor alpha		MACMU		365
RARA isoform 4		PONAB		365
Retinoic acid receptor alpha		CERAT		365
Retinoic acid receptor alpha		RHIRO		365
+56

Cross-referencesⁱ

Web resourcesⁱ

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

Retinoic acid receptor entry

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X06614 mRNA Translation: CAA29829.1 X06538 mRNA Translation: CAA29787.1 AF088895 AF088894 Genomic DNA Translation: AAD05222.1 FJ487576 mRNA Translation: ACK86665.1 AC080112 Genomic DNA No translation available. BC008727 mRNA Translation: AAH08727.1 BC071733 mRNA Translation: AAH71733.1 X56058, X58685 mRNA Translation: CAA39533.1 X58685 mRNA Translation: CAA41532.1 U41742 mRNA Translation: AAB00112.1 Different initiation. U41743 mRNA Translation: AAB00113.1 Different initiation. AF283809 Genomic DNA Translation: AAF87249.1 AB067754 mRNA Translation: BAB62809.1 Different initiation.
CCDSⁱ	CCDS11366.1 [P10276-1] CCDS42317.1 [P10276-2] CCDS45671.1 [P10276-3]
PIRⁱ	A29491
RefSeqⁱ	NP_000955.1, NM_000964.3 [P10276-1] NP_001019980.1, NM_001024809.3 [P10276-2] NP_001138773.1, NM_001145301.2 NP_001138774.1, NM_001145302.2 [P10276-3] XP_005257610.1, XM_005257553.1 [P10276-1] XP_005257611.1, XM_005257554.1 [P10276-1] XP_011523397.1, XM_011525095.1 [P10276-1]
UniGeneⁱ	Hs.654583

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
	1DKF	X-ray	2.50	B	182-416	[»]
	1DSZ	X-ray	1.70	A	82-167	[»]
	3A9E	X-ray	2.75	B	153-421	[»]
	3KMR	X-ray	1.80	A	176-421	[»]
	3KMZ	X-ray	2.10	A/B	176-421	[»]
	4DQM	X-ray	2.75	A/C	182-415	[»]
	5K13	X-ray	1.85	A	181-426	[»]
ProteinModelPortalⁱ	P10276
SMRⁱ	P10276
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111849, 116 interactors
ComplexPortalⁱ	CPX-508 RXRalpha-RARalpha retinoic acid receptor complex CPX-816 RXRalpha-RARalpha-NCOA2 retinoic acid receptor complex
CORUMⁱ	P10276
DIPⁱ	DIP-34N
IntActⁱ	P10276, 68 interactors
MINTⁱ	P10276
STRINGⁱ	9606.ENSP00000254066

Chemistry databases

BindingDBⁱ	P10276
ChEMBLⁱ	CHEMBL2055
DrugBankⁱ	DB00459 Acitretin DB00210 Adapalene DB00523 Alitretinoin DB00926 Etretinate DB00982 Isotretinoin DB05785 LGD-1550 DB04942 Tamibarotene DB00799 Tazarotene
GuidetoPHARMACOLOGYⁱ	590

Protein family/group databases

MoonDBⁱ	P10276 Predicted

MoonDBⁱ

P10276 Predicted

PTM databases

iPTMnetⁱ	P10276
PhosphoSitePlusⁱ	P10276

Polymorphism and mutation databases

BioMutaⁱ	RARA
DMDMⁱ	133483

Proteomic databases

EPDⁱ	P10276
PaxDbⁱ	P10276
PeptideAtlasⁱ	P10276
PRIDEⁱ	P10276
ProteomicsDBⁱ	52592 52593 [P10276-2] 52594 [P10276-3]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	5914
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000254066; ENSP00000254066; ENSG00000131759 [P10276-1] ENST00000394081; ENSP00000377643; ENSG00000131759 [P10276-2] ENST00000394089; ENSP00000377649; ENSG00000131759 [P10276-1] ENST00000425707; ENSP00000389993; ENSG00000131759 [P10276-3]
GeneIDⁱ	5914
KEGGⁱ	hsa:5914
UCSCⁱ	uc002hun.3 human [P10276-1]

Organism-specific databases

CTDⁱ	5914
DisGeNETⁱ	5914
EuPathDBⁱ	HostDB:ENSG00000131759.17
GeneCardsⁱ	RARA
HGNCⁱ	HGNC:9864 RARA
HPAⁱ	HPA058282
MalaCardsⁱ	RARA
MIMⁱ	180240 gene 612376 phenotype
neXtProtⁱ	NX_P10276
OpenTargetsⁱ	ENSG00000131759
Orphanetⁱ	520 Acute promyelocytic leukemia
PharmGKBⁱ	PA34225
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG3575 Eukaryota ENOG410XRZC LUCA
GeneTreeⁱ	ENSGT00870000136372
HOGENOMⁱ	HOG000010312
HOVERGENⁱ	HBG005606
InParanoidⁱ	P10276
KOⁱ	K08527
OMAⁱ	QECSESY
PhylomeDBⁱ	P10276
TreeFamⁱ	TF328382

Enzyme and pathway databases

Reactomeⁱ	R-HSA-383280 Nuclear Receptor transcription pathway R-HSA-4090294 SUMOylation of intracellular receptors R-HSA-5362517 Signaling by Retinoic Acid R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
SignaLinkⁱ	P10276
SIGNORⁱ	P10276

Miscellaneous databases

ChiTaRSⁱ	RARA human
EvolutionaryTraceⁱ	P10276
GeneWikiⁱ	Retinoic_acid_receptor_alpha
GenomeRNAiⁱ	5914
Protein Ontology More...PROⁱ	PR:P10276
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000131759 Expressed in 217 organ(s), highest expression level in nasal cavity epithelium
CleanExⁱ	HS_RARA
ExpressionAtlasⁱ	P10276 baseline and differential
Genevisibleⁱ	P10276 HS

Family and domain databases

Gene3Dⁱ	3.30.50.10, 1 hit
InterProⁱ	View protein in InterPro IPR035500 NHR_like_dom_sf IPR000536 Nucl_hrmn_rcpt_lig-bd IPR001723 Nuclear_hrmn_rcpt IPR003078 Retinoic_acid_rcpt IPR001628 Znf_hrmn_rcpt IPR013088 Znf_NHR/GATA
Pfamⁱ	View protein in Pfam PF00104 Hormone_recep, 1 hit PF00105 zf-C4, 1 hit
PRINTSⁱ	PR01292 RETNOICACIDR PR00398 STRDHORMONER PR00047 STROIDFINGER
SMARTⁱ	View protein in SMART SM00430 HOLI, 1 hit SM00399 ZnF_C4, 1 hit
SUPFAMⁱ	SSF48508 SSF48508, 1 hit
PROSITEⁱ	View protein in PROSITE PS51843 NR_LBD, 1 hit PS00031 NUCLEAR_REC_DBD_1, 1 hit PS51030 NUCLEAR_REC_DBD_2, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RARA_HUMAN
Accessionⁱ	P10276Primary (citable) accession number: P10276 Secondary accession number(s): B8Y636 , P78456, Q13440, Q13441, Q96S41, Q9NQS0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	October 1, 1989
	Last modified:	September 12, 2018
	This is version 232 of the entry and version 2 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, Reference proteome

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P10276 (RARA_HUMAN)

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Retinoic acid receptor alpha

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

Caution

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

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

Nucleus

Other locations

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

Mutagenesis

Sites

Keywords - Diseasei

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

Amino acid modifications

Keywords - PTMi

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

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

Domains and Repeats

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

Zinc finger

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Computationally mapped potential isoform sequencesi

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Computationally mapped potential isoform sequencesⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ