Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

Retinoic acid nuclear receptor gamma variant 1

Gene

RARG

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

ReceptorUniRule annotationImported

Keywords - Biological processi

Transcription, Transcription regulationUniRule annotationSAAS annotation

Keywords - Ligandi

DNA-bindingUniRule annotationSAAS annotation, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Submitted name:
Retinoic acid nuclear receptor gamma variant 1Imported
Submitted name:
Retinoic acid receptor gammaImported
Submitted name:
Retinoic acid receptor, gamma, isoform CRA_bImported
Submitted name:
cDNA FLJ75202, highly similar to Homo sapiens, retinoic acid receptor, gammaImported
Gene namesi
Name:RARGImported
Synonyms:NR1B3Imported
ORF Names:hCG_31521Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

  • Nucleus SAAS annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

NucleusUniRule annotationSAAS annotation

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34227.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000377947.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 16276Nuclear receptor DNA-bindingInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the nuclear hormone receptor family.UniRule annotationSAAS annotation
Contains nuclear receptor DNA-binding domain.SAAS annotation

Keywords - Domaini

Zinc-fingerUniRule annotationSAAS annotation

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOVERGENiHBG005606.
KOiK08529.
OMAiNKERLFV.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR003078. Retinoic_acid_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A8K3H3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATNKERLFA AGALGPGSGY PGAGFPFAFP GALRGSPPFE MLSPSFRGLG
60 70 80 90 100
QPDLPKEMAS LSVETQSTSS EEMVPSSPSP PPPPRVYKPC FVCNDKSSGY
110 120 130 140 150
HYGVSSCEGC KGFFRRSIQK NMVYTCHRDK NCIINKVTRN RCQYCRLQKC
160 170 180 190 200
FEVGMSKEAV RNDRNKKKKE VKEEGSPDSY ELSPQLEELI TKVSKAHQET
210 220 230 240 250
FPSLCQLGKY TTNSSADHRV QLDLGLWDKF SELATKCIIK IVEFAKRLPG
260 270 280 290 300
FTGLSIADQI TLLKAACLDI LMLRICTRYT PEQDTMTFSD GLTLNRTQMH
310 320 330 340 350
NAGFGPLTDL VFAFAGQLLP LEMDDTETGL LSAICLICGD RMDLEEPEKV
360 370 380 390 400
DKLQEPLLEA LRLYARRRRP SQPYMFPRML MKITDLRGIS TKGAERAITL
410 420 430 440 450
KMEIPGPMPP LIREMLENPE MFEDDSSQPG PHPNASSEDE VPGGQGKGGL

KSPA
Length:454
Mass (Da):50,342
Last modified:December 4, 2007 - v1
Checksum:i1EE27B22772D4AFD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ692828 mRNA. Translation: ADZ17339.1.
AK290588 mRNA. Translation: BAF83277.1.
AB307689 mRNA. Translation: BAH02280.1.
CH471054 Genomic DNA. Translation: EAW96677.1.
CH471054 Genomic DNA. Translation: EAW96678.1.
RefSeqiNP_000957.1. NM_000966.5.
XP_005269113.1. XM_005269056.2.
XP_005269114.1. XM_005269057.1.
UniGeneiHs.1497.
Hs.733399.

Genome annotation databases

GeneIDi5916.
KEGGihsa:5916.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
HQ692828 mRNA. Translation: ADZ17339.1.
AK290588 mRNA. Translation: BAF83277.1.
AB307689 mRNA. Translation: BAH02280.1.
CH471054 Genomic DNA. Translation: EAW96677.1.
CH471054 Genomic DNA. Translation: EAW96678.1.
RefSeqiNP_000957.1. NM_000966.5.
XP_005269113.1. XM_005269056.2.
XP_005269114.1. XM_005269057.1.
UniGeneiHs.1497.
Hs.733399.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000377947.

Protocols and materials databases

DNASUi5916.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi5916.
KEGGihsa:5916.

Organism-specific databases

CTDi5916.
PharmGKBiPA34227.

Phylogenomic databases

eggNOGiKOG3575. Eukaryota.
ENOG410XRZC. LUCA.
HOVERGENiHBG005606.
KOiK08529.
OMAiNKERLFV.

Miscellaneous databases

ChiTaRSiRARG. human.
GenomeRNAii5916.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR003078. Retinoic_acid_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. Cited for: NUCLEOTIDE SEQUENCE.
  3. Nozawa A., Kobayashi T., Kodani Y., Sawasaki T., Endo Y.
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  4. Cited for: NUCLEOTIDE SEQUENCE.
  5. "Comprehensive DNA-binding analysis of human hormone nuclear receptors by fluorescence correlation spectroscopy based on cell-free system."
    Kobayashi T., Kodani Y., Sawasaki T., Endo Y.
    Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  6. "Isolation of cDNA coding for multiple human nuclear receptor clones."
    Kaighin V.A., Martin A.L., Aronstam R.S.
    Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: ProstateImported.

Entry informationi

Entry nameiA8K3H3_HUMAN
AccessioniPrimary (citable) accession number: A8K3H3
Entry historyi
Integrated into UniProtKB/TrEMBL: December 4, 2007
Last sequence update: December 4, 2007
Last modified: June 8, 2016
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
DisclaimerAny 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.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.