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P18911

- RARG_MOUSE

UniProt

P18911 - RARG_MOUSE

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Protein

Retinoic acid receptor gamma

Gene

Rarg

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 RAR/RXR 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, acts mainly as an activator of gene expression due to weak binding to corepressors By similarity. Required for limb bud development. In concert with RARA or RARB, required for skeletal growth, matrix homeostasis and growth plate function.By similarity2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi90 – 15566Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri90 – 11021NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri126 – 15025NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: BHF-UCL
  2. retinoic acid receptor activity Source: Ensembl
  3. retinoid X receptor binding Source: BHF-UCL
  4. RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
  5. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  6. steroid hormone receptor activity Source: InterPro
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. anterior/posterior pattern specification Source: MGI
  2. bone development Source: UniProtKB
  3. bone morphogenesis Source: MGI
  4. camera-type eye development Source: MGI
  5. cellular response to retinoic acid Source: MGI
  6. chondrocyte development Source: UniProtKB
  7. embryonic camera-type eye development Source: MGI
  8. embryonic eye morphogenesis Source: MGI
  9. embryonic hindlimb morphogenesis Source: MGI
  10. epithelium development Source: MGI
  11. face development Source: MGI
  12. gland development Source: MGI
  13. glandular epithelial cell development Source: MGI
  14. growth plate cartilage chondrocyte growth Source: UniProtKB
  15. growth plate cartilage development Source: MGI
  16. Harderian gland development Source: MGI
  17. limb development Source: UniProtKB
  18. multicellular organism growth Source: MGI
  19. negative regulation of apoptotic process Source: MGI
  20. negative regulation of cartilage development Source: MGI
  21. negative regulation of cell differentiation Source: MGI
  22. negative regulation of cell proliferation Source: MGI
  23. negative regulation of chondrocyte differentiation Source: MGI
  24. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  25. neural tube closure Source: MGI
  26. positive regulation of apoptotic process Source: MGI
  27. positive regulation of cell proliferation Source: MGI
  28. positive regulation of gene expression Source: MGI
  29. positive regulation of programmed cell death Source: MGI
  30. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  31. prostate gland epithelium morphogenesis Source: MGI
  32. regulation of gene expression Source: MGI
  33. regulation of myelination Source: Ensembl
  34. reproductive structure development Source: MGI
  35. retina development in camera-type eye Source: MGI
  36. retinal pigment epithelium development Source: MGI
  37. retinoic acid receptor signaling pathway Source: MGI
  38. trachea cartilage development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoic acid receptor gamma
Short name:
RAR-gamma
Alternative name(s):
Nuclear receptor subfamily 1 group B member 3
Gene namesi
Name:Rarg
Synonyms:Nr1b3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:97858. Rarg.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleus Source: MGI
  2. transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Rarg and Rarb double null mice exhibit growth retardation 3 weeks after birth. Defects are found in the growth plates with deficiency in cartilage. Growth retardation was noticable in limb sketal elements such as femurs. Early lethality and male sterility due to squamous metaplasia of the seminal vesicles and prostate are also observed. Isoform 2 mutants appear normal. The Rarg and Cyp26b1 double null mutation is able to partially rescue limb skeletal morphology without restoring normal expression of proximo-distal patterning genes.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 458458Retinoic acid receptor gammaPRO_0000053474Add
BLAST

Proteomic databases

PRIDEiP18911.

PTM databases

PhosphoSiteiP18911.

Expressioni

Developmental stagei

In E9.5-E12.5 embryos, expression throughout limb bud mesenchyme. This expression overlaps with that of CYP26B1. Also strongly expressed in the caudal and craniofacial regions.1 Publication

Gene expression databases

BgeeiP18911.
CleanExiMM_RARG.
ExpressionAtlasiP18911. baseline and differential.
GenevestigatoriP18911.

Interactioni

Subunit structurei

Homodimer By similarity. Heterodimer with a RXR molecule By similarity. Binds DNA preferentially as a RAR/RXR heterodimer By similarity. Forms a complex with PUS1 and the SRA1 RNA in the nucleus.By similarity1 Publication

Protein-protein interaction databases

BioGridi202595. 4 interactions.
DIPiDIP-42822N.
IntActiP18911. 1 interaction.
MINTiMINT-2834553.

Structurei

3D structure databases

ProteinModelPortaliP18911.
SMRiP18911. Positions 89-419.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8989ModulatingAdd
BLAST
Regioni156 – 20146HingeAdd
BLAST
Regioni202 – 421220Ligand-bindingAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri90 – 11021NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri126 – 15025NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG297448.
GeneTreeiENSGT00760000118837.
HOGENOMiHOG000010312.
HOVERGENiHBG005606.
InParanoidiP18911.
KOiK08529.
OMAiRSPQPDQ.
OrthoDBiEOG738053.
PhylomeDBiP18911.
TreeFamiTF328382.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR003078. Retinoic_acid_rcpt.
IPR001723. Str_hrmn_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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P18911-1) [UniParc]FASTAAdd to Basket

Also known as: A

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
MATNKERLFA PGALGPGSGY 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 MFEDDSSKPG PHPKASSEDE APGGQGKRGQ

SPQPDQGP
Length:458
Mass (Da):50,891
Last modified:February 5, 2008 - v3
Checksum:i1D13D2F1482D7194
GO
Isoform 2 (identifier: P18911-2) [UniParc] [UniParc]FASTAAdd to Basket

Also known as: B

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MATNKERLFA...PDLPKEMASL → MYDCMESFVP...FAWAQPASLQ

Show »
Length:447
Mass (Da):49,849
Checksum:i75E0BCB50BC9AD3B
GO
Isoform 3 (identifier: P18911-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MATNKERLFA...DLPKEMASLS → MHKGDNSGHQ...LSSHAAFHSA

Show »
Length:434
Mass (Da):48,708
Checksum:iD0885E92CB7B2966
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti63 – 631V → E in BAE28323. (PubMed:16141072)Curated
Sequence conflicti78 – 781P → A in BAE28323. (PubMed:16141072)Curated
Sequence conflicti176 – 1761S → L in AAH13709. (PubMed:15489334)Curated
Sequence conflicti369 – 3724RPSQ → DPAK in AAA40035. (PubMed:2157970)Curated
Sequence conflicti369 – 3724RPSQ → DPAK in AAA40036. (PubMed:2157970)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6262MATNK…MASLS → MHKGDNSGHQQVPRKRGHGM RVLLLSFCLSSHAAFHSA in isoform 3. 1 PublicationVSP_031081Add
BLAST
Alternative sequencei1 – 6161MATNK…EMASL → MYDCMESFVPGPRRLYGAAG PGAGLLRRATGSSCFAGLES FAWAQPASLQ in isoform 2. 2 PublicationsVSP_031082Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15848 mRNA. Translation: CAA33845.1.
M34475 mRNA. Translation: AAA40036.1.
M34476 mRNA. Translation: AAA40035.1.
AK148064 mRNA. Translation: BAE28323.1.
BC012923 mRNA. Translation: AAH12923.1.
BC013709 mRNA. Translation: AAH13709.1.
M32068 mRNA. Translation: AAA40032.1.
M32069 mRNA. Translation: AAA40033.1.
M32070 mRNA. Translation: AAA40034.1.
CCDSiCCDS27875.1. [P18911-1]
CCDS37226.1. [P18911-2]
PIRiB34714.
S05052. A34714.
RefSeqiNP_001036192.1. NM_001042727.2. [P18911-2]
NP_035374.3. NM_011244.4. [P18911-1]
XP_006520712.1. XM_006520649.1. [P18911-1]
XP_006520713.1. XM_006520650.1. [P18911-1]
UniGeneiMm.1273.

Genome annotation databases

EnsembliENSMUST00000043172; ENSMUSP00000048838; ENSMUSG00000001288. [P18911-1]
ENSMUST00000063339; ENSMUSP00000067266; ENSMUSG00000001288. [P18911-2]
GeneIDi19411.
KEGGimmu:19411.
UCSCiuc007xvc.1. mouse. [P18911-2]
uc007xvd.1. mouse. [P18911-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X15848 mRNA. Translation: CAA33845.1 .
M34475 mRNA. Translation: AAA40036.1 .
M34476 mRNA. Translation: AAA40035.1 .
AK148064 mRNA. Translation: BAE28323.1 .
BC012923 mRNA. Translation: AAH12923.1 .
BC013709 mRNA. Translation: AAH13709.1 .
M32068 mRNA. Translation: AAA40032.1 .
M32069 mRNA. Translation: AAA40033.1 .
M32070 mRNA. Translation: AAA40034.1 .
CCDSi CCDS27875.1. [P18911-1 ]
CCDS37226.1. [P18911-2 ]
PIRi B34714.
S05052. A34714.
RefSeqi NP_001036192.1. NM_001042727.2. [P18911-2 ]
NP_035374.3. NM_011244.4. [P18911-1 ]
XP_006520712.1. XM_006520649.1. [P18911-1 ]
XP_006520713.1. XM_006520650.1. [P18911-1 ]
UniGenei Mm.1273.

3D structure databases

ProteinModelPortali P18911.
SMRi P18911. Positions 89-419.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202595. 4 interactions.
DIPi DIP-42822N.
IntActi P18911. 1 interaction.
MINTi MINT-2834553.

Chemistry

BindingDBi P18911.
ChEMBLi CHEMBL4177.
GuidetoPHARMACOLOGYi 592.

PTM databases

PhosphoSitei P18911.

Proteomic databases

PRIDEi P18911.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000043172 ; ENSMUSP00000048838 ; ENSMUSG00000001288 . [P18911-1 ]
ENSMUST00000063339 ; ENSMUSP00000067266 ; ENSMUSG00000001288 . [P18911-2 ]
GeneIDi 19411.
KEGGi mmu:19411.
UCSCi uc007xvc.1. mouse. [P18911-2 ]
uc007xvd.1. mouse. [P18911-1 ]

Organism-specific databases

CTDi 5916.
MGIi MGI:97858. Rarg.

Phylogenomic databases

eggNOGi NOG297448.
GeneTreei ENSGT00760000118837.
HOGENOMi HOG000010312.
HOVERGENi HBG005606.
InParanoidi P18911.
KOi K08529.
OMAi RSPQPDQ.
OrthoDBi EOG738053.
PhylomeDBi P18911.
TreeFami TF328382.

Miscellaneous databases

NextBioi 296533.
PROi P18911.
SOURCEi Search...

Gene expression databases

Bgeei P18911.
CleanExi MM_RARG.
ExpressionAtlasi P18911. baseline and differential.
Genevestigatori P18911.

Family and domain databases

Gene3Di 1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR003078. Retinoic_acid_rcpt.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view ]
Pfami PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of murine alpha and beta retinoic acid receptors and a novel receptor gamma predominantly expressed in skin."
    Zelent A., Krust A., Petkovich M., Kastner P., Chambon P.
    Nature 339:714-717(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  2. "Identification of a novel isoform of the retinoic acid receptor gamma expressed in the mouse embryo."
    Giguere V., Shago M., Zirngibl R., Tate P., Rossant J., Varmuza S.
    Mol. Cell. Biol. 10:2335-2340(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: Czech II.
    Tissue: Mammary tumor.
  5. "Murine isoforms of retinoic acid receptor gamma with specific patterns of expression."
    Kastner P., Krust A., Mendelsohn C., Garnier J.-M., Zelent A., Leroy P., Staub A., Chambon P.
    Proc. Natl. Acad. Sci. U.S.A. 87:2700-2704(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-74 (ISOFORMS 1; 2 AND 3).
  6. "Function of retinoic acid receptor gamma in the mouse."
    Lohnes D., Kastner P., Dierich A., Mark M., LeMeur M., Chambon P.
    Cell 73:643-658(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  7. "Regulation of nuclear receptor activity by a pseudouridine synthase through posttranscriptional modification of steroid receptor RNA activator."
    Zhao X., Patton J.R., Davis S.L., Florence B., Ames S.J., Spanjaard R.A.
    Mol. Cell 15:549-558(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH PUS1 AND SRA1, SUBCELLULAR LOCATION.
  8. "Retinoic acid receptors are required for skeletal growth, matrix homeostasis and growth plate function in postnatal mouse."
    Williams J.A., Kondo N., Okabe T., Takeshita N., Pilchak D.M., Koyama E., Ochiai T., Jensen D., Chu M.L., Kane M.A., Napoli J.L., Enomoto-Iwamoto M., Ghyselinck N., Chambon P., Pacifici M., Iwamoto M.
    Dev. Biol. 328:315-327(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.
  9. "Analysis of Cyp26b1/Rarg compound-null mice reveals two genetically separable effects of retinoic acid on limb outgrowth."
    Pennimpede T., Cameron D.A., MacLean G.A., Petkovich M.
    Dev. Biol. 339:179-186(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, POSSIBLE FUNCTION, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiRARG_MOUSE
AccessioniPrimary (citable) accession number: P18911
Secondary accession number(s): P20787
, Q3UG86, Q62149, Q91VK5, Q91YX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: February 5, 2008
Last modified: October 29, 2014
This is version 154 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3