RSLBA_HUMAN
ID RSLBA_HUMAN Reviewed; 242 AA.
AC Q6T310; B2RN97;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ras-like protein family member 11A;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
GN Name=RASL11A {ECO:0000312|HGNC:HGNC:23802};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS07577.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15033445; DOI=10.1016/j.bbrc.2004.02.091;
RA Louro R., Nakaya H.I., Paquola A.C.M., Martins E.A.L., da Silva A.M.,
RA Verjovski-Almeida S., Reis E.M.;
RT "Rasl11a, member of a novel small monomeric GTPase gene family, is
RT differentially expressed in prostate tumors.";
RL Biochem. Biophys. Res. Commun. 316:618-627(2004).
RN [2] {ECO:0000312|EMBL:AL159977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3] {ECO:0000312|EMBL:EAX08402.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAI32704.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI32704.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=17628721; DOI=10.1016/j.bbaexp.2007.05.005;
RA Stolle K., Schnoor M., Fuellen G., Spitzer M., Cullen P., Lorkowski S.;
RT "Cloning, genomic organization, and tissue-specific expression of the
RT RASL11B gene.";
RL Biochim. Biophys. Acta 1769:514-524(2007).
CC -!- FUNCTION: Regulator of rDNA transcription. Acts in cooperation UBF/UBTF
CC and positively regulates RNA polymerase I transcription (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2;
CC Evidence={ECO:0000250|UniProtKB:P01116};
CC -!- SUBUNIT: Interacts with UBF/UBTF. {ECO:0000250}.
CC -!- INTERACTION:
CC Q6T310; P42858: HTT; NbExp=3; IntAct=EBI-4401868, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}. Note=Associates
CC with rDNA transcription unit throughout the cell cycle. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Down-regulated in prostate tumors
CC compared to normal prostate tissue. High levels found in colon tumor
CC and normal colon tissue followed by small intestine, liver, jejunum,
CC ileum, bladder and aorta. Lowest levels observed in endothelial cells.
CC {ECO:0000269|PubMed:15033445, ECO:0000269|PubMed:17628721}.
CC -!- DEVELOPMENTAL STAGE: Down-regulated during development of THP-1
CC monocytes into macrophages. {ECO:0000269|PubMed:17628721}.
CC -!- INDUCTION: Down-regulated by TGFB1. {ECO:0000269|PubMed:17628721}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000255}.
CC -!- CAUTION: Although highly related to the Ras family, lacks the conserved
CC prenylation motif at the C-terminus, which serves to target Ras
CC proteins to membrane compartments. {ECO:0000305}.
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DR EMBL; AY439004; AAS07577.1; -; mRNA.
DR EMBL; AL159977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08402.1; -; Genomic_DNA.
DR EMBL; BC132703; AAI32704.1; -; mRNA.
DR EMBL; BC136761; AAI36762.1; -; mRNA.
DR CCDS; CCDS9321.1; -.
DR RefSeq; NP_001318055.1; NM_001331126.1.
DR RefSeq; NP_996563.1; NM_206827.1.
DR AlphaFoldDB; Q6T310; -.
DR SMR; Q6T310; -.
DR BioGRID; 132307; 13.
DR IntAct; Q6T310; 1.
DR STRING; 9606.ENSP00000241463; -.
DR iPTMnet; Q6T310; -.
DR PhosphoSitePlus; Q6T310; -.
DR BioMuta; RASL11A; -.
DR DMDM; 74749333; -.
DR jPOST; Q6T310; -.
DR MassIVE; Q6T310; -.
DR PaxDb; Q6T310; -.
DR PeptideAtlas; Q6T310; -.
DR PRIDE; Q6T310; -.
DR ProteomicsDB; 67364; -.
DR Antibodypedia; 62567; 28 antibodies from 11 providers.
DR DNASU; 387496; -.
DR Ensembl; ENST00000241463.5; ENSP00000241463.5; ENSG00000122035.7.
DR GeneID; 387496; -.
DR KEGG; hsa:387496; -.
DR MANE-Select; ENST00000241463.5; ENSP00000241463.5; NM_206827.2; NP_996563.1.
DR UCSC; uc001urd.1; human.
DR CTD; 387496; -.
DR DisGeNET; 387496; -.
DR GeneCards; RASL11A; -.
DR HGNC; HGNC:23802; RASL11A.
DR HPA; ENSG00000122035; Low tissue specificity.
DR MIM; 612403; gene.
DR neXtProt; NX_Q6T310; -.
DR OpenTargets; ENSG00000122035; -.
DR PharmGKB; PA134906253; -.
DR VEuPathDB; HostDB:ENSG00000122035; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000161208; -.
DR HOGENOM; CLU_041217_9_7_1; -.
DR InParanoid; Q6T310; -.
DR OMA; TMSGHCL; -.
DR OrthoDB; 1384728at2759; -.
DR PhylomeDB; Q6T310; -.
DR TreeFam; TF318030; -.
DR BRENDA; 3.6.5.2; 2681.
DR PathwayCommons; Q6T310; -.
DR SignaLink; Q6T310; -.
DR BioGRID-ORCS; 387496; 8 hits in 1071 CRISPR screens.
DR GenomeRNAi; 387496; -.
DR Pharos; Q6T310; Tdark.
DR PRO; PR:Q6T310; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q6T310; protein.
DR Bgee; ENSG00000122035; Expressed in mucosa of stomach and 101 other tissues.
DR Genevisible; Q6T310; HS.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR Pfam; PF00071; Ras; 1.
DR SMART; SM00174; RHO; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51421; RAS; 1.
PE 1: Evidence at protein level;
KW GTP-binding; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..242
FT /note="Ras-like protein family member 11A"
FT /id="PRO_0000308360"
FT REGION 17..241
FT /note="Small GTPase-like"
FT BINDING 34..41
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96A58"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96A58"
FT BINDING 147..150
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96A58"
SQ SEQUENCE 242 AA; 27006 MW; 0AC5B11854666BC1 CRC64;
MRPLSMSGHF LLAPIPESSS DYLLPKDIKL AVLGAGRVGK SAMIVRFLTK RFIGDYEPNT
GKLYSRLVYV EGDQLSLQIQ DTPGGVQIQD SLPQVVDSLS KCVQWAEGFL LVYSITDYDS
YLSIRPLYQH IRKVHPDSKA PVIIVGNKGD LLHARQVQTQ DGIQLANELG SLFLEISTSE
NYEDVCDVFQ HLCKEVSKMH GLSGERRRAS IIPRPRSPNM QDLKRRFKQA LSPKVKAPSA
LG
