RSLBB_HUMAN
ID RSLBB_HUMAN Reviewed; 248 AA.
AC Q9BPW5; B2RC51; Q96KC5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Ras-like protein family member 11B;
DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P01116};
GN Name=RASL11B {ECO:0000312|EMBL:AAH01846.1};
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:AAX46798.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP 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).
RN [2] {ECO:0000312|EMBL:BAB55008.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Embryo {ECO:0000312|EMBL:BAB55008.1};
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3] {ECO:0000312|EMBL:EAX05441.1}
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:AAH01087.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung {ECO:0000312|EMBL:AAH25694.1}, and
RC Muscle {ECO:0000312|EMBL:AAH01087.1};
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, ECO:0000312|EMBL:DAA02135.1}
RP IDENTIFICATION.
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).
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 -!- INTERACTION:
CC Q9BPW5; Q8WXD5: GEMIN6; NbExp=3; IntAct=EBI-745409, EBI-752301;
CC Q9BPW5; Q96QZ7-3: MAGI1; NbExp=3; IntAct=EBI-745409, EBI-8769674;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in placenta
CC and primary macrophages. {ECO:0000269|PubMed:17628721}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during development of primary
CC monocytes into macrophages. {ECO:0000269|PubMed:17628721}.
CC -!- INDUCTION: By TGFB1. {ECO:0000269|PubMed:17628721}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC {ECO:0000255}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RASL11BID44265ch4q12.html";
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DR EMBL; AY839725; AAX46798.1; -; mRNA.
DR EMBL; AK027267; BAB55008.1; -; mRNA.
DR EMBL; AK314942; BAG37448.1; -; mRNA.
DR EMBL; CH471057; EAX05441.1; -; Genomic_DNA.
DR EMBL; BC001087; AAH01087.1; -; mRNA.
DR EMBL; BC001846; AAH01846.1; -; mRNA.
DR EMBL; BC025694; AAH25694.1; -; mRNA.
DR EMBL; BK001672; DAA02135.1; -; mRNA.
DR CCDS; CCDS3490.1; -.
DR RefSeq; NP_076429.1; NM_023940.2.
DR AlphaFoldDB; Q9BPW5; -.
DR SMR; Q9BPW5; -.
DR BioGRID; 122444; 21.
DR IntAct; Q9BPW5; 3.
DR STRING; 9606.ENSP00000248706; -.
DR iPTMnet; Q9BPW5; -.
DR PhosphoSitePlus; Q9BPW5; -.
DR BioMuta; RASL11B; -.
DR DMDM; 74732795; -.
DR MassIVE; Q9BPW5; -.
DR PaxDb; Q9BPW5; -.
DR PeptideAtlas; Q9BPW5; -.
DR PRIDE; Q9BPW5; -.
DR ProteomicsDB; 78580; -.
DR Antibodypedia; 23900; 97 antibodies from 25 providers.
DR DNASU; 65997; -.
DR Ensembl; ENST00000248706.5; ENSP00000248706.3; ENSG00000128045.7.
DR GeneID; 65997; -.
DR KEGG; hsa:65997; -.
DR MANE-Select; ENST00000248706.5; ENSP00000248706.3; NM_023940.3; NP_076429.1.
DR UCSC; uc003gzt.4; human.
DR CTD; 65997; -.
DR DisGeNET; 65997; -.
DR GeneCards; RASL11B; -.
DR HGNC; HGNC:23804; RASL11B.
DR HPA; ENSG00000128045; Tissue enhanced (lymphoid tissue, ovary).
DR MIM; 612404; gene.
DR neXtProt; NX_Q9BPW5; -.
DR OpenTargets; ENSG00000128045; -.
DR PharmGKB; PA134872992; -.
DR VEuPathDB; HostDB:ENSG00000128045; -.
DR eggNOG; KOG0395; Eukaryota.
DR GeneTree; ENSGT00940000158643; -.
DR HOGENOM; CLU_041217_9_7_1; -.
DR InParanoid; Q9BPW5; -.
DR OMA; KEVEPQH; -.
DR OrthoDB; 1384728at2759; -.
DR PhylomeDB; Q9BPW5; -.
DR TreeFam; TF318030; -.
DR PathwayCommons; Q9BPW5; -.
DR SignaLink; Q9BPW5; -.
DR BioGRID-ORCS; 65997; 9 hits in 1065 CRISPR screens.
DR ChiTaRS; RASL11B; human.
DR GeneWiki; RASL11B; -.
DR GenomeRNAi; 65997; -.
DR Pharos; Q9BPW5; Tbio.
DR PRO; PR:Q9BPW5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q9BPW5; protein.
DR Bgee; ENSG00000128045; Expressed in right ovary and 92 other tissues.
DR Genevisible; Q9BPW5; HS.
DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0005160; F:transforming growth factor beta receptor binding; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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; Reference proteome.
FT CHAIN 1..248
FT /note="Ras-like protein family member 11B"
FT /id="PRO_0000308365"
FT REGION 29..246
FT /note="Small GTPase-like"
FT REGION 205..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40..47
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96A58"
FT BINDING 87..94
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96A58"
FT BINDING 152..155
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96A58"
FT CONFLICT 3
FT /note="L -> H (in Ref. 2; BAB55008)"
FT /evidence="ECO:0000305"
FT CONFLICT 50
FT /note="V -> L (in Ref. 2; BAB55008)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 27508 MW; E45301814B6C2ABC CRC64;
MRLIQNMCTI AEYPAPGNAA ASDCCVGAAG RRLVKIAVVG ASGVGKTALV VRFLTKRFIG
DYERNAGNLY TRQVQIEGET LALQVQDTPG IQVHENSLSC SEQLNRCIRW ADAVVIVFSI
TDYKSYELIS QLHQHVQQLH LGTRLPVVVV ANKADLLHIK QVDPQLGLQL ASMLGCSFYE
VSVSENYNDV YSAFHVLCKE VSHKQQPSST PEKRRTSLIP RPKSPNMQDL KRRFKQALSA
KVRTVTSV
