HBS1L_MOUSE
ID HBS1L_MOUSE Reviewed; 682 AA.
AC Q69ZS7; Q91Z32; Q9CVT2; Q9CZ95; Q9WTY5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=HBS1-like protein;
GN Name=Hbs1l; Synonyms=Hbs1, Kiaa1038;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=NIH Swiss; TISSUE=Embryo;
RX PubMed=9872408; DOI=10.1016/s0014-5793(98)01492-6;
RA Wallrapp C., Verrier S.-B., Zhouravleva G., Philippe H., Philippe M.,
RA Gress T.M., Jean-Jean O.;
RT "The product of the mammalian orthologue of the Saccharomyces cerevisiae
RT HBS1 gene is phylogenetically related to eukaryotic release factor 3 (eRF3)
RT but does not carry eRF3-like activity.";
RL FEBS Lett. 440:387-392(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-150, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-620, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP STRUCTURE BY NMR OF 51-120.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of HBS1-like domain in hypothetical protein BAB28515.";
RL Submitted (AUG-2004) to the PDB data bank.
CC -!- FUNCTION: Cotranslational quality control factor involved in the No-Go
CC Decay (NGD) pathway. In the presence of ABCE1 and PELO, is required for
CC 48S complex formation from 80S ribosomes and dissociation of vacant 80S
CC ribosomes. Together with PELO and in presence of ABCE1, recognizes
CC stalled ribosomes and promotes dissociation of elongation complexes
CC assembled on non-stop mRNAs; this triggers endonucleolytic cleavage of
CC the mRNA, a mechanism to release non-functional ribosomes and to
CC degrade damaged mRNAs as part of the No-Go Decay (NGD) pathway.
CC {ECO:0000250|UniProtKB:Q9Y450}.
CC -!- SUBUNIT: Interacts with the SKI complex.
CC {ECO:0000250|UniProtKB:Q9Y450}.
CC -!- INTERACTION:
CC Q69ZS7; Q80X73: Pelo; NbExp=2; IntAct=EBI-16114976, EBI-16114899;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q69ZS7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69ZS7-2; Sequence=VSP_013626;
CC Name=3;
CC IsoId=Q69ZS7-3; Sequence=VSP_013627, VSP_013628;
CC -!- TISSUE SPECIFICITY: Detected in embryos. {ECO:0000269|PubMed:9872408}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32369.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF087672; AAD23351.1; -; mRNA.
DR EMBL; AK173091; BAD32369.1; ALT_INIT; mRNA.
DR EMBL; AK006626; BAB24679.1; -; mRNA.
DR EMBL; AK012856; BAB28515.1; -; mRNA.
DR EMBL; BC010251; AAH10251.1; -; mRNA.
DR CCDS; CCDS35862.1; -. [Q69ZS7-1]
DR RefSeq; NP_062676.2; NM_019702.2. [Q69ZS7-1]
DR PDB; 1UFZ; NMR; -; A=51-120.
DR PDBsum; 1UFZ; -.
DR AlphaFoldDB; Q69ZS7; -.
DR SMR; Q69ZS7; -.
DR BioGRID; 207968; 5.
DR DIP; DIP-61684N; -.
DR IntAct; Q69ZS7; 2.
DR MINT; Q69ZS7; -.
DR STRING; 10090.ENSMUSP00000020153; -.
DR iPTMnet; Q69ZS7; -.
DR PhosphoSitePlus; Q69ZS7; -.
DR EPD; Q69ZS7; -.
DR jPOST; Q69ZS7; -.
DR MaxQB; Q69ZS7; -.
DR PaxDb; Q69ZS7; -.
DR PeptideAtlas; Q69ZS7; -.
DR PRIDE; Q69ZS7; -.
DR ProteomicsDB; 270946; -. [Q69ZS7-1]
DR ProteomicsDB; 270947; -. [Q69ZS7-2]
DR ProteomicsDB; 270948; -. [Q69ZS7-3]
DR Antibodypedia; 32972; 383 antibodies from 27 providers.
DR Ensembl; ENSMUST00000219915; ENSMUSP00000151689; ENSMUSG00000019977. [Q69ZS7-1]
DR GeneID; 56422; -.
DR KEGG; mmu:56422; -.
DR UCSC; uc007eom.1; mouse. [Q69ZS7-3]
DR UCSC; uc007eoo.1; mouse. [Q69ZS7-1]
DR CTD; 10767; -.
DR MGI; MGI:1891704; Hbs1l.
DR VEuPathDB; HostDB:ENSMUSG00000019977; -.
DR eggNOG; KOG0458; Eukaryota.
DR GeneTree; ENSGT00940000156274; -.
DR HOGENOM; CLU_007265_3_6_1; -.
DR InParanoid; Q69ZS7; -.
DR OMA; SVEDEHC; -.
DR OrthoDB; 1150082at2759; -.
DR PhylomeDB; Q69ZS7; -.
DR TreeFam; TF105833; -.
DR Reactome; R-MMU-429958; mRNA decay by 3' to 5' exoribonuclease.
DR BioGRID-ORCS; 56422; 19 hits in 71 CRISPR screens.
DR ChiTaRS; Hbs1l; mouse.
DR EvolutionaryTrace; Q69ZS7; -.
DR PRO; PR:Q69ZS7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q69ZS7; protein.
DR Bgee; ENSMUSG00000019977; Expressed in spermatid and 262 other tissues.
DR ExpressionAtlas; Q69ZS7; baseline and differential.
DR Genevisible; Q69ZS7; MM.
DR GO; GO:0005525; F:GTP binding; ISS:MGI.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR015033; HBS1-like_N.
DR InterPro; IPR037189; HBS1-like_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR Pfam; PF08938; HBS1_N; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF109732; SSF109732; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Elongation factor;
KW GTP-binding; Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Translation regulation.
FT CHAIN 1..682
FT /note="HBS1-like protein"
FT /id="PRO_0000091492"
FT DOMAIN 256..480
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 128..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..272
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 321..325
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 342..345
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 404..407
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 443..445
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 265..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 342..346
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 404..407
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y450"
FT MOD_RES 620
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9872408"
FT /id="VSP_013626"
FT VAR_SEQ 141..167
FT /note="KSVISRSSQSESEIVPKVAKMTVSGKK -> VLFSSFGVSPQNVHHSYLQSE
FT NHLDSS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013627"
FT VAR_SEQ 168..682
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_013628"
FT CONFLICT 201
FT /note="A -> R (in Ref. 1; AAD23351)"
FT /evidence="ECO:0000305"
FT CONFLICT 251..252
FT /note="KR -> NAV (in Ref. 1; AAD23351)"
FT /evidence="ECO:0000305"
FT CONFLICT 568
FT /note="G -> A (in Ref. 3; AAH10251)"
FT /evidence="ECO:0000305"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:1UFZ"
FT HELIX 63..68
FT /evidence="ECO:0007829|PDB:1UFZ"
FT HELIX 71..87
FT /evidence="ECO:0007829|PDB:1UFZ"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:1UFZ"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:1UFZ"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:1UFZ"
FT CONFLICT Q69ZS7-3:146
FT /note="F -> L (in Ref. 3; BAB24679)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 682 AA; 75100 MW; 53ADD45EC0872968 CRC64;
MARHRNVRGY NYDEDFEDDD LYGQSVEDDY CISPSTAAQF IYSRRDNPEE EYGYEDLRES
SNSLLNHQLS EIDQARLYSC LDHMREVLGD AVPDDILTEA ILKHKFDVQK ALSVVLEQDG
VQPWKEKSER AVCAGQPSKG KSVISRSSQS ESEIVPKVAK MTVSGKKQTM GFEVPGLTSE
ENGLSVRAPH KGPPGDDVSV ASPNIPETGT PKSALPPPSL QTSEELGSTP TPVRKSGKLR
QQIDVKAELE KRQGGKQLLN LVVIGHVDAG KSTLMGHMLY LLGNVNKRTM HKYEQESKKA
GKASFAYAWV LDETGEERER GVTMDVGMTK FETTTKVITL MDAPGHKDFI PNMITGAAQA
DVAVLVVDAS RGEFEAGFET GGQTREHGLL VRSLGVTQLA VAVNKMDQVN WQQERFQEIT
GKLGHFLKQA GFKESDVAFI PTSGLSGENL TARSQSSDLT TWYKGMCLLE QIDSFKPPQR
SIDKPFRLCV SDVFKDQGSG FCVTGKIEAG YIQTGDRLLA MPPNETCTAK GITLHDEPVD
WAAAGDHVNL TLVGMDIIKI NVGCIFCGPK EPIKACTRFR ARILVFNIEV PITKGFPVLL
HYQTVSEPAV IKRLISVLNK STGEVTKKKP KLLTKGQNAL VELQTQRPVA LELYKDFKEL
GRFMLRYGGS TVAAGVVTEI KE
