ID HBS1L_HUMAN Reviewed; 684 AA. AC Q9Y450; B7Z365; Q4VX89; Q4VX90; Q5T7G3; Q8NDW9; Q9UPW3; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 28-JAN-2026, entry version 196. DE RecName: Full=HBS1-like protein {ECO:0000305}; DE EC=3.6.5.- {ECO:0000250|UniProtKB:P32769}; DE AltName: Full=ERFS; GN Name=HBS1L {ECO:0000303|PubMed:28204585, ECO:0000312|HGNC:HGNC:4834}; GN Synonyms=HBS1 {ECO:0000303|PubMed:9872408}, KIAA1038 GN {ECO:0000303|PubMed:10470851}; 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] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Pancreatic cancer; 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 [MRNA] (ISOFORMS 1 AND 2). RA Close J.P., Game L.G., Clark B., Thein S.L.; RT "An integrated physical and transcript map of human 6q23 encompassing a RT quantitative trait loci for foetal haemaglobin expression."; RL Thesis (2002), University of Oxford, United Kingdom. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Hippocampus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix, and Placenta; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 189-684 (ISOFORMS 1/3). RC TISSUE=Brain; RX PubMed=10470851; DOI=10.1093/dnares/6.3.197; RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:197-205(1999). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246 (ISOFORM 2), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND SER-127, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=21448132; DOI=10.1038/emboj.2011.93; RA Pisareva V.P., Skabkin M.A., Hellen C.U., Pestova T.V., Pisarev A.V.; RT "Dissociation by Pelota, Hbs1 and ABCE1 of mammalian vacant 80S ribosomes RT and stalled elongation complexes."; RL EMBO J. 30:1804-1817(2011). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP VARIANT 615-ARG--GLU-684 DEL. RX PubMed=24288412; DOI=10.1182/blood-2013-09-528315; RA Sankaran V.G., Joshi M., Agrawal A., Schmitz-Abe K., Towne M.C., RA Marinakis N., Markianos K., Berry G.T., Agrawal P.B.; RT "Rare complete loss of function provides insight into a pleiotropic genome- RT wide association study locus."; RL Blood 122:3845-3847(2013). RN [15] RP FUNCTION. RX PubMed=23667253; DOI=10.1074/jbc.m112.448977; RA Saito S., Hosoda N., Hoshino S.; RT "The Hbs1-Dom34 protein complex functions in non-stop mRNA decay in RT mammalian cells."; RL J. Biol. Chem. 288:17832-17843(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-67; SER-127; SER-154 RP AND THR-231, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP FUNCTION (ISOFORM 2), ASSOCIATION WITH THE SKI COMPLEX, ASSOCIATION WITH RP THE EXOSOME COMPLEX AND SKI COMPLEX (ISOFORM 2), INTERACTION WITH SKIC2 AND RP EXOSC3 (ISOFORM 2), AND SUBCELLULAR LOCATION (ISOFORM 2). RX PubMed=28204585; DOI=10.1093/nar/gkw862; RA Kalisiak K., Kulinski T.M., Tomecki R., Cysewski D., Pietras Z., RA Chlebowski A., Kowalska K., Dziembowski A.; RT "A short splicing isoform of HBS1L links the cytoplasmic exosome and SKI RT complexes in humans."; RL Nucleic Acids Res. 45:2068-2080(2017). RN [18] RP FUNCTION. RX PubMed=32006463; DOI=10.1016/j.molcel.2020.01.011; RA Zinoviev A., Ayupov R.K., Abaeva I.S., Hellen C.U.T., Pestova T.V.; RT "Extraction of mRNA from stalled ribosomes by the Ski complex."; RL Mol. Cell 77:1340-1349(2020). RN [19] RP VARIANT 615-ARG--GLU-684 DEL. RX PubMed=30707697; DOI=10.1371/journal.pgen.1007917; RA O'Connell A.E., Gerashchenko M.V., O'Donohue M.F., Rosen S.M., RA Huntzinger E., Gleeson D., Galli A., Ryder E., Cao S., Murphy Q., RA Kazerounian S., Morton S.U., Schmitz-Abe K., Gladyshev V.N., Gleizes P.E., RA Seraphin B., Agrawal P.B.; RT "Mammalian Hbs1L deficiency causes congenital anomalies and developmental RT delay associated with Pelota depletion and 80S monosome accumulation."; RL PLoS Genet. 15:e1007917-e1007917(2019). RN [20] {ECO:0007744|PDB:5LZW, ECO:0007744|PDB:5LZX, ECO:0007744|PDB:5LZY, ECO:0007744|PDB:5LZZ} RP STRUCTURE BY ELECTRON MICROSCOPY (3.47 ANGSTROMS) IN COMPLEX WITH CTP; PELO RP AND STALLED RIBOSOME, FUNCTION, AND IDENTIFICATION IN THE PELOTA-HBS1L RP COMPLEX. RX PubMed=27863242; DOI=10.1016/j.cell.2016.10.046; RA Shao S., Murray J., Brown A., Taunton J., Ramakrishnan V., Hegde R.S.; RT "Decoding mammalian ribosome-mRNA states by translational GTPase RT complexes."; RL Cell 167:1229-1240(2016). CC -!- FUNCTION: GTPase component of the Pelota-HBS1L complex, a complex that CC recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway CC (PubMed:21448132, PubMed:23667253, PubMed:27863242). The Pelota-HBS1L CC complex recognizes ribosomes stalled at the 3' end of an mRNA and CC engages stalled ribosomes by destabilizing mRNA in the mRNA channel CC (PubMed:27863242). Following mRNA extraction from stalled ribosomes by CC the SKI complex, the Pelota-HBS1L complex promotes recruitment of CC ABCE1, which drives the disassembly of stalled ribosomes, followed by CC degradation of damaged mRNAs as part of the NGD pathway CC (PubMed:21448132, PubMed:32006463). {ECO:0000269|PubMed:21448132, CC ECO:0000269|PubMed:23667253, ECO:0000269|PubMed:27863242, CC ECO:0000269|PubMed:32006463}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000250|UniProtKB:P32769}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P32769}; CC -!- SUBUNIT: Component of the Pelota-HBS1L complex, also named Dom34-Hbs1 CC complex, composed of PELO and HBS1L (PubMed:27863242). Interacts with CC the SKI complex (PubMed:23667253, PubMed:28204585). CC {ECO:0000269|PubMed:23667253, ECO:0000269|PubMed:27863242, CC ECO:0000269|PubMed:28204585}. CC -!- SUBUNIT: [Isoform 2]: Associates with SKI complex; the interaction with CC SKIC2 is direct (PubMed:28204585). Associates with the exosome complex; CC the interaction with EXOSC3 is direct (PubMed:28204585). CC {ECO:0000269|PubMed:28204585}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21448132}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm CC {ECO:0000269|PubMed:28204585}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=HBS1LV1 {ECO:0000303|PubMed:28204585}; CC IsoId=Q9Y450-1; Sequence=Displayed; CC Name=2; Synonyms=HBS1LV3 {ECO:0000303|PubMed:28204585}; CC IsoId=Q9Y450-2; Sequence=VSP_013624; CC Name=3; CC IsoId=Q9Y450-4; Sequence=VSP_041068; CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, liver, muscle, CC kidney and pancreas. {ECO:0000269|PubMed:9872408}. CC -!- DISEASE: Note=Defects in HBS1L have been found in one patient with a CC developmental disorder characterized by growth restriction, facial CC dysmorphism and developmental delay (PubMed:24288412, PubMed:30707697). CC Additional pleiotropic features include sparse hair and eyebrows, deep- CC set eyes with blue sclerae, bifid uvula with a submucous cleft palate, CC velopharyngeal insufficiency, C2-C3 vertebral fusion, scoliosis, CC vesicoureteral reflux with a bladder diverticulum and significant CC hypotonia (PubMed:24288412, PubMed:30707697). Deficiency is caused by CC the complete absence of isoform 1 and isoform 3, while isoform 2 is CC relatively unaffected in this patient (PubMed:30707697). CC {ECO:0000269|PubMed:24288412, ECO:0000269|PubMed:30707697}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. CC {ECO:0000255|PROSITE-ProRule:PRU01059}. 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; U87791; AAD00645.1; -; mRNA. DR EMBL; AJ459826; CAD30873.1; -; mRNA. DR EMBL; AJ459827; CAD30874.1; -; mRNA. DR EMBL; AK295545; BAH12101.1; -; mRNA. DR EMBL; AL353596; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL445190; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW47982.1; -; Genomic_DNA. DR EMBL; BC001465; AAH01465.1; -; mRNA. DR EMBL; BC040849; AAH40849.1; -; mRNA. DR EMBL; AB028961; BAA82990.1; -; mRNA. DR CCDS; CCDS47479.1; -. [Q9Y450-4] DR CCDS; CCDS47480.1; -. [Q9Y450-2] DR CCDS; CCDS5173.1; -. [Q9Y450-1] DR RefSeq; NP_001138630.1; NM_001145158.2. [Q9Y450-4] DR RefSeq; NP_001138679.1; NM_001145207.2. [Q9Y450-2] DR RefSeq; NP_006611.1; NM_006620.4. [Q9Y450-1] DR PDB; 5LZW; EM; 3.53 A; jj=1-684. DR PDB; 5LZX; EM; 3.67 A; jj=1-684. DR PDB; 5LZY; EM; 3.99 A; jj=1-684. DR PDB; 5LZZ; EM; 3.47 A; jj=1-684. DR PDB; 9G8M; EM; 3.30 A; E=123-234. DR PDB; 9G8N; EM; 3.70 A; E=123-234. DR PDB; 9G8O; EM; 3.40 A; E=123-234. DR PDB; 9G8P; EM; 7.00 A; E=123-234. DR PDB; 9G8R; EM; 3.40 A; E=123-234. DR PDBsum; 5LZW; -. DR PDBsum; 5LZX; -. DR PDBsum; 5LZY; -. DR PDBsum; 5LZZ; -. DR PDBsum; 9G8M; -. DR PDBsum; 9G8N; -. DR PDBsum; 9G8O; -. DR PDBsum; 9G8P; -. DR PDBsum; 9G8R; -. DR AlphaFoldDB; Q9Y450; -. DR EMDB; EMD-4134; -. DR EMDB; EMD-4135; -. DR EMDB; EMD-4136; -. DR EMDB; EMD-4137; -. DR EMDB; EMD-51132; -. DR EMDB; EMD-51133; -. DR EMDB; EMD-51134; -. DR EMDB; EMD-51135; -. DR EMDB; EMD-51137; -. DR SMR; Q9Y450; -. DR BioGRID; 115986; 132. DR ComplexPortal; CPX-26579; Pelota-HBS1L ribosome dissociation complex. DR FunCoup; Q9Y450; 1710. DR MINT; Q9Y450; -. DR STRING; 9606.ENSP00000356811; -. DR GlyCosmos; Q9Y450; 1 site, 1 glycan. DR GlyGen; Q9Y450; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q9Y450; -. DR MetOSite; Q9Y450; -. DR PhosphoSitePlus; Q9Y450; -. DR SwissPalm; Q9Y450; -. DR BioMuta; HBS1L; -. DR DMDM; 68566500; -. DR jPOST; Q9Y450; -. DR MassIVE; Q9Y450; -. DR PaxDb; 9606-ENSP00000356811; -. DR PeptideAtlas; Q9Y450; -. DR ProteomicsDB; 86102; -. [Q9Y450-1] DR ProteomicsDB; 86103; -. [Q9Y450-2] DR ProteomicsDB; 86104; -. [Q9Y450-4] DR Pumba; Q9Y450; -. DR Antibodypedia; 32972; 391 antibodies from 26 providers. DR DNASU; 10767; -. DR Ensembl; ENST00000367822.9; ENSP00000356796.5; ENSG00000112339.16. [Q9Y450-2] DR Ensembl; ENST00000367826.6; ENSP00000356800.2; ENSG00000112339.16. [Q9Y450-4] DR Ensembl; ENST00000367837.10; ENSP00000356811.5; ENSG00000112339.16. [Q9Y450-1] DR GeneID; 10767; -. DR KEGG; hsa:10767; -. DR MANE-Select; ENST00000367837.10; ENSP00000356811.5; NM_006620.4; NP_006611.1. DR UCSC; uc003qez.4; human. [Q9Y450-1] DR AGR; HGNC:4834; -. DR ClinPGx; PA29209; -. DR CTD; 10767; -. DR DisGeNET; 10767; -. DR GeneCards; HBS1L; -. DR HGNC; HGNC:4834; HBS1L. DR HPA; ENSG00000112339; Low tissue specificity. DR MIM; 612450; gene. DR OpenTargets; ENSG00000112339; -. DR VEuPathDB; HostDB:ENSG00000112339; -. DR eggNOG; KOG0458; Eukaryota. DR GeneTree; ENSGT00940000156274; -. DR HOGENOM; CLU_432731_0_0_1; -. DR InParanoid; Q9Y450; -. DR OMA; VVQITCH; -. DR OrthoDB; 342024at2759; -. DR PAN-GO; Q9Y450; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q9Y450; -. DR PathwayCommons; Q9Y450; -. DR Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease. DR SignaLink; Q9Y450; -. DR Agora; ENSG00000112339; -. DR BioGRID-ORCS; 10767; 108 hits in 1160 CRISPR screens. DR ChiTaRS; HBS1L; human. DR GenomeRNAi; 10767; -. DR Pharos; Q9Y450; Tbio. DR PRO; PR:Q9Y450; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9Y450; protein. DR Bgee; ENSG00000112339; Expressed in calcaneal tendon and 204 other cell types or tissues. DR ExpressionAtlas; Q9Y450; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0022626; C:cytosolic ribosome; IDA:UniProt. DR GO; GO:1990533; C:Dom34-Hbs1 complex; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; TAS:ProtInc. DR GO; GO:0003924; F:GTPase activity; ISS:UniProt. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IDA:UniProtKB. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB. DR GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR CDD; cd01883; EF1_alpha; 1. DR CDD; cd16267; HBS1-like_II; 1. DR CDD; cd04093; HBS1_C_III; 1. DR FunFam; 1.10.8.10:FF:000039; HBS1-like translational GTPase; 1. DR FunFam; 2.40.30.10:FF:000035; HBS1-like translational GTPase; 1. DR FunFam; 2.40.30.10:FF:000020; Translation elongation factor EF-1; 1. DR FunFam; 3.40.50.300:FF:000204; Translation elongation factor Tu; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. DR InterPro; IPR004161; EFTu-like_2. DR InterPro; IPR054696; GTP-eEF1A_C. 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; IPR050100; TRAFAC_GTPase_members. DR InterPro; IPR009000; Transl_B-barrel_sf. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1. DR Pfam; PF22594; GTP-eEF1A_C; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF08938; HBS1_N; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1. DR SUPFAM; SSF109732; HBS1-like domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Elongation factor; GTP-binding; Hydrolase; Nucleotide-binding; KW Phosphoprotein; Protein biosynthesis; Proteomics identification; KW Reference proteome; Translation regulation. FT CHAIN 1..684 FT /note="HBS1-like protein" FT /id="PRO_0000091491" FT DOMAIN 258..482 FT /note="tr-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 170..241 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 267..274 FT /note="G1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 323..327 FT /note="G2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 344..347 FT /note="G3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 406..409 FT /note="G4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 445..447 FT /note="G5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT COMPBIAS 212..232 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 267..274 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:27863242, FT ECO:0007744|PDB:5LZW" FT BINDING 406..409 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:27863242, FT ECO:0007744|PDB:5LZW" FT BINDING 445..447 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:27863242, FT ECO:0007744|PDB:5LZW" FT MOD_RES 49 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 67 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 117 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 127 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 152 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q69ZS7" FT MOD_RES 154 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 231 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 622 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q69ZS7" FT VAR_SEQ 37..78 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041068" FT VAR_SEQ 145..684 FT /note="KPVDSQTSRSESEIVPKVAKMTVSGKKQTMGFEVPGVSSEENGHSFHTPQKG FT PPIEDAIASSDVLETASKSANPPHTIQASEEQSSTPAPVKKSGKLRQQIDVKAELEKRQ FT GGKQLLNLVVIGHVDAGKSTLMGHMLYLLGNINKRTMHKYEQESKKAGKASFAYAWVLD FT ETGEERERGVTMDVGMTKFETTTKVITLMDAPGHKDFIPNMITGAAQADVAVLVVDASR FT GEFEAGFETGGQTREHGLLVRSLGVTQLAVAVNKMDQVNWQQERFQEITGKLGHFLKQA FT GFKESDVGFIPTSGLSGENLITRSQSSELTKWYKGLCLLEQIDSFKPPQRSIDKPFRLC FT VSDVFKDQGSGFCITGKIEAGYIQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHV FT SLTLVGMDIIKINVGCIFCGPKVPIKACTRFRARILIFNIEIPITKGFPVLLHYQTVSE FT PAVIKRLISVLNKSTGEVTKKKPKFLTKGQNALVELQTQRPIALELYKDFKELGRFMLR FT YGGSTIAAGVVTEIKE -> VLFSSSEVSADNVQSSYPQSANHLDYSSKPFDFASSVGK FT YGLSHNSSVPTHCLLHRKKKLDTRKSEKKLESCKLTKELSLANLIHDMSRDSCESQPSV FT RLSSTDSLESLLSKNLDADLLRPHASECISKDDSAFKEIPDLKTIIIKGTTPNNSLYIQ FT NNSLSDFQNIPVQDSLGSSNNPLYLTSSLENMTVDNLNASKETEVGNVSLVEQSAKNHT FT FKNDNLQFSQCESPSLTELFQEHKENNISQCFTLSDLCNQSSASFTDLSLGSFPLSQLA FT NRCQSSPGISELTGSLSSLAFHKASPTRDLENLSLSELIAETIDVDNSQIKKESFEVSL FT SEVRSPGIDSNIDLSVLIKNPDFVPKPVVDPSIAPSSRTKVLSSKLGKNSNFAKDNKKN FT NKGSLTRKPPFSLSWTKALAARPSAFASTLCLRYPLKSCKRRTLDLYKTFLYSRQVQDV FT KDKEISPLVAITPFDFKSASPDDIVKANQKKAFTRE (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_013624" FT VARIANT 440 FT /note="G -> S (in dbSNP:rs4435957)" FT /id="VAR_048963" FT VARIANT 615..684 FT /note="Missing (found in a patient with developmental FT disorder; uncertain significance)" FT /evidence="ECO:0000269|PubMed:24288412, FT ECO:0000269|PubMed:30707697" FT /id="VAR_087990" FT HELIX 155..164 FT /evidence="ECO:0007829|PDB:9G8R" FT REGION Q9Y450-2:546..572 FT /note="Interaction with the exosome complex" FT /evidence="ECO:0000269|PubMed:28204585" FT MOD_RES Q9Y450-2:246 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" SQ SEQUENCE 684 AA; 75473 MW; D457ACA3941C4B4B CRC64; MARHRNVRGY NYDEDFEDDD LYGQSVEDDY CISPSTAAQF IYSRRDKPSV EPVEEYDYED LKESSNSVSN HQLSGFDQAR LYSCLDHMRE VLGDAVPDEI LIEAVLKNKF DVQKALSGVL EQDRVQSLKD KNEATVSTGK IAKGKPVDSQ TSRSESEIVP KVAKMTVSGK KQTMGFEVPG VSSEENGHSF HTPQKGPPIE DAIASSDVLE TASKSANPPH TIQASEEQSS TPAPVKKSGK LRQQIDVKAE LEKRQGGKQL LNLVVIGHVD AGKSTLMGHM LYLLGNINKR TMHKYEQESK KAGKASFAYA WVLDETGEER ERGVTMDVGM TKFETTTKVI TLMDAPGHKD FIPNMITGAA QADVAVLVVD ASRGEFEAGF ETGGQTREHG LLVRSLGVTQ LAVAVNKMDQ VNWQQERFQE ITGKLGHFLK QAGFKESDVG FIPTSGLSGE NLITRSQSSE LTKWYKGLCL LEQIDSFKPP QRSIDKPFRL CVSDVFKDQG SGFCITGKIE AGYIQTGDRL LAMPPNETCT VKGITLHDEP VDWAAAGDHV SLTLVGMDII KINVGCIFCG PKVPIKACTR FRARILIFNI EIPITKGFPV LLHYQTVSEP AVIKRLISVL NKSTGEVTKK KPKFLTKGQN ALVELQTQRP IALELYKDFK ELGRFMLRYG GSTIAAGVVT EIKE //