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 27-MAR-2024, entry version 188.
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},
GN KIAA1038 {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 + H(+) + phosphate; 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 -!- INTERACTION:
CC Q9Y450; Q9BRX2: PELO; NbExp=4; IntAct=EBI-2868258, EBI-1043580;
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}.
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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_001145158.1. [Q9Y450-4]
DR RefSeq; NP_001138679.1; NM_001145207.1. [Q9Y450-2]
DR RefSeq; NP_006611.1; NM_006620.3. [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 PDBsum; 5LZW; -.
DR PDBsum; 5LZX; -.
DR PDBsum; 5LZY; -.
DR PDBsum; 5LZZ; -.
DR AlphaFoldDB; Q9Y450; -.
DR EMDB; EMD-4135; -.
DR EMDB; EMD-4136; -.
DR EMDB; EMD-4137; -.
DR SMR; Q9Y450; -.
DR BioGRID; 115986; 118.
DR IntAct; Q9Y450; 41.
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 EPD; Q9Y450; -.
DR jPOST; Q9Y450; -.
DR MassIVE; Q9Y450; -.
DR MaxQB; 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; 434 antibodies from 27 providers.
DR DNASU; 10767; -.
DR Ensembl; ENST00000367822.9; ENSP00000356796.5; ENSG00000112339.15. [Q9Y450-2]
DR Ensembl; ENST00000367826.6; ENSP00000356800.2; ENSG00000112339.15. [Q9Y450-4]
DR Ensembl; ENST00000367837.10; ENSP00000356811.5; ENSG00000112339.15. [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 CTD; 10767; -.
DR DisGeNET; 10767; -.
DR GeneCards; HBS1L; -.
DR HGNC; HGNC:4834; HBS1L.
DR HPA; ENSG00000112339; Low tissue specificity.
DR MIM; 612450; gene.
DR neXtProt; NX_Q9Y450; -.
DR OpenTargets; ENSG00000112339; -.
DR PharmGKB; PA29209; -.
DR VEuPathDB; HostDB:ENSG00000112339; -.
DR eggNOG; KOG0458; Eukaryota.
DR GeneTree; ENSGT00940000156274; -.
DR HOGENOM; CLU_432731_0_0_1; -.
DR InParanoid; Q9Y450; -.
DR OMA; CFETEHR; -.
DR OrthoDB; 5477300at2759; -.
DR PhylomeDB; Q9Y450; -.
DR TreeFam; TF105833; -.
DR PathwayCommons; Q9Y450; -.
DR Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease.
DR SignaLink; Q9Y450; -.
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 Genevisible; Q9Y450; HS.
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: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 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; 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 PANTHER; PTHR23115:SF188; HBS1-LIKE PROTEIN; 1.
DR PANTHER; PTHR23115; TRANSLATION FACTOR; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 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; Reference proteome;
KW 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 208..237
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 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
//
