HBS1L_HUMAN
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 03-AUG-2022, entry version 179.
DE RecName: Full=HBS1-like protein;
DE AltName: Full=ERFS;
GN Name=HBS1L; Synonyms=HBS1, KIAA1038;
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.
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 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 [15]
RP FUNCTION (ISOFORM 2), ASSOCIATION WITH THE SKI COMPLEX, ASSOCIATION WITH
RP THE EXOSOME COMPLEX AND SKI COMPLEX (ISOFORM 2), INTERACTION WITH SKIV2L
RP AND 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).
CC -!- FUNCTION: Cotranslational quality control factor involved in the No-Go
CC Decay (NGD) pathway (PubMed:21448132). In the presence of ABCE1 and
CC PELO, is required for 48S complex formation from 80S ribosomes and
CC dissociation of vacant 80S ribosomes (PubMed:21448132). Together with
CC PELO and in presence of ABCE1, recognizes stalled ribosomes and
CC promotes dissociation of elongation complexes assembled on non-stop
CC mRNAs; this triggers endonucleolytic cleavage of the mRNA, a mechanism
CC to release non-functional ribosomes and to degrade damaged mRNAs as
CC part of the No-Go Decay (NGD) pathway (PubMed:21448132).
CC {ECO:0000269|PubMed:21448132}.
CC -!- FUNCTION: [Isoform 2]: Facilitates the association of the exosome
CC complex with the SKI complex. {ECO:0000269|PubMed:28204585}.
CC -!- SUBUNIT: Interacts with the SKI complex. {ECO:0000269|PubMed:28204585}.
CC -!- SUBUNIT: [Isoform 2]: Associates with SKI complex; the interaction with
CC SKIV2L is direct (PubMed:28204585). Associates with the exosome
CC complex; 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: [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 -!- 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 SMR; Q9Y450; -.
DR BioGRID; 115986; 101.
DR IntAct; Q9Y450; 39.
DR MINT; Q9Y450; -.
DR STRING; 9606.ENSP00000356811; -.
DR GlyGen; Q9Y450; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y450; -.
DR MetOSite; Q9Y450; -.
DR PhosphoSitePlus; Q9Y450; -.
DR BioMuta; HBS1L; -.
DR DMDM; 68566500; -.
DR EPD; Q9Y450; -.
DR jPOST; Q9Y450; -.
DR MassIVE; Q9Y450; -.
DR MaxQB; Q9Y450; -.
DR PaxDb; Q9Y450; -.
DR PeptideAtlas; Q9Y450; -.
DR PRIDE; Q9Y450; -.
DR ProteomicsDB; 86102; -. [Q9Y450-1]
DR ProteomicsDB; 86103; -. [Q9Y450-2]
DR ProteomicsDB; 86104; -. [Q9Y450-4]
DR Antibodypedia; 32972; 383 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 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; SVEDEHC; -.
DR OrthoDB; 397175at2759; -.
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; 104 hits in 1082 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 203 other tissues.
DR ExpressionAtlas; Q9Y450; baseline and differential.
DR Genevisible; Q9Y450; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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; IBA:GO_Central.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
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 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; 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; Cytoplasm;
KW Elongation factor; GTP-binding; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; 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 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:0000250"
FT BINDING 344..348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 406..409
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
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 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
