Full text data of HBS1L
HBS1L
(HBS1, KIAA1038)
[Confidence: low (only semi-automatic identification from reviews)]
HBS1-like protein (ERFS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
HBS1-like protein (ERFS)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y450
ID HBS1L_HUMAN Reviewed; 684 AA.
AC Q9Y450; B7Z365; Q4VX89; Q4VX90; Q5T7G3; Q8NDW9; Q9UPW3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 114.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT cerevisiae HBS1 gene is phylogenetically related to eukaryotic release
RT factor 3 (eRF3) 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
RT a 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large 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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y450-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y450-2; Sequence=VSP_013624;
CC Note=Contains a phosphoserine at position 246;
CC Name=3;
CC IsoId=Q9Y450-4; Sequence=VSP_041068;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, liver,
CC muscle, kidney and pancreas.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
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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; CAI17912.1; -; Genomic_DNA.
DR EMBL; AL445190; CAI17912.1; JOINED; Genomic_DNA.
DR EMBL; AL353596; CAI17913.1; -; Genomic_DNA.
DR EMBL; AL445190; CAI17913.1; JOINED; Genomic_DNA.
DR EMBL; AL353596; CAI17914.1; -; Genomic_DNA.
DR EMBL; AL445190; CAI95161.1; -; Genomic_DNA.
DR EMBL; AL353596; CAI95161.1; JOINED; Genomic_DNA.
DR EMBL; AL445190; CAI95162.1; -; Genomic_DNA.
DR EMBL; AL353596; CAI95162.1; JOINED; 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 RefSeq; NP_001138630.1; NM_001145158.1.
DR RefSeq; NP_001138679.1; NM_001145207.1.
DR RefSeq; NP_006611.1; NM_006620.3.
DR UniGene; Hs.378532; -.
DR ProteinModelPortal; Q9Y450; -.
DR SMR; Q9Y450; 60-123, 258-683.
DR IntAct; Q9Y450; 8.
DR MINT; MINT-6784072; -.
DR STRING; 9606.ENSP00000356811; -.
DR PhosphoSite; Q9Y450; -.
DR DMDM; 68566500; -.
DR PaxDb; Q9Y450; -.
DR PeptideAtlas; Q9Y450; -.
DR PRIDE; Q9Y450; -.
DR DNASU; 10767; -.
DR Ensembl; ENST00000367822; ENSP00000356796; ENSG00000112339.
DR Ensembl; ENST00000367826; ENSP00000356800; ENSG00000112339.
DR Ensembl; ENST00000367837; ENSP00000356811; ENSG00000112339.
DR GeneID; 10767; -.
DR KEGG; hsa:10767; -.
DR UCSC; uc003qey.2; human.
DR CTD; 10767; -.
DR GeneCards; GC06M135281; -.
DR HGNC; HGNC:4834; HBS1L.
DR HPA; HPA029728; -.
DR HPA; HPA029729; -.
DR MIM; 612450; gene.
DR neXtProt; NX_Q9Y450; -.
DR PharmGKB; PA29209; -.
DR eggNOG; COG5256; -.
DR HOVERGEN; HBG000179; -.
DR InParanoid; Q9Y450; -.
DR KO; K14416; -.
DR OMA; SFKPPQR; -.
DR OrthoDB; EOG7JMGCV; -.
DR PhylomeDB; Q9Y450; -.
DR ChiTaRS; HBS1L; human.
DR GenomeRNAi; 10767; -.
DR NextBio; 40885; -.
DR PMAP-CutDB; Q9Y450; -.
DR PRO; PR:Q9Y450; -.
DR ArrayExpress; Q9Y450; -.
DR Bgee; Q9Y450; -.
DR CleanEx; HS_HBS1L; -.
DR Genevestigator; Q9Y450; -.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR015033; HBS1-like_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
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 ProDom; PD278081; DUF1916; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00301; EFACTOR_GTP; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Elongation factor;
KW GTP-binding; Nucleotide-binding; Phosphoprotein; Polymorphism;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1 684 HBS1-like protein.
FT /FTId=PRO_0000091491.
FT NP_BIND 267 274 GTP (By similarity).
FT NP_BIND 344 348 GTP (By similarity).
FT NP_BIND 406 409 GTP (By similarity).
FT MOD_RES 117 117 Phosphoserine.
FT MOD_RES 127 127 Phosphoserine.
FT VAR_SEQ 37 78 Missing (in isoform 3).
FT /FTId=VSP_041068.
FT VAR_SEQ 145 684 KPVDSQTSRSESEIVPKVAKMTVSGKKQTMGFEVPGVSSEE
FT NGHSFHTPQKGPPIEDAIASSDVLETASKSANPPHTIQASE
FT EQSSTPAPVKKSGKLRQQIDVKAELEKRQGGKQLLNLVVIG
FT HVDAGKSTLMGHMLYLLGNINKRTMHKYEQESKKAGKASFA
FT YAWVLDETGEERERGVTMDVGMTKFETTTKVITLMDAPGHK
FT DFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHG
FT LLVRSLGVTQLAVAVNKMDQVNWQQERFQEITGKLGHFLKQ
FT AGFKESDVGFIPTSGLSGENLITRSQSSELTKWYKGLCLLE
FT QIDSFKPPQRSIDKPFRLCVSDVFKDQGSGFCITGKIEAGY
FT IQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTL
FT VGMDIIKINVGCIFCGPKVPIKACTRFRARILIFNIEIPIT
FT KGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKFLT
FT KGQNALVELQTQRPIALELYKDFKELGRFMLRYGGSTIAAG
FT VVTEIKE -> VLFSSSEVSADNVQSSYPQSANHLDYSSKP
FT FDFASSVGKYGLSHNSSVPTHCLLHRKKKLDTRKSEKKLES
FT CKLTKELSLANLIHDMSRDSCESQPSVRLSSTDSLESLLSK
FT NLDADLLRPHASECISKDDSAFKEIPDLKTIIIKGTTPNNS
FT LYIQNNSLSDFQNIPVQDSLGSSNNPLYLTSSLENMTVDNL
FT NASKETEVGNVSLVEQSAKNHTFKNDNLQFSQCESPSLTEL
FT FQEHKENNISQCFTLSDLCNQSSASFTDLSLGSFPLSQLAN
FT RCQSSPGISELTGSLSSLAFHKASPTRDLENLSLSELIAET
FT IDVDNSQIKKESFEVSLSEVRSPGIDSNIDLSVLIKNPDFV
FT PKPVVDPSIAPSSRTKVLSSKLGKNSNFAKDNKKNNKGSLT
FT RKPPFSLSWTKALAARPSAFASTLCLRYPLKSCKRRTLDLY
FT KTFLYSRQVQDVKDKEISPLVAITPFDFKSASPDDIVKANQ
FT KKAFTRE (in isoform 2).
FT /FTId=VSP_013624.
FT VARIANT 440 440 G -> S (in dbSNP:rs4435957).
FT /FTId=VAR_048963.
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
//
ID HBS1L_HUMAN Reviewed; 684 AA.
AC Q9Y450; B7Z365; Q4VX89; Q4VX90; Q5T7G3; Q8NDW9; Q9UPW3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 114.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT cerevisiae HBS1 gene is phylogenetically related to eukaryotic release
RT factor 3 (eRF3) 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
RT a 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large 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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y450-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y450-2; Sequence=VSP_013624;
CC Note=Contains a phosphoserine at position 246;
CC Name=3;
CC IsoId=Q9Y450-4; Sequence=VSP_041068;
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, placenta, liver,
CC muscle, kidney and pancreas.
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC -----------------------------------------------------------------------
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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; CAI17912.1; -; Genomic_DNA.
DR EMBL; AL445190; CAI17912.1; JOINED; Genomic_DNA.
DR EMBL; AL353596; CAI17913.1; -; Genomic_DNA.
DR EMBL; AL445190; CAI17913.1; JOINED; Genomic_DNA.
DR EMBL; AL353596; CAI17914.1; -; Genomic_DNA.
DR EMBL; AL445190; CAI95161.1; -; Genomic_DNA.
DR EMBL; AL353596; CAI95161.1; JOINED; Genomic_DNA.
DR EMBL; AL445190; CAI95162.1; -; Genomic_DNA.
DR EMBL; AL353596; CAI95162.1; JOINED; 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 RefSeq; NP_001138630.1; NM_001145158.1.
DR RefSeq; NP_001138679.1; NM_001145207.1.
DR RefSeq; NP_006611.1; NM_006620.3.
DR UniGene; Hs.378532; -.
DR ProteinModelPortal; Q9Y450; -.
DR SMR; Q9Y450; 60-123, 258-683.
DR IntAct; Q9Y450; 8.
DR MINT; MINT-6784072; -.
DR STRING; 9606.ENSP00000356811; -.
DR PhosphoSite; Q9Y450; -.
DR DMDM; 68566500; -.
DR PaxDb; Q9Y450; -.
DR PeptideAtlas; Q9Y450; -.
DR PRIDE; Q9Y450; -.
DR DNASU; 10767; -.
DR Ensembl; ENST00000367822; ENSP00000356796; ENSG00000112339.
DR Ensembl; ENST00000367826; ENSP00000356800; ENSG00000112339.
DR Ensembl; ENST00000367837; ENSP00000356811; ENSG00000112339.
DR GeneID; 10767; -.
DR KEGG; hsa:10767; -.
DR UCSC; uc003qey.2; human.
DR CTD; 10767; -.
DR GeneCards; GC06M135281; -.
DR HGNC; HGNC:4834; HBS1L.
DR HPA; HPA029728; -.
DR HPA; HPA029729; -.
DR MIM; 612450; gene.
DR neXtProt; NX_Q9Y450; -.
DR PharmGKB; PA29209; -.
DR eggNOG; COG5256; -.
DR HOVERGEN; HBG000179; -.
DR InParanoid; Q9Y450; -.
DR KO; K14416; -.
DR OMA; SFKPPQR; -.
DR OrthoDB; EOG7JMGCV; -.
DR PhylomeDB; Q9Y450; -.
DR ChiTaRS; HBS1L; human.
DR GenomeRNAi; 10767; -.
DR NextBio; 40885; -.
DR PMAP-CutDB; Q9Y450; -.
DR PRO; PR:Q9Y450; -.
DR ArrayExpress; Q9Y450; -.
DR Bgee; Q9Y450; -.
DR CleanEx; HS_HBS1L; -.
DR Genevestigator; Q9Y450; -.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006184; P:GTP catabolic process; IEA:GOC.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR015033; HBS1-like_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
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 ProDom; PD278081; DUF1916; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00301; EFACTOR_GTP; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Elongation factor;
KW GTP-binding; Nucleotide-binding; Phosphoprotein; Polymorphism;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1 684 HBS1-like protein.
FT /FTId=PRO_0000091491.
FT NP_BIND 267 274 GTP (By similarity).
FT NP_BIND 344 348 GTP (By similarity).
FT NP_BIND 406 409 GTP (By similarity).
FT MOD_RES 117 117 Phosphoserine.
FT MOD_RES 127 127 Phosphoserine.
FT VAR_SEQ 37 78 Missing (in isoform 3).
FT /FTId=VSP_041068.
FT VAR_SEQ 145 684 KPVDSQTSRSESEIVPKVAKMTVSGKKQTMGFEVPGVSSEE
FT NGHSFHTPQKGPPIEDAIASSDVLETASKSANPPHTIQASE
FT EQSSTPAPVKKSGKLRQQIDVKAELEKRQGGKQLLNLVVIG
FT HVDAGKSTLMGHMLYLLGNINKRTMHKYEQESKKAGKASFA
FT YAWVLDETGEERERGVTMDVGMTKFETTTKVITLMDAPGHK
FT DFIPNMITGAAQADVAVLVVDASRGEFEAGFETGGQTREHG
FT LLVRSLGVTQLAVAVNKMDQVNWQQERFQEITGKLGHFLKQ
FT AGFKESDVGFIPTSGLSGENLITRSQSSELTKWYKGLCLLE
FT QIDSFKPPQRSIDKPFRLCVSDVFKDQGSGFCITGKIEAGY
FT IQTGDRLLAMPPNETCTVKGITLHDEPVDWAAAGDHVSLTL
FT VGMDIIKINVGCIFCGPKVPIKACTRFRARILIFNIEIPIT
FT KGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKFLT
FT KGQNALVELQTQRPIALELYKDFKELGRFMLRYGGSTIAAG
FT VVTEIKE -> VLFSSSEVSADNVQSSYPQSANHLDYSSKP
FT FDFASSVGKYGLSHNSSVPTHCLLHRKKKLDTRKSEKKLES
FT CKLTKELSLANLIHDMSRDSCESQPSVRLSSTDSLESLLSK
FT NLDADLLRPHASECISKDDSAFKEIPDLKTIIIKGTTPNNS
FT LYIQNNSLSDFQNIPVQDSLGSSNNPLYLTSSLENMTVDNL
FT NASKETEVGNVSLVEQSAKNHTFKNDNLQFSQCESPSLTEL
FT FQEHKENNISQCFTLSDLCNQSSASFTDLSLGSFPLSQLAN
FT RCQSSPGISELTGSLSSLAFHKASPTRDLENLSLSELIAET
FT IDVDNSQIKKESFEVSLSEVRSPGIDSNIDLSVLIKNPDFV
FT PKPVVDPSIAPSSRTKVLSSKLGKNSNFAKDNKKNNKGSLT
FT RKPPFSLSWTKALAARPSAFASTLCLRYPLKSCKRRTLDLY
FT KTFLYSRQVQDVKDKEISPLVAITPFDFKSASPDDIVKANQ
FT KKAFTRE (in isoform 2).
FT /FTId=VSP_013624.
FT VARIANT 440 440 G -> S (in dbSNP:rs4435957).
FT /FTId=VAR_048963.
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
//
MIM
612450
*RECORD*
*FIELD* NO
612450
*FIELD* TI
*612450 HBS1-LIKE PROTEIN; HBS1L
;;HBS1, S. CEREVISIAE, HOMOLOG OF;;
ERF3-SIMILAR PROTEIN; ERFS;;
read moreKIAA1038
*FIELD* TX
CLONING
By searching for genes in a region of chromosome 6 that shows copy
number variations associated with pancreatic cancer, Wallrapp et al.
(1998) cloned HBS1L, which they called ERFS. The deduced 684-amino acid
protein contains 4 GTP-binding motifs and has a calculated molecular
mass of about 75 kD. Wallrapp et al. (1998) also identified mouse Hbs1l,
which encodes a deduced 600-amino acid protein that has an N-terminal
truncation compared with human HBS1L. The mouse and human proteins share
89% identity. Northern blot analysis detected a 3.0-kb transcript in all
human tissues examined, with highest expression in heart and skeletal
muscle, and lowest expression in lung and kidney. Hbs1l was expressed at
all stages of mouse embryonic development examined.
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Kikuno et al. (1999) cloned HBS1L, which they designated
KIAA1038. The transcript contains repetitive elements in its 3-prime
end, and the deduced protein shares significant similarity with Ef1a
(EEF1A1; 130590) from a thermophilic archaeon. RT-PCR ELISA detected low
HBS1L expression in adult heart, brain, liver, and spinal cord, and in
several specific adult brain regions.
MAPPING
By genomic sequence analysis, Wallrapp et al. (1998) mapped the HBS1L
gene to chromosome 6q24.
MOLECULAR GENETICS
For a discussion of a possible association between variation in the
HBS1L gene and fetal hemoglobin levels, see HBFQTL2 (142470).
*FIELD* RF
1. Kikuno, R.; Nagase, T.; Ishikawa, K.; Hirosawa, M.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XIV. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 6: 197-205, 1999.
2. Wallrapp, C.; Verrier, S.-B.; Zhouravleva, G.; Philippe, H.; Philippe,
M.; Gress, T. M.; Jean-Jean, O.: The product of the mammalian orthologue
of the Saccharomyces cerevisiae HBS1 gene is phylogenetically related
to eukaryotic release factor 3 (eRF3) but does not carry eRF3-like
activity. FEBS Lett. 440: 387-392, 1998.
*FIELD* CD
Patricia A. Hartz: 12/3/2008
*FIELD* ED
ckniffin: 06/03/2009
mgross: 12/3/2008
*RECORD*
*FIELD* NO
612450
*FIELD* TI
*612450 HBS1-LIKE PROTEIN; HBS1L
;;HBS1, S. CEREVISIAE, HOMOLOG OF;;
ERF3-SIMILAR PROTEIN; ERFS;;
read moreKIAA1038
*FIELD* TX
CLONING
By searching for genes in a region of chromosome 6 that shows copy
number variations associated with pancreatic cancer, Wallrapp et al.
(1998) cloned HBS1L, which they called ERFS. The deduced 684-amino acid
protein contains 4 GTP-binding motifs and has a calculated molecular
mass of about 75 kD. Wallrapp et al. (1998) also identified mouse Hbs1l,
which encodes a deduced 600-amino acid protein that has an N-terminal
truncation compared with human HBS1L. The mouse and human proteins share
89% identity. Northern blot analysis detected a 3.0-kb transcript in all
human tissues examined, with highest expression in heart and skeletal
muscle, and lowest expression in lung and kidney. Hbs1l was expressed at
all stages of mouse embryonic development examined.
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Kikuno et al. (1999) cloned HBS1L, which they designated
KIAA1038. The transcript contains repetitive elements in its 3-prime
end, and the deduced protein shares significant similarity with Ef1a
(EEF1A1; 130590) from a thermophilic archaeon. RT-PCR ELISA detected low
HBS1L expression in adult heart, brain, liver, and spinal cord, and in
several specific adult brain regions.
MAPPING
By genomic sequence analysis, Wallrapp et al. (1998) mapped the HBS1L
gene to chromosome 6q24.
MOLECULAR GENETICS
For a discussion of a possible association between variation in the
HBS1L gene and fetal hemoglobin levels, see HBFQTL2 (142470).
*FIELD* RF
1. Kikuno, R.; Nagase, T.; Ishikawa, K.; Hirosawa, M.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XIV. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 6: 197-205, 1999.
2. Wallrapp, C.; Verrier, S.-B.; Zhouravleva, G.; Philippe, H.; Philippe,
M.; Gress, T. M.; Jean-Jean, O.: The product of the mammalian orthologue
of the Saccharomyces cerevisiae HBS1 gene is phylogenetically related
to eukaryotic release factor 3 (eRF3) but does not carry eRF3-like
activity. FEBS Lett. 440: 387-392, 1998.
*FIELD* CD
Patricia A. Hartz: 12/3/2008
*FIELD* ED
ckniffin: 06/03/2009
mgross: 12/3/2008