BET1L_HUMAN
ID BET1L_HUMAN Reviewed; 111 AA.
AC Q9NYM9; B3KMY0;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=BET1-like protein;
DE AltName: Full=Golgi SNARE with a size of 15 kDa;
DE Short=GOS-15;
DE Short=GS15;
DE AltName: Full=Vesicle transport protein GOS15;
GN Name=BET1L {ECO:0000312|HGNC:HGNC:19348};
GN Synonyms=GS15 {ECO:0000312|HGNC:HGNC:19348};
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] {ECO:0000312|EMBL:AAF37877.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bui T.D., Hong W.;
RT "Homo sapiens Golgi SNARE GS15 sequence.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3] {ECO:0000312|EMBL:AAH08971.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin {ECO:0000312|EMBL:AAH08971.1};
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 [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-37, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Vesicle SNARE required for targeting and fusion of retrograde
CC transport vesicles with the Golgi complex. Required for the integrity
CC of the Golgi complex (By similarity). {ECO:0000250|UniProtKB:O35152}.
CC -!- SUBUNIT: Component of a SNARE complex consisting of STX5, YKT6, GOSR2
CC and BET1L. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type IV membrane protein {ECO:0000250}. Golgi apparatus, trans-
CC Golgi network membrane {ECO:0000250}. Note=Present throughout the Golgi
CC apparatus, with increasing concentration from cis-Golgi to the trans-
CC Golgi face of the stacks. {ECO:0000250}.
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DR EMBL; AF234160; AAF37877.1; -; mRNA.
DR EMBL; AK022958; BAG51142.1; -; mRNA.
DR EMBL; BC008971; AAH08971.1; -; mRNA.
DR CCDS; CCDS41582.1; -.
DR RefSeq; NP_001092257.1; NM_001098787.1.
DR AlphaFoldDB; Q9NYM9; -.
DR SMR; Q9NYM9; -.
DR BioGRID; 119425; 43.
DR IntAct; Q9NYM9; 8.
DR STRING; 9606.ENSP00000372210; -.
DR iPTMnet; Q9NYM9; -.
DR PhosphoSitePlus; Q9NYM9; -.
DR SwissPalm; Q9NYM9; -.
DR BioMuta; BET1L; -.
DR DMDM; 74734714; -.
DR EPD; Q9NYM9; -.
DR jPOST; Q9NYM9; -.
DR MassIVE; Q9NYM9; -.
DR MaxQB; Q9NYM9; -.
DR PaxDb; Q9NYM9; -.
DR PeptideAtlas; Q9NYM9; -.
DR PRIDE; Q9NYM9; -.
DR ProteomicsDB; 83254; -.
DR TopDownProteomics; Q9NYM9; -.
DR Antibodypedia; 41928; 44 antibodies from 17 providers.
DR DNASU; 51272; -.
DR Ensembl; ENST00000382762.8; ENSP00000372210.3; ENSG00000177951.18.
DR GeneID; 51272; -.
DR KEGG; hsa:51272; -.
DR MANE-Select; ENST00000382762.8; ENSP00000372210.3; NM_001098787.2; NP_001092257.1.
DR UCSC; uc001loe.3; human.
DR CTD; 51272; -.
DR DisGeNET; 51272; -.
DR GeneCards; BET1L; -.
DR HGNC; HGNC:19348; BET1L.
DR HPA; ENSG00000177951; Low tissue specificity.
DR MIM; 615417; gene.
DR neXtProt; NX_Q9NYM9; -.
DR OpenTargets; ENSG00000177951; -.
DR PharmGKB; PA134970036; -.
DR VEuPathDB; HostDB:ENSG00000177951; -.
DR eggNOG; KOG3385; Eukaryota.
DR GeneTree; ENSGT00940000160208; -.
DR InParanoid; Q9NYM9; -.
DR OMA; RLMCYLI; -.
DR OrthoDB; 1536545at2759; -.
DR PhylomeDB; Q9NYM9; -.
DR TreeFam; TF323307; -.
DR PathwayCommons; Q9NYM9; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR SignaLink; Q9NYM9; -.
DR BioGRID-ORCS; 51272; 11 hits in 1077 CRISPR screens.
DR ChiTaRS; BET1L; human.
DR GeneWiki; BET1L; -.
DR GenomeRNAi; 51272; -.
DR Pharos; Q9NYM9; Tbio.
DR PRO; PR:Q9NYM9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NYM9; protein.
DR Bgee; ENSG00000177951; Expressed in body of pancreas and 155 other tissues.
DR ExpressionAtlas; Q9NYM9; baseline and differential.
DR Genevisible; Q9NYM9; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IDA:HGNC-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HGNC-UCL.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0000138; C:Golgi trans cisterna; IBA:GO_Central.
DR GO; GO:0030173; C:integral component of Golgi membrane; IEA:InterPro.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:HGNC-UCL.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000156; P:regulation of retrograde vesicle-mediated transport, Golgi to ER; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:HGNC-UCL.
DR CDD; cd15853; SNARE_Bet1; 1.
DR InterPro; IPR039897; BET1.
DR InterPro; IPR039899; BET1_SNARE.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR12791; PTHR12791; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..111
FT /note="BET1-like protein"
FT /id="PRO_0000233056"
FT TOPO_DOM 1..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..111
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 15..77
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
SQ SEQUENCE 111 AA; 12388 MW; 76E2C5099EC7EE5E CRC64;
MADWARAQSP GAVEEILDRE NKRMADSLAS KVTRLKSLAL DIDRDAEDQN RYLDGMDSDF
TSMTSLLTGS VKRFSTMARS GQDNRKLLCG MAVGLIVAFF ILSYFLSRAR T
