BET1_HUMAN
ID BET1_HUMAN Reviewed; 118 AA.
AC O15155; Q96EA0;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=BET1 homolog;
DE Short=hBET1;
DE AltName: Full=Golgi vesicular membrane-trafficking protein p18;
GN Name=BET1;
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).
RX PubMed=9382863; DOI=10.1083/jcb.139.5.1157;
RA Zhang T., Wong S.H., Tang B.L., Xu Y., Peter F., Subramaniam V.N., Hong W.;
RT "The mammalian protein (rbet1) homologous to yeast Bet1p is primarily
RT associated with the pre-Golgi intermediate compartment and is involved in
RT vesicular transport from the endoplasmic reticulum to the Golgi
RT apparatus.";
RL J. Cell Biol. 139:1157-1168(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP 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 [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-50, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP 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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Required for vesicular transport from the ER to the Golgi
CC complex. Functions as a SNARE involved in the docking process of ER-
CC derived vesicles with the cis-Golgi membrane (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with STX17. {ECO:0000250}.
CC -!- INTERACTION:
CC O15155; P29274: ADORA2A; NbExp=3; IntAct=EBI-749204, EBI-2902702;
CC O15155; Q68DC2: ANKS6; NbExp=3; IntAct=EBI-749204, EBI-7054139;
CC O15155; Q13520: AQP6; NbExp=3; IntAct=EBI-749204, EBI-13059134;
CC O15155; P07307-3: ASGR2; NbExp=3; IntAct=EBI-749204, EBI-12808270;
CC O15155; Q8WWH4: ASZ1; NbExp=3; IntAct=EBI-749204, EBI-12239061;
CC O15155; P04233-2: CD74; NbExp=3; IntAct=EBI-749204, EBI-12222807;
CC O15155; P11912: CD79A; NbExp=3; IntAct=EBI-749204, EBI-7797864;
CC O15155; Q99675: CGRRF1; NbExp=3; IntAct=EBI-749204, EBI-2130213;
CC O15155; Q8N5K1: CISD2; NbExp=3; IntAct=EBI-749204, EBI-1045797;
CC O15155; O95471: CLDN7; NbExp=3; IntAct=EBI-749204, EBI-740744;
CC O15155; Q8IUN9: CLEC10A; NbExp=3; IntAct=EBI-749204, EBI-2873246;
CC O15155; Q9BUF7-2: CRB3; NbExp=3; IntAct=EBI-749204, EBI-17233035;
CC O15155; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-749204, EBI-6942903;
CC O15155; P49447: CYB561; NbExp=3; IntAct=EBI-749204, EBI-8646596;
CC O15155; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-749204, EBI-2680384;
CC O15155; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-749204, EBI-18535450;
CC O15155; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-749204, EBI-781551;
CC O15155; Q8TBP5: FAM174A; NbExp=3; IntAct=EBI-749204, EBI-18636064;
CC O15155; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-749204, EBI-18304435;
CC O15155; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-749204, EBI-18938272;
CC O15155; O14653: GOSR2; NbExp=5; IntAct=EBI-749204, EBI-4401517;
CC O15155; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-749204, EBI-13345167;
CC O15155; Q8TED1: GPX8; NbExp=3; IntAct=EBI-749204, EBI-11721746;
CC O15155; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-749204, EBI-10266796;
CC O15155; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-749204, EBI-749265;
CC O15155; P48051: KCNJ6; NbExp=3; IntAct=EBI-749204, EBI-12017638;
CC O15155; Q6UWN5: LYPD5; NbExp=3; IntAct=EBI-749204, EBI-17200970;
CC O15155; P43360: MAGEA6; NbExp=3; IntAct=EBI-749204, EBI-1045155;
CC O15155; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-749204, EBI-11956541;
CC O15155; O14880: MGST3; NbExp=3; IntAct=EBI-749204, EBI-724754;
CC O15155; Q9H115: NAPB; NbExp=3; IntAct=EBI-749204, EBI-3921185;
CC O15155; O14684: PTGES; NbExp=3; IntAct=EBI-749204, EBI-11161398;
CC O15155; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-749204, EBI-7545592;
CC O15155; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-749204, EBI-10192441;
CC O15155; Q9BXS9-3: SLC26A6; NbExp=3; IntAct=EBI-749204, EBI-12814225;
CC O15155; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-749204, EBI-5235586;
CC O15155; Q8WWF3: SSMEM1; NbExp=3; IntAct=EBI-749204, EBI-17280858;
CC O15155; Q16623: STX1A; NbExp=3; IntAct=EBI-749204, EBI-712466;
CC O15155; P61266: STX1B; NbExp=3; IntAct=EBI-749204, EBI-9071709;
CC O15155; P32856-2: STX2; NbExp=3; IntAct=EBI-749204, EBI-11956649;
CC O15155; Q12846: STX4; NbExp=6; IntAct=EBI-749204, EBI-744942;
CC O15155; Q8N6Q1: TMCO5A; NbExp=3; IntAct=EBI-749204, EBI-12821895;
CC O15155; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-749204, EBI-10982110;
CC O15155; Q53FP2: TMEM35A; NbExp=3; IntAct=EBI-749204, EBI-11722971;
CC O15155; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-749204, EBI-18178701;
CC O15155; Q96HE8: TMEM80; NbExp=3; IntAct=EBI-749204, EBI-11742770;
CC O15155; Q9Y320: TMX2; NbExp=3; IntAct=EBI-749204, EBI-6447886;
CC O15155; Q8N6Y0: USHBP1; NbExp=2; IntAct=EBI-749204, EBI-739895;
CC O15155-2; Q86V38: ATN1; NbExp=3; IntAct=EBI-25846497, EBI-11954292;
CC O15155-2; Q92876: KLK6; NbExp=3; IntAct=EBI-25846497, EBI-2432309;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type IV membrane protein {ECO:0000250}. Golgi apparatus,
CC cis-Golgi network membrane {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}. Note=Concentrated most in the intermediate
CC compartment/cis-Golgi network and the cis-Golgi cisternae 1 and 2.
CC Greatly reduced in concentration at the trans end of the Golgi
CC apparatus (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15155-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15155-2; Sequence=VSP_056216;
CC -!- SIMILARITY: Belongs to the BET1 family. {ECO:0000305}.
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DR EMBL; AF007551; AAB62941.1; -; mRNA.
DR EMBL; AC006378; AAD47132.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76802.1; -; Genomic_DNA.
DR EMBL; BC000899; AAH00899.1; -; mRNA.
DR EMBL; BC012595; AAH12595.1; -; mRNA.
DR CCDS; CCDS5635.1; -. [O15155-1]
DR CCDS; CCDS83203.1; -. [O15155-2]
DR RefSeq; NP_001304668.1; NM_001317739.1. [O15155-2]
DR RefSeq; NP_005859.1; NM_005868.5. [O15155-1]
DR PDB; 3EGX; X-ray; 3.30 A; D=24-32.
DR PDBsum; 3EGX; -.
DR AlphaFoldDB; O15155; -.
DR SMR; O15155; -.
DR BioGRID; 115571; 393.
DR IntAct; O15155; 322.
DR MINT; O15155; -.
DR STRING; 9606.ENSP00000222547; -.
DR GlyGen; O15155; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15155; -.
DR MetOSite; O15155; -.
DR PhosphoSitePlus; O15155; -.
DR SwissPalm; O15155; -.
DR BioMuta; BET1; -.
DR EPD; O15155; -.
DR jPOST; O15155; -.
DR MassIVE; O15155; -.
DR PaxDb; O15155; -.
DR PeptideAtlas; O15155; -.
DR PRIDE; O15155; -.
DR ProteomicsDB; 48479; -. [O15155-1]
DR ProteomicsDB; 76387; -.
DR TopDownProteomics; O15155-1; -. [O15155-1]
DR Antibodypedia; 64131; 46 antibodies from 13 providers.
DR DNASU; 10282; -.
DR Ensembl; ENST00000222547.8; ENSP00000222547.3; ENSG00000105829.13. [O15155-1]
DR Ensembl; ENST00000433727.5; ENSP00000391228.1; ENSG00000105829.13. [O15155-2]
DR GeneID; 10282; -.
DR KEGG; hsa:10282; -.
DR MANE-Select; ENST00000222547.8; ENSP00000222547.3; NM_005868.6; NP_005859.1.
DR UCSC; uc064fkr.1; human. [O15155-1]
DR CTD; 10282; -.
DR DisGeNET; 10282; -.
DR GeneCards; BET1; -.
DR HGNC; HGNC:14562; BET1.
DR HPA; ENSG00000105829; Low tissue specificity.
DR MIM; 605456; gene.
DR neXtProt; NX_O15155; -.
DR OpenTargets; ENSG00000105829; -.
DR PharmGKB; PA25338; -.
DR VEuPathDB; HostDB:ENSG00000105829; -.
DR eggNOG; KOG3385; Eukaryota.
DR GeneTree; ENSGT00940000162637; -.
DR HOGENOM; CLU_086133_2_1_1; -.
DR InParanoid; O15155; -.
DR OMA; DENERMT; -.
DR PhylomeDB; O15155; -.
DR TreeFam; TF323307; -.
DR PathwayCommons; O15155; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR SignaLink; O15155; -.
DR BioGRID-ORCS; 10282; 318 hits in 1016 CRISPR screens.
DR ChiTaRS; BET1; human.
DR EvolutionaryTrace; O15155; -.
DR GeneWiki; BET1; -.
DR GenomeRNAi; 10282; -.
DR Pharos; O15155; Tdark.
DR PRO; PR:O15155; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O15155; protein.
DR Bgee; ENSG00000105829; Expressed in body of pancreas and 198 other tissues.
DR ExpressionAtlas; O15155; baseline and differential.
DR Genevisible; O15155; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
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:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0048280; P:vesicle fusion with Golgi apparatus; IBA:GO_Central.
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 SMART; SM00397; t_SNARE; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Endoplasmic reticulum;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..118
FT /note="BET1 homolog"
FT /id="PRO_0000206884"
FT TOPO_DOM 1..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..115
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116..118
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT DOMAIN 26..88
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 80..118
FT /note="KTMGKLKILSRGSQTKLLCYMMLFSLFVFFIIYWIIKLR -> LCPM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056216"
SQ SEQUENCE 118 AA; 13289 MW; B83B76ACBB3DA57E CRC64;
MRRAGLGEGV PPGNYGNYGY ANSGYSACEE ENERLTESLR SKVTAIKSLS IEIGHEVKTQ
NKLLAEMDSQ FDSTTGFLGK TMGKLKILSR GSQTKLLCYM MLFSLFVFFI IYWIIKLR
