ID SC61B_HUMAN Reviewed; 96 AA. AC P60468; P38390; P38391; Q6IBC1; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 174. DE RecName: Full=Protein transport protein Sec61 subunit beta; GN Name=SEC61B {ECO:0000303|PubMed:28375157, GN ECO:0000312|HGNC:HGNC:16993}; 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]. RX PubMed=8107851; DOI=10.1038/367654a0; RA Hartmann E., Sommer T., Prehn S., Goerlich D., Jentsch S., Rapoport T.A.; RT "Evolutionary conservation of components of the protein translocation RT complex."; RL Nature 367:654-657(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 PROTEIN SEQUENCE OF 2-20, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION RP AT SER-7, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=12475939; DOI=10.1091/mbc.e02-04-0198; RA Meacock S.L., Lecomte F.J., Crawshaw S.G., High S.; RT "Different transmembrane domains associate with distinct endoplasmic RT reticulum components during membrane integration of a polytopic protein."; RL Mol. Biol. Cell 13:4114-4129(2002). RN [7] 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-14 AND SER-17, AND 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 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 [10] RP FUNCTION, AND INTERACTION WITH TRAM1. RX PubMed=19121997; DOI=10.1074/jbc.m807568200; RA Oresic K., Ng C.L., Tortorella D.; RT "TRAM1 participates in human cytomegalovirus US2- and US11-mediated RT dislocation of an endoplasmic reticulum membrane glycoprotein."; RL J. Biol. Chem. 284:5905-5914(2009). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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 [13] 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 [14] RP MUTAGENESIS OF CYS-39, AND PALMITOYLATION AT CYS-39. RX PubMed=21044946; DOI=10.1194/jlr.d011106; RA Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A., RA Stamler J.S., Casey P.J.; RT "Site-specific analysis of protein S-acylation by resin-assisted capture."; RL J. Lipid Res. 52:393-398(2011). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT PRO-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT SER-17, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE RP ANALYSIS], AND 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 [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9; SER-14 AND SER-17, 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). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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 [19] RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION RP 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). RN [20] RP INVOLVEMENT IN PCLD. RX PubMed=28375157; DOI=10.1172/jci90129; RA Besse W., Dong K., Choi J., Punia S., Fedeles S.V., Choi M., RA Gallagher A.R., Huang E.B., Gulati A., Knight J., Mane S., Tahvanainen E., RA Tahvanainen P., Sanna-Cherchi S., Lifton R.P., Watnick T., Pei Y.P., RA Torres V.E., Somlo S.; RT "Isolated polycystic liver disease genes define effectors of polycystin-1 RT function."; RL J. Clin. Invest. 127:1772-1785(2017). RN [21] RP SUBCELLULAR LOCATION. RX PubMed=27044890; DOI=10.1083/jcb.201508106; RA Dickson E.J., Jensen J.B., Vivas O., Kruse M., Traynor-Kaplan A.E., RA Hille B.; RT "Dynamic formation of ER-PM junctions presents a lipid phosphatase to RT regulate phosphoinositides."; RL J. Cell Biol. 213:33-48(2016). RN [22] RP STRUCTURE BY ELECTRON MICROSCOPY (3.8 ANGSTROMS) IN COMPLEX WITH THE RP RIBOSOME-ASSOCIATED ER TRANSLOCON COMPLEX, FUNCTION, AND INTERACTION WITH RP TMCO1; CCDC47; NCLN; NOMO; TMEM147; SEC61A1 AND SEC61G. RX PubMed=32820719; DOI=10.7554/elife.56889; RA McGilvray P.T., Anghel S.A., Sundaram A., Zhong F., Trnka M.J., RA Fuller J.R., Hu H., Burlingame A.L., Keenan R.J.; RT "An ER translocon for multi-pass membrane protein biogenesis."; RL Elife 9:0-0(2020). RN [23] RP FUNCTION, INTERACTION WITH THE MULTI-PASS TRANSLOCON COMPLEX, AND RP SUBCELLULAR LOCATION. RX PubMed=36261522; DOI=10.1038/s41586-022-05330-8; RA Sundaram A., Yamsek M., Zhong F., Hooda Y., Hegde R.S., Keenan R.J.; RT "Substrate-driven assembly of a translocon for multipass membrane RT proteins."; RL Nature 611:167-172(2022). CC -!- FUNCTION: Component of SEC61 channel-forming translocon complex that CC mediates transport of signal peptide-containing precursor polypeptides CC across the endoplasmic reticulum (ER) (PubMed:12475939). Forms a CC ribosome receptor and a gated pore in the ER membrane, both functions CC required for cotranslational translocation of nascent polypeptides CC (PubMed:12475939). The SEC61 channel is also involved in ER membrane CC insertion of transmembrane proteins: it mediates membrane insertion of CC the first few transmembrane segments of proteins, while insertion of CC subsequent transmembrane regions of multi-pass membrane proteins is CC mediated by the multi-pass translocon (MPT) complex (PubMed:32820719, CC PubMed:36261522). The SEC61 channel cooperates with the translocating CC protein TRAM1 to import nascent proteins into the ER (PubMed:19121997). CC {ECO:0000269|PubMed:12475939, ECO:0000269|PubMed:19121997, CC ECO:0000269|PubMed:32820719, ECO:0000269|PubMed:36261522}. CC -!- SUBUNIT: The SEC61 channel-forming translocon complex consists of CC channel-forming core components SEC61A1, SEC61B and SEC61G and CC different auxiliary components such as SEC62 and SEC63 (By similarity). CC The SEC61 channel associates with the multi-pass translocon (MPT) CC complex (PubMed:32820719, PubMed:36261522). Interacts with TRAM1 CC (PubMed:19121997). {ECO:0000250|UniProtKB:P60467, CC ECO:0000269|PubMed:19121997, ECO:0000269|PubMed:32820719, CC ECO:0000269|PubMed:36261522}. CC -!- INTERACTION: CC P60468; P51572: BCAP31; NbExp=7; IntAct=EBI-1788819, EBI-77683; CC P60468; P0DTD8: 7b; Xeno; NbExp=3; IntAct=EBI-1788819, EBI-25475914; CC P60468; Q12154: GET3; Xeno; NbExp=4; IntAct=EBI-1788819, EBI-2989; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:12475939, ECO:0000269|PubMed:27044890}; Single-pass CC membrane protein {ECO:0000255}. CC -!- DISEASE: Note=Loss-of-function SEC61B variations may cause autosomal CC dominant polycystic liver disease (PCLD) in patients that lack CC variations in known causative genes, such as PRKCSH and SEC63. CC {ECO:0000305|PubMed:28375157}. CC -!- SIMILARITY: Belongs to the SEC61-beta family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L25085; AAA19706.1; -; mRNA. DR EMBL; CR456883; CAG33164.1; -; mRNA. DR EMBL; AL137067; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001734; AAH01734.1; -; mRNA. DR CCDS; CCDS6741.1; -. DR PIR; S42410; S42410. DR RefSeq; NP_006799.1; NM_006808.2. DR PDB; 6W6L; EM; 3.84 A; 3=1-96. DR PDB; 8B6L; EM; 7.60 A; B=1-96. DR PDB; 8DNV; EM; 3.03 A; C=1-96. DR PDB; 8DNW; EM; 3.40 A; C=1-96. DR PDB; 8DNX; EM; 2.98 A; C=1-96. DR PDB; 8DNY; EM; 2.85 A; C=1-96. DR PDB; 8DNZ; EM; 2.57 A; C=1-96. DR PDB; 8DO0; EM; 2.86 A; C=1-96. DR PDB; 8DO1; EM; 3.01 A; C=1-96. DR PDB; 8DO2; EM; 2.95 A; C=1-96. DR PDB; 8DO3; EM; 3.22 A; C=1-96. DR PDBsum; 6W6L; -. DR PDBsum; 8B6L; -. DR PDBsum; 8DNV; -. DR PDBsum; 8DNW; -. DR PDBsum; 8DNX; -. DR PDBsum; 8DNY; -. DR PDBsum; 8DNZ; -. DR PDBsum; 8DO0; -. DR PDBsum; 8DO1; -. DR PDBsum; 8DO2; -. DR PDBsum; 8DO3; -. DR AlphaFoldDB; P60468; -. DR EMDB; EMD-15870; -. DR EMDB; EMD-27581; -. DR EMDB; EMD-27582; -. DR EMDB; EMD-27583; -. DR EMDB; EMD-27584; -. DR EMDB; EMD-27585; -. DR EMDB; EMD-27586; -. DR EMDB; EMD-27587; -. DR EMDB; EMD-27588; -. DR EMDB; EMD-27589; -. DR EMDB; EMD-29608; -. DR EMDB; EMD-29609; -. DR EMDB; EMD-29610; -. DR EMDB; EMD-29611; -. DR EMDB; EMD-29612; -. DR EMDB; EMD-29613; -. DR EMDB; EMD-29614; -. DR EMDB; EMD-29616; -. DR EMDB; EMD-29617; -. DR EMDB; EMD-29635; -. DR SMR; P60468; -. DR BioGRID; 116152; 777. DR ComplexPortal; CPX-8073; SEC61 protein-conducting channel complex, SEC1A1 variant. DR ComplexPortal; CPX-8169; SEC61 protein-conducting channel complex, SEC1A2 variant. DR CORUM; P60468; -. DR DIP; DIP-40997N; -. DR IntAct; P60468; 73. DR MINT; P60468; -. DR STRING; 9606.ENSP00000223641; -. DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family. DR GlyCosmos; P60468; 2 sites, 1 glycan. DR GlyGen; P60468; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P60468; -. DR PhosphoSitePlus; P60468; -. DR SwissPalm; P60468; -. DR BioMuta; SEC61B; -. DR DMDM; 42560366; -. DR EPD; P60468; -. DR jPOST; P60468; -. DR MassIVE; P60468; -. DR MaxQB; P60468; -. DR PaxDb; 9606-ENSP00000223641; -. DR PeptideAtlas; P60468; -. DR ProteomicsDB; 57208; -. DR Pumba; P60468; -. DR TopDownProteomics; P60468; -. DR Antibodypedia; 14546; 201 antibodies from 30 providers. DR DNASU; 10952; -. DR Ensembl; ENST00000223641.5; ENSP00000223641.4; ENSG00000106803.10. DR GeneID; 10952; -. DR KEGG; hsa:10952; -. DR MANE-Select; ENST00000223641.5; ENSP00000223641.4; NM_006808.3; NP_006799.1. DR UCSC; uc004azh.4; human. DR AGR; HGNC:16993; -. DR CTD; 10952; -. DR DisGeNET; 10952; -. DR GeneCards; SEC61B; -. DR HGNC; HGNC:16993; SEC61B. DR HPA; ENSG00000106803; Low tissue specificity. DR MIM; 609214; gene. DR neXtProt; NX_P60468; -. DR OpenTargets; ENSG00000106803; -. DR PharmGKB; PA134888963; -. DR VEuPathDB; HostDB:ENSG00000106803; -. DR eggNOG; KOG3457; Eukaryota. DR GeneTree; ENSGT00390000003561; -. DR HOGENOM; CLU_133423_4_0_1; -. DR InParanoid; P60468; -. DR OMA; TNSGGMW; -. DR OrthoDB; 9185at2759; -. DR PhylomeDB; P60468; -. DR TreeFam; TF313144; -. DR PathwayCommons; P60468; -. DR Reactome; R-HSA-1236974; ER-Phagosome pathway. DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane. DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. DR SignaLink; P60468; -. DR SIGNOR; P60468; -. DR BioGRID-ORCS; 10952; 389 hits in 1166 CRISPR screens. DR ChiTaRS; SEC61B; human. DR GeneWiki; SEC61B; -. DR GenomeRNAi; 10952; -. DR Pharos; P60468; Tbio. DR PRO; PR:P60468; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P60468; Protein. DR Bgee; ENSG00000106803; Expressed in parotid gland and 203 other cell types or tissues. DR ExpressionAtlas; P60468; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB. DR GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IDA:UniProtKB. DR GO; GO:0031205; C:endoplasmic reticulum Sec complex; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005784; C:Sec61 translocon complex; IBA:GO_Central. DR GO; GO:0048408; F:epidermal growth factor binding; IPI:UniProtKB. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IBA:GO_Central. DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IMP:UniProtKB. DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central. DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB. DR InterPro; IPR030671; Sec61-beta/Sbh. DR InterPro; IPR016482; SecG/Sec61-beta/Sbh. DR PANTHER; PTHR13509:SF3; PROTEIN TRANSPORT PROTEIN SEC61 SUBUNIT BETA; 1. DR PANTHER; PTHR13509; SEC61 SUBUNIT BETA; 1. DR Pfam; PF03911; Sec61_beta; 1. DR PIRSF; PIRSF006398; Sec61_beta_euk; 1. DR Genevisible; P60468; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; KW Endoplasmic reticulum; Lipoprotein; Membrane; Palmitate; Phosphoprotein; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:25944712" FT CHAIN 2..96 FT /note="Protein transport protein Sec61 subunit beta" FT /id="PRO_0000157254" FT TOPO_DOM 2..70 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 71..91 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 92..96 FT /note="Lumenal" FT /evidence="ECO:0000305" FT REGION 1..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 31..54 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylproline" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 7 FT /note="Phosphoserine" FT /evidence="ECO:0000269|Ref.5" FT MOD_RES 9 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 13 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 17 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 LIPID 39 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000305|PubMed:21044946" FT MUTAGEN 39 FT /note="C->S: Abolishes S-acylation." FT /evidence="ECO:0000269|PubMed:21044946" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:8DNW" FT HELIX 70..95 FT /evidence="ECO:0007829|PDB:8DNZ" SQ SEQUENCE 96 AA; 9974 MW; 5FAFF4197A62FA49 CRC64; MPGPTPSGTN VGSSGRSPSK AVAARAAGST VRQRKNASCG TRSAGRTTSA GTGGMWRFYT EDSPGLKVGP VPVLVMSLLF IASVFMLHIW GKYTRS //