SC61B_HUMAN
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 03-AUG-2022, entry version 165.
DE RecName: Full=Protein transport protein Sec61 subunit beta;
GN Name=SEC61B {ECO:0000303|PubMed:28375157, 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 FUNCTION, AND INTERACTION WITH TMCO1; CCDC47; NCLN; NOMO; TMEM147; SEC61A1
RP 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).
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). Component of a
CC ribosome-associated ER translocon complex involved in multi-pass
CC membrane protein transport into the ER membrane and biogenesis
CC (PubMed:32820719). The SEC61 channel cooperates with the translocating
CC protein TRAM1 to import nascent proteins into the ER (PubMed:19121997).
CC Required for PKD1/Polycystin-1 biogenesis (By similarity).
CC {ECO:0000250|UniProtKB:Q9CQS8, ECO:0000269|PubMed:12475939,
CC ECO:0000269|PubMed:19121997, ECO:0000269|PubMed:32820719}.
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 ribosome-associated ER translocon complex includes SEC61A1, SEC61B,
CC SEC61G, TMCO1, CCDC47, NCLN/Nicalin, NOMO and TMEM147; in the absence
CC of ribosomes, only the complex forms with NCLN/Nicalin, NOMO and
CC TMEM147 remains intact (PubMed:32820719). Interacts with TRAM1
CC (PubMed:19121997). {ECO:0000250|UniProtKB:P60467,
CC ECO:0000269|PubMed:19121997, ECO:0000269|PubMed:32820719}.
CC -!- INTERACTION:
CC P60468; P51572: BCAP31; NbExp=7; IntAct=EBI-1788819, EBI-77683;
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}.
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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 PDBsum; 6W6L; -.
DR AlphaFoldDB; P60468; -.
DR SMR; P60468; -.
DR BioGRID; 116152; 631.
DR CORUM; P60468; -.
DR DIP; DIP-40997N; -.
DR IntAct; P60468; 71.
DR MINT; P60468; -.
DR STRING; 9606.ENSP00000223641; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR GlyGen; P60468; 2 sites, 1 O-linked glycan (2 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; P60468; -.
DR PeptideAtlas; P60468; -.
DR PRIDE; P60468; -.
DR ProteomicsDB; 57208; -.
DR TopDownProteomics; P60468; -.
DR Antibodypedia; 14546; 169 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 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; WGKYTRG; -.
DR OrthoDB; 1634609at2759; -.
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; 357 hits in 1081 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 201 other tissues.
DR ExpressionAtlas; P60468; baseline and differential.
DR Genevisible; P60468; HS.
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:0016021; C:integral component of membrane; NAS: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; PTHR13509; 1.
DR Pfam; PF03911; Sec61_beta; 1.
DR PIRSF; PIRSF006398; Sec61_beta_euk; 1.
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:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 96 AA; 9974 MW; 5FAFF4197A62FA49 CRC64;
MPGPTPSGTN VGSSGRSPSK AVAARAAGST VRQRKNASCG TRSAGRTTSA GTGGMWRFYT
EDSPGLKVGP VPVLVMSLLF IASVFMLHIW GKYTRS
