SGTA_HUMAN
ID SGTA_HUMAN Reviewed; 313 AA.
AC O43765; D6W610; Q6FIA9; Q9BTZ9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein alpha;
DE AltName: Full=Alpha-SGT;
DE AltName: Full=Vpu-binding protein;
DE Short=UBP;
GN Name=SGTA; Synonyms=SGT, SGT1;
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=9740675; DOI=10.1006/geno.1998.5385;
RA Kordes E., Savelyeva L., Schwab M., Rommelaere J., Jauniaux J.-C.,
RA Cziepluch C.;
RT "Isolation and characterization of human SGT and identification of
RT homologues in Saccharomyces cerevisiae and Caenorhabditis elegans.";
RL Genomics 52:90-94(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10567422; DOI=10.1074/jbc.274.48.34425;
RA Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C.;
RT "Specific interaction of the 70-kDa heat shock cognate protein with the
RT tetratricopeptide repeats.";
RL J. Biol. Chem. 274:34425-34432(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH HIV-1V PU AND GAG
RP (MICROBIAL INFECTION).
RX PubMed=9573291; DOI=10.1128/jvi.72.6.5189-5197.1998;
RA Callahan M.A., Handley M.A., Lee Y.H., Talbot K.J., Harper J.W.,
RA Panganiban A.T.;
RT "Functional interaction of human immunodeficiency virus type 1 Vpu and Gag
RT with a novel member of the tetratricopeptide repeat protein family.";
RL J. Virol. 72:5189-5197(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tobaben S., Stahl B.;
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Muscle, and Uterus;
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 [10]
RP PROTEIN SEQUENCE OF 138-160; 165-174 AND 185-196.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [11]
RP SUBUNIT, AND INTERACTION WITH HSP90AA1 AND SLC2A1.
RX PubMed=15708368; DOI=10.1016/j.abb.2004.12.020;
RA Liou S.T., Wang C.;
RT "Small glutamine-rich tetratricopeptide repeat-containing protein is
RT composed of three structural units with distinct functions.";
RL Arch. Biochem. Biophys. 435:253-263(2005).
RN [12]
RP INTERACTION WITH HSP90AB1, AND SUBCELLULAR LOCATION.
RX PubMed=16580629; DOI=10.1016/j.bbrc.2006.03.090;
RA Yin H., Wang H., Zong H., Chen X., Wang Y., Yun X., Wu Y., Wang J., Gu J.;
RT "SGT, a Hsp90beta binding partner, is accumulated in the nucleus during
RT cell apoptosis.";
RL Biochem. Biophys. Res. Commun. 343:1153-1158(2006).
RN [13]
RP INTERACTION WITH SARS-COV ACCESSORY PROTEIN 7A (MICROBIAL INFECTION).
RX PubMed=16580632; DOI=10.1016/j.bbrc.2006.03.091;
RA Fielding B.C., Gunalan V., Tan T.H.P., Chou C.-F., Shen S., Khan S.,
RA Lim S.G., Hong W., Tan Y.-J.;
RT "Severe acute respiratory syndrome coronavirus protein 7a interacts with
RT hSGT.";
RL Biochem. Biophys. Res. Commun. 343:1201-1208(2006).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [15]
RP INTERACTION WITH DNAJC5 AND DNAJC5B.
RX PubMed=17034881; DOI=10.1016/j.bbamcr.2006.08.054;
RA Boal F., Le Pevelen S., Cziepluch C., Scotti P., Lang J.;
RT "Cysteine-string protein isoform beta (Cspbeta) is targeted to the trans-
RT Golgi network as a non-palmitoylated CSP in clonal beta-cells.";
RL Biochim. Biophys. Acta 1773:109-119(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81; SER-301; THR-303
RP AND SER-305, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81 AND SER-305, AND
RP IDENTIFICATION BY MASS 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-303, 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 [20]
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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-305, AND
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., 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 [22]
RP FUNCTION, AND INTERACTION WITH BAG6.
RX PubMed=23129660; DOI=10.1073/pnas.1209997109;
RA Leznicki P., High S.;
RT "SGTA antagonizes BAG6-mediated protein triage.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:19214-19219(2012).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; THR-81 AND SER-301, 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 [24]
RP FUNCTION, AND INTERACTION WITH BAG6.
RX PubMed=25179605; DOI=10.1242/jcs.155648;
RA Wunderley L., Leznicki P., Payapilly A., High S.;
RT "SGTA regulates the cytosolic quality control of hydrophobic substrates.";
RL J. Cell Sci. 127:4728-4739(2014).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-81; THR-303 AND SER-305, AND
RP IDENTIFICATION BY 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 [26]
RP FUNCTION (MICROBIAL INFECTION), IDENTIFICATION IN A COMPLEX WITH DNAJB12
RP AND DNAJB14, AND INTERACTION WITH HSPA8.
RX PubMed=24675744; DOI=10.1371/journal.ppat.1004007;
RA Walczak C.P., Ravindran M.S., Inoue T., Tsai B.;
RT "A cytosolic chaperone complexes with dynamic membrane J-proteins and
RT mobilizes a nonenveloped virus out of the endoplasmic reticulum.";
RL PLoS Pathog. 10:E1004007-E1004007(2014).
RN [27]
RP FUNCTION, AND MUTAGENESIS OF CYS-38.
RX PubMed=25535373; DOI=10.1073/pnas.1402745112;
RA Mock J.Y., Chartron J.W., Zaslaver M., Xu Y., Ye Y., Clemons W.M. Jr.;
RT "Bag6 complex contains a minimal tail-anchor-targeting module and a mock
RT BAG domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:106-111(2015).
RN [28]
RP FUNCTION, AND INTERACTION WITH BAG6.
RX PubMed=27193484; DOI=10.1038/srep26433;
RA Krysztofinska E.M., Martinez-Lumbreras S., Thapaliya A., Evans N.J.,
RA High S., Isaacson R.L.;
RT "Structural and functional insights into the E3 ligase, RNF126.";
RL Sci. Rep. 6:26433-26433(2016).
RN [29]
RP FUNCTION.
RX PubMed=28104892; DOI=10.1126/science.aah6130;
RA Shao S., Rodrigo-Brenni M.C., Kivlen M.H., Hegde R.S.;
RT "Mechanistic basis for a molecular triage reaction.";
RL Science 355:298-302(2017).
RN [30]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 84-210, SUBUNIT (MICROBIAL
RP INFECTION), AND FUNCTION.
RX PubMed=18759457; DOI=10.1021/bi800758a;
RA Dutta S., Tan Y.J.;
RT "Structural and functional characterization of human SGT and its
RT interaction with Vpu of the human immunodeficiency virus type 1.";
RL Biochemistry 47:10123-10131(2008).
CC -!- FUNCTION: Co-chaperone that binds misfolded and hydrophobic patches-
CC containing client proteins in the cytosol. Mediates their targeting to
CC the endoplasmic reticulum but also regulates their sorting to the
CC proteasome when targeting fails (PubMed:28104892). Functions in tail-
CC anchored/type II transmembrane proteins membrane insertion constituting
CC with ASNA1 and the BAG6 complex a targeting module (PubMed:28104892).
CC Functions upstream of the BAG6 complex and ASNA1, binding more rapidly
CC the transmembrane domain of newly synthesized proteins
CC (PubMed:28104892, PubMed:25535373). It is also involved in the
CC regulation of the endoplasmic reticulum-associated misfolded protein
CC catabolic process via its interaction with BAG6: collaborates with the
CC BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated
CC states (PubMed:23129660, PubMed:25179605). Competes with RNF126 for
CC interaction with BAG6, preventing the ubiquitination of client proteins
CC associated with the BAG6 complex (PubMed:27193484). Binds directly to
CC HSC70 and HSP70 and regulates their ATPase activity (PubMed:18759457).
CC {ECO:0000269|PubMed:18759457, ECO:0000269|PubMed:23129660,
CC ECO:0000269|PubMed:25179605, ECO:0000269|PubMed:25535373,
CC ECO:0000269|PubMed:27193484, ECO:0000269|PubMed:28104892}.
CC -!- FUNCTION: (Microbial infection) In case of infection by polyomavirus,
CC involved in the virus endoplasmic reticulum membrane penetration and
CC infection via interaction with DNAJB12, DNAJB14 and HSPA8/Hsc70
CC (PubMed:24675744). {ECO:0000269|PubMed:24675744}.
CC -!- SUBUNIT: Homodimer (PubMed:15708368). Homooligomer (By similarity).
CC Interacts with DNAJC5 and DNAJC5B. Interacts (via TPR repeats) with
CC HSP90AA1 (PubMed:15708368). Interacts (via Gln-rich region) with SLC2A1
CC (PubMed:15708368). Interacts with HSP90AB1 (PubMed:16580629). Interacts
CC (via TPR repeats) with HSPA8/Hsc70; the interaction is direct
CC (PubMed:24675744). Interacts with BAG6 (via ubiquitin-like domain);
CC interaction prevents interaction between BAG6 and RNF126
CC (PubMed:23129660, PubMed:25179605, PubMed:27193484). Forms a
CC multiprotein complex, at least composed of DNAJB12, DNAJB14,
CC HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and HSPA8/Hsc70 is
CC direct (PubMed:24675744). {ECO:0000250|UniProtKB:O70593,
CC ECO:0000269|PubMed:15708368, ECO:0000269|PubMed:16580629,
CC ECO:0000269|PubMed:17034881, ECO:0000269|PubMed:18759457,
CC ECO:0000269|PubMed:23129660, ECO:0000269|PubMed:24675744,
CC ECO:0000269|PubMed:25179605, ECO:0000269|PubMed:27193484}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Vpu and Gag from HIV-1.
CC {ECO:0000269|PubMed:18759457, ECO:0000269|PubMed:9573291}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SARS-CoV accessory
CC protein 7a. {ECO:0000269|PubMed:16580632}.
CC -!- INTERACTION:
CC O43765; Q9UKJ8: ADAM21; NbExp=3; IntAct=EBI-347996, EBI-12046857;
CC O43765; A8K660: ADIPOQ; NbExp=3; IntAct=EBI-347996, EBI-10174479;
CC O43765; Q15848: ADIPOQ; NbExp=7; IntAct=EBI-347996, EBI-10827839;
CC O43765; O95994: AGR2; NbExp=3; IntAct=EBI-347996, EBI-712648;
CC O43765; Q8TD06: AGR3; NbExp=6; IntAct=EBI-347996, EBI-3925742;
CC O43765; Q16853: AOC3; NbExp=3; IntAct=EBI-347996, EBI-3921628;
CC O43765; O95816: BAG2; NbExp=2; IntAct=EBI-347996, EBI-355275;
CC O43765; P46379: BAG6; NbExp=6; IntAct=EBI-347996, EBI-347552;
CC O43765; P46379-2: BAG6; NbExp=3; IntAct=EBI-347996, EBI-10988864;
CC O43765; P35070: BTC; NbExp=6; IntAct=EBI-347996, EBI-6590057;
CC O43765; Q86Z23: C1QL4; NbExp=3; IntAct=EBI-347996, EBI-12062109;
CC O43765; Q9BXJ1: C1QTNF1; NbExp=4; IntAct=EBI-347996, EBI-750200;
CC O43765; Q9BXJ0: C1QTNF5; NbExp=3; IntAct=EBI-347996, EBI-19947914;
CC O43765; Q9BXI9: C1QTNF6; NbExp=9; IntAct=EBI-347996, EBI-10301084;
CC O43765; Q6UWT4: C5orf46; NbExp=3; IntAct=EBI-347996, EBI-11986083;
CC O43765; P40259: CD79B; NbExp=6; IntAct=EBI-347996, EBI-2873732;
CC O43765; Q8TCZ2: CD99L2; NbExp=8; IntAct=EBI-347996, EBI-2824782;
CC O43765; P55291: CDH15; NbExp=8; IntAct=EBI-347996, EBI-10215061;
CC O43765; P07510-2: CHRNG; NbExp=3; IntAct=EBI-347996, EBI-11979451;
CC O43765; A0A0S2Z3K0: COL1A2; NbExp=3; IntAct=EBI-347996, EBI-16431143;
CC O43765; P08123: COL1A2; NbExp=11; IntAct=EBI-347996, EBI-983038;
CC O43765; Q4VAQ0: COL8A2; NbExp=3; IntAct=EBI-347996, EBI-10241815;
CC O43765; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-347996, EBI-852194;
CC O43765; P09603: CSF1; NbExp=6; IntAct=EBI-347996, EBI-2872294;
CC O43765; P01037: CST1; NbExp=3; IntAct=EBI-347996, EBI-1056240;
CC O43765; P78358: CTAG1B; NbExp=3; IntAct=EBI-347996, EBI-1188472;
CC O43765; P07711: CTSL; NbExp=3; IntAct=EBI-347996, EBI-1220160;
CC O43765; Q9UHQ9: CYB5R1; NbExp=3; IntAct=EBI-347996, EBI-953870;
CC O43765; P59861: DEFB131A; NbExp=5; IntAct=EBI-347996, EBI-12304807;
CC O43765; Q9UBP4: DKK3; NbExp=3; IntAct=EBI-347996, EBI-954409;
CC O43765; Q6E0U4: DMKN; NbExp=3; IntAct=EBI-347996, EBI-7943171;
CC O43765; Q9HAV5: EDA2R; NbExp=3; IntAct=EBI-347996, EBI-526033;
CC O43765; Q9UNE0-2: EDAR; NbExp=3; IntAct=EBI-347996, EBI-12964110;
CC O43765; A0A0S2Z3V1: EFEMP1; NbExp=3; IntAct=EBI-347996, EBI-16434097;
CC O43765; Q12805: EFEMP1; NbExp=14; IntAct=EBI-347996, EBI-536772;
CC O43765; O95967: EFEMP2; NbExp=7; IntAct=EBI-347996, EBI-743414;
CC O43765; Q96DN0: ERP27; NbExp=7; IntAct=EBI-347996, EBI-953772;
CC O43765; P30040: ERP29; NbExp=3; IntAct=EBI-347996, EBI-946830;
CC O43765; Q9HBU6: ETNK1; NbExp=3; IntAct=EBI-347996, EBI-2834493;
CC O43765; Q9NVM1: EVA1B; NbExp=6; IntAct=EBI-347996, EBI-10314666;
CC O43765; Q9Y624: F11R; NbExp=11; IntAct=EBI-347996, EBI-742600;
CC O43765; Q96RJ6: FERD3L; NbExp=3; IntAct=EBI-347996, EBI-10183007;
CC O43765; Q9NSA1: FGF21; NbExp=3; IntAct=EBI-347996, EBI-3909329;
CC O43765; Q9Y680: FKBP7; NbExp=6; IntAct=EBI-347996, EBI-3918971;
CC O43765; Q12841: FSTL1; NbExp=3; IntAct=EBI-347996, EBI-2349801;
CC O43765; P54710-2: FXYD2; NbExp=5; IntAct=EBI-347996, EBI-13084584;
CC O43765; P58549: FXYD7; NbExp=8; IntAct=EBI-347996, EBI-10216171;
CC O43765; O75084: FZD7; NbExp=3; IntAct=EBI-347996, EBI-746917;
CC O43765; P22466: GAL; NbExp=6; IntAct=EBI-347996, EBI-6624768;
CC O43765; Q9UBC7: GALP; NbExp=3; IntAct=EBI-347996, EBI-12244186;
CC O43765; P09681: GIP; NbExp=6; IntAct=EBI-347996, EBI-8588553;
CC O43765; Q14440: GPErik; NbExp=3; IntAct=EBI-347996, EBI-10232920;
CC O43765; Q96SL4: GPX7; NbExp=7; IntAct=EBI-347996, EBI-749411;
CC O43765; P28799: GRN; NbExp=7; IntAct=EBI-347996, EBI-747754;
CC O43765; Q02747: GUCA2A; NbExp=8; IntAct=EBI-347996, EBI-12244272;
CC O43765; A0A0C4DFT7: GYPA; NbExp=3; IntAct=EBI-347996, EBI-12044847;
CC O43765; B8Q183: GYPA; NbExp=4; IntAct=EBI-347996, EBI-10176190;
CC O43765; P02724: GYPA; NbExp=3; IntAct=EBI-347996, EBI-702665;
CC O43765; P48723: HSPA13; NbExp=8; IntAct=EBI-347996, EBI-750892;
CC O43765; P46695: IER3; NbExp=6; IntAct=EBI-347996, EBI-1748945;
CC O43765; P24592: IGFBP6; NbExp=3; IntAct=EBI-347996, EBI-947015;
CC O43765; Q6PIQ7: IGL@; NbExp=3; IntAct=EBI-347996, EBI-6677651;
CC O43765; Q8N355: IGL@; NbExp=4; IntAct=EBI-347996, EBI-748681;
CC O43765; P40189: IL6ST; NbExp=3; IntAct=EBI-347996, EBI-1030834;
CC O43765; Q14653: IRF3; NbExp=3; IntAct=EBI-347996, EBI-2650369;
CC O43765; Q13568: IRF5; NbExp=3; IntAct=EBI-347996, EBI-3931258;
CC O43765; Q6GPH6: ITPRIPL1; NbExp=3; IntAct=EBI-347996, EBI-953819;
CC O43765; Q6GPH6-2: ITPRIPL1; NbExp=3; IntAct=EBI-347996, EBI-12337095;
CC O43765; Q8N6L0: KASH5; NbExp=8; IntAct=EBI-347996, EBI-749265;
CC O43765; Q09470: KCNA1; NbExp=3; IntAct=EBI-347996, EBI-8286599;
CC O43765; Q16322: KCNA10; NbExp=3; IntAct=EBI-347996, EBI-12265328;
CC O43765; Q9UJ90: KCNE5; NbExp=3; IntAct=EBI-347996, EBI-11981259;
CC O43765; P02538: KRT6A; NbExp=3; IntAct=EBI-347996, EBI-702198;
CC O43765; Q86UP2: KTN1; NbExp=3; IntAct=EBI-347996, EBI-359761;
CC O43765; Q86UP2-3: KTN1; NbExp=3; IntAct=EBI-347996, EBI-12007212;
CC O43765; Q6ISS4: LAIR2; NbExp=6; IntAct=EBI-347996, EBI-10250491;
CC O43765; O43561: LAT; NbExp=3; IntAct=EBI-347996, EBI-1222766;
CC O43765; O43561-2: LAT; NbExp=3; IntAct=EBI-347996, EBI-8070286;
CC O43765; P80188: LCN2; NbExp=5; IntAct=EBI-347996, EBI-11911016;
CC O43765; O15165-2: LDLRAD4; NbExp=3; IntAct=EBI-347996, EBI-13302279;
CC O43765; Q8N112: LSMEM2; NbExp=3; IntAct=EBI-347996, EBI-10264855;
CC O43765; Q96G30: MRAP2; NbExp=6; IntAct=EBI-347996, EBI-9537218;
CC O43765; Q96HJ5: MS4A3; NbExp=3; IntAct=EBI-347996, EBI-12806656;
CC O43765; P08118: MSMB; NbExp=3; IntAct=EBI-347996, EBI-10195681;
CC O43765; Q969H8: MYDGF; NbExp=8; IntAct=EBI-347996, EBI-718622;
CC O43765; Q99972: MYOC; NbExp=3; IntAct=EBI-347996, EBI-11692272;
CC O43765; Q8IW45: NAXD; NbExp=7; IntAct=EBI-347996, EBI-8650724;
CC O43765; Q13232: NME3; NbExp=12; IntAct=EBI-347996, EBI-713684;
CC O43765; Q9HCQ7: NPVF; NbExp=3; IntAct=EBI-347996, EBI-1753111;
CC O43765; Q9GZP1: NRSN2; NbExp=3; IntAct=EBI-347996, EBI-724857;
CC O43765; Q5JUK9: PAGE3; NbExp=6; IntAct=EBI-347996, EBI-10244544;
CC O43765; C3PTT6: PAUF; NbExp=3; IntAct=EBI-347996, EBI-3505892;
CC O43765; Q96AQ6: PBXIP1; NbExp=4; IntAct=EBI-347996, EBI-740845;
CC O43765; Q9UN74: PCDHA4; NbExp=3; IntAct=EBI-347996, EBI-712273;
CC O43765; Q9Y5G9: PCDHGA4; NbExp=3; IntAct=EBI-347996, EBI-12956949;
CC O43765; Q96PD5-2: PGLYRP2; NbExp=3; IntAct=EBI-347996, EBI-12758027;
CC O43765; Q9UL19: PLAAT4; NbExp=4; IntAct=EBI-347996, EBI-10323452;
CC O43765; Q969W9-2: PMEPA1; NbExp=3; IntAct=EBI-347996, EBI-13318883;
CC O43765; P23284: PPIB; NbExp=6; IntAct=EBI-347996, EBI-359252;
CC O43765; P45877: PPIC; NbExp=6; IntAct=EBI-347996, EBI-953909;
CC O43765; Q96NZ9: PRAP1; NbExp=9; IntAct=EBI-347996, EBI-2116102;
CC O43765; Q8TAS3: PRRG2; NbExp=3; IntAct=EBI-347996, EBI-10272071;
CC O43765; Q9UIG4: PSORS1C2; NbExp=5; IntAct=EBI-347996, EBI-11974061;
CC O43765; Q15293: RCN1; NbExp=3; IntAct=EBI-347996, EBI-948278;
CC O43765; Q5GAN6: RNASE10; NbExp=5; IntAct=EBI-347996, EBI-12423312;
CC O43765; P50876: RNF144A; NbExp=3; IntAct=EBI-347996, EBI-2340657;
CC O43765; Q96K19-5: RNF170; NbExp=3; IntAct=EBI-347996, EBI-12055631;
CC O43765; P04843: RPN1; NbExp=7; IntAct=EBI-347996, EBI-355963;
CC O43765; P31431: SDC4; NbExp=6; IntAct=EBI-347996, EBI-3913237;
CC O43765; Q9HCN8: SDF2L1; NbExp=3; IntAct=EBI-347996, EBI-2339921;
CC O43765; P05121: SERPINE1; NbExp=6; IntAct=EBI-347996, EBI-953978;
CC O43765; O75830: SERPINI2; NbExp=3; IntAct=EBI-347996, EBI-750144;
CC O43765; Q16586: SGCA; NbExp=13; IntAct=EBI-347996, EBI-5663553;
CC O43765; Q16586-2: SGCA; NbExp=4; IntAct=EBI-347996, EBI-16434133;
CC O43765; O43765: SGTA; NbExp=4; IntAct=EBI-347996, EBI-347996;
CC O43765; Q96EQ0: SGTB; NbExp=3; IntAct=EBI-347996, EBI-744081;
CC O43765; Q96DD7: SHISA4; NbExp=3; IntAct=EBI-347996, EBI-18035902;
CC O43765; Q8N114-3: SHISA5; NbExp=3; IntAct=EBI-347996, EBI-13369834;
CC O43765; P03973: SLPI; NbExp=6; IntAct=EBI-347996, EBI-355293;
CC O43765; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-347996, EBI-10226799;
CC O43765; Q96QK8: SMIM14; NbExp=3; IntAct=EBI-347996, EBI-373430;
CC O43765; Q71RC9: SMIM5; NbExp=9; IntAct=EBI-347996, EBI-12334905;
CC O43765; P08294: SOD3; NbExp=3; IntAct=EBI-347996, EBI-10195782;
CC O43765; Q5DT21: SPINK9; NbExp=3; IntAct=EBI-347996, EBI-13119580;
CC O43765; P16150: SPN; NbExp=5; IntAct=EBI-347996, EBI-10049055;
CC O43765; P10451: SPP1; NbExp=8; IntAct=EBI-347996, EBI-723648;
CC O43765; Q8TCT8: SPPL2A; NbExp=7; IntAct=EBI-347996, EBI-750784;
CC O43765; P10124: SRGN; NbExp=10; IntAct=EBI-347996, EBI-744915;
CC O43765; Q86TD4-2: SRL; NbExp=3; IntAct=EBI-347996, EBI-12304565;
CC O43765; E0CX11: STMP1; NbExp=3; IntAct=EBI-347996, EBI-18397783;
CC O43765; P51687: SUOX; NbExp=3; IntAct=EBI-347996, EBI-3921347;
CC O43765; Q9BT88: SYT11; NbExp=7; IntAct=EBI-347996, EBI-751770;
CC O43765; Q9H2B2: SYT4; NbExp=7; IntAct=EBI-347996, EBI-751132;
CC O43765; Q07654: TFF3; NbExp=3; IntAct=EBI-347996, EBI-10224676;
CC O43765; P02786: TFRC; NbExp=6; IntAct=EBI-347996, EBI-355727;
CC O43765; P01135: TGFA; NbExp=3; IntAct=EBI-347996, EBI-1034374;
CC O43765; P01135-2: TGFA; NbExp=6; IntAct=EBI-347996, EBI-12367411;
CC O43765; Q6P9G4: TMEM154; NbExp=3; IntAct=EBI-347996, EBI-13329239;
CC O43765; Q8WUU8: TMEM174; NbExp=6; IntAct=EBI-347996, EBI-10276729;
CC O43765; Q96A57-2: TMEM230; NbExp=3; IntAct=EBI-347996, EBI-17546822;
CC O43765; Q5JXX7: TMEM31; NbExp=3; IntAct=EBI-347996, EBI-10244617;
CC O43765; Q9Y2Y6: TMEM98; NbExp=3; IntAct=EBI-347996, EBI-7333781;
CC O43765; O60235: TMPRSS11D; NbExp=3; IntAct=EBI-347996, EBI-7639969;
CC O43765; Q71RG4: TMUB2; NbExp=3; IntAct=EBI-347996, EBI-2820477;
CC O43765; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-347996, EBI-717441;
CC O43765; O14836: TNFRSF13B; NbExp=3; IntAct=EBI-347996, EBI-519160;
CC O43765; O14836-2: TNFRSF13B; NbExp=8; IntAct=EBI-347996, EBI-12023110;
CC O43765; Q9NS68-2: TNFRSF19; NbExp=3; IntAct=EBI-347996, EBI-12089038;
CC O43765; O75509: TNFRSF21; NbExp=3; IntAct=EBI-347996, EBI-2313231;
CC O43765; O43508: TNFSF12; NbExp=3; IntAct=EBI-347996, EBI-6932080;
CC O43765; Q9C035-3: TRIM5; NbExp=3; IntAct=EBI-347996, EBI-12840050;
CC O43765; Q5BVD1: TTMP; NbExp=6; IntAct=EBI-347996, EBI-10243654;
CC O43765; Q9GZX9: TWSG1; NbExp=3; IntAct=EBI-347996, EBI-10304067;
CC O43765; O95881: TXNDC12; NbExp=3; IntAct=EBI-347996, EBI-2564581;
CC O43765; P11441: UBL4A; NbExp=5; IntAct=EBI-347996, EBI-356983;
CC O43765; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-347996, EBI-947187;
CC O43765; O75631: UPK3A; NbExp=3; IntAct=EBI-347996, EBI-10188907;
CC O43765; P01282: VIP; NbExp=3; IntAct=EBI-347996, EBI-751454;
CC O43765; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-347996, EBI-10316321;
CC O43765; Q8WWY7: WFDC12; NbExp=3; IntAct=EBI-347996, EBI-11958577;
CC O43765; Q8IUB5: WFDC13; NbExp=5; IntAct=EBI-347996, EBI-12041955;
CC O43765; Q8TCV5: WFDC5; NbExp=3; IntAct=EBI-347996, EBI-12175871;
CC O43765; Q8NAP8: ZBTB8B; NbExp=3; IntAct=EBI-347996, EBI-17494306;
CC O43765; O60844: ZG16; NbExp=12; IntAct=EBI-347996, EBI-746479;
CC O43765; Q96DA0: ZG16B; NbExp=3; IntAct=EBI-347996, EBI-953824;
CC O43765; A0A1U9X8X8; NbExp=3; IntAct=EBI-347996, EBI-17234977;
CC O43765; P59635: 7a; Xeno; NbExp=3; IntAct=EBI-347996, EBI-25492879;
CC O43765; P0DTD8: 7b; Xeno; NbExp=3; IntAct=EBI-347996, EBI-25475914;
CC O43765; P0DTD3: 9c; Xeno; NbExp=3; IntAct=EBI-347996, EBI-25475917;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16580629}. Nucleus
CC {ECO:0000269|PubMed:16580629}. Note=Co-localizes with HSP90AB1 in the
CC cytoplasm. Increased nuclear accumulation seen during cell apoptosis.
CC {ECO:0000269|PubMed:16580629}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The second tetratricopeptide repeat (TPR 2) mediates the
CC interaction with SARS-CoV accessory protein 7a.
CC -!- SIMILARITY: Belongs to the SGT family. {ECO:0000305}.
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DR EMBL; AJ223828; CAA11565.1; -; mRNA.
DR EMBL; AJ133129; CAB39725.1; -; mRNA.
DR EMBL; AF408399; AAL01051.1; -; mRNA.
DR EMBL; AF368279; AAP29457.1; -; mRNA.
DR EMBL; AL050156; CAB43297.2; -; mRNA.
DR EMBL; CR533517; CAG38548.1; -; mRNA.
DR EMBL; CR542282; CAG47077.1; -; mRNA.
DR EMBL; AC006538; AAD13117.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69366.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69367.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69368.1; -; Genomic_DNA.
DR EMBL; BC000390; AAH00390.1; -; mRNA.
DR EMBL; BC002989; AAH02989.2; -; mRNA.
DR EMBL; BC005165; AAH05165.1; -; mRNA.
DR EMBL; BC008885; AAH08885.1; -; mRNA.
DR CCDS; CCDS12094.1; -.
DR RefSeq; NP_003012.1; NM_003021.3.
DR RefSeq; XP_011526480.1; XM_011528178.2.
DR PDB; 2VYI; X-ray; 2.40 A; A/B=84-210.
DR PDB; 4CPG; NMR; -; A/B=1-69.
DR PDB; 4GOD; X-ray; 1.40 A; A/B=4-54.
DR PDB; 4GOE; X-ray; 1.45 A; A/B=4-54.
DR PDB; 4GOF; X-ray; 1.35 A; A/B=4-54.
DR PDBsum; 2VYI; -.
DR PDBsum; 4CPG; -.
DR PDBsum; 4GOD; -.
DR PDBsum; 4GOE; -.
DR PDBsum; 4GOF; -.
DR AlphaFoldDB; O43765; -.
DR BMRB; O43765; -.
DR SASBDB; O43765; -.
DR SMR; O43765; -.
DR BioGRID; 112347; 265.
DR IntAct; O43765; 212.
DR MINT; O43765; -.
DR STRING; 9606.ENSP00000221566; -.
DR GlyGen; O43765; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43765; -.
DR PhosphoSitePlus; O43765; -.
DR SwissPalm; O43765; -.
DR BioMuta; SGTA; -.
DR EPD; O43765; -.
DR jPOST; O43765; -.
DR MassIVE; O43765; -.
DR MaxQB; O43765; -.
DR PaxDb; O43765; -.
DR PeptideAtlas; O43765; -.
DR PRIDE; O43765; -.
DR ProteomicsDB; 49156; -.
DR TopDownProteomics; O43765; -.
DR Antibodypedia; 23040; 278 antibodies from 33 providers.
DR DNASU; 6449; -.
DR Ensembl; ENST00000221566.7; ENSP00000221566.1; ENSG00000104969.11.
DR Ensembl; ENST00000676943.1; ENSP00000504495.1; ENSG00000104969.11.
DR Ensembl; ENST00000677149.1; ENSP00000503397.1; ENSG00000104969.11.
DR GeneID; 6449; -.
DR KEGG; hsa:6449; -.
DR MANE-Select; ENST00000221566.7; ENSP00000221566.1; NM_003021.4; NP_003012.1.
DR UCSC; uc002lwi.2; human.
DR CTD; 6449; -.
DR DisGeNET; 6449; -.
DR GeneCards; SGTA; -.
DR HGNC; HGNC:10819; SGTA.
DR HPA; ENSG00000104969; Low tissue specificity.
DR MIM; 603419; gene.
DR neXtProt; NX_O43765; -.
DR OpenTargets; ENSG00000104969; -.
DR PharmGKB; PA35727; -.
DR VEuPathDB; HostDB:ENSG00000104969; -.
DR eggNOG; KOG0553; Eukaryota.
DR GeneTree; ENSGT00940000159037; -.
DR HOGENOM; CLU_044224_0_0_1; -.
DR InParanoid; O43765; -.
DR OMA; MMCNLMS; -.
DR OrthoDB; 687493at2759; -.
DR PhylomeDB; O43765; -.
DR TreeFam; TF313092; -.
DR PathwayCommons; O43765; -.
DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR SignaLink; O43765; -.
DR BioGRID-ORCS; 6449; 18 hits in 1079 CRISPR screens.
DR ChiTaRS; SGTA; human.
DR EvolutionaryTrace; O43765; -.
DR GeneWiki; SGTA; -.
DR GenomeRNAi; 6449; -.
DR Pharos; O43765; Tbio.
DR PRO; PR:O43765; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O43765; protein.
DR Bgee; ENSG00000104969; Expressed in apex of heart and 162 other tissues.
DR ExpressionAtlas; O43765; baseline and differential.
DR Genevisible; O43765; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016020; C:membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0072380; C:TRC complex; IBA:GO_Central.
DR GO; GO:1904288; F:BAT3 complex binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:1903070; P:negative regulation of ER-associated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; IMP:ParkinsonsUK-UCL.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR032374; SGTA_dimer.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF16546; SGTA_dimer; 1.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; TPR repeat.
FT CHAIN 1..313
FT /note="Small glutamine-rich tetratricopeptide repeat-
FT containing protein alpha"
FT /id="PRO_0000106365"
FT REPEAT 91..124
FT /note="TPR 1"
FT REPEAT 125..158
FT /note="TPR 2"
FT REPEAT 159..192
FT /note="TPR 3"
FT REGION 66..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 81
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70593"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 303
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MUTAGEN 38
FT /note="C->A: Reduces tail-anchored proteins transfer."
FT /evidence="ECO:0000269|PubMed:25535373"
FT HELIX 5..21
FT /evidence="ECO:0007829|PDB:4GOF"
FT HELIX 26..43
FT /evidence="ECO:0007829|PDB:4GOF"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:4CPG"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:4CPG"
FT HELIX 87..103
FT /evidence="ECO:0007829|PDB:2VYI"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:2VYI"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:2VYI"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:2VYI"
FT HELIX 159..171
FT /evidence="ECO:0007829|PDB:2VYI"
FT HELIX 175..188
FT /evidence="ECO:0007829|PDB:2VYI"
FT HELIX 193..206
FT /evidence="ECO:0007829|PDB:2VYI"
SQ SEQUENCE 313 AA; 34063 MW; 80B3C71B41F3CB55 CRC64;
MDNKKRLAYA IIQFLHDQLR HGGLSSDAQE SLEVAIQCLE TAFGVTVEDS DLALPQTLPE
IFEAAATGKE MPQDLRSPAR TPPSEEDSAE AERLKTEGNE QMKVENFEAA VHFYGKAIEL
NPANAVYFCN RAAAYSKLGN YAGAVQDCER AICIDPAYSK AYGRMGLALS SLNKHVEAVA
YYKKALELDP DNETYKSNLK IAELKLREAP SPTGGVGSFD IAGLLNNPGF MSMASNLMNN
PQIQQLMSGM ISGGNNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR
SRTPSASNDD QQE
