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Golgi to ER traffic protein 4 homolog (Conserved edge-expressed protein) (Transmembrane domain recognition complex 35 kDa subunit) (TRC35)

 GET4_HUMAN              Reviewed;         327 AA.
Q7L5D6; A4D2Q1; B3KNC7; Q9UFC9; Q9Y309;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
18-JUL-2018, entry version 123.
RecName: Full=Golgi to ER traffic protein 4 homolog {ECO:0000305};
AltName: Full=Conserved edge-expressed protein;
AltName: Full=Transmembrane domain recognition complex 35 kDa subunit;
Short=TRC35;
Name=GET4 {ECO:0000312|HGNC:HGNC:21690}; Synonyms=C7orf20, CEE, TRC35;
ORFNames=CGI-20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Ovary, Testis, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-14 AND 111-122, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Lung carcinoma;
Bienvenut W.V., Vousden K.H., Lukashchuk N.;
Submitted (MAR-2008) to UniProtKB.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-327 (ISOFORM 1).
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[7]
IDENTIFICATION.
PubMed=18249086; DOI=10.1016/j.ygeno.2007.10.017;
Fernandes J.M.O., Macqueen D.J., Lee H.-T., Johnston I.A.;
"Genomic, evolutionary, and expression analyses of cee, an ancient
gene involved in normal growth and development.";
Genomics 91:315-325(2008).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
AND IDENTIFICATION IN THE BAG6/BAT3 COMPLEX.
PubMed=20676083; DOI=10.1038/nature09296;
Mariappan M., Li X., Stefanovic S., Sharma A., Mateja A., Keenan R.J.,
Hegde R.S.;
"A ribosome-associating factor chaperones tail-anchored membrane
proteins.";
Nature 466:1120-1124(2010).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
FUNCTION, INTERACTION WITH BAG6, AND SUBCELLULAR LOCATION.
PubMed=21636303; DOI=10.1016/j.molcel.2011.05.010;
Wang Q., Liu Y., Soetandyo N., Baek K., Hegde R., Ye Y.;
"A ubiquitin ligase-associated chaperone holdase maintains
polypeptides in soluble states for proteasome degradation.";
Mol. Cell 42:758-770(2011).
[12]
FUNCTION.
PubMed=21743475; DOI=10.1038/nature10181;
Hessa T., Sharma A., Mariappan M., Eshleman H.D., Gutierrez E.,
Hegde R.S.;
"Protein targeting and degradation are coupled for elimination of
mislocalized proteins.";
Nature 475:394-397(2011).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
INTERACTION WITH BAG6, IDENTIFICATION IN THE BAG6/BAT3 COMPLEX,
FUNCTION, AND MUTAGENESIS OF ASP-84.
PubMed=25535373; DOI=10.1073/pnas.1402745112;
Mock J.Y., Chartron J.W., Zaslaver M., Xu Y., Ye Y., Clemons W.M. Jr.;
"Bag6 complex contains a minimal tail-anchor-targeting module and a
mock BAG domain.";
Proc. Natl. Acad. Sci. U.S.A. 112:106-111(2015).
[18]
FUNCTION.
PubMed=28104892; DOI=10.1126/science.aah6130;
Shao S., Rodrigo-Brenni M.C., Kivlen M.H., Hegde R.S.;
"Mechanistic basis for a molecular triage reaction.";
Science 355:298-302(2017).
[19] {ECO:0000244|PDB:6AU8}
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 23-305 IN COMPLEX WITH BAG6,
SUBCELLULAR LOCATION, INTERACTION WITH BAG6, MUTAGENESIS OF TYR-182;
PHE-188; PHE-195; TRP-241; PHE-242; VAL-257; LEU-258; CYS-259; TYR-262
AND LEU-266, AND UBIQUITINATION BY RNF126.
PubMed=29042515; DOI=10.1073/pnas.1702940114;
Mock J.Y., Xu Y., Ye Y., Clemons W.M. Jr.;
"Structural basis for regulation of the nucleo-cytoplasmic
distribution of Bag6 by TRC35.";
Proc. Natl. Acad. Sci. U.S.A. 114:11679-11684(2017).
-!- FUNCTION: As part of a cytosolic protein quality control complex,
the BAG6/BAT3 complex, maintains misfolded and hydrophobic
patches-containing proteins in a soluble state and participates to
their proper delivery to the endoplasmic reticulum or
alternatively can promote their sorting to the proteasome where
they undergo degradation (PubMed:20676083, PubMed:21636303,
PubMed:21743475, PubMed:28104892). The BAG6/BAT3 complex is
involved in the post-translational delivery of tail-anchored/type
II transmembrane proteins to the endoplasmic reticulum membrane.
Recruited to ribosomes, it interacts with the transmembrane region
of newly synthesized tail-anchored proteins and together with SGTA
and ASNA1 mediates their delivery to the endoplasmic reticulum
(PubMed:20676083, PubMed:28104892, PubMed:25535373). Client
proteins that cannot be properly delivered to the endoplasmic
reticulum are ubiquitinated and sorted to the proteasome
(PubMed:28104892). Similarly, the BAG6/BAT3 complex also functions
as a sorting platform for proteins of the secretory pathway that
are mislocalized to the cytosol either delivering them to the
proteasome for degradation or to the endoplasmic reticulum
(PubMed:21743475). The BAG6/BAT3 complex also plays a role in the
endoplasmic reticulum-associated degradation (ERAD), a quality
control mechanism that eliminates unwanted proteins of the
endoplasmic reticulum through their retrotranslocation to the
cytosol and their targeting to the proteasome. It maintains these
retrotranslocated proteins in an unfolded yet soluble state
condition in the cytosol to ensure their proper delivery to the
proteasome (PubMed:21636303). {ECO:0000269|PubMed:20676083,
ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:21743475,
ECO:0000269|PubMed:25535373, ECO:0000269|PubMed:28104892}.
-!- SUBUNIT: Component of the BAG6/BAT3 complex, at least composed of
BAG6, UBL4A and GET4/TRC35 (PubMed:20676083, PubMed:25535373).
Interacts with BAG6; the interaction is direct and localizes BAG6
to the cytosol (PubMed:21636303, PubMed:29042515,
PubMed:25535373). {ECO:0000269|PubMed:20676083,
ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:25535373,
ECO:0000269|PubMed:29042515}.
-!- INTERACTION:
O43681:ASNA1; NbExp=3; IntAct=EBI-711823, EBI-2515857;
O43741:PRKAB2; NbExp=6; IntAct=EBI-711823, EBI-1053424;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303,
ECO:0000269|PubMed:29042515}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q7L5D6-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=Q7L5D6-2; Sequence=VSP_017652;
-!- PTM: Ubiquitinated by RNF12, leading to proteasomal degradation.
When unassembled from BAG6; ubiquitinylation is modulated by BAG6
quality control role and effectuated by RNF126.
{ECO:0000269|PubMed:29042515}.
-!- SIMILARITY: Belongs to the GET4 family. {ECO:0000305}.
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EMBL; AK024305; BAG51289.1; -; mRNA.
EMBL; AK097899; BAG53546.1; -; mRNA.
EMBL; AK125863; BAG54258.1; -; mRNA.
EMBL; AL133014; CAB61355.1; -; mRNA.
EMBL; CH236965; EAL23708.1; -; Genomic_DNA.
EMBL; BC003550; AAH03550.2; -; mRNA.
EMBL; AF132954; AAD27729.1; -; mRNA.
CCDS; CCDS5317.1; -. [Q7L5D6-1]
PIR; T42648; T42648.
RefSeq; NP_057033.2; NM_015949.2. [Q7L5D6-1]
UniGene; Hs.107387; -.
UniGene; Hs.743756; -.
PDB; 6AU8; X-ray; 1.80 A; A=23-305.
PDBsum; 6AU8; -.
ProteinModelPortal; Q7L5D6; -.
SMR; Q7L5D6; -.
BioGrid; 119636; 64.
ComplexPortal; CPX-132; BAT3 complex.
IntAct; Q7L5D6; 49.
MINT; Q7L5D6; -.
STRING; 9606.ENSP00000265857; -.
MoonDB; Q7L5D6; Predicted.
iPTMnet; Q7L5D6; -.
PhosphoSitePlus; Q7L5D6; -.
BioMuta; GET4; -.
DMDM; 74738593; -.
EPD; Q7L5D6; -.
MaxQB; Q7L5D6; -.
PaxDb; Q7L5D6; -.
PeptideAtlas; Q7L5D6; -.
PRIDE; Q7L5D6; -.
ProteomicsDB; 68807; -.
ProteomicsDB; 68808; -. [Q7L5D6-2]
DNASU; 51608; -.
Ensembl; ENST00000265857; ENSP00000265857; ENSG00000239857. [Q7L5D6-1]
Ensembl; ENST00000407192; ENSP00000385646; ENSG00000239857. [Q7L5D6-2]
GeneID; 51608; -.
KEGG; hsa:51608; -.
UCSC; uc003sjl.2; human. [Q7L5D6-1]
CTD; 51608; -.
EuPathDB; HostDB:ENSG00000239857.6; -.
GeneCards; GET4; -.
H-InvDB; HIX0033841; -.
H-InvDB; HIX0201122; -.
HGNC; HGNC:21690; GET4.
HPA; HPA019765; -.
MIM; 612056; gene.
neXtProt; NX_Q7L5D6; -.
OpenTargets; ENSG00000239857; -.
PharmGKB; PA165618100; -.
eggNOG; KOG3024; Eukaryota.
eggNOG; ENOG410XRWE; LUCA.
GeneTree; ENSGT00390000015750; -.
HOGENOM; HOG000264232; -.
HOVERGEN; HBG059877; -.
InParanoid; Q7L5D6; -.
OMA; QMYRTLF; -.
OrthoDB; EOG091G0DTD; -.
PhylomeDB; Q7L5D6; -.
TreeFam; TF315163; -.
GeneWiki; C7orf20; -.
GenomeRNAi; 51608; -.
PRO; PR:Q7L5D6; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000239857; -.
CleanEx; HS_C7orf20; -.
ExpressionAtlas; Q7L5D6; baseline and differential.
Genevisible; Q7L5D6; HS.
GO; GO:0071818; C:BAT3 complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
GO; GO:0051220; P:cytoplasmic sequestering of protein; IMP:ParkinsonsUK-UCL.
GO; GO:1904378; P:maintenance of unfolded protein involved in ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; IDA:UniProtKB.
Gene3D; 1.25.40.10; -; 1.
InterPro; IPR011990; TPR-like_helical_dom_sf.
InterPro; IPR007317; UPF0363.
PANTHER; PTHR12875; PTHR12875; 1.
Pfam; PF04190; DUF410; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Phosphoprotein;
Reference proteome; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
CHAIN 2 327 Golgi to ER traffic protein 4 homolog.
/FTId=PRO_0000228104.
REGION 195 271 Interacts with BAG6.
{ECO:0000269|PubMed:25535373,
ECO:0000269|PubMed:29042515}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.5}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 53 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_017652.
MUTAGEN 84 84 D->K: Reduces tail-anchored protein
delivery. {ECO:0000269|PubMed:25535373}.
MUTAGEN 182 182 Y->A: No effect on interaction with BAG6.
{ECO:0000269|PubMed:29042515}.
MUTAGEN 188 188 F->A: No effect on interaction with BAG6.
{ECO:0000269|PubMed:29042515}.
MUTAGEN 195 195 F->A: No effect on interaction with BAG6.
{ECO:0000269|PubMed:29042515}.
MUTAGEN 241 241 W->A: No effect on interaction with BAG6.
{ECO:0000269|PubMed:29042515}.
MUTAGEN 242 242 F->A: No effect on interaction with BAG6.
{ECO:0000269|PubMed:29042515}.
MUTAGEN 257 257 V->A: No effect on interaction with BAG6.
{ECO:0000269|PubMed:29042515}.
MUTAGEN 258 258 L->A: No effect on interaction with BAG6.
{ECO:0000269|PubMed:29042515}.
MUTAGEN 259 259 C->A: No effect on interaction with BAG6.
{ECO:0000269|PubMed:29042515}.
MUTAGEN 262 262 Y->A: Inhibits interaction with BAG6.
{ECO:0000269|PubMed:29042515}.
MUTAGEN 266 266 L->A: No effect on interaction with BAG6.
{ECO:0000269|PubMed:29042515}.
CONFLICT 9 22 EQESARNGGRNRGG -> DRRAPATALQPRA (in Ref.
6; AAD27729). {ECO:0000305}.
CONFLICT 177 177 N -> D (in Ref. 6; AAD27729).
{ECO:0000305}.
HELIX 26 35 {ECO:0000244|PDB:6AU8}.
HELIX 39 55 {ECO:0000244|PDB:6AU8}.
HELIX 59 75 {ECO:0000244|PDB:6AU8}.
HELIX 79 95 {ECO:0000244|PDB:6AU8}.
HELIX 102 114 {ECO:0000244|PDB:6AU8}.
HELIX 120 133 {ECO:0000244|PDB:6AU8}.
HELIX 143 155 {ECO:0000244|PDB:6AU8}.
HELIX 159 167 {ECO:0000244|PDB:6AU8}.
HELIX 172 186 {ECO:0000244|PDB:6AU8}.
HELIX 189 191 {ECO:0000244|PDB:6AU8}.
HELIX 192 205 {ECO:0000244|PDB:6AU8}.
HELIX 209 222 {ECO:0000244|PDB:6AU8}.
HELIX 235 248 {ECO:0000244|PDB:6AU8}.
HELIX 252 261 {ECO:0000244|PDB:6AU8}.
HELIX 263 266 {ECO:0000244|PDB:6AU8}.
HELIX 272 284 {ECO:0000244|PDB:6AU8}.
HELIX 294 298 {ECO:0000244|PDB:6AU8}.
HELIX 301 303 {ECO:0000244|PDB:6AU8}.
SEQUENCE 327 AA; 36504 MW; 4D6C4233181B0512 CRC64;
MAAAAAMAEQ ESARNGGRNR GGVQRVEGKL RASVEKGDYY EAHQMYRTLF FRYMSQSKHT
EARELMYSGA LLFFSHGQQN SAADLSMLVL ESLEKAEVEV ADELLENLAK VFSLMDPNSP
ERVTFVSRAL KWSSGGSGKL GHPRLHQLLA LTLWKEQNYC ESRYHFLHSA DGEGCANMLV
EYSTSRGFRS EVDMFVAQAV LQFLCLKNKS SASVVFTTYT QKHPSIEDGP PFVEPLLNFI
WFLLLAVDGG KLTVFTVLCE QYQPSLRRDP MYNEYLDRIG QLFFGVPPKQ TSSYGGLLGN
LLTSLMGSSE QEDGEESPSD GSPIELD


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