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Large proline-rich protein BAG6 (BAG family molecular chaperone regulator 6) (BCL2-associated athanogene 6) (BAG-6) (HLA-B-associated transcript 3) (Protein Scythe)

 BAG6_MOUSE              Reviewed;        1154 AA.
Q9Z1R2; Q8SNA3;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
23-MAY-2018, entry version 137.
RecName: Full=Large proline-rich protein BAG6 {ECO:0000305};
AltName: Full=BAG family molecular chaperone regulator 6;
AltName: Full=BCL2-associated athanogene 6 {ECO:0000312|MGI:MGI:1919439};
Short=BAG-6 {ECO:0000303|PubMed:20713601};
AltName: Full=HLA-B-associated transcript 3 {ECO:0000303|PubMed:14656967};
AltName: Full=Protein Scythe {ECO:0000303|PubMed:16287848};
Name=Bag6 {ECO:0000312|MGI:MGI:1919439};
Synonyms=Bat3 {ECO:0000303|PubMed:14656967};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129;
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-1154.
STRAIN=FVB/N; TISSUE=Colon;
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).
[4]
DISRUPTION PHENOTYPE.
PubMed=16287848; DOI=10.1128/MCB.25.23.10329-10337.2005;
Desmots F., Russell H.R., Lee Y., Boyd K., McKinnon P.J.;
"The reaper-binding protein scythe modulates apoptosis and
proliferation during mammalian development.";
Mol. Cell. Biol. 25:10329-10337(2005).
[5]
DISRUPTION PHENOTYPE.
PubMed=17403783; DOI=10.1101/gad.1534107;
Sasaki T., Gan E.C., Wakeham A., Kornbluth S., Mak T.W., Okada H.;
"HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-
mediated acetylation of p53.";
Genes Dev. 21:848-861(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-995, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
FUNCTION, INTERACTION WITH AIFM1, AND SUBCELLULAR LOCATION.
PubMed=18056262; DOI=10.1074/jbc.M706419200;
Desmots F., Russell H.R., Michel D., McKinnon P.J.;
"Scythe regulates apoptosis-inducing factor stability during
endoplasmic reticulum stress-induced apoptosis.";
J. Biol. Chem. 283:3264-3271(2008).
[8]
FUNCTION, AND INTERACTION WITH HSPA2.
PubMed=18678708; DOI=10.1083/jcb.200802113;
Sasaki T., Marcon E., McQuire T., Arai Y., Moens P.B., Okada H.;
"Bat3 deficiency accelerates the degradation of Hsp70-2/HspA2 during
spermatogenesis.";
J. Cell Biol. 182:449-458(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-995, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
FUNCTION.
PubMed=20713601; DOI=10.1083/jcb.200908092;
Minami R., Hayakawa A., Kagawa H., Yanagi Y., Yokosawa H.,
Kawahara H.;
"BAG-6 is essential for selective elimination of defective proteasomal
substrates.";
J. Cell Biol. 190:637-650(2010).
[11]
INTERACTION WITH ZFAND2B.
PubMed=24160817; DOI=10.1042/BJ20130710;
Glinka T., Alter J., Braunstein I., Tzach L., Wei Sheng C.,
Geifman S., Edelmann M.J., Kessler B.M., Stanhill A.;
"Signal-peptide-mediated translocation is regulated by a p97-AIRAPL
complex.";
Biochem. J. 457:253-261(2014).
[12]
INTERACTION WITH ZFAND2B.
PubMed=26337389; DOI=10.1091/mbc.E15-02-0085;
Braunstein I., Zach L., Allan S., Kalies K.U., Stanhill A.;
"Proteasomal degradation of preemptive quality control (pQC)
substrates is mediated by an AIRAPL-p97 complex.";
Mol. Biol. Cell 26:3719-3727(2015).
[13]
INTERACTION WITH ZFAND2B.
PubMed=26876100; DOI=10.1016/j.str.2015.12.017;
Rahighi S., Braunstein I., Ternette N., Kessler B., Kawasaki M.,
Kato R., Matsui T., Weiss T.M., Stanhill A., Wakatsuki S.;
"Selective Binding of AIRAPL Tandem UIMs to Lys48-Linked Tri-Ubiquitin
Chains.";
Structure 24:412-422(2016).
-!- FUNCTION: ATP-independent molecular chaperone preventing the
aggregation of misfolded and hydrophobic patches-containing
proteins (PubMed:18056262, PubMed:18678708, PubMed:20713601).
Functions as part of a cytosolic protein quality control complex,
the BAG6/BAT3 complex, which maintains these client 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:20713601). 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. Client
proteins that cannot be properly delivered to the endoplasmic
reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein
ligase associated with BAG6 and are sorted to the proteasome. SGTA
which prevents the recruitment of RNF126 to BAG6 may negatively
regulate the ubiquitination and the proteasomal degradation of
client proteins. 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. 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 (By similarity). BAG6 is
also required for selective ubiquitin-mediated degradation of
defective nascent chain polypeptides by the proteasome. In this
context, it may participate to the production of antigenic
peptides and play a role in antigen presentation in immune
response (PubMed:20713601). BAG6 is also involved in endoplasmic
reticulum stress-induced pre-emptive quality control, a mechanism
that selectively attenuates the translocation of newly synthesized
proteins into the endoplasmic reticulum and reroutes them to the
cytosol for proteasomal degradation. BAG6 may ensure the proper
degradation of these proteins and thereby protects the endoplasmic
reticulum from protein overload upon stress (By similarity). By
inhibiting the polyubiquitination and subsequent proteasomal
degradation of HSPA2 it may also play a role in the assembly of
the synaptonemal complex during spermatogenesis (PubMed:18678708).
Also positively regulates apoptosis by interacting with and
stabilizing the proapoptotic factor AIFM1 (PubMed:18056262). By
controlling the steady-state expression of the IGF1R receptor,
indirectly regulates the insulin-like growth factor receptor
signaling pathway (By similarity). {ECO:0000250|UniProtKB:P46379,
ECO:0000269|PubMed:18056262, ECO:0000269|PubMed:18678708,
ECO:0000269|PubMed:20713601}.
-!- FUNCTION: Involved in DNA damage-induced apoptosis: following DNA
damage, accumulates in the nucleus and forms a complex with
p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation
leading to increase p53/TP53 transcriptional activity. When
nuclear, may also act as a component of some chromatin regulator
complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).
{ECO:0000250|UniProtKB:P46379}.
-!- FUNCTION: Released extracellularly via exosomes, it is a ligand of
the natural killer/NK cells receptor NCR3 and stimulates NK cells
cytotoxicity. It may thereby trigger NK cells cytotoxicity against
neighboring tumor cells and immature myeloid dendritic cells (DC).
{ECO:0000250|UniProtKB:P46379}.
-!- FUNCTION: May mediate ricin-induced apoptosis.
{ECO:0000250|UniProtKB:P46379}.
-!- SUBUNIT: Component of the BAG6/BAT3 complex, also named BAT3
complex, at least composed of BAG6, UBL4A and GET4/TRC35.
Interacts with GET4; the interaction is direct and localizes BAG6
in the cytosol (By similarity). Interacts with AIFM1
(PubMed:18056262). Interacts with HSPA2 (PubMed:18678708).
Interacts with CTCFL. Interacts with p300/EP300. Interacts (via
ubiquitin-like domain) with RNF126; required for BAG6-dependent
ubiquitination of proteins mislocalized to the cytosol. Interacts
(via ubiquitin-like domain) with SGTA; SGTA competes with RNF126
by binding the same region of BAG6, thereby promoting
deubiquitination of BAG6-target proteins and rescuing them from
degradation. Interacts with ricin A chain. Interacts with VCP and
AMFR; both form the VCP/p97-AMFR/gp78 complex. Interacts with
SYVN1. Interacts with USP13; the interaction is direct and may
mediate UBL4A deubiquitination (By similarity). Interacts with
ZFAND2B (PubMed:24160817, PubMed:26337389, PubMed:26876100).
{ECO:0000250|UniProtKB:P46379, ECO:0000269|PubMed:18056262,
ECO:0000269|PubMed:18678708, ECO:0000269|PubMed:24160817,
ECO:0000269|PubMed:26337389, ECO:0000269|PubMed:26876100}.
-!- INTERACTION:
P11798-2:Camk2a; NbExp=3; IntAct=EBI-644645, EBI-400402;
O35305:Tnfrsf11a; NbExp=4; IntAct=EBI-644645, EBI-647362;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:18056262}. Nucleus
{ECO:0000250|UniProtKB:P46379}. Secreted, exosome
{ECO:0000250|UniProtKB:P46379}. Note=Normally localized in cytosol
and nucleus, it can also be released extracellularly, in exosomes,
by tumor and myeloid dendritic cells.
{ECO:0000250|UniProtKB:P46379}.
-!- DOMAIN: The ubiquitin-like domain mediates interaction with the E3
ubiquitin-protein ligase RNF126 which is responsible for the BAG6-
dependent ubiquitination of client proteins. SGTA also binds this
domain and competes with RNF126 to antagonize client protein
ubiquitination and degradation. The ubiquitin-like domain also
mediates the interaction with USP13.
{ECO:0000250|UniProtKB:P46379}.
-!- PTM: Ricin can induce a cleavage by the caspase CASP3. The
released C-terminal peptide induces apoptosis.
{ECO:0000250|UniProtKB:P46379}.
-!- DISRUPTION PHENOTYPE: Lethality associated with pronounced
developmental defects in the lung, kidney and brain. Lethality is
either embryonic consecutive to abnormal brain development or
perinatal associated with pronounced developmental defects in the
lung and kidney. These developmental defects were associated with
widespread aberrant apoptosis and proliferation. Lethality can be
partially rescued in an ICR genetic background: mice are slightly
smaller in size than their wild-type counterparts and show
impaired genotoxic stress responses. {ECO:0000269|PubMed:16287848,
ECO:0000269|PubMed:17403783}.
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EMBL; AF109719; AAC82479.1; -; Genomic_DNA.
EMBL; CR974444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC026647; AAH26647.1; -; mRNA.
CCDS; CCDS28688.1; -.
RefSeq; NP_476512.1; NM_057171.2.
UniGene; Mm.203962; -.
ProteinModelPortal; Q9Z1R2; -.
SMR; Q9Z1R2; -.
BioGrid; 230309; 7.
DIP; DIP-49391N; -.
IntAct; Q9Z1R2; 8.
MINT; Q9Z1R2; -.
STRING; 10090.ENSMUSP00000025250; -.
iPTMnet; Q9Z1R2; -.
PhosphoSitePlus; Q9Z1R2; -.
EPD; Q9Z1R2; -.
MaxQB; Q9Z1R2; -.
PaxDb; Q9Z1R2; -.
PRIDE; Q9Z1R2; -.
Ensembl; ENSMUST00000025250; ENSMUSP00000025250; ENSMUSG00000024392.
GeneID; 224727; -.
KEGG; mmu:224727; -.
UCSC; uc008cgb.2; mouse.
CTD; 7917; -.
MGI; MGI:1919439; Bag6.
eggNOG; KOG4248; Eukaryota.
eggNOG; ENOG410XS9P; LUCA.
GeneTree; ENSGT00390000016199; -.
HOVERGEN; HBG002193; -.
InParanoid; Q9Z1R2; -.
OMA; PMVAPNA; -.
OrthoDB; EOG091G0XSR; -.
PhylomeDB; Q9Z1R2; -.
TreeFam; TF328437; -.
ChiTaRS; Bag6; mouse.
PRO; PR:Q9Z1R2; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024392; -.
CleanEx; MM_BAT3; -.
ExpressionAtlas; Q9Z1R2; baseline and differential.
Genevisible; Q9Z1R2; MM.
GO; GO:0071818; C:BAT3 complex; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0051787; F:misfolded protein binding; ISO:MGI.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:MGI.
GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:UniProtKB.
GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
GO; GO:0007420; P:brain development; IMP:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0009790; P:embryo development; IMP:UniProtKB.
GO; GO:0061857; P:endoplasmic reticulum stress-induced pre-emptive quality control; ISS:UniProtKB.
GO; GO:0071712; P:ER-associated misfolded protein catabolic process; ISS:UniProtKB.
GO; GO:0002429; P:immune response-activating cell surface receptor signaling pathway; ISO:MGI.
GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISS:UniProtKB.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISS:UniProtKB.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IMP:UniProtKB.
GO; GO:0001822; P:kidney development; IMP:UniProtKB.
GO; GO:0030324; P:lung development; IMP:UniProtKB.
GO; GO:1904378; P:maintenance of unfolded protein involved in ERAD pathway; ISO:MGI.
GO; GO:0030101; P:natural killer cell activation; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0045861; P:negative regulation of proteolysis; IMP:UniProtKB.
GO; GO:1904294; P:positive regulation of ERAD pathway; ISO:MGI.
GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
GO; GO:0007130; P:synaptonemal complex assembly; IMP:UniProtKB.
GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
InterPro; IPR021925; BAG6.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR019954; Ubiquitin_CS.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF12057; DUF3538; 1.
Pfam; PF00240; ubiquitin; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS00299; UBIQUITIN_1; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; Chaperone; Chromatin regulator;
Complete proteome; Cytoplasm; Differentiation; Immunity; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Secreted; Spermatogenesis;
Transport.
CHAIN 1 1154 Large proline-rich protein BAG6.
/FTId=PRO_0000114898.
DOMAIN 17 92 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
REPEAT 237 271 1. {ECO:0000250|UniProtKB:P46379}.
REPEAT 416 444 2. {ECO:0000250|UniProtKB:P46379}.
REPEAT 597 624 3. {ECO:0000250|UniProtKB:P46379}.
REPEAT 630 658 4. {ECO:0000250|UniProtKB:P46379}.
REGION 237 658 4 X 29 AA approximate repeats.
{ECO:0000250|UniProtKB:P46379}.
REGION 1044 1154 Mediates interaction with UBL4A and GET4
and is sufficient for the delivery of
client proteins to the endoplasmic
reticulum.
{ECO:0000250|UniProtKB:P46379}.
COMPBIAS 196 274 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
COMPBIAS 395 720 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
COMPBIAS 564 610 Ala-rich.
SITE 1023 1024 Cleavage; by CASP3.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 96 96 Phosphoserine.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 117 117 Phosphothreonine.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 986 986 Phosphoserine.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 995 995 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1075 1075 Phosphothreonine.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 1103 1103 Phosphoserine.
{ECO:0000250|UniProtKB:P46379}.
MOD_RES 1139 1139 Phosphoserine.
{ECO:0000250|UniProtKB:P46379}.
CONFLICT 528 528 Missing (in Ref. 3; AAH26647).
{ECO:0000305}.
CONFLICT 1012 1012 P -> S (in Ref. 3; AAH26647).
{ECO:0000305}.
SEQUENCE 1154 AA; 121037 MW; 7F3FD14DF5AC1211 CRC64;
MEPSDSASTA MEEPDSLEVL VKTLDSQTRT FIVGAQMNVK EFKEHIAASV SIPSEKQRLI
YQGRVLQDDK KLQEYNVGGK VIHLVERAPP QTQLPSGASS GTGSASATHG GAPLPGTRGP
GASVHDRNAN SYVMVGTFNL PSDGSAVDVH INMEQAPIQS EPRVRLVMAQ HMIRDIQTLL
SRMECRGGTQ AQASQPPPQT PQTVASETVA LNSQTSEPVE SEAPPREPME SEEMEERPPT
QTPELAPSGP APAGPAPAGP APAPETNAPN HPSPAEHVEV LQELQRLQRR LQPFLQRYCE
VLGAAATTDY NNNHEGREED QRLINLVGES LRLLGNTFVA LSDLRCNLAC APPRHLHVVR
PMSHYTTPMV LQQAAIPIQI NVGTTVTMTG NGARPPPAPG AEAATPGSAQ ATSLPPSSTT
VDSSTEGAPP PGPAPPPASS HPRVIRISHQ SVEPVVMMHM NIQDSGAQPG GVPSAPTGPL
GPPGHGQTLG QQVPGFPTAP TRVVIARPTP PQARPSHPGG PPVSGALQGA GLGTNTSLAQ
MVSGLVGQLL MQPVLVAQGT PGMAQAQAQA QAQAQAQAQA PAPAPAPAPA PATASASAGT
TNTATTAGPA PGGPAQPPPP QPSAADLQFS QLLGNLLGPA GPGAGGPGMA SPTITVAMPG
VPAFLQGMTD FLQASQTAPP PPPPPPPPPP APEQQSTPPP GSPSGGTASP GGLGPESLPP
EFFTSVVQGV LSSLLGSLGA RAGSSESIAA FIQRLSGSSN IFEPGADGAL GFFGALLSLL
CQNFSMVDVV MLLHGHFQPL QRLQPQLRSF FHQHYLGGQE PTPSNIRMAT HTLITGLEEY
VRESFSLVQV QPGVDIIRTN LEFLQEQFNS IAAHVLHCTD SGFGARLLEL CNQGLFECLA
LNLHCLGGQQ MELAAVINGR IRRMSRGVNP SLVSWLTTMM GLRLQVVLEH MPVGPDAILR
YVRRVGDPPQ TLPEEPMEVQ GAERTSPEPQ RENASPAPGT TAEEAMSRGP PPAPEGGSRD
EQDGASADAE PWAAAVPPEW VPIIQQDIQS QRKVKPQPPL SDAYLSGMPA KRRKTMQGEG
PQLLLSEAVS RAAKAAGARP LTSPESLSRD LEAPEVQESY RQQLRSDIQK RLQEDPNYSP
QRFPNAHRAF ADDP


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EIAAB30895 Apoptosis-associated nuclear protein,Homo sapiens,Human,PHLDA1,PHRIP,Pleckstrin homology-like domain family A member 1,PQR protein,PQ-rich protein,Proline- and glutamine-rich protein,Proline- and hist
EIAAB32455 Homo sapiens,Human,Lacrimal proline-rich protein,LPRP,Nasopharyngeal carcinoma-associated proline-rich protein 4,PROL4,Proline-rich protein 4,PRR4
27-631 LHX6 is a member of a large protein family that contains the LIM domain, a unique cysteine-rich zinc-binding domain. The encoded protein may function as a transcriptional regulator and may be involved 0.1 mg
25-066 LHX4 is a member of a large protein family which contains the LIM domain, a unique cysteine-rich zinc-binding domain. The encoded protein may function as a transcriptional regulator and be involved in 0.05 mg
EIAAB30896 Mouse,Mus musculus,Phlda1,Pleckstrin homology-like domain family A member 1,PQR protein,PQ-rich protein,Proline- and glutamine-rich protein,T-cell death-associated gene 51 protein,Tdag51
CE40 BAG Family Molecular Chaperone Regulator 2 BAG2 500
CE40 BAG Family Molecular Chaperone Regulator 2 BAG2 lmg
EIAAB30897 Phlda1,Pleckstrin homology-like domain family A member 1,Pqr,PQR protein,PQ-rich protein,Proline- and glutamine-rich protein,Rat,Rattus norvegicus
CE40 Human BAG Family Molecular Chaperone Regulator 2 BAG2 l0
CSB-EL002529RA Rat BAG family molecular chaperone regulator 1(BAG1) ELISA kit 96T
BAG3_HUMAN Human ELISA Kit FOR BAG family molecular chaperone regulator 3 96T
C103 Human BAG Family Molecular Chaperone Regulator 2 BAG2 50
E14188c Bovine ELISA Kit FOR BAG family molecular chaperone regulator 5 96T
CSB-EL002533RA Rat BAG family molecular chaperone regulator 5(BAG5) ELISA kit 96T
EIAAB32271 Basic salivary proline-rich protein 4,Homo sapiens,Human,Parotid o protein,PRB4,Salivary proline-rich protein II-1,Salivary proline-rich protein Po
CSB-EL002532HU Human BAG family molecular chaperone regulator 4(BAG4) ELISA kit 96T
CSB-EL002531HU Human BAG family molecular chaperone regulator 3(BAG3) ELISA kit 96T
CSB-EL002533HU Human BAG family molecular chaperone regulator 5(BAG5) ELISA kit 96T
abx109563 Polyclonal Rabbit BAG family molecular chaperone regulator 3 Antibody 100 μg


 

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