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Myb-binding protein 1A (Myb-binding protein of 160 kDa)

 MBB1A_MOUSE             Reviewed;        1344 AA.
Q7TPV4; O35851; Q80Y66; Q8R4X2; Q99KP0;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 2.
10-OCT-2018, entry version 142.
RecName: Full=Myb-binding protein 1A;
AltName: Full=Myb-binding protein of 160 kDa;
Name=Mybbp1a; Synonyms=P160;
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 [MRNA], PROTEIN SEQUENCE OF 43-53; 205-211;
286-290; 458-465 AND 488-496, FUNCTION, INTERACTION WITH JUN AND MYB,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9447996; DOI=10.1128/MCB.18.2.989;
Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A.,
Gilbert D.J., Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A.,
Ishii S., Gonda T.J.;
"Molecular cloning reveals that the p160 Myb-binding protein is a
novel, predominantly nucleolar protein which may play a role in
transactivation by Myb.";
Mol. Cell. Biol. 18:989-1002(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Keough R.A., Gonda T.J.;
"Structural organization of the murine myb-binding protein p160
(Mybbp1a) gene.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C3H/He; TISSUE=Eye, Mammary gland, and Osteoblast;
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]
PARTIAL PROTEIN SEQUENCE, FUNCTION, AND INTERACTION WITH AHR.
PubMed=11956195; DOI=10.1074/jbc.M200740200;
Jones L.C., Okino S.T., Gonda T.J., Whitlock J.P. Jr.;
"Myb-binding protein 1a augments AhR-dependent gene expression.";
J. Biol. Chem. 277:22515-22519(2002).
[6]
SUBCELLULAR LOCATION, INTERACTION WITH KPNA2, MUTAGENESIS OF LEU-249;
VAL-251; LEU-272 AND LEU-274, AND DOMAINS NES AND NLS.
PubMed=12941609; DOI=10.1016/S0014-4827(03)00262-3;
Keough R.A., Macmillan E.M., Lutwyche J.K., Gardner J.M., Tavner F.J.,
Jans D.A., Henderson B.R., Gonda T.J.;
"Myb-binding protein 1a is a nucleocytoplasmic shuttling protein that
utilizes CRM1-dependent and independent nuclear export pathways.";
Exp. Cell Res. 289:108-123(2003).
[7]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
PPARGC1A.
PubMed=14744933; DOI=10.1101/gad.1152204;
Fan M., Rhee J., St Pierre J., Handschin C., Puigserver P., Lin J.,
Jaeger S., Erdjument-Bromage H., Tempst P., Spiegelman B.M.;
"Suppression of mitochondrial respiration through recruitment of p160
myb binding protein to PGC-1alpha: modulation by p38 MAPK.";
Genes Dev. 18:278-289(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1277 AND SER-1280, 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1253 AND SER-1280, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-1253, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CLOCK AND CRY1.
PubMed=19129230; DOI=10.1093/nar/gkn1013;
Hara Y., Onishi Y., Oishi K., Miyazaki K., Fukamizu A., Ishida N.;
"Molecular characterization of Mybbp1a as a co-repressor on the
Period2 promoter.";
Nucleic Acids Res. 37:1115-1126(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1164; SER-1244;
SER-1253; THR-1256; THR-1277; SER-1280; SER-1323 AND SER-1325, 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).
[15]
CITRULLINATION AT ARG-1322.
PubMed=24463520; DOI=10.1038/nature12942;
Christophorou M.A., Castelo-Branco G., Halley-Stott R.P.,
Oliveira C.S., Loos R., Radzisheuskaya A., Mowen K.A., Bertone P.,
Silva J.C., Zernicka-Goetz M., Nielsen M.L., Gurdon J.B.,
Kouzarides T.;
"Citrullination regulates pluripotency and histone H1 binding to
chromatin.";
Nature 507:104-108(2014).
-!- FUNCTION: May activate or repress transcription via interactions
with sequence specific DNA-binding proteins (PubMed:9447996,
PubMed:11956195, PubMed:14744933). Repression may be mediated at
least in part by histone deacetylase activity (HDAC activity)
(PubMed:14744933). Acts as a corepressor and in concert with CRY1,
represses the transcription of the core circadian clock component
PER2 (PubMed:19129230). Preferentially binds to dimethylated
histone H3 'Lys-9' (H3K9me2) on the PER2 promoter
(PubMed:19129230). Has a role in rRNA biogenesis together with
PWP1 (By similarity). {ECO:0000250|UniProtKB:Q9BQG0,
ECO:0000269|PubMed:11956195, ECO:0000269|PubMed:14744933,
ECO:0000269|PubMed:19129230, ECO:0000269|PubMed:9447996}.
-!- SUBUNIT: Component of the B-WICH complex, at least composed of
SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and
DDX21 (By similarity). Binds to and represses JUN and MYB via the
leucine zipper regions present in these proteins. Also binds to
and represses PPARGC1A: this interaction is abrogated when
PPARGC1A is phosphorylated by MAPK1/ERK. Binds to and stimulates
transcription by AHR. Binds to KPNA2. Interacts with CLOCK and
CRY1. {ECO:0000250|UniProtKB:Q9BQG0, ECO:0000269|PubMed:11956195,
ECO:0000269|PubMed:12941609, ECO:0000269|PubMed:14744933,
ECO:0000269|PubMed:19129230, ECO:0000269|PubMed:9447996}.
-!- INTERACTION:
P12813:Nr4a1; NbExp=3; IntAct=EBI-1373622, EBI-10896863;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12941609}.
Nucleus, nucleolus {ECO:0000269|PubMed:12941609,
ECO:0000269|PubMed:19129230}. Cytoplasm
{ECO:0000269|PubMed:12941609}. Note=Predominantly nucleolar. Also
shuttles between the nucleus and cytoplasm. Nuclear import may be
mediated by KPNA2, while export appears to depend partially on
XPO1/CRM1. {ECO:0000269|PubMed:12941609}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:9447996}.
-!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
-!- SIMILARITY: Belongs to the MYBBP1A family. {ECO:0000305}.
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EMBL; U63648; AAC39954.1; -; mRNA.
EMBL; AF345640; AAL83748.1; -; Genomic_DNA.
EMBL; AL662812; CAI52004.1; -; Genomic_DNA.
EMBL; BC004078; AAH04078.1; -; mRNA.
EMBL; BC048858; AAH48858.1; -; mRNA.
EMBL; BC052889; AAH52889.1; -; mRNA.
CCDS; CCDS24986.1; -.
PIR; T34188; T34188.
RefSeq; NP_058056.2; NM_016776.2.
UniGene; Mm.147946; -.
ProteinModelPortal; Q7TPV4; -.
SMR; Q7TPV4; -.
BioGrid; 201999; 17.
ComplexPortal; CPX-1133; B-WICH chromatin remodelling complex.
CORUM; Q7TPV4; -.
DIP; DIP-39831N; -.
IntAct; Q7TPV4; 17.
MINT; Q7TPV4; -.
STRING; 10090.ENSMUSP00000044827; -.
iPTMnet; Q7TPV4; -.
PhosphoSitePlus; Q7TPV4; -.
SwissPalm; Q7TPV4; -.
EPD; Q7TPV4; -.
MaxQB; Q7TPV4; -.
PaxDb; Q7TPV4; -.
PRIDE; Q7TPV4; -.
Ensembl; ENSMUST00000045633; ENSMUSP00000044827; ENSMUSG00000040463.
GeneID; 18432; -.
KEGG; mmu:18432; -.
UCSC; uc007jyy.1; mouse.
CTD; 10514; -.
MGI; MGI:106181; Mybbp1a.
eggNOG; KOG1926; Eukaryota.
eggNOG; ENOG410YFVF; LUCA.
GeneTree; ENSGT00390000017457; -.
HOGENOM; HOG000113488; -.
HOVERGEN; HBG081961; -.
InParanoid; Q7TPV4; -.
KO; K02331; -.
OMA; RDFQIRV; -.
OrthoDB; EOG091G00YE; -.
PhylomeDB; Q7TPV4; -.
TreeFam; TF317401; -.
Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
ChiTaRS; Mybbp1a; mouse.
PMAP-CutDB; Q7TPV4; -.
PRO; PR:Q7TPV4; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000040463; Expressed in 315 organ(s), highest expression level in 4-8 cell stage embryo.
CleanEx; MM_MYBBP1A; -.
ExpressionAtlas; Q7TPV4; baseline and differential.
Genevisible; Q7TPV4; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070888; F:E-box binding; IPI:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; TAS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI.
GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:2000210; P:positive regulation of anoikis; ISO:MGI.
GO; GO:0071158; P:positive regulation of cell cycle arrest; ISO:MGI.
GO; GO:0022904; P:respiratory electron transport chain; IDA:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR007015; DNA_pol_V/MYBBP1A.
PANTHER; PTHR13213; PTHR13213; 1.
Pfam; PF04931; DNA_pol_phi; 1.
SUPFAM; SSF48371; SSF48371; 3.
1: Evidence at protein level;
Acetylation; Activator; Biological rhythms; Citrullination;
Complete proteome; Cytoplasm; Direct protein sequencing;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
Repressor; Ribosome biogenesis; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19131326}.
CHAIN 2 1344 Myb-binding protein 1A.
/FTId=PRO_0000096256.
REGION 2 580 Interaction with MYB.
{ECO:0000269|PubMed:9447996}.
REGION 1152 1344 Required for nuclear and nucleolar
localization.
{ECO:0000269|PubMed:12941609}.
MOTIF 238 256 Nuclear export signal 1.
{ECO:0000269|PubMed:12941609}.
MOTIF 261 279 Nuclear export signal 2.
{ECO:0000269|PubMed:12941609}.
COMPBIAS 698 752 Asp-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 69 69 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9BQG0}.
MOD_RES 156 156 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9BQG0}.
MOD_RES 1160 1160 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BQG0}.
MOD_RES 1164 1164 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1187 1187 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BQG0}.
MOD_RES 1191 1191 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9BQG0}.
MOD_RES 1219 1219 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BQG0}.
MOD_RES 1244 1244 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1251 1251 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9BQG0}.
MOD_RES 1253 1253 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1256 1256 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1277 1277 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1280 1280 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1303 1303 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BQG0}.
MOD_RES 1318 1318 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BQG0}.
MOD_RES 1322 1322 Citrulline.
{ECO:0000269|PubMed:24463520}.
MOD_RES 1323 1323 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1325 1325 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1329 1329 Phosphoserine.
{ECO:0000250|UniProtKB:Q9BQG0}.
CROSSLNK 1149 1149 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9BQG0}.
MUTAGEN 249 249 L->A: Reduced nuclear export; when
associated with A-251.
{ECO:0000269|PubMed:12941609}.
MUTAGEN 251 251 V->A: Reduced nuclear export; when
associated with A-249.
{ECO:0000269|PubMed:12941609}.
MUTAGEN 272 272 L->A: Reduced nuclear export; when
associated with A-274.
{ECO:0000269|PubMed:12941609}.
MUTAGEN 274 274 L->A: Reduced nuclear export; when
associated with A-272.
{ECO:0000269|PubMed:12941609}.
CONFLICT 87 87 R -> T (in Ref. 1; AAC39954 and 2;
AAL83748). {ECO:0000305}.
CONFLICT 88 88 P -> A (in Ref. 1; AAC39954).
{ECO:0000305}.
CONFLICT 505 508 DRNR -> HASG (in Ref. 4; AAH04078).
{ECO:0000305}.
CONFLICT 1282 1282 I -> V (in Ref. 4; AAH52889).
{ECO:0000305}.
SEQUENCE 1344 AA; 152037 MW; 64D3420981CD0767 CRC64;
MAEMKSPTKA EPATPAEAAQ SDRHSLLEHS REFLDFFWDI AKPDQETRLR ATEKLLEYLR
TRPNDSEMKY ALKRLITGLG VGREAARPCY SLALAQLLQS FEDIPLCDIL DQIQEKYSLQ
AMNKAMMRPS LFANLFGVLA LFQSGRLVKD KEALMKSVQL LKILSQHPNH LQGQPIKALV
DILSEVPESM FQEILPKVLK GNMKVILRSP KYLELFLLAK QRVPTKLESL MGSVDLFSED
NIPSLVNILK VAANSVKKEH KLPNVALDLL RLALKESRFE LFWKKVLEEG LLKNPSWTSS
YMCFRLLGAS LPLLSEEQLQ LVMRGDLIRH FGENMVISKP QNLFKIIPEI STYVGTFLEG
CQDDPKRQLT MMVAFTTITN QGLPVMPTFW RVTRFLNAEA LQSYVAWLRD MFLQPDLNSL
VDFSTANQKR AQDASLNVPE RAVFRLRKWI IHRLVSLVDH LHLEKDEAVV EQIARFCLFH
AFFKTKKATP QIPETKQHFS FPLDDRNRGV FVSAFFSLLQ TLSVKFRQTP DLAENGKPWT
YRLVQLADML LNHNRNVTSV TSLTTQQRQA WDQMMSTLKE LEARSSETRA IAFQHLLLLV
GLHIFKSPAE SCDVLGDIQT CIKKSMEQNP RRSRSRAKAS QEPVWVEVMV EILLSLLAQP
SNLMRQVVRS VFGHICPHLT PRCLQLILAV LSPVTNEDED DNVVVTDDAD EKQLQHGEDE
DSDNEDNKNS ESDMDSEDGE ESEEEDRDKD VDPGFRQQLM EVLKAGNALG GVDNEEEEEL
GDEAMMALDQ NLASLFKEQK MRIQARNEEK NKLQKEKKLR RDFQIRALDL IEVLVTKQPE
HPLILELLEP LLNVIQHSMR SKGSTKQEQD LLHKTARIFM HHLCRARRYC HEVGPCAEAL
HAQVERLVQQ AGSQADASVA LYYFNASLYL LRVLKGNTNK RHQDGHKLHG ADTEDSEDQA
ANCLDLDFVT RVYSASLESL LTKRNSSLTV PMFLSLFSRY PVICKNLLPV LAQHVAGPSR
PRHQAQACLM LQKTLSAREL RVCFEDPEWE QLITQLLGKA TQTLQTLGEA QSKGEHQKEL
SILELLNTLL RTVNHEKLSV DLTAPLGVLQ SKQQKLQQSL QQGNHSSGSN RLYDLYWQAM
RMLGVQRPKS EKKNAKDIPS DTQSPVSTKR KKKGFLPETK KRKKLKSEGT TPEKNAASQQ
DAVTEGAMPA ATGKDQPPST GKKKRKRVKA STPSQVNGIT GAKSPAPSNP TLSPSTPAKT
PKLQKKKEKL SQVNGATPVS PIEPESKKHH QEALSTKEVI RKSPHPQSAL PKKRARLSLV
SRSPSLLQSG VKKRRVASRR VQTP


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EIAAB33940 DXS8237E,G patch domain-containing protein 9,GPATC9,GPATCH9,Homo sapiens,Human,KIAA0122,RBM10,RNA-binding motif protein 10,RNA-binding protein 10,RNA-binding protein S1-1,S1-1
EIAAB10707 Damage-specific DNA-binding protein 1,DDB p127 subunit,DDB1,DDBa,DNA damage-binding protein 1,DNA damage-binding protein a,HBV X-associated protein 1,Homo sapiens,Human,UV-damaged DNA-binding factor,U
EIAAB45443 AIE-75-binding protein,AIEBP,Homo sapiens,Human,MCC2,MCC-2,USH1C-binding protein 1,USHBP1,Usher syndrome type-1C protein-binding protein 1
E1257h ELISA kit DEF3,Homo sapiens,Human,Lung cancer antigen NY-LU-12,Protein G16,RBM6,RNA-binding motif protein 6,RNA-binding protein 6,RNA-binding protein DEF-3 96T
U1257h CLIA DEF3,Homo sapiens,Human,Lung cancer antigen NY-LU-12,Protein G16,RBM6,RNA-binding motif protein 6,RNA-binding protein 6,RNA-binding protein DEF-3 96T
E1257h ELISA DEF3,Homo sapiens,Human,Lung cancer antigen NY-LU-12,Protein G16,RBM6,RNA-binding motif protein 6,RNA-binding protein 6,RNA-binding protein DEF-3 96T
EIAAB47038 Hivep3,Human immunodeficiency virus type I enhancer-binding protein 3 homolog,Kappa-B and V(D)J recombination signal sequences-binding protein,Kappa-binding protein 1,KB-binding and regognition compon
E0497h ELISA 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galactoside-binding protein,GALBP,Galectin-3,Homo sapiens,Human,IgE-binding protein,L-31,Laminin-binding pr 96T
U0497h CLIA 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galactoside-binding protein,GALBP,Galectin-3,Homo sapiens,Human,IgE-binding protein,L-31,Laminin-binding pro 96T
18-003-43569 CUG-BP- and ETR-3-like factor 2 - CELF-2; Bruno-like protein 3; RNA-binding protein BRUNOL-3; CUG triplet repeat RNA-binding protein 2; CUG-BP2; ELAV-type RNA-binding protein 3; ETR-3; Neuroblastoma a 0.1 mg Protein A


 

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