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Activated RNA polymerase II transcriptional coactivator p15 (Positive cofactor 4) (PC4) (SUB1 homolog) (p14)

 TCP4_HUMAN              Reviewed;         127 AA.
P53999; Q96L29;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 162.
RecName: Full=Activated RNA polymerase II transcriptional coactivator p15;
AltName: Full=Positive cofactor 4;
Short=PC4;
AltName: Full=SUB1 homolog;
AltName: Full=p14;
Name=SUB1; Synonyms=PC4, RPO2TC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
PubMed=8062392; DOI=10.1016/0092-8674(94)90429-4;
Kretzschmar M., Kaiser K., Lottspeich F., Meisterernst M.;
"A novel mediator of class II gene transcription with homology to
viral immediate-early transcriptional regulators.";
Cell 78:525-534(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-11 AND 81-97, AND
FUNCTION.
PubMed=8062391; DOI=10.1016/0092-8674(94)90428-6;
Ge H., Roeder R.G.;
"Purification, cloning, and characterization of a human coactivator,
PC4, that mediates transcriptional activation of class II genes.";
Cell 78:513-523(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-11.
TISSUE=Bone marrow, Cervix, Lung, and Prostate;
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]
PHOSPHORYLATION, AND MASS SPECTROMETRY.
PubMed=7809103; DOI=10.1073/pnas.91.26.12691;
Ge H., Zhao Y., Chait B.T., Roeder R.G.;
"Phosphorylation negatively regulates the function of coactivator
PC4.";
Proc. Natl. Acad. Sci. U.S.A. 91:12691-12695(1994).
[5]
FUNCTION, AND DNA-BINDING.
PubMed=7628453;
Kaiser K., Stelzer G., Meisterernst M.;
"The coactivator p15 (PC4) initiates transcriptional activation during
TFIIA-TFIID-promoter complex formation.";
EMBO J. 14:3520-3527(1995).
[6]
FUNCTION, AND PHOSPHORYLATION BY CK2.
PubMed=9482861; DOI=10.1073/pnas.95.5.2192;
Malik S., Guermah M., Roeder R.G.;
"A dynamic model for PC4 coactivator function in RNA polymerase II
transcription.";
Proc. Natl. Acad. Sci. U.S.A. 95:2192-2197(1998).
[7]
INTERACTION WITH CSTF2.
PubMed=11389848; DOI=10.1016/S1097-2765(01)00236-2;
Calvo O., Manley J.L.;
"Evolutionarily conserved interaction between CstF-64 and PC4 links
transcription, polyadenylation, and termination.";
Mol. Cell 7:1013-1023(2001).
[8]
MASS SPECTROMETRY, FUNCTION, DNA-BINDING, AND PHOSPHORYLATION AT
SER-11; SER-13; SER-15; SER-17 AND SER-19.
PubMed=16689930; DOI=10.1111/j.1742-4658.2006.05165.x;
Jonker H.R.A., Wechselberger R.W., Pinkse M., Kaptein R.,
Folkers G.E.;
"Gradual phosphorylation regulates PC4 coactivator function.";
FEBS J. 273:1430-1444(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-19, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35 AND LYS-68, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND 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).
[15]
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-17; SER-19; SER-55;
SER-56; SER-57; SER-58 AND SER-118, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-9; SER-10;
SER-13; SER-15; SER-17; SER-19 AND SER-118, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[21]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 63-127, FUNCTION, AND
SUBUNIT.
PubMed=9360603; DOI=10.1038/nsb1197-900;
Brandsen J., Werten S., van der Vliet P.C., Meisterernst M., Kroon J.,
Gros P.;
"C-terminal domain of transcription cofactor PC4 reveals dimeric ssDNA
binding site.";
Nat. Struct. Biol. 4:900-903(1997).
[22]
STRUCTURE BY NMR, FUNCTION, AND MUTAGENESIS OF LYS-68; ARG-75;
77-PHE--LYS-80; ARG-86 AND LYS-101.
PubMed=16605275; DOI=10.1021/bi052531b;
Jonker H.R.A., Wechselberger R.W., Boelens R., Kaptein R.,
Folkers G.E.;
"The intrinsically unstructured domain of PC4 modulates the activity
of the structured core through inter- and intramolecular
interactions.";
Biochemistry 45:5067-5081(2006).
[23]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 63-127 IN COMPLEX WITH
SINGLE-STRANDED DNA, AND SUBUNIT.
PubMed=16415882; DOI=10.1038/nsmb1044;
Werten S., Moras D.;
"A global transcription cofactor bound to juxtaposed strands of
unwound DNA.";
Nat. Struct. Biol. 13:181-182(2006).
-!- FUNCTION: General coactivator that functions cooperatively with
TAFs and mediates functional interactions between upstream
activators and the general transcriptional machinery. May be
involved in stabilizing the multiprotein transcription complex.
Binds single-stranded DNA. Also binds, in vitro, non-specifically
to double-stranded DNA (ds DNA). {ECO:0000269|PubMed:16605275,
ECO:0000269|PubMed:16689930, ECO:0000269|PubMed:7628453,
ECO:0000269|PubMed:8062391, ECO:0000269|PubMed:8062392,
ECO:0000269|PubMed:9360603, ECO:0000269|PubMed:9482861}.
-!- SUBUNIT: Homodimer. Interacts with CSTF2.
{ECO:0000269|PubMed:11389848, ECO:0000269|PubMed:16415882,
ECO:0000269|PubMed:9360603}.
-!- INTERACTION:
P04326:- (xeno); NbExp=3; IntAct=EBI-998260, EBI-7333987;
P68400:CSNK2A1; NbExp=2; IntAct=EBI-998260, EBI-347804;
P33240-1:CSTF2; NbExp=3; IntAct=EBI-998260, EBI-711374;
P03132:Rep68 (xeno); NbExp=3; IntAct=EBI-998260, EBI-7387242;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- PTM: Activity is controlled by protein kinases that target the
regulatory region. Phosphorylation inactivates both ds DNA-binding
and cofactor function, but does not affect binding to ssDNA. Seems
to be phosphorylated in vivo by CK2 in at least 7 sites in the N-
terminal Ser-rich region. {ECO:0000269|PubMed:16689930,
ECO:0000269|PubMed:7809103, ECO:0000269|PubMed:9482861}.
-!- MASS SPECTROMETRY: Mass=14266; Mass_error=4; Method=MALDI;
Range=2-127; Evidence={ECO:0000269|PubMed:7809103};
-!- MASS SPECTROMETRY: Mass=14263; Method=Electrospray; Range=2-127;
Evidence={ECO:0000269|PubMed:16689930};
-!- SIMILARITY: Belongs to the transcriptional coactivator PC4 family.
{ECO:0000305}.
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EMBL; X79805; CAA56200.1; -; mRNA.
EMBL; U12979; AAA20980.1; -; mRNA.
EMBL; BC009610; AAH09610.1; -; mRNA.
EMBL; BC010537; AAH10537.1; -; mRNA.
EMBL; BC018189; AAH18189.1; -; mRNA.
EMBL; BC022339; AAH22339.1; -; mRNA.
CCDS; CCDS3897.1; -.
PIR; A54670; A54670.
RefSeq; NP_006704.3; NM_006713.3.
RefSeq; XP_011512246.1; XM_011513944.2.
RefSeq; XP_016864475.1; XM_017008986.1.
RefSeq; XP_016864476.1; XM_017008987.1.
UniGene; Hs.229641; -.
PDB; 1PCF; X-ray; 1.74 A; A/B/C/D/E/F/G/H=63-127.
PDB; 2C62; X-ray; 1.74 A; A/B=63-127.
PDB; 2PHE; NMR; -; A/B=63-127.
PDB; 4USG; X-ray; 1.97 A; A/B=63-127.
PDBsum; 1PCF; -.
PDBsum; 2C62; -.
PDBsum; 2PHE; -.
PDBsum; 4USG; -.
ProteinModelPortal; P53999; -.
SMR; P53999; -.
BioGrid; 116127; 68.
CORUM; P53999; -.
DIP; DIP-29044N; -.
IntAct; P53999; 24.
MINT; MINT-138673; -.
STRING; 9606.ENSP00000265073; -.
iPTMnet; P53999; -.
PhosphoSitePlus; P53999; -.
SwissPalm; P53999; -.
BioMuta; SUB1; -.
DMDM; 1709514; -.
EPD; P53999; -.
PaxDb; P53999; -.
PeptideAtlas; P53999; -.
PRIDE; P53999; -.
TopDownProteomics; P53999; -.
Ensembl; ENST00000265073; ENSP00000265073; ENSG00000113387.
Ensembl; ENST00000502897; ENSP00000427100; ENSG00000113387.
Ensembl; ENST00000506237; ENSP00000422078; ENSG00000113387.
Ensembl; ENST00000512913; ENSP00000422806; ENSG00000113387.
Ensembl; ENST00000515355; ENSP00000426850; ENSG00000113387.
GeneID; 10923; -.
KEGG; hsa:10923; -.
CTD; 10923; -.
DisGeNET; 10923; -.
EuPathDB; HostDB:ENSG00000113387.11; -.
GeneCards; SUB1; -.
HGNC; HGNC:19985; SUB1.
HPA; CAB015351; -.
HPA; HPA001311; -.
MIM; 600503; gene.
neXtProt; NX_P53999; -.
OpenTargets; ENSG00000113387; -.
PharmGKB; PA142670858; -.
eggNOG; KOG2712; Eukaryota.
eggNOG; ENOG410XUB8; LUCA.
GeneTree; ENSGT00390000008802; -.
HOVERGEN; HBG028243; -.
InParanoid; P53999; -.
OMA; MVDIREH; -.
OrthoDB; EOG091G14VO; -.
PhylomeDB; P53999; -.
TreeFam; TF313859; -.
SIGNOR; P53999; -.
ChiTaRS; SUB1; human.
EvolutionaryTrace; P53999; -.
GeneWiki; SUB1; -.
GenomeRNAi; 10923; -.
PRO; PR:P53999; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113387; -.
CleanEx; HS_SUB1; -.
ExpressionAtlas; P53999; baseline and differential.
Genevisible; P53999; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005667; C:transcription factor complex; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; IEA:Ensembl.
GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IBA:GO_Central.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
Gene3D; 2.30.31.10; -; 1.
InterPro; IPR003173; PC4.
InterPro; IPR009044; ssDNA-bd_transcriptional_reg.
Pfam; PF02229; PC4; 1.
SUPFAM; SSF54447; SSF54447; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Complete proteome;
Direct protein sequencing; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:8062391}.
CHAIN 2 127 Activated RNA polymerase II
transcriptional coactivator p15.
/FTId=PRO_0000215944.
REGION 2 50 Regulatory.
REGION 77 101 Interaction with ssDNA.
COMPBIAS 4 19 Ser-rich.
COMPBIAS 23 53 Lys-rich.
COMPBIAS 50 58 Ser-rich.
SITE 50 51 Cleavage.
MOD_RES 4 4 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000269|PubMed:16689930}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16689930}.
MOD_RES 15 15 Phosphoserine.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16689930}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16689930}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16689930}.
MOD_RES 35 35 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 53 53 N6-acetyllysine.
{ECO:0000250|UniProtKB:P11031}.
MOD_RES 55 55 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 68 68 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CROSSLNK 68 68 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 68 68 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VARIANT 11 11 S -> G (in dbSNP:rs17850527).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_032870.
MUTAGEN 68 68 K->G: Reduced ssDNA binding.
{ECO:0000269|PubMed:16605275}.
MUTAGEN 75 75 R->G: Reduced ssDNA binding.
{ECO:0000269|PubMed:16605275}.
MUTAGEN 77 80 FKGK->AGG: Loss of ssDNA binding.
{ECO:0000269|PubMed:16605275}.
MUTAGEN 86 86 R->G: Loss of ssDNA binding.
{ECO:0000269|PubMed:16605275}.
MUTAGEN 101 101 K->G: Loss of ssDNA binding.
{ECO:0000269|PubMed:16605275}.
STRAND 63 67 {ECO:0000244|PDB:1PCF}.
STRAND 70 77 {ECO:0000244|PDB:1PCF}.
STRAND 80 90 {ECO:0000244|PDB:1PCF}.
STRAND 92 94 {ECO:0000244|PDB:2PHE}.
STRAND 96 105 {ECO:0000244|PDB:1PCF}.
HELIX 107 126 {ECO:0000244|PDB:1PCF}.
SEQUENCE 127 AA; 14395 MW; 0DAE0CAAAD5E4E15 CRC64;
MPKSKELVSS SSSGSDSDSE VDKKLKRKKQ VAPEKPVKKQ KTGETSRALS SSKQSSSSRD
DNMFQIGKMR YVSVRDFKGK VLIDIREYWM DPEGEMKPGR KGISLNPEQW SQLKEQISDI
DDAVRKL


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PR-725 PC4 Positive Cofactor 4, Transcriptional Coactivator, wild type human, recombinant, E. coli 10
PR-725 Proteins: PC4 Positive Cofactor 4, Transcriptional Coactivator, wild typehuman, recombinant, E. coli 10
PR-726 PC4-mt (F77P) Positive Cofactor 4, F77P mutant, Transcriptional Coactivator human, recombinant, E. coli 10
TCP4_CHICK Chicken ELISA Kit FOR Activated RNA polymerase II transcriptional coactivator p15 96T


 

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