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DNA-directed RNA polymerases I, II, and III subunit RPABC3 (RNA polymerases I, II, and III subunit ABC3) (DNA-directed RNA polymerase II subunit H) (DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide) (RPB17) (RPB8 homolog) (hRPB8)

 RPAB3_HUMAN             Reviewed;         150 AA.
P52434; C9J413; C9JBJ6; C9JCU7; C9JUA8; P53802; Q969R0;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
10-OCT-2018, entry version 188.
RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC3;
Short=RNA polymerases I, II, and III subunit ABC3;
AltName: Full=DNA-directed RNA polymerase II subunit H;
AltName: Full=DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide;
AltName: Full=RPB17;
AltName: Full=RPB8 homolog;
Short=hRPB8;
Name=POLR2H;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8524256; DOI=10.1128/MCB.15.12.6895;
McKune K., Moore P.A., Hull M.W., Woychik N.A.;
"Six human RNA polymerase subunits functionally substitute for their
yeast counterparts.";
Mol. Cell. Biol. 15:6895-6900(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7651387; DOI=10.1128/MCB.15.9.4702;
Shpakovski G.V., Acker J., Wintzerith M., Lacroix J.F., Thuriaux P.,
Vigneron M.;
"Four subunits that are shared by the three classes of RNA polymerase
are functionally interchangeable between Homo sapiens and
Saccharomyces cerevisiae.";
Mol. Cell. Biol. 15:4702-4710(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
Shpakovski G.V., Lebedenko E.N., Grandemange S., Schaller S.,
Vigneron M., Kedinger C.;
"Organization of genes encoding subunits of eucaryotic nuclear RNA
polymerases shows non random intron distribution and correlates with
the subunit modular structure.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[5]
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).
[6]
PROTEIN SEQUENCE OF 2-13 AND 99-111, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma, and Cervix carcinoma;
Bienvenut W.V.;
Submitted (AUG-2005) to UniProtKB.
[7]
FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, AND
SUBCELLULAR LOCATION.
PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
Kershnar E., Wu S.-Y., Chiang C.-M.;
"Immunoaffinity purification and functional characterization of human
transcription factor IIH and RNA polymerase II from clonal cell lines
that conditionally express epitope-tagged subunits of the multiprotein
complexes.";
J. Biol. Chem. 273:34444-34453(1998).
[8]
IDENTIFICATION IN THE RNA POL I COMPLEX.
PubMed=16809778; DOI=10.1128/MCB.00230-06;
Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J.,
Zomerdijk J.C.B.M.;
"RNA polymerase I-specific subunit CAST/hPAF49 has a role in the
activation of transcription by upstream binding factor.";
Mol. Cell. Biol. 26:5436-5448(2006).
[9]
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).
[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]
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).
[12]
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).
[13]
STRUCTURE BY NMR, DNA-BINDING REGION, SUBUNIT, AND INTERACTION WITH
POLR2A.
PubMed=16632472; DOI=10.1074/jbc.M513241200;
Kang X., Hu Y., Li Y., Guo X., Jiang X., Lai L., Xia B., Jin C.;
"Structural, biochemical, and dynamic characterizations of the hRPB8
subunit of human RNA polymerases.";
J. Biol. Chem. 281:18216-18226(2006).
-!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
of DNA into RNA using the four ribonucleoside triphosphates as
substrates. Common component of RNA polymerases I, II and III
which synthesize ribosomal RNA precursors, mRNA precursors and
many functional non-coding RNAs, and small RNAs, such as 5S rRNA
and tRNAs, respectively. {ECO:0000269|PubMed:9852112}.
-!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase
II (Pol II) and RNA polymerase III (Pol III) complexes consisting
of at least 13, 12 and 17 subunits, respectively. Directly
interacts with POLR2A. {ECO:0000269|PubMed:16632472,
ECO:0000269|PubMed:16809778, ECO:0000269|PubMed:9852112}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:9852112, ECO:0000269|Ref.6}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P52434-1; Sequence=Displayed;
Name=2;
IsoId=P52434-2; Sequence=VSP_055018;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
Name=3;
IsoId=P52434-3; Sequence=VSP_055017;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
Name=4;
IsoId=P52434-4; Sequence=VSP_055019;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
Name=5;
IsoId=P52434-5; Sequence=VSP_055017, VSP_055018;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- SIMILARITY: Belongs to the eukaryotic RPB8 RNA polymerase subunit
family. {ECO:0000305}.
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EMBL; U37689; AAA91458.1; -; mRNA.
EMBL; Z49199; CAA89060.1; -; mRNA.
EMBL; AJ252079; CAB92189.1; -; Genomic_DNA.
EMBL; AJ252080; CAB92189.1; JOINED; Genomic_DNA.
EMBL; AC078797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000739; AAH00739.1; -; mRNA.
CCDS; CCDS3264.1; -. [P52434-1]
CCDS; CCDS63859.1; -. [P52434-4]
CCDS; CCDS63860.1; -. [P52434-2]
CCDS; CCDS63861.1; -. [P52434-3]
CCDS; CCDS63862.1; -. [P52434-5]
PIR; S55370; S55370.
RefSeq; NP_001265627.1; NM_001278698.1. [P52434-4]
RefSeq; NP_001265628.1; NM_001278699.2. [P52434-3]
RefSeq; NP_001265629.1; NM_001278700.1. [P52434-3]
RefSeq; NP_001265643.1; NM_001278714.1. [P52434-2]
RefSeq; NP_001265644.1; NM_001278715.1. [P52434-5]
RefSeq; NP_006223.2; NM_006232.4. [P52434-1]
RefSeq; XP_006713729.1; XM_006713666.2. [P52434-4]
RefSeq; XP_006713730.1; XM_006713667.2. [P52434-4]
RefSeq; XP_016862125.1; XM_017006636.1. [P52434-2]
RefSeq; XP_016862126.1; XM_017006637.1. [P52434-5]
UniGene; Hs.432574; -.
PDB; 2F3I; NMR; -; A=1-150.
PDB; 5IY6; EM; 7.20 A; H=1-150.
PDB; 5IY7; EM; 8.60 A; H=1-150.
PDB; 5IY8; EM; 7.90 A; H=1-150.
PDB; 5IY9; EM; 6.30 A; H=1-150.
PDB; 5IYA; EM; 5.40 A; H=1-150.
PDB; 5IYB; EM; 3.90 A; H=1-150.
PDB; 5IYC; EM; 3.90 A; H=1-150.
PDB; 5IYD; EM; 3.90 A; H=1-150.
PDBsum; 2F3I; -.
PDBsum; 5IY6; -.
PDBsum; 5IY7; -.
PDBsum; 5IY8; -.
PDBsum; 5IY9; -.
PDBsum; 5IYA; -.
PDBsum; 5IYB; -.
PDBsum; 5IYC; -.
PDBsum; 5IYD; -.
ProteinModelPortal; P52434; -.
SMR; P52434; -.
BioGrid; 111433; 67.
CORUM; P52434; -.
DIP; DIP-27556N; -.
IntAct; P52434; 21.
MINT; P52434; -.
STRING; 9606.ENSP00000296223; -.
iPTMnet; P52434; -.
PhosphoSitePlus; P52434; -.
DMDM; 20178325; -.
EPD; P52434; -.
MaxQB; P52434; -.
PaxDb; P52434; -.
PeptideAtlas; P52434; -.
PRIDE; P52434; -.
ProteomicsDB; 56485; -.
TopDownProteomics; P52434-1; -. [P52434-1]
DNASU; 5437; -.
Ensembl; ENST00000429568; ENSP00000415536; ENSG00000163882. [P52434-4]
Ensembl; ENST00000430783; ENSP00000411883; ENSG00000163882. [P52434-2]
Ensembl; ENST00000438240; ENSP00000398622; ENSG00000163882. [P52434-3]
Ensembl; ENST00000443489; ENSP00000393773; ENSG00000163882. [P52434-5]
Ensembl; ENST00000452961; ENSP00000399882; ENSG00000163882. [P52434-3]
Ensembl; ENST00000456318; ENSP00000392913; ENSG00000163882. [P52434-1]
GeneID; 5437; -.
KEGG; hsa:5437; -.
UCSC; uc032smc.2; human. [P52434-1]
CTD; 5437; -.
DisGeNET; 5437; -.
EuPathDB; HostDB:ENSG00000163882.9; -.
GeneCards; POLR2H; -.
HGNC; HGNC:9195; POLR2H.
HPA; HPA037745; -.
HPA; HPA055813; -.
MIM; 606023; gene.
neXtProt; NX_P52434; -.
OpenTargets; ENSG00000163882; -.
PharmGKB; PA33515; -.
eggNOG; KOG3400; Eukaryota.
eggNOG; ENOG4111FT0; LUCA.
GeneTree; ENSGT00390000018195; -.
HOGENOM; HOG000175572; -.
HOVERGEN; HBG036116; -.
InParanoid; P52434; -.
KO; K03016; -.
OMA; FEYVMFG; -.
OrthoDB; EOG091G0QJA; -.
PhylomeDB; P52434; -.
TreeFam; TF103043; -.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
Reactome; R-HSA-167161; HIV Transcription Initiation.
Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
Reactome; R-HSA-167172; Transcription of the HIV genome.
Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
Reactome; R-HSA-167287; HIV elongation arrest and recovery.
Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-6803529; FGFR2 alternative splicing.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-HSA-72086; mRNA Capping.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
Reactome; R-HSA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation.
Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
ChiTaRS; POLR2H; human.
EvolutionaryTrace; P52434; -.
GeneWiki; POLR2H; -.
GenomeRNAi; 5437; -.
PRO; PR:P52434; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000163882; Expressed in 228 organ(s), highest expression level in mucosa of transverse colon.
CleanEx; HS_POLR2H; -.
ExpressionAtlas; P52434; baseline and differential.
Genevisible; P52434; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032993; C:protein-DNA complex; IDA:CAFA.
GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB.
GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0003697; F:single-stranded DNA binding; IDA:CAFA.
GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0042795; P:snRNA transcription by RNA polymerase II; TAS:Reactome.
GO; GO:0006363; P:termination of RNA polymerase I transcription; TAS:Reactome.
GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0006383; P:transcription by RNA polymerase III; IEA:GOC.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; TAS:Reactome.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
InterPro; IPR012340; NA-bd_OB-fold.
InterPro; IPR005570; RNA_pol_Rpb8.
PANTHER; PTHR10917; PTHR10917; 1.
Pfam; PF03870; RNA_pol_Rpb8; 1.
PIRSF; PIRSF000779; RNA_pol_Rpb8; 1.
SMART; SM00658; RPOL8c; 1.
SUPFAM; SSF50249; SSF50249; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; DNA-binding; DNA-directed RNA polymerase;
Nucleus; Reference proteome; Transcription.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
CHAIN 2 150 DNA-directed RNA polymerases I, II, and
III subunit RPABC3.
/FTId=PRO_0000073997.
REGION 16 40 Non-specific ssDNA binding.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
VAR_SEQ 1 36 Missing (in isoform 3 and isoform 5).
{ECO:0000305}.
/FTId=VSP_055017.
VAR_SEQ 84 112 RADQFEYVMYGKVYRIEGDETSTEAATRL -> S (in
isoform 2 and isoform 5). {ECO:0000305}.
/FTId=VSP_055018.
VAR_SEQ 113 150 SAYVSYGGLLMRLQGDANNLHGFEVDSRVYLLMKKLAF ->
LRLRAAEWQCSRITGWGLLFQLCVRVLWGPAHEAAGGCQQP
AWIRGGLQSLSPDEEASLLNLA (in isoform 4).
{ECO:0000305}.
/FTId=VSP_055019.
CONFLICT 19 19 G -> A (in Ref. 1; AAA91458).
{ECO:0000305}.
STRAND 7 16 {ECO:0000244|PDB:2F3I}.
STRAND 25 35 {ECO:0000244|PDB:2F3I}.
STRAND 38 44 {ECO:0000244|PDB:2F3I}.
STRAND 48 50 {ECO:0000244|PDB:2F3I}.
STRAND 56 59 {ECO:0000244|PDB:2F3I}.
STRAND 66 70 {ECO:0000244|PDB:2F3I}.
TURN 71 73 {ECO:0000244|PDB:2F3I}.
STRAND 75 77 {ECO:0000244|PDB:2F3I}.
TURN 85 88 {ECO:0000244|PDB:2F3I}.
STRAND 89 92 {ECO:0000244|PDB:2F3I}.
STRAND 94 97 {ECO:0000244|PDB:2F3I}.
STRAND 104 107 {ECO:0000244|PDB:2F3I}.
STRAND 110 118 {ECO:0000244|PDB:2F3I}.
STRAND 121 127 {ECO:0000244|PDB:2F3I}.
HELIX 129 132 {ECO:0000244|PDB:2F3I}.
STRAND 142 147 {ECO:0000244|PDB:2F3I}.
SEQUENCE 150 AA; 17143 MW; 944D0860809F1425 CRC64;
MAGILFEDIF DVKDIDPEGK KFDRVSRLHC ESESFKMDLI LDVNIQIYPV DLGDKFRLVI
ASTLYEDGTL DDGEYNPTDD RPSRADQFEY VMYGKVYRIE GDETSTEAAT RLSAYVSYGG
LLMRLQGDAN NLHGFEVDSR VYLLMKKLAF


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EIAAB35760 DNA-directed RNA polymerase II subunit H,DNA-directed RNA polymerases I, II, and III subunit RPABC3,Mouse,Mus musculus,Polr2h,RNA polymerases I, II, and III subunit ABC3,RPB17,RPB8 homolog
EIAAB35759 DNA-directed RNA polymerase II subunit H,DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide,DNA-directed RNA polymerases I, II, and III subunit RPABC3,Homo sapiens,hRPB8,Human,POLR2H,RNA
EIAAB35768 AC40,DNA-directed RNA polymerase I subunit C,DNA-directed RNA polymerases I and III 40 kDa polypeptide,DNA-directed RNA polymerases I and III subunit RPAC1,Mouse,Mus musculus,Polr1c,RNA polymerases I
EIAAB35767 AC40,DNA-directed RNA polymerase I subunit C,DNA-directed RNA polymerases I and III 40 kDa polypeptide,DNA-directed RNA polymerases I and III subunit RPAC1,Homo sapiens,Human,POLR1C,POLR1E,RNA polymer
EIAAB35755 DNA-directed RNA polymerase II subunit F,DNA-directed RNA polymerases I, II, and III 14.4 kDa polypeptide,DNA-directed RNA polymerases I, II, and III subunit RPABC2,Homo sapiens,Human,POLR2F,POLRF,RNA
EIAAB35754 DNA-directed RNA polymerase II 23 kDa polypeptide,DNA-directed RNA polymerase II subunit E,DNA-directed RNA polymerases I, II, and III subunit RPABC1,Homo sapiens,Human,POLR2E,RNA polymerases I, II, a
EIAAB35756 DNA-directed RNA polymerase II subunit F,DNA-directed RNA polymerases I, II, and III subunit RPABC2,Mouse,Mus musculus,Polr2f,RNA polymerases I, II, and III subunit ABC2,RPB6 homolog
EIAAB35753 Bos taurus,Bovine,DNA-directed RNA polymerase II subunit E,DNA-directed RNA polymerases I, II, and III subunit RPABC1,POLR2E,RNA polymerases I, II, and III subunit ABC1,RPB5 homolog
EIAAB35758 DNA-directed RNA polymerase II subunit F,DNA-directed RNA polymerases I, II, and III subunit RPABC2,Polr2f,Rat,Rattus norvegicus,RNA polymerases I, II, and III subunit ABC2,RPB6 homolog
EIAAB35752 DNA-directed RNA polymerase II subunit E,DNA-directed RNA polymerases I, II, and III subunit RPABC1,Polr2e,Rat,Rattus norvegicus,RNA polymerases I, II, and III subunit ABC1,RPB5 homolog
EIAAB35751 DNA-directed RNA polymerase II subunit E,DNA-directed RNA polymerases I, II, and III subunit RPABC1,Mouse,Mus musculus,Polr2e,RNA polymerases I, II, and III subunit ABC1,RPB5 homolog
EIAAB35765 DNA-directed RNA polymerase III subunit L,DNA-directed RNA polymerases I, II, and III subunit RPABC5,Mouse,Mus musculus,Polr2l,RNA polymerases I, II, and III subunit ABC5,RPB10 homolog
EIAAB35757 Bos taurus,Bovine,DNA-directed RNA polymerase II subunit F,DNA-directed RNA polymerases I, II, and III subunit RPABC2,POLR2F,RNA polymerases I, II, and III subunit ABC2,RPB6 homolog
EIAAB35771 AC19,DNA-directed RNA polymerase I subunit D,DNA-directed RNA polymerases I and III subunit RPAC2,Homo sapiens,hRPA19,Human,POLR1D,RNA polymerase I 16 kDa subunit,RNA polymerases I and III subunit AC2
EIAAB35772 AC19,DNA-directed RNA polymerase I subunit D,DNA-directed RNA polymerases I and III subunit RPAC2,Mouse,Mus musculus,Polr1d,RNA polymerase I 16 kDa subunit,RNA polymerases I and III subunit AC2,RPA16,
EIAAB35761 Bos taurus,Bovine,DNA-directed RNA polymerase II subunit K,DNA-directed RNA polymerases I, II, and III subunit RPABC4,POLR2K,RNA polymerases I, II, and III subunit ABC4
EIAAB35766 Bos taurus,Bovine,DNA-directed RNA polymerase III subunit L,DNA-directed RNA polymerases I, II, and III subunit RPABC5,POLR2L,RNA polymerases I, II, and III subunit ABC5
EIAAB35763 ABC10-alpha,DNA-directed RNA polymerase II subunit K,DNA-directed RNA polymerases I, II, and III subunit RPABC4,Homo sapiens,Human,POLR2K,RNA polymerase II 7.0 kDa subunit,RNA polymerases I, II, and I
EIAAB35762 DNA-directed RNA polymerase II subunit K,DNA-directed RNA polymerases I, II, and III subunit RPABC4,Metallothionein-I gene transcription activator,Mouse,Mt1a,Mus musculus,Polr2k,RNA polymerases I, II,
EIAAB35764 DNA-directed RNA polymerase III subunit L,DNA-directed RNA polymerases I, II, and III subunit RPABC5,Homo sapiens,Human,POLR2L,RNA polymerase II 7.6 kDa subunit,RNA polymerases I, II, and III subunit
EIAAB35770 Bos taurus,Bovine,DNA-directed RNA polymerase I subunit D,DNA-directed RNA polymerases I and III subunit RPAC2,POLR1D,RNA polymerases I and III subunit AC2
EIAAB35769 Bos taurus,Bovine,DNA-directed RNA polymerase I subunit C,DNA-directed RNA polymerases I and III subunit RPAC1,POLR1C,RNA polymerases I and III subunit AC1
20-372-60269 polymerase (RNA) II (DNA directed) polypeptide F (POLR2F). mRNA - Mouse monoclonal anti-human POLR2F antibody; RNA polymerases I. II. and III subunit ABC2; DNA-directed RNA polymerase II subunit F; RP 0.1 mg
CSB-EL018335MO Mouse DNA-directed RNA polymerases I, II, and III subunit RPABC3(POLR2H) ELISA kit 96T
CSB-EL018335HU Human DNA-directed RNA polymerases I, II, and III subunit RPABC3(POLR2H) ELISA kit 96T


 

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