Full text data of POLR2D
POLR2D
[Confidence: low (only semi-automatic identification from reviews)]
DNA-directed RNA polymerase II subunit RPB4; RNA polymerase II subunit B4 (DNA-directed RNA polymerase II subunit D; RNA polymerase II 16 kDa subunit; RPB16)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
DNA-directed RNA polymerase II subunit RPB4; RNA polymerase II subunit B4 (DNA-directed RNA polymerase II subunit D; RNA polymerase II 16 kDa subunit; RPB16)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O15514
ID RPB4_HUMAN Reviewed; 142 AA.
AC O15514; Q52LT4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB4;
DE Short=RNA polymerase II subunit B4;
DE AltName: Full=DNA-directed RNA polymerase II subunit D;
DE AltName: Full=RNA polymerase II 16 kDa subunit;
DE Short=RPB16;
GN Name=POLR2D;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Cervix carcinoma;
RX PubMed=9528765;
RA Khazak V., Estojak J., Cho H., Majors J.A., Sonoda G., Testa J.R.,
RA Golemis E.A.;
RT "Analysis of the interaction of the novel RNA polymerase II (pol II)
RT subunit hsRPB4 with its partner hsRPB7 and with pol II.";
RL Mol. Cell. Biol. 18:1935-1945(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
RA Kershnar E., Wu S.-Y., Chiang C.-M.;
RT "Immunoaffinity purification and functional characterization of human
RT transcription factor IIH and RNA polymerase II from clonal cell lines
RT that conditionally express epitope-tagged subunits of the multiprotein
RT complexes.";
RL J. Biol. Chem. 273:34444-34453(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF THE POL II RPB4-RPB7
RP SUBCOMPLEX.
RX PubMed=16282592; DOI=10.1093/nar/gki945;
RA Meka H., Werner F., Cordell S.C., Onesti S., Brick P.;
RT "Crystal structure and RNA binding of the Rpb4/Rpb7 subunits of human
RT RNA polymerase II.";
RL Nucleic Acids Res. 33:6435-6444(2005).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC of DNA into RNA using the four ribonucleoside triphosphates as
CC substrates. Component of RNA polymerase II which synthesizes mRNA
CC precursors and many functional non-coding RNAs. Pol II is the
CC central component of the basal RNA polymerase II transcription
CC machinery. It is composed of mobile elements that move relative to
CC each other. RPB4 is part of a subcomplex with RPB7 that binds to a
CC pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp
CC element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7
CC in the closed conformation thus preventing double-stranded DNA to
CC enter the active site cleft. The RPB4-RPB7 subcomplex binds
CC single-stranded DNA and RNA (By similarity).
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex
CC consisting of 12 subunits. RPB4 and RPB7 form a subcomplex that
CC protrudes from the 10-subunit Pol II core complex.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB4 RNA polymerase subunit
CC family.
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CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U89387; AAC52056.1; -; Genomic_DNA.
DR EMBL; U85510; AAC80226.1; -; mRNA.
DR EMBL; BC017205; AAH17205.1; -; mRNA.
DR EMBL; BC093795; AAH93795.1; -; mRNA.
DR EMBL; BC093797; AAH93797.1; -; mRNA.
DR RefSeq; NP_004796.1; NM_004805.3.
DR UniGene; Hs.715348; -.
DR PDB; 2C35; X-ray; 2.70 A; A/C/E/G=1-142.
DR PDBsum; 2C35; -.
DR ProteinModelPortal; O15514; -.
DR SMR; O15514; 14-141.
DR DIP; DIP-32912N; -.
DR IntAct; O15514; 8.
DR STRING; 9606.ENSP00000272645; -.
DR PhosphoSite; O15514; -.
DR PaxDb; O15514; -.
DR PeptideAtlas; O15514; -.
DR PRIDE; O15514; -.
DR DNASU; 5433; -.
DR Ensembl; ENST00000272645; ENSP00000272645; ENSG00000144231.
DR GeneID; 5433; -.
DR KEGG; hsa:5433; -.
DR UCSC; uc002tpj.3; human.
DR CTD; 5433; -.
DR GeneCards; GC02M128649; -.
DR HGNC; HGNC:9191; POLR2D.
DR HPA; HPA046092; -.
DR MIM; 606017; gene.
DR neXtProt; NX_O15514; -.
DR PharmGKB; PA33511; -.
DR eggNOG; COG5250; -.
DR HOGENOM; HOG000195281; -.
DR HOVERGEN; HBG002800; -.
DR InParanoid; O15514; -.
DR KO; K03012; -.
DR OMA; NRETITA; -.
DR OrthoDB; EOG7RFTK1; -.
DR PhylomeDB; O15514; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_1892; Elongation arrest and recovery.
DR Reactome; REACT_216; DNA Repair.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; POLR2D; human.
DR EvolutionaryTrace; O15514; -.
DR GeneWiki; RNA_polymerase_II_subunit_B4; -.
DR GenomeRNAi; 5433; -.
DR NextBio; 21021; -.
DR PRO; PR:O15514; -.
DR ArrayExpress; O15514; -.
DR Bgee; O15514; -.
DR CleanEx; HS_POLR2D; -.
DR Genevestigator; O15514; -.
DR GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:UniProtKB.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IMP:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR010997; HRDC-like.
DR InterPro; IPR005574; RNA_pol_II_Rpb4.
DR InterPro; IPR006590; RNA_pol_II_Rpb4_core.
DR Pfam; PF03874; RNA_pol_Rpb4; 1.
DR SMART; SM00657; RPOL4c; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; DNA-directed RNA polymerase; Nucleus;
KW Reference proteome; Transcription.
FT CHAIN 1 142 DNA-directed RNA polymerase II subunit
FT RPB4.
FT /FTId=PRO_0000073981.
FT HELIX 17 19
FT STRAND 24 28
FT HELIX 34 49
FT HELIX 59 70
FT HELIX 77 88
FT HELIX 94 103
FT HELIX 108 114
FT HELIX 116 118
FT TURN 119 121
FT HELIX 124 137
SQ SEQUENCE 142 AA; 16311 MW; 8A670386C433BE93 CRC64;
MAAGGSDPRA GDVEEDASQL IFPKEFETAE TLLNSEVHML LEHRKQQNES AEDEQELSEV
FMKTLNYTAR FSRFKNRETI ASVRSLLLQK KLHKFELACL ANLCPETAEE SKALIPSLEG
RFEDEELQQI LDDIQTKRSF QY
//
ID RPB4_HUMAN Reviewed; 142 AA.
AC O15514; Q52LT4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1998, sequence version 1.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB4;
DE Short=RNA polymerase II subunit B4;
DE AltName: Full=DNA-directed RNA polymerase II subunit D;
DE AltName: Full=RNA polymerase II 16 kDa subunit;
DE Short=RPB16;
GN Name=POLR2D;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Cervix carcinoma;
RX PubMed=9528765;
RA Khazak V., Estojak J., Cho H., Majors J.A., Sonoda G., Testa J.R.,
RA Golemis E.A.;
RT "Analysis of the interaction of the novel RNA polymerase II (pol II)
RT subunit hsRPB4 with its partner hsRPB7 and with pol II.";
RL Mol. Cell. Biol. 18:1935-1945(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
RA Kershnar E., Wu S.-Y., Chiang C.-M.;
RT "Immunoaffinity purification and functional characterization of human
RT transcription factor IIH and RNA polymerase II from clonal cell lines
RT that conditionally express epitope-tagged subunits of the multiprotein
RT complexes.";
RL J. Biol. Chem. 273:34444-34453(1998).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF THE POL II RPB4-RPB7
RP SUBCOMPLEX.
RX PubMed=16282592; DOI=10.1093/nar/gki945;
RA Meka H., Werner F., Cordell S.C., Onesti S., Brick P.;
RT "Crystal structure and RNA binding of the Rpb4/Rpb7 subunits of human
RT RNA polymerase II.";
RL Nucleic Acids Res. 33:6435-6444(2005).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC of DNA into RNA using the four ribonucleoside triphosphates as
CC substrates. Component of RNA polymerase II which synthesizes mRNA
CC precursors and many functional non-coding RNAs. Pol II is the
CC central component of the basal RNA polymerase II transcription
CC machinery. It is composed of mobile elements that move relative to
CC each other. RPB4 is part of a subcomplex with RPB7 that binds to a
CC pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp
CC element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7
CC in the closed conformation thus preventing double-stranded DNA to
CC enter the active site cleft. The RPB4-RPB7 subcomplex binds
CC single-stranded DNA and RNA (By similarity).
CC -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex
CC consisting of 12 subunits. RPB4 and RPB7 form a subcomplex that
CC protrudes from the 10-subunit Pol II core complex.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB4 RNA polymerase subunit
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U89387; AAC52056.1; -; Genomic_DNA.
DR EMBL; U85510; AAC80226.1; -; mRNA.
DR EMBL; BC017205; AAH17205.1; -; mRNA.
DR EMBL; BC093795; AAH93795.1; -; mRNA.
DR EMBL; BC093797; AAH93797.1; -; mRNA.
DR RefSeq; NP_004796.1; NM_004805.3.
DR UniGene; Hs.715348; -.
DR PDB; 2C35; X-ray; 2.70 A; A/C/E/G=1-142.
DR PDBsum; 2C35; -.
DR ProteinModelPortal; O15514; -.
DR SMR; O15514; 14-141.
DR DIP; DIP-32912N; -.
DR IntAct; O15514; 8.
DR STRING; 9606.ENSP00000272645; -.
DR PhosphoSite; O15514; -.
DR PaxDb; O15514; -.
DR PeptideAtlas; O15514; -.
DR PRIDE; O15514; -.
DR DNASU; 5433; -.
DR Ensembl; ENST00000272645; ENSP00000272645; ENSG00000144231.
DR GeneID; 5433; -.
DR KEGG; hsa:5433; -.
DR UCSC; uc002tpj.3; human.
DR CTD; 5433; -.
DR GeneCards; GC02M128649; -.
DR HGNC; HGNC:9191; POLR2D.
DR HPA; HPA046092; -.
DR MIM; 606017; gene.
DR neXtProt; NX_O15514; -.
DR PharmGKB; PA33511; -.
DR eggNOG; COG5250; -.
DR HOGENOM; HOG000195281; -.
DR HOVERGEN; HBG002800; -.
DR InParanoid; O15514; -.
DR KO; K03012; -.
DR OMA; NRETITA; -.
DR OrthoDB; EOG7RFTK1; -.
DR PhylomeDB; O15514; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_1675; mRNA Processing.
DR Reactome; REACT_1788; Transcription.
DR Reactome; REACT_1892; Elongation arrest and recovery.
DR Reactome; REACT_216; DNA Repair.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; POLR2D; human.
DR EvolutionaryTrace; O15514; -.
DR GeneWiki; RNA_polymerase_II_subunit_B4; -.
DR GenomeRNAi; 5433; -.
DR NextBio; 21021; -.
DR PRO; PR:O15514; -.
DR ArrayExpress; O15514; -.
DR Bgee; O15514; -.
DR CleanEx; HS_POLR2D; -.
DR Genevestigator; O15514; -.
DR GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:UniProtKB.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IMP:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
DR GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
DR GO; GO:0016032; P:viral process; TAS:Reactome.
DR InterPro; IPR010997; HRDC-like.
DR InterPro; IPR005574; RNA_pol_II_Rpb4.
DR InterPro; IPR006590; RNA_pol_II_Rpb4_core.
DR Pfam; PF03874; RNA_pol_Rpb4; 1.
DR SMART; SM00657; RPOL4c; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; DNA-directed RNA polymerase; Nucleus;
KW Reference proteome; Transcription.
FT CHAIN 1 142 DNA-directed RNA polymerase II subunit
FT RPB4.
FT /FTId=PRO_0000073981.
FT HELIX 17 19
FT STRAND 24 28
FT HELIX 34 49
FT HELIX 59 70
FT HELIX 77 88
FT HELIX 94 103
FT HELIX 108 114
FT HELIX 116 118
FT TURN 119 121
FT HELIX 124 137
SQ SEQUENCE 142 AA; 16311 MW; 8A670386C433BE93 CRC64;
MAAGGSDPRA GDVEEDASQL IFPKEFETAE TLLNSEVHML LEHRKQQNES AEDEQELSEV
FMKTLNYTAR FSRFKNRETI ASVRSLLLQK KLHKFELACL ANLCPETAEE SKALIPSLEG
RFEDEELQQI LDDIQTKRSF QY
//
MIM
606017
*RECORD*
*FIELD* NO
606017
*FIELD* TI
*606017 POLYMERASE II, RNA, SUBUNIT D; POLR2D
;;RPB4, S. CEREVISIAE, HOMOLOG OF;;
RNA POLYMERASE II, 16.3-KD SUBUNIT
read more*FIELD* TX
The DNA-dependent RNA polymerase II (EC 2.7.7.6) is responsible for the
transcription of protein-encoding genes. It is composed of 10 to 14
subunits ranging in mass from approximately 220 kD (POLR2A; 180660) to
approximately 7 kD (POLR2K; 606033). For general information on the
structure and function of RNA polymerase II, see 180660.
CLONING
Using POLR2G (602013), the human homolog of yeast RPB7, as a probe in a
2-hybrid screen, Khazak et al. (1998) identified POLR2D, the human
homolog of yeast RPB4. The full-length POLR2D cDNA encodes a 142-amino
acid protein with a calculated molecular mass of 16.3 kD. The protein
shares 98% sequence identity with its mouse homolog. Northern blot
analysis detected 2- and 5.5-kb POLR2D transcripts in all tissues
tested, with highest levels in skeletal muscle and heart.
Immunofluorescence studies demonstrated that POLR2D is localized in the
nucleus.
GENE STRUCTURE
Khazak et al. (1998) determined that the POLR2D gene contains 4 exons
and spans approximately 13 kb of genomic DNA.
GENE FUNCTION
Khazak et al. (1998) demonstrated that POLR2D associates strongly and
specifically with POLR2G when expressed in yeast or in mammalian cells
and copurifies with intact pol II. The association of POLR2D and POLR2G
appeared to require sequences spanning the N-terminal half of the POLR2D
protein, whereas no truncation of POLR2G was observed to associate with
POLR2D. Khazak et al. (1998) showed that POLR2D does not detectably
associate with yeast RPB7 and only partially complements RPB4 null
phenotypes in yeast.
MAPPING
By FISH, Khazak et al. (1998) mapped the POLR2D gene to chromosome 2q21.
*FIELD* RF
1. Khazak, V.; Estojak, J.; Cho, H.; Majors, J.; Sonoda, G.; Testa,
J. R.; Golemis, E. A.: Analysis of the interaction of the novel RNA
polymerase II (pol II) subunit hsRPB4 with its partner hsRPB7 and
with pol II. Molec. Cell. Biol. 18: 1935-1945, 1998.
*FIELD* CD
Carol A. Bocchini: 6/15/2001
*FIELD* ED
carol: 06/19/2001
alopez: 6/19/2001
carol: 6/19/2001
mgross: 6/15/2001
carol: 6/15/2001
*RECORD*
*FIELD* NO
606017
*FIELD* TI
*606017 POLYMERASE II, RNA, SUBUNIT D; POLR2D
;;RPB4, S. CEREVISIAE, HOMOLOG OF;;
RNA POLYMERASE II, 16.3-KD SUBUNIT
read more*FIELD* TX
The DNA-dependent RNA polymerase II (EC 2.7.7.6) is responsible for the
transcription of protein-encoding genes. It is composed of 10 to 14
subunits ranging in mass from approximately 220 kD (POLR2A; 180660) to
approximately 7 kD (POLR2K; 606033). For general information on the
structure and function of RNA polymerase II, see 180660.
CLONING
Using POLR2G (602013), the human homolog of yeast RPB7, as a probe in a
2-hybrid screen, Khazak et al. (1998) identified POLR2D, the human
homolog of yeast RPB4. The full-length POLR2D cDNA encodes a 142-amino
acid protein with a calculated molecular mass of 16.3 kD. The protein
shares 98% sequence identity with its mouse homolog. Northern blot
analysis detected 2- and 5.5-kb POLR2D transcripts in all tissues
tested, with highest levels in skeletal muscle and heart.
Immunofluorescence studies demonstrated that POLR2D is localized in the
nucleus.
GENE STRUCTURE
Khazak et al. (1998) determined that the POLR2D gene contains 4 exons
and spans approximately 13 kb of genomic DNA.
GENE FUNCTION
Khazak et al. (1998) demonstrated that POLR2D associates strongly and
specifically with POLR2G when expressed in yeast or in mammalian cells
and copurifies with intact pol II. The association of POLR2D and POLR2G
appeared to require sequences spanning the N-terminal half of the POLR2D
protein, whereas no truncation of POLR2G was observed to associate with
POLR2D. Khazak et al. (1998) showed that POLR2D does not detectably
associate with yeast RPB7 and only partially complements RPB4 null
phenotypes in yeast.
MAPPING
By FISH, Khazak et al. (1998) mapped the POLR2D gene to chromosome 2q21.
*FIELD* RF
1. Khazak, V.; Estojak, J.; Cho, H.; Majors, J.; Sonoda, G.; Testa,
J. R.; Golemis, E. A.: Analysis of the interaction of the novel RNA
polymerase II (pol II) subunit hsRPB4 with its partner hsRPB7 and
with pol II. Molec. Cell. Biol. 18: 1935-1945, 1998.
*FIELD* CD
Carol A. Bocchini: 6/15/2001
*FIELD* ED
carol: 06/19/2001
alopez: 6/19/2001
carol: 6/19/2001
mgross: 6/15/2001
carol: 6/15/2001