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DNA-directed DNA/RNA polymerase mu (Pol Mu) (EC 2.7.7.7) (Terminal transferase)

 DPOLM_HUMAN             Reviewed;         494 AA.
Q9NP87; D3DVK4; Q6P5X8; Q86WQ9;
16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
10-MAY-2017, entry version 146.
RecName: Full=DNA-directed DNA/RNA polymerase mu;
Short=Pol Mu;
EC=2.7.7.7;
AltName: Full=Terminal transferase;
Name=POLM; Synonyms=polmu;
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).
TISSUE=Placenta;
PubMed=10747040; DOI=10.1093/emboj/19.7.1731;
Dominguez O., Ruiz J.F., Lain de Lera T., Garcia-Diaz M.,
Gonzalez M.A., Kirchhoff T., Martinez-A C., Bernad A., Blanco L.;
"DNA polymerase mu (Pol mu), homologous to TdT, could act as a DNA
mutator in eukaryotic cells.";
EMBO J. 19:1731-1742(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10982892; DOI=10.1093/nar/28.18.3684;
Aoufouchi S., Flatter E., Dahan A., Faili A., Bertocci B., Storck S.,
Delbos F., Cocea L., Gupta N., Weill J.-C., Reynaud C.-A.;
"Two novel human and mouse DNA polymerases of the polX family.";
Nucleic Acids Res. 28:3684-3693(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASP-107; ALA-220;
PHE-246 AND PHE-484.
NIEHS SNPs program;
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Blood, and Brain;
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).
[7]
FUNCTION.
PubMed=12640116; DOI=10.1128/MCB.23.7.2309-2315.2003;
Nick McElhinny S.A., Ramsden D.A.;
"Polymerase mu is a DNA-directed DNA/RNA polymerase.";
Mol. Cell. Biol. 23:2309-2315(2003).
[8]
FUNCTION, AND SUGAR DISCRIMINATION SITE.
PubMed=12888504; DOI=10.1093/nar/gkg637;
Ruiz J.F., Juarez R., Garcia-Diaz M., Terrados G., Picher A.J.,
Gonzalez-Barrera S., Fernandez de Henestrosa A.R., Blanco L.;
"Lack of sugar discrimination by human Pol mu requires a single
glycine residue.";
Nucleic Acids Res. 31:4441-4449(2003).
[9]
FUNCTION.
PubMed=17483519; DOI=10.1093/nar/gkm243;
Capp J.P., Boudsocq F., Besnard A.G., Lopez B.S., Cazaux C.,
Hoffmann J.S., Canitrot Y.;
"Involvement of DNA polymerase mu in the repair of a specific subset
of DNA double-strand breaks in mammalian cells.";
Nucleic Acids Res. 35:3551-3560(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, 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).
[11]
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, 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).
[15]
STRUCTURE BY NMR OF 21-124, AND FUNCTION.
PubMed=17915942; DOI=10.1021/bi7007728;
DeRose E.F., Clarkson M.W., Gilmore S.A., Galban C.J., Tripathy A.,
Havener J.M., Mueller G.A., Ramsden D.A., London R.E., Lee A.L.;
"Solution structure of polymerase mu's BRCT Domain reveals an element
essential for its role in nonhomologous end joining.";
Biochemistry 46:12100-12110(2007).
[16]
STRUCTURE BY NMR OF 18-147.
RIKEN structural genomics initiative (RSGI);
"Solution structure of BRCT domain of DNA polymerase mu.";
Submitted (JAN-2007) to the PDB data bank.
-!- FUNCTION: Gap-filling polymerase involved in repair of DNA double-
strand breaks by non-homologous end joining (NHEJ). Participates
in immunoglobulin (Ig) light chain gene rearrangement in V(D)J
recombination. {ECO:0000269|PubMed:12640116,
ECO:0000269|PubMed:12888504, ECO:0000269|PubMed:17483519,
ECO:0000269|PubMed:17915942}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- INTERACTION:
P14079:tax (xeno); NbExp=3; IntAct=EBI-9675790, EBI-9675698;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9NP87-1; Sequence=Displayed;
Name=2;
IsoId=Q9NP87-2; Sequence=VSP_055290;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9NP87-3; Sequence=VSP_055288, VSP_055289, VSP_055291;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in a number of tissues. Abundant in
thymus.
-!- MISCELLANEOUS: DPOLM has a reduced ability to distinguish dNTP and
rNTP as substrates, and elongates them on DNA primer strand with a
similar efficiency. It is able to polymerize nucleotides on RNA
primer strands.
-!- SIMILARITY: Belongs to the DNA polymerase type-X family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/polm/";
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EMBL; AJ131891; CAB65075.2; -; mRNA.
EMBL; AF176097; AAF26284.1; -; mRNA.
EMBL; AY899911; AAW65376.1; -; Genomic_DNA.
EMBL; AC017116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471128; EAW61122.1; -; Genomic_DNA.
EMBL; CH471128; EAW61123.1; -; Genomic_DNA.
EMBL; CH471128; EAW61124.1; -; Genomic_DNA.
EMBL; CH471128; EAW61126.1; -; Genomic_DNA.
EMBL; BC049202; AAH49202.2; -; mRNA.
EMBL; BC062590; AAH62590.1; -; mRNA.
CCDS; CCDS34625.1; -. [Q9NP87-1]
CCDS; CCDS64635.1; -. [Q9NP87-2]
CCDS; CCDS64636.1; -. [Q9NP87-3]
RefSeq; NP_001271259.1; NM_001284330.1. [Q9NP87-3]
RefSeq; NP_001271260.1; NM_001284331.1. [Q9NP87-2]
RefSeq; NP_037416.1; NM_013284.3. [Q9NP87-1]
UniGene; Hs.596982; -.
UniGene; Hs.598038; -.
PDB; 2DUN; NMR; -; A=24-143.
PDB; 2HTF; NMR; -; A=21-124.
PDB; 4LZD; X-ray; 1.85 A; A=132-397, A=411-494.
PDB; 4LZG; X-ray; 1.60 A; A=132-397, A=411-494.
PDB; 4M04; X-ray; 1.90 A; A=132-397, A=411-494.
PDB; 4M0A; X-ray; 1.85 A; A=132-397, A=411-494.
PDB; 4YCX; X-ray; 2.10 A; A=134-494.
PDB; 4YD1; X-ray; 1.75 A; A=134-494.
PDB; 4YD2; X-ray; 2.47 A; A=134-397, A=411-494.
PDBsum; 2DUN; -.
PDBsum; 2HTF; -.
PDBsum; 4LZD; -.
PDBsum; 4LZG; -.
PDBsum; 4M04; -.
PDBsum; 4M0A; -.
PDBsum; 4YCX; -.
PDBsum; 4YD1; -.
PDBsum; 4YD2; -.
ProteinModelPortal; Q9NP87; -.
SMR; Q9NP87; -.
BioGrid; 118168; 14.
IntAct; Q9NP87; 3.
STRING; 9606.ENSP00000242248; -.
BindingDB; Q9NP87; -.
ChEMBL; CHEMBL1914260; -.
iPTMnet; Q9NP87; -.
PhosphoSitePlus; Q9NP87; -.
DMDM; 17366980; -.
EPD; Q9NP87; -.
MaxQB; Q9NP87; -.
PaxDb; Q9NP87; -.
PeptideAtlas; Q9NP87; -.
PRIDE; Q9NP87; -.
Ensembl; ENST00000242248; ENSP00000242248; ENSG00000122678. [Q9NP87-1]
Ensembl; ENST00000335195; ENSP00000335141; ENSG00000122678. [Q9NP87-2]
Ensembl; ENST00000395831; ENSP00000379174; ENSG00000122678. [Q9NP87-3]
GeneID; 27434; -.
KEGG; hsa:27434; -.
UCSC; uc003tjt.5; human. [Q9NP87-1]
CTD; 27434; -.
DisGeNET; 27434; -.
GeneCards; MIR6838; -.
GeneCards; POLM; -.
H-InvDB; HIX0167826; -.
HGNC; HGNC:9185; POLM.
HPA; HPA058900; -.
HPA; HPA066007; -.
MIM; 606344; gene.
neXtProt; NX_Q9NP87; -.
OpenTargets; ENSG00000122678; -.
PharmGKB; PA33505; -.
eggNOG; KOG2534; Eukaryota.
eggNOG; COG1796; LUCA.
GeneTree; ENSGT00530000063002; -.
HOGENOM; HOG000263600; -.
HOVERGEN; HBG003670; -.
InParanoid; Q9NP87; -.
KO; K03513; -.
OMA; PEQKTFF; -.
OrthoDB; EOG091G073W; -.
PhylomeDB; Q9NP87; -.
TreeFam; TF103012; -.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
EvolutionaryTrace; Q9NP87; -.
GeneWiki; DNA_polymerase_mu; -.
GenomeRNAi; 27434; -.
PRO; PR:Q9NP87; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000122678; -.
CleanEx; HS_POLM; -.
ExpressionAtlas; Q9NP87; baseline and differential.
Genevisible; Q9NP87; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IEA:Ensembl.
CDD; cd00027; BRCT; 1.
CDD; cd00141; NT_POLXc; 1.
Gene3D; 3.30.210.10; -; 1.
Gene3D; 3.40.50.10190; -; 1.
InterPro; IPR001357; BRCT_dom.
InterPro; IPR002054; DNA-dir_DNA_pol_X.
InterPro; IPR027249; DNA/RNApol_mu.
InterPro; IPR019843; DNA_pol-X_BS.
InterPro; IPR010996; DNA_pol_b-like_N.
InterPro; IPR028207; DNA_pol_B_palm_palm.
InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
InterPro; IPR022312; DNA_pol_X.
InterPro; IPR029398; PolB_thumb.
InterPro; IPR001726; TdT/Mu.
Pfam; PF14792; DNA_pol_B_palm; 1.
Pfam; PF14791; DNA_pol_B_thumb; 1.
Pfam; PF10391; DNA_pol_lambd_f; 1.
Pfam; PF14716; HHH_8; 1.
PIRSF; PIRSF000817; DNA_NT; 1.
PIRSF; PIRSF501176; DNApol_mu; 1.
PRINTS; PR00869; DNAPOLX.
PRINTS; PR00871; DNAPOLXTDT.
SMART; SM00483; POLXc; 1.
SUPFAM; SSF47802; SSF47802; 1.
SUPFAM; SSF52113; SSF52113; 1.
PROSITE; PS50172; BRCT; 1.
PROSITE; PS00522; DNA_POLYMERASE_X; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; DNA damage;
DNA recombination; DNA repair; DNA-directed DNA polymerase; Magnesium;
Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Transferase.
CHAIN 1 494 DNA-directed DNA/RNA polymerase mu.
/FTId=PRO_0000218787.
DOMAIN 22 122 BRCT. {ECO:0000255|PROSITE-
ProRule:PRU00033}.
REGION 323 332 Involved in ssDNA binding. {ECO:0000250}.
METAL 330 330 Magnesium. {ECO:0000250}.
METAL 332 332 Magnesium. {ECO:0000250}.
METAL 418 418 Magnesium. {ECO:0000250}.
SITE 433 433 Responsible for the low discrimination
between dNTP and rNTP.
MOD_RES 12 12 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 234 276 YQTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQKLTQ
QQ -> APAPPGPEHPSPAVRCRCPAAGGGGSCGAGPAWGH
RHADRRLP (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055288.
VAR_SEQ 277 356 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055289.
VAR_SEQ 279 356 GLQHHQDLSTPVLRSDVDALQQVVEEAVGQALPGATVTLTG
GFRRGKLQGHDVDFLITHPKEGQEAGLLPRVMCRLQD ->
APPGPEHPSPAVRCRCPAAGGGGSCGAGPAWGHRHADRRLP
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055290.
VAR_SEQ 467 494 KTFFQAASEEDIFRHLGLEYLPPEQRNA -> GSSSGKTPR
SRKSCFCCRRHFSKRLQRKTSSDTWALSTFLQSRETPEPAC
VPHFHSGNWAAPNLATECLQADMLPPDPHLHPSPPRPGSSG
GQLCLQDQLSPCWCAAGCDEVGALSASLITV (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_055291.
VARIANT 107 107 E -> D (in dbSNP:rs28382635).
{ECO:0000269|Ref.3}.
/FTId=VAR_022287.
VARIANT 220 220 G -> A (in dbSNP:rs28382644).
{ECO:0000269|Ref.3}.
/FTId=VAR_022288.
VARIANT 246 246 V -> F (in dbSNP:rs28382653).
{ECO:0000269|Ref.3}.
/FTId=VAR_022289.
VARIANT 484 484 L -> F (in dbSNP:rs28382661).
{ECO:0000269|Ref.3}.
/FTId=VAR_022290.
STRAND 26 34 {ECO:0000244|PDB:2DUN}.
HELIX 36 39 {ECO:0000244|PDB:2DUN}.
HELIX 42 54 {ECO:0000244|PDB:2DUN}.
STRAND 55 58 {ECO:0000244|PDB:2DUN}.
STRAND 68 73 {ECO:0000244|PDB:2DUN}.
HELIX 76 89 {ECO:0000244|PDB:2DUN}.
STRAND 98 101 {ECO:0000244|PDB:2DUN}.
HELIX 102 111 {ECO:0000244|PDB:2DUN}.
TURN 119 121 {ECO:0000244|PDB:2DUN}.
HELIX 142 144 {ECO:0000244|PDB:4LZG}.
HELIX 154 169 {ECO:0000244|PDB:4LZG}.
HELIX 173 188 {ECO:0000244|PDB:4LZG}.
STRAND 189 191 {ECO:0000244|PDB:4M04}.
HELIX 196 199 {ECO:0000244|PDB:4LZG}.
HELIX 207 219 {ECO:0000244|PDB:4LZG}.
HELIX 223 230 {ECO:0000244|PDB:4LZG}.
HELIX 232 241 {ECO:0000244|PDB:4LZG}.
HELIX 248 256 {ECO:0000244|PDB:4LZG}.
HELIX 262 266 {ECO:0000244|PDB:4LZG}.
HELIX 269 271 {ECO:0000244|PDB:4LZG}.
HELIX 274 281 {ECO:0000244|PDB:4LZG}.
HELIX 283 286 {ECO:0000244|PDB:4LZG}.
HELIX 292 309 {ECO:0000244|PDB:4LZG}.
STRAND 314 317 {ECO:0000244|PDB:4LZG}.
HELIX 319 322 {ECO:0000244|PDB:4LZG}.
STRAND 326 329 {ECO:0000244|PDB:4LZG}.
STRAND 331 336 {ECO:0000244|PDB:4LZG}.
TURN 340 345 {ECO:0000244|PDB:4LZG}.
HELIX 346 356 {ECO:0000244|PDB:4LZG}.
STRAND 360 362 {ECO:0000244|PDB:4LZG}.
STRAND 387 396 {ECO:0000244|PDB:4LZG}.
STRAND 411 421 {ECO:0000244|PDB:4LZG}.
HELIX 424 426 {ECO:0000244|PDB:4LZG}.
HELIX 427 435 {ECO:0000244|PDB:4LZG}.
HELIX 438 452 {ECO:0000244|PDB:4LZG}.
STRAND 455 457 {ECO:0000244|PDB:4YD1}.
STRAND 461 463 {ECO:0000244|PDB:4LZG}.
TURN 464 467 {ECO:0000244|PDB:4LZG}.
HELIX 475 481 {ECO:0000244|PDB:4LZG}.
HELIX 489 491 {ECO:0000244|PDB:4LZG}.
SEQUENCE 494 AA; 54816 MW; B944059725F8B61F CRC64;
MLPKRRRARV GSPSGDAASS TPPSTRFPGV AIYLVEPRMG RSRRAFLTGL ARSKGFRVLD
ACSSEATHVV MEETSAEEAV SWQERRMAAA PPGCTPPALL DISWLTESLG AGQPVPVECR
HRLEVAGPRK GPLSPAWMPA YACQRPTPLT HHNTGLSEAL EILAEAAGFE GSEGRLLTFC
RAASVLKALP SPVTTLSQLQ GLPHFGEHSS RVVQELLEHG VCEEVERVRR SERYQTMKLF
TQIFGVGVKT ADRWYREGLR TLDDLREQPQ KLTQQQKAGL QHHQDLSTPV LRSDVDALQQ
VVEEAVGQAL PGATVTLTGG FRRGKLQGHD VDFLITHPKE GQEAGLLPRV MCRLQDQGLI
LYHQHQHSCC ESPTRLAQQS HMDAFERSFC IFRLPQPPGA AVGGSTRPCP SWKAVRVDLV
VAPVSQFPFA LLGWTGSKLF QRELRRFSRK EKGLWLNSHG LFDPEQKTFF QAASEEDIFR
HLGLEYLPPE QRNA


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EIAAB35812 C128,DNA-directed RNA polymerase III 127.6 kDa polypeptide,DNA-directed RNA polymerase III subunit B,DNA-directed RNA polymerase III subunit RPC2,Homo sapiens,Human,POLR3B,RNA polymerase III subunit C
EIAAB35794 A-152E5.7,DNA-directed RNA polymerase II 33 kDa polypeptide,DNA-directed RNA polymerase II subunit C,DNA-directed RNA polymerase II subunit RPB3,Homo sapiens,Human,POLR2C,RNA polymerase II subunit 3,R
EIAAB35793 DNA-directed RNA polymerase II 33 kDa polypeptide,DNA-directed RNA polymerase II subunit C,DNA-directed RNA polymerase II subunit RPB3,Mouse,Mus musculus,Polr2c,RNA polymerase II subunit 3,RNA polymer
EIAAB35791 DNA-directed RNA polymerase II 140 kDa polypeptide,DNA-directed RNA polymerase II subunit B,DNA-directed RNA polymerase II subunit RPB2,Mouse,Mus musculus,Polr2b,RNA polymerase II subunit 2,RNA polyme
EIAAB35813 C128,DNA-directed RNA polymerase III 127.6 kDa polypeptide,DNA-directed RNA polymerase III subunit B,DNA-directed RNA polymerase III subunit RPC2,Mouse,Mus musculus,Polr3b,RNA polymerase III subunit C
EIAAB35736 A190,DNA-directed RNA polymerase I largest subunit,DNA-directed RNA polymerase I subunit A,DNA-directed RNA polymerase I subunit RPA1,Homo sapiens,Human,POLR1A,RNA polymerase I 194 kDa subunit,RNA pol
EIAAB35785 DNA-directed RNA polymerase II subunit A,DNA-directed RNA polymerase II subunit RPB1,DNA-directed RNA polymerase III largest subunit,Mouse,Mus musculus,Polr2a,RNA polymerase II subunit B1,Rpii215,Rpo2
EIAAB35784 DNA-directed RNA polymerase II subunit A,DNA-directed RNA polymerase II subunit RPB1,DNA-directed RNA polymerase III largest subunit,Homo sapiens,Human,POLR2,POLR2A,RNA polymerase II subunit B1,RNA-di
EIAAB35808 DNA-directed RNA polymerase III largest subunit,DNA-directed RNA polymerase III subunit A,DNA-directed RNA polymerase III subunit RPC1,Homo sapiens,Human,POLR3A,RNA polymerase III 155 kDa subunit,RNA
EIAAB35737 DNA-directed RNA polymerase I largest subunit,DNA-directed RNA polymerase I subunit A,DNA-directed RNA polymerase I subunit RPA1,Mouse,Mus musculus,Polr1a,RNA polymerase I 194 kDa subunit,RNA polymera
EIAAB35735 A194,DNA-directed RNA polymerase I largest subunit,DNA-directed RNA polymerase I subunit A,DNA-directed RNA polymerase I subunit RPA1,Polr1a,Rat,Rattus norvegicus,RNA polymerase I 194 kDa subunit,RNA
20-372-60270 polymerase (RNA) II (DNA directed) polypeptide G (POLR2G) - Mouse monoclonal anti-human POLR2G antibody; RNA polymerase II subunit B7; DNA-directed RNA polymerase II subunit G; DNA-directed RNA polyme 0.1 mg
EIAAB35832 Bos taurus,Bovine,DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide,DNA-directed RNA polymerase III subunit H,DNA-directed RNA polymerase III subunit RPC8,POLR3H,RNA polymerase III subunit
EIAAB35750 DNA-directed RNA polymerase I subunit E,DNA-directed RNA polymerase I subunit RPA49,Homo sapiens,Human,PAF53,POLR1E,PRAF1,RNA polymerase I subunit A49,RNA polymerase I-associated factor 1,RNA polymera
EIAAB35749 DNA-directed RNA polymerase I subunit E,DNA-directed RNA polymerase I subunit RPA49,Mouse,Mus musculus,Paf53,Polr1e,Praf1,RNA polymerase I subunit A49,RNA polymerase I-associated factor 1,RNA polymera
EIAAB35809 DNA-directed RNA polymerase III subunit K,DNA-directed RNA polymerase III subunit RPC10,Homo sapiens,hRPC11,HsC11p,Human,My010,POLR3K,RNA polymerase III 12.5 kDa subunit,RNA polymerase III subunit C10
EIAAB35822 DNA-directed RNA polymerase III 80 kDa polypeptide,DNA-directed RNA polymerase III subunit RPC5,Homo sapiens,Human,KIAA1452,POLR3E,RNA polymerase III subunit C5
EIAAB35743 DNA-directed RNA polymerase I 135 kDa polypeptide,DNA-directed RNA polymerase I subunit RPA2,Homo sapiens,Human,POLR1B,RNA polymerase I subunit 2,RPA135
EIAAB35787 DNA-directed RNA polymerase II subunit J-1,DNA-directed RNA polymerase II subunit RPB11-a,Homo sapiens,Human,POLR2J,POLR2J1,RNA polymerase II 13.3 kDa subunit,RNA polymerase II subunit B11-a,RPB11a
EIAAB35802 DNA-directed RNA polymerase II subunit I,DNA-directed RNA polymerase II subunit RPB9,Homo sapiens,Human,POLR2I,RNA polymerase II 14.5 kDa subunit,RNA polymerase II subunit B9,RPB14.5
EIAAB35815 DNA-directed RNA polymerase III subunit C,DNA-directed RNA polymerase III subunit RPC3,Homo sapiens,Human,POLR3C,RNA polymerase III 62 kDa subunit,RNA polymerase III subunit C3,RPC62
EIAAB35786 DNA-directed RNA polymerase II subunit J,DNA-directed RNA polymerase II subunit RPB11,Mouse,Mus musculus,Polr2j,RNA polymerase II 13.3 kDa subunit,RNA polymerase II subunit B11,RPB14,Rpo2-4


 

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