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Terminal uridylyltransferase cid1 (TUTase cid1) (EC 2.7.7.19) (EC 2.7.7.52) (Caffeine-induced death protein 1) (Poly(A) polymerase cid1) (PAP) (Poly(U) polymerase cid1) (PUP)

 CID1_SCHPO              Reviewed;         405 AA.
O13833; O94608;
14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 2.
28-FEB-2018, entry version 120.
RecName: Full=Terminal uridylyltransferase cid1 {ECO:0000305};
Short=TUTase cid1 {ECO:0000305};
EC=2.7.7.19 {ECO:0000269|PubMed:12218190, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298, ECO:0000269|PubMed:25712096};
EC=2.7.7.52 {ECO:0000269|PubMed:17353264, ECO:0000269|PubMed:17449726, ECO:0000269|PubMed:19430462, ECO:0000269|PubMed:22751018, ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298};
AltName: Full=Caffeine-induced death protein 1 {ECO:0000303|PubMed:10757807};
AltName: Full=Poly(A) polymerase cid1 {ECO:0000303|PubMed:12218190};
Short=PAP {ECO:0000303|PubMed:12218190};
AltName: Full=Poly(U) polymerase cid1 {ECO:0000303|PubMed:17449726};
Short=PUP {ECO:0000303|PubMed:22608966};
Name=cid1 {ECO:0000303|PubMed:10757807}; ORFNames=SPAC19D5.03;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
STRAIN=972 / ATCC 24843;
PubMed=10757807; DOI=10.1128/MCB.20.9.3234-3244.2000;
Wang S.-W., Toda T., MacCallum R., Harris A.L., Norbury C.;
"Cid1, a fission yeast protein required for S-M checkpoint control
when DNA polymerase delta or epsilon is inactivated.";
Mol. Cell. Biol. 20:3234-3244(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-101 AND ASP-103, AND
SUBCELLULAR LOCATION.
PubMed=12218190; DOI=10.1073/pnas.192467799;
Read R.L., Martinho R.G., Wang S.W., Carr A.M., Norbury C.J.;
"Cytoplasmic poly(A) polymerases mediate cellular responses to S phase
arrest.";
Proc. Natl. Acad. Sci. U.S.A. 99:12079-12084(2002).
[4]
FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
PubMed=17353264; DOI=10.1128/MCB.02209-06;
Rissland O.S., Mikulasova A., Norbury C.J.;
"Efficient RNA polyuridylation by noncanonical poly(A) polymerases.";
Mol. Cell. Biol. 27:3612-3624(2007).
[5]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=17449726; DOI=10.1261/rna.514007;
Kwak J.E., Wickens M.;
"A family of poly(U) polymerases.";
RNA 13:860-867(2007).
[6]
FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
PubMed=19430462; DOI=10.1038/nsmb.1601;
Rissland O.S., Norbury C.J.;
"Decapping is preceded by 3' uridylation in a novel pathway of bulk
mRNA turnover.";
Nat. Struct. Mol. Biol. 16:616-623(2009).
[7]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH UTP,
RNA-BINDING, MUTAGENESIS OF ASP-101; ASP-103; LYS-133; ARG-137;
ARG-277; LYS-282; LYS-321; ARG-323; ASP-330; GLU-333 AND HIS-336, AND
CATALYTIC ACTIVITY.
PubMed=22751018; DOI=10.1038/nsmb.2329;
Yates L.A., Fleurdepine S., Rissland O.S., De Colibus L., Harlos K.,
Norbury C.J., Gilbert R.J.;
"Structural basis for the activity of a cytoplasmic RNA terminal
uridylyl transferase.";
Nat. Struct. Mol. Biol. 19:782-787(2012).
[8]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 33-377 IN COMPLEX WITH ATP;
CTP AND UTP, COFACTOR, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-160 AND
HIS-336, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=22885303; DOI=10.1093/nar/gks740;
Lunde B.M., Magler I., Meinhart A.;
"Crystal structures of the Cid1 poly (U) polymerase reveal the
mechanism for UTP selectivity.";
Nucleic Acids Res. 40:9815-9824(2012).
[9]
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 40-377 IN COMPLEX WITH UTP
AND MAGNESIUM, AND RNA-BINDING.
PubMed=22608966; DOI=10.1016/j.str.2012.04.006;
Munoz-Tello P., Gabus C., Thore S.;
"Functional implications from the Cid1 poly(U) polymerase crystal
structure.";
Structure 20:977-986(2012).
[10]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 40-377 IN COMPLEX WITH UTP,
MUTAGENESIS OF LYS-144; ASP-160; ASN-165 AND PHE-332, AND CATALYTIC
ACTIVITY.
PubMed=24322298; DOI=10.1093/nar/gkt1278;
Munoz-Tello P., Gabus C., Thore S.;
"A critical switch in the enzymatic properties of the Cid1 protein
deciphered from its product-bound crystal structure.";
Nucleic Acids Res. 42:3372-3380(2014).
[11]
X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 40-405, MUTAGENESIS OF
PHE-88; ASN-164 AND ASN-165, AND CATALYTIC ACTIVITY.
PubMed=25712096; DOI=10.1093/nar/gkv122;
Yates L.A., Durrant B.P., Fleurdepine S., Harlos K., Norbury C.J.,
Gilbert R.J.;
"Structural plasticity of Cid1 provides a basis for its distributive
RNA terminal uridylyl transferase activity.";
Nucleic Acids Res. 43:2968-2979(2015).
-!- FUNCTION: Cytoplasmic uridylyltransferase that mediates the
terminal uridylation of mRNAs with short poly(A) tails such as
such as act1, hcn1 and urg1 mRNAs, hence facilitating global mRNA
decay (PubMed:17353264, PubMed:17449726, PubMed:19430462,
PubMed:22751018, PubMed:22885303). Uridylates the 3' ends of actin
mRNAs upon S-phase arrest (PubMed:17353264). Has also a weak
poly(A) polymerase (PAP) activity (PubMed:22751018,
PubMed:22885303). Residue His-336 is responsible for the
specificity for UTP (PubMed:22751018, PubMed:22885303). Involved
in cell cycle arrest where in association with crb2/rhp9 and chk1
it inhibits unscheduled mitosis (PubMed:10757807).
{ECO:0000269|PubMed:10757807, ECO:0000269|PubMed:17353264,
ECO:0000269|PubMed:17449726, ECO:0000269|PubMed:22751018,
ECO:0000269|PubMed:22885303}.
-!- CATALYTIC ACTIVITY: UTP + RNA(n) = diphosphate + RNA(n+1).
{ECO:0000269|PubMed:17353264, ECO:0000269|PubMed:17449726,
ECO:0000269|PubMed:19430462, ECO:0000269|PubMed:22751018,
ECO:0000269|PubMed:22885303, ECO:0000269|PubMed:24322298,
ECO:0000269|PubMed:25712096}.
-!- CATALYTIC ACTIVITY: ATP + RNA(n) = diphosphate + RNA(n+1).
{ECO:0000269|PubMed:12218190, ECO:0000269|PubMed:22751018,
ECO:0000269|PubMed:22885303}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:17353264,
ECO:0000269|PubMed:22885303};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:17353264};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=12 uM for UTP {ECO:0000269|PubMed:22885303};
KM=312 uM for ATP {ECO:0000269|PubMed:22885303};
Note=Mutation of His-336 to Asn decreases the Km for ATP to 65
uM and increases the Km for UTP to 45 uM.
{ECO:0000269|PubMed:22885303};
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12218190}.
-!- DISRUPTION PHENOTYPE: Stabilizes urg1 transcripts
(PubMed:19430462). {ECO:0000269|PubMed:19430462}.
-!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
{ECO:0000305}.
-!- CAUTION: Has been first identified as a cytoplasmic poly(A)
polymerase (PAP) implicated in cell cycle checkpoint controls
(PubMed:12218190). Further studies showed that cid1 had robust
poly(U) polymerase activity in vitro and that is was rather an RNA
uridylyltransferase (PubMed:17353264, PubMed:17449726).
{ECO:0000269|PubMed:17353264, ECO:0000269|PubMed:17449726,
ECO:0000269|PubMed:19430462}.
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EMBL; CU329670; CAB50789.1; -; Genomic_DNA.
EMBL; AF105076; AAD16889.1; -; mRNA.
PIR; T37963; T37963.
RefSeq; NP_594901.1; NM_001020330.2.
PDB; 4E7X; X-ray; 3.20 A; A/B/C/D=1-405.
PDB; 4E80; X-ray; 3.02 A; A/B/C/D=1-405.
PDB; 4E8F; X-ray; 2.60 A; A/B=1-405.
PDB; 4EP7; X-ray; 2.28 A; A/B=40-377.
PDB; 4FH3; X-ray; 2.00 A; A=33-377.
PDB; 4FH5; X-ray; 2.30 A; A=33-377.
PDB; 4FHP; X-ray; 2.50 A; A=33-377.
PDB; 4FHV; X-ray; 2.10 A; A=33-377.
PDB; 4FHW; X-ray; 2.50 A; A=33-377.
PDB; 4FHX; X-ray; 2.70 A; A=33-377.
PDB; 4FHY; X-ray; 2.70 A; A=33-377.
PDB; 4NKT; X-ray; 1.90 A; A/B=40-377.
PDB; 4NKU; X-ray; 1.94 A; A/B=40-377.
PDB; 4UD4; X-ray; 1.74 A; A/B=40-405.
PDB; 4UD5; X-ray; 2.52 A; A/B=40-405.
PDBsum; 4E7X; -.
PDBsum; 4E80; -.
PDBsum; 4E8F; -.
PDBsum; 4EP7; -.
PDBsum; 4FH3; -.
PDBsum; 4FH5; -.
PDBsum; 4FHP; -.
PDBsum; 4FHV; -.
PDBsum; 4FHW; -.
PDBsum; 4FHX; -.
PDBsum; 4FHY; -.
PDBsum; 4NKT; -.
PDBsum; 4NKU; -.
PDBsum; 4UD4; -.
PDBsum; 4UD5; -.
ProteinModelPortal; O13833; -.
SMR; O13833; -.
BioGrid; 278883; 28.
STRING; 4896.SPAC19D5.03.1; -.
iPTMnet; O13833; -.
MaxQB; O13833; -.
PaxDb; O13833; -.
PRIDE; O13833; -.
EnsemblFungi; SPAC19D5.03.1; SPAC19D5.03.1:pep; SPAC19D5.03.
GeneID; 2542420; -.
KEGG; spo:SPAC19D5.03; -.
EuPathDB; FungiDB:SPAC19D5.03; -.
PomBase; SPAC19D5.03; cid1.
InParanoid; O13833; -.
KO; K13291; -.
OrthoDB; EOG092C34LM; -.
PhylomeDB; O13833; -.
PRO; PR:O13833; -.
Proteomes; UP000002485; Chromosome I.
GO; GO:0005737; C:cytoplasm; IDA:PomBase.
GO; GO:0005829; C:cytosol; HDA:PomBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IDA:PomBase.
GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0003723; F:RNA binding; IDA:PomBase.
GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:PomBase.
GO; GO:0002134; F:UTP binding; IDA:PomBase.
GO; GO:0036450; P:polyuridylation-dependent decapping of nuclear-transcribed mRNA; IMP:PomBase.
GO; GO:0071076; P:RNA 3' uridylation; IDA:PomBase.
InterPro; IPR002058; PAP_assoc.
InterPro; IPR002934; Polymerase_NTP_transf_dom.
Pfam; PF01909; NTP_transf_2; 1.
Pfam; PF03828; PAP_assoc; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Cytoplasm; Magnesium;
Manganese; Metal-binding; Nucleotide-binding; Nucleotidyltransferase;
Reference proteome; Transferase.
CHAIN 1 405 Terminal uridylyltransferase cid1.
/FTId=PRO_0000120312.
DOMAIN 267 336 PAP-associated. {ECO:0000255}.
REGION 168 172 Substrate binding.
{ECO:0000269|PubMed:22608966,
ECO:0000269|PubMed:22751018,
ECO:0000269|PubMed:22885303}.
REGION 211 212 Substrate binding.
{ECO:0000269|PubMed:22608966,
ECO:0000269|PubMed:22751018,
ECO:0000269|PubMed:22885303,
ECO:0000269|PubMed:24322298}.
METAL 101 101 Magnesium; catalytic.
{ECO:0000269|PubMed:22885303}.
METAL 103 103 Magnesium; catalytic.
{ECO:0000269|PubMed:22885303}.
BINDING 90 90 Substrate. {ECO:0000269|PubMed:22608966,
ECO:0000269|PubMed:22751018,
ECO:0000269|PubMed:22885303,
ECO:0000269|PubMed:24322298}.
BINDING 101 101 Substrate. {ECO:0000269|PubMed:22885303}.
BINDING 103 103 Substrate. {ECO:0000269|PubMed:22885303}.
BINDING 171 171 Substrate. {ECO:0000269|PubMed:22885303,
ECO:0000269|PubMed:24322298}.
BINDING 193 193 Substrate. {ECO:0000269|PubMed:22608966,
ECO:0000269|PubMed:22751018,
ECO:0000269|PubMed:22885303,
ECO:0000269|PubMed:24322298}.
BINDING 197 197 Substrate. {ECO:0000269|PubMed:22608966,
ECO:0000269|PubMed:22751018,
ECO:0000269|PubMed:22885303,
ECO:0000269|PubMed:24322298}.
BINDING 211 211 Substrate. {ECO:0000269|PubMed:22885303}.
BINDING 336 336 Substrate. {ECO:0000269|PubMed:22608966,
ECO:0000269|PubMed:22751018,
ECO:0000269|PubMed:22885303,
ECO:0000269|PubMed:24322298}.
BINDING 340 340 Substrate. {ECO:0000269|PubMed:22885303}.
MUTAGEN 88 88 F->D: Impairs catalytic activity.
{ECO:0000269|PubMed:25712096}.
MUTAGEN 101 101 D->A: Abolishes catalytic activity but
does not affect RNA binding; when
associated with A-103.
{ECO:0000269|PubMed:12218190,
ECO:0000269|PubMed:22751018}.
MUTAGEN 103 103 D->A: Abolishes catalytic activity but
does not affect RNA binding; when
associated with A-101.
{ECO:0000269|PubMed:12218190,
ECO:0000269|PubMed:22751018}.
MUTAGEN 133 133 K->A: Impairs binding to RNA; when
associated with A-137; A-321 and A-323.
Impairs also binding to RNA; when
associated with A-137; A-277 and A-282.
{ECO:0000269|PubMed:22751018}.
MUTAGEN 137 137 R->A: Impairs binding to RNA; when
associated with A-133; A-321 and A-323.
Impairs also binding to RNA; when
associated with A-133; A-277 and A-282.
{ECO:0000269|PubMed:22751018}.
MUTAGEN 144 144 K->A: Reduces association with a 15-mer A
stretch but does not affect association
with a 15-mer U stretch.
{ECO:0000269|PubMed:24322298}.
MUTAGEN 160 160 D->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:22885303,
ECO:0000269|PubMed:24322298}.
MUTAGEN 164 164 N->P: Predominantly performs
monouridylation.
{ECO:0000269|PubMed:25712096}.
MUTAGEN 165 165 N->A,P: Abolishes catalytic activity.
{ECO:0000269|PubMed:24322298,
ECO:0000269|PubMed:25712096}.
MUTAGEN 277 277 R->A: Impairs binding to RNA; when
associated with A-282; A-133 and A-137.
Impairs also binding to RNA; when
associated with A-282; A-321 and A-323.
{ECO:0000269|PubMed:22751018}.
MUTAGEN 282 282 K->A: Impairs binding to RNA; when
associated with A-277; A-133 and A-137.
Impairs also binding to RNA; when
associated with A-277; A-321 and A-323.
{ECO:0000269|PubMed:22751018}.
MUTAGEN 321 321 K->A: Impairs binding to RNA; when
associated with A-323; A-277 and A-282.
Impairs also binding to RNA; when
associated with A-323; A-133 and A-137.
{ECO:0000269|PubMed:22751018}.
MUTAGEN 323 323 R->A: Impairs binding to RNA; when
associated with A-321; A-277 and A-282.
Impairs also binding to RNA; when
associated with A-321; A-133 and A-137.
{ECO:0000269|PubMed:22751018}.
MUTAGEN 330 330 D->A: Leads to diminished TUTase
activity. {ECO:0000269|PubMed:22751018}.
MUTAGEN 332 332 F->A: Reduces capacity for binding RNAs.
{ECO:0000269|PubMed:24322298}.
MUTAGEN 333 333 E->A: Leads to diminished TUTase
activity. {ECO:0000269|PubMed:22751018}.
MUTAGEN 336 336 H->A,N: Abolishes the UTP specificity and
converts Cid1 from a TUTase into a
poly(A) polymerase (PAP).
{ECO:0000269|PubMed:22751018,
ECO:0000269|PubMed:22885303}.
HELIX 42 55 {ECO:0000244|PDB:4UD4}.
HELIX 59 79 {ECO:0000244|PDB:4UD4}.
STRAND 84 89 {ECO:0000244|PDB:4UD4}.
HELIX 90 93 {ECO:0000244|PDB:4UD4}.
STRAND 97 99 {ECO:0000244|PDB:4FH3}.
STRAND 102 107 {ECO:0000244|PDB:4UD4}.
HELIX 115 127 {ECO:0000244|PDB:4UD4}.
STRAND 131 137 {ECO:0000244|PDB:4UD4}.
STRAND 140 147 {ECO:0000244|PDB:4UD4}.
STRAND 159 164 {ECO:0000244|PDB:4UD4}.
HELIX 166 181 {ECO:0000244|PDB:4UD4}.
HELIX 185 198 {ECO:0000244|PDB:4UD4}.
HELIX 204 206 {ECO:0000244|PDB:4UD4}.
HELIX 211 224 {ECO:0000244|PDB:4UD4}.
STRAND 226 228 {ECO:0000244|PDB:4UD4}.
TURN 234 236 {ECO:0000244|PDB:4UD4}.
HELIX 256 258 {ECO:0000244|PDB:4UD4}.
HELIX 268 281 {ECO:0000244|PDB:4UD4}.
TURN 285 287 {ECO:0000244|PDB:4UD4}.
STRAND 288 290 {ECO:0000244|PDB:4EP7}.
STRAND 292 294 {ECO:0000244|PDB:4UD4}.
HELIX 301 304 {ECO:0000244|PDB:4UD4}.
STRAND 310 313 {ECO:0000244|PDB:4UD5}.
STRAND 319 322 {ECO:0000244|PDB:4UD5}.
STRAND 325 329 {ECO:0000244|PDB:4EP7}.
STRAND 331 333 {ECO:0000244|PDB:4UD4}.
HELIX 338 341 {ECO:0000244|PDB:4UD4}.
HELIX 344 361 {ECO:0000244|PDB:4UD4}.
STRAND 364 367 {ECO:0000244|PDB:4UD4}.
HELIX 370 374 {ECO:0000244|PDB:4UD4}.
SEQUENCE 405 AA; 46257 MW; 0AA24B4411B61027 CRC64;
MNISSAQFIP GVHTVEEIEA EIHKNLHISK SCSYQKVPNS HKEFTKFCYE VYNEIKISDK
EFKEKRAALD TLRLCLKRIS PDAELVAFGS LESGLALKNS DMDLCVLMDS RVQSDTIALQ
FYEELIAEGF EGKFLQRARI PIIKLTSDTK NGFGASFQCD IGFNNRLAIH NTLLLSSYTK
LDARLKPMVL LVKHWAKRKQ INSPYFGTLS SYGYVLMVLY YLIHVIKPPV FPNLLLSPLK
QEKIVDGFDV GFDDKLEDIP PSQNYSSLGS LLHGFFRFYA YKFEPREKVV TFRRPDGYLT
KQEKGWTSAT EHTGSADQII KDRYILAIED PFEISHNVGR TVSSSGLYRI RGEFMAASRL
LNSRSYPIPY DSLFEEAPIP PRRQKKTDEQ SNKKLLNETD GDNSE


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EIAAB40389 Bos taurus,Bovine,RBM21,RNA-binding motif protein 21,RNA-binding protein 21,Speckle targeted PIP5K1A-regulated poly(A) polymerase,Star-PAP,TUT1,U6 snRNA-specific terminal uridylyltransferase 1,U6-TUTa
EIAAB40390 Homo sapiens,Human,RBM21,RNA-binding motif protein 21,RNA-binding protein 21,Speckle targeted PIP5K1A-regulated poly(A) polymerase,Star-PAP,TUT1,U6 snRNA-specific terminal uridylyltransferase 1,U6-TUT
25-532 TUT1 is a nucleotidyl transferase that functions as both a terminal uridylyltransferase and a nuclear poly (A) polymerase. TUT1 specifically adds and removes nucleotides from the 3' end of small nucle 0.05 mg
25-128 TUT1 is a nucleotidyl transferase that functions as both a terminal uridylyltransferase and a nuclear poly (A) polymerase. TUT1 specifically adds and removes nucleotides from the 3' end of small nucle 0.05 mg
EIAAB29933 Homo sapiens,Human,PARP7,PARP-7,Poly [ADP-ribose] polymerase 7,TCDD-inducible poly [ADP-ribose] polymerase,TIPARP
EIAAB29848 Homo sapiens,Human,Neo-PAP,Neo-poly(A) polymerase,PAP2,PAPG,PAP-gamma,PAPOLG,Poly(A) polymerase gamma,Polynucleotide adenylyltransferase gamma,SRP RNA 3'-adenylating enzyme
EIAAB29926 193 kDa vault protein,ADPRTL1,Homo sapiens,Human,KIAA0177,PARP4,PARP-4,PARPL,PARP-related_IalphaI-related H5_proline-rich,PH5P,Poly [ADP-ribose] polymerase 4,Vault poly(ADP-ribose) polymerase,VPARP
EIAAB29846 Homo sapiens,Human,PAP-beta,PAPOLB,PAPT,Poly(A) polymerase beta,Polynucleotide adenylyltransferase beta,Testis-specific poly(A) polymerase
EIAAB29845 Mouse,Mus musculus,PAP-beta,Papolb,Papt,Poly(A) polymerase beta,Polynucleotide adenylyltransferase beta,Testis-specific poly(A) polymerase,Tpap
EIAAB29839 DNA polymerase kappa,DNA polymerase sigma,Homo sapiens,Human,LAK-1,PAP-associated domain-containing protein 7,PAPD7,POLS,Terminal uridylyltransferase 5,Topoisomerase-related function protein 4-1,TRF4,
MCA1522T MOUSE ANTI POLY(ADP_RIBOSE) POLYMERASE, Product Type Monoclonal Antibody, Specificity POLY(ADP_RIBOSE) POLYMERASE, Target Species Human, Host Mouse, Format S_N, Isotypes IgG1, Applications C, P 0.2 ml
SCH-MCA1522T MOUSE ANTI POLY(ADP_RIBOSE) POLYMERASE, Product Type Monoclonal Antibody, Specificity POLY(ADP_RIBOSE) POLYMERASE, Target Species Human, Host Mouse, Format S_N, Isotypes IgG1, Applications C, P 0.2 ml
SCH-MCA1522G MOUSE ANTI POLY(ADP_RIBOSE) POLYMERASE, Product Type Monoclonal Antibody, Specificity POLY(ADP_RIBOSE) POLYMERASE, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications 0.1 mg
MCA1522G MOUSE ANTI POLY(ADP_RIBOSE) POLYMERASE, Product Type Monoclonal Antibody, Specificity POLY(ADP_RIBOSE) POLYMERASE, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications 0.1 mg
20-783-70611 MOUSE ANTI POLY(ADP-RIBOSE) POLYMERASE - POLY (ADP-RIBOSE) POLYMERASE; Monoclonal 0.1 mg
MCA2911Z MOUSE ANTI HUMAN POLY(ADP_RIBOSE) POLYMERASE Azide Free, Product Type Monoclonal Antibody, Specificity POLY(ADP_RIBOSE) POLYMERASE, Target Species Human, Host Mouse, Format Azide Free, Isotypes 0.1 mg
18-003-42430 Poly [ADP-ribose] polymerase 2 - EC 2.4.2.30; PARP-2; NAD(+) ADP-ribosyltransferase 2; Poly[ADP-ribose] synthetase 2; pADPRT-2; hPARP-2 Polyclonal 0.05 mg Aff Pur
18-003-42429 Poly [ADP-ribose] polymerase 1 - EC 2.4.2.30; PARP-1; ADPRT; NAD(+) ADP-ribosyltransferase 1; Poly[ADP-ribose] synthetase 1 Polyclonal 0.1 mg Protein A
EIAAB29923 Adprt2,ADPRT-2,Adprtl2,Aspartl2,Mouse,mPARP-2,Mus musculus,NAD(+) ADP-ribosyltransferase 2,pADPRT-2,Parp2,PARP-2,Poly [ADP-ribose] polymerase 2,Poly[ADP-ribose] synthase 2
EIAAB29924 ADPRT2,ADPRT-2,ADPRTL2,Homo sapiens,hPARP-2,Human,NAD(+) ADP-ribosyltransferase 2,pADPRT-2,PARP2,PARP-2,Poly [ADP-ribose] polymerase 2,Poly[ADP-ribose] synthase 2
EIAAB29925 ADPRT3,ADPRT-3,ADPRTL3,Homo sapiens,hPARP-3,Human,IRT1,NAD(+) ADP-ribosyltransferase 3,pADPRT-3,PARP3,PARP-3,Poly [ADP-ribose] polymerase 3,Poly[ADP-ribose] synthase 3
EIAAB29836 Homo sapiens,Human,PAP-associated domain-containing protein 5,PAPD5,Terminal uridylyltransferase 3,Topoisomerase-related function protein 4-2,TRF4-2,TUTase 3


 

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