PAI2B_MOUSE
ID PAI2B_MOUSE Reviewed; 136 AA.
AC Q91W45; B9EJI7; Q69ZQ4; Q8BL93;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Polyadenylate-binding protein-interacting protein 2B;
DE Short=PABP-interacting protein 2B;
DE Short=PAIP-2B;
DE Short=Poly(A)-binding protein-interacting protein 2B;
GN Name=Paip2b; Synonyms=Kiaa1155;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Eye, and Mammary tumor;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16804161; DOI=10.1261/rna.106506;
RA Berlanga J.J., Baass A., Sonenberg N.;
RT "Regulation of poly(A) binding protein function in translation:
RT Characterization of the Paip2 homolog, Paip2B.";
RL RNA 12:1556-1568(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Inhibits translation of capped and polyadenylated mRNAs by
CC displacing PABPC1 from the poly(A) tail.
CC {ECO:0000250|UniProtKB:Q9ULR5}.
CC -!- SUBUNIT: Interacts (via central acidic portion and C-terminus) with
CC PABPC1 (via the second and third RRM domains and the C-terminus).
CC {ECO:0000250|UniProtKB:Q9ULR5}.
CC -!- TISSUE SPECIFICITY: Expressed at very high levels in pancreas, at high
CC levels in testis and at moderately high levels in brain, heart and lung
CC (at protein level). {ECO:0000269|PubMed:16804161}.
CC -!- PTM: Ubiquitinated in vitro. {ECO:0000250|UniProtKB:Q9ULR5}.
CC -!- SIMILARITY: Belongs to the PAIP2 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-14 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32392.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173114; BAD32392.1; ALT_INIT; mRNA.
DR EMBL; AK045922; BAC32533.1; -; mRNA.
DR EMBL; AK159287; BAE34963.1; -; mRNA.
DR EMBL; AK168804; BAE40634.1; -; mRNA.
DR EMBL; BC017133; AAH17133.2; -; mRNA.
DR EMBL; BC034096; AAH34096.2; -; mRNA.
DR EMBL; BC147239; AAI47240.1; -; mRNA.
DR EMBL; BC147240; AAI47241.1; -; mRNA.
DR CCDS; CCDS20287.1; -.
DR RefSeq; NP_666281.2; NM_146169.2.
DR AlphaFoldDB; Q91W45; -.
DR STRING; 10090.ENSMUSP00000050404; -.
DR PhosphoSitePlus; Q91W45; -.
DR EPD; Q91W45; -.
DR MaxQB; Q91W45; -.
DR PaxDb; Q91W45; -.
DR PeptideAtlas; Q91W45; -.
DR PRIDE; Q91W45; -.
DR ProteomicsDB; 295453; -.
DR Antibodypedia; 56903; 14 antibodies from 9 providers.
DR DNASU; 232164; -.
DR Ensembl; ENSMUST00000058383; ENSMUSP00000050404; ENSMUSG00000045896.
DR GeneID; 232164; -.
DR KEGG; mmu:232164; -.
DR UCSC; uc009cok.2; mouse.
DR CTD; 400961; -.
DR MGI; MGI:2386865; Paip2b.
DR VEuPathDB; HostDB:ENSMUSG00000045896; -.
DR eggNOG; ENOG502S63Z; Eukaryota.
DR GeneTree; ENSGT00390000017284; -.
DR HOGENOM; CLU_134152_0_0_1; -.
DR InParanoid; Q91W45; -.
DR OMA; QGLNGHE; -.
DR OrthoDB; 1624094at2759; -.
DR PhylomeDB; Q91W45; -.
DR TreeFam; TF326855; -.
DR BioGRID-ORCS; 232164; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Paip2b; mouse.
DR PRO; PR:Q91W45; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91W45; protein.
DR Bgee; ENSMUSG00000045896; Expressed in primary oocyte and 254 other tissues.
DR ExpressionAtlas; Q91W45; baseline and differential.
DR Genevisible; Q91W45; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; ISS:UniProtKB.
DR GO; GO:0008143; F:poly(A) binding; ISO:MGI.
DR GO; GO:0030371; F:translation repressor activity; IBA:GO_Central.
DR GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR040396; PAIP2-like.
DR PANTHER; PTHR13154; PTHR13154; 1.
DR Pfam; PF07145; PAM2; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Repressor; Translation regulation; Ubl conjugation.
FT CHAIN 1..136
FT /note="Polyadenylate-binding protein-interacting protein
FT 2B"
FT /id="PRO_0000317295"
FT REGION 15..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 21
FT /note="S -> G (in Ref. 2; BAC32533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 136 AA; 15472 MW; 55D9D63C5133C2FA CRC64;
MTTLNTGSAR ISIMNGSSVA STSPSVKCKE DQGLNGHEEK ENPFAEYMWM ENEEDFNRQV
EEELQEQDFL DRCFQEMLDE EDQDWFIPAR DLPQAVGHLQ QQLNGLSVGD SHESEDILSK
SNLNPDAKEF VPGVKY
