Full text data of PAIP1
PAIP1
[Confidence: low (only semi-automatic identification from reviews)]
Polyadenylate-binding protein-interacting protein 1; PABP-interacting protein 1; PAIP-1; Poly(A)-binding protein-interacting protein 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Polyadenylate-binding protein-interacting protein 1; PABP-interacting protein 1; PAIP-1; Poly(A)-binding protein-interacting protein 1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9H074
ID PAIP1_HUMAN Reviewed; 479 AA.
AC Q9H074; A6NKV8; O60455; Q96B61; Q9BS63;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Polyadenylate-binding protein-interacting protein 1;
DE Short=PABP-interacting protein 1;
DE Short=PAIP-1;
DE Short=Poly(A)-binding protein-interacting protein 1;
GN Name=PAIP1;
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 [MRNA] (ISOFORM 1), FUNCTION IN TRANSLATION
RP INITIATION STIMULATION, AND INTERACTION WITH PABPC1 AND EIF4A.
RC TISSUE=Placenta;
RX PubMed=9548260; DOI=10.1038/33198;
RA Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.;
RT "Interaction of polyadenylate-binding protein with the eIF4G homologue
RT PAIP enhances translation.";
RL Nature 392:520-523(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-249 (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, AND IDENTIFICATION
RP IN A COMPLEX WITH HNRPD; SYNCRIP; PABPC1 AND UNR.
RX PubMed=11051545; DOI=10.1016/S0092-8674(00)00102-1;
RA Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H.,
RA Shyu A.-B.;
RT "A mechanism for translationally coupled mRNA turnover: interaction
RT between the poly(A) tail and a c-fos RNA coding determinant via a
RT protein complex.";
RL Cell 103:29-40(2000).
RN [7]
RP INTERACTION WITH PABPC1.
RX PubMed=10970864; DOI=10.1093/emboj/19.17.4723;
RA Gray N.K., Coller J.M., Dickson K.S., Wickens M.;
RT "Multiple portions of poly(A)-binding protein stimulate translation in
RT vivo.";
RL EMBO J. 19:4723-4733(2000).
RN [8]
RP INTERACTION WITH PABPC1.
RX PubMed=11172725; DOI=10.1016/S1097-2765(01)00168-X;
RA Khaleghpour K., Svitkin Y.V., Craig A.W.B., DeMaria C.T., Deo R.C.,
RA Burley S.K., Sonenberg N.;
RT "Translational repression by a novel partner of human poly(A) binding
RT protein, Paip2.";
RL Mol. Cell 7:205-216(2001).
RN [9]
RP INTERACTION WITH PABPC1.
RX PubMed=11997512; DOI=10.1128/MCB.22.11.3769-3782.2002;
RA Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A.,
RA O'Connor-McCourt M., Sonenberg N.;
RT "Paip1 interacts with poly(A) binding protein through two independent
RT binding motifs.";
RL Mol. Cell. Biol. 22:3769-3782(2002).
RN [10]
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).
CC -!- FUNCTION: Acts as a coactivator in the regulation of translation
CC initiation of poly(A)-containing mRNAs. Its stimulatory activity
CC on translation is mediated via its action on PABPC1. Competes with
CC PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1
CC may potentiate contacts between mRNA termini. May also be involved
CC in translationally coupled mRNA turnover. Implicated with other
CC RNA-binding proteins in the cytoplasmic
CC deadenylation/translational and decay interplay of the FOS mRNA
CC mediated by the major coding-region determinant of instability
CC (mCRD) domain.
CC -!- SUBUNIT: Interacts with the RRM1-RRM2 and C-terminus regions of
CC PABPC1 in a 1:1 stoichiometry. Interacts with EIF4A.
CC -!- INTERACTION:
CC P11940:PABPC1; NbExp=11; IntAct=EBI-81519, EBI-81531;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H074-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H074-2; Sequence=VSP_010005;
CC Name=3;
CC IsoId=Q9H074-3; Sequence=VSP_047503;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: Only the PABPC1-interacting motif-1 (PAM1) stimulates
CC translation initiation.
CC -!- SIMILARITY: Contains 1 MIF4G domain.
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DR EMBL; AF013758; AAC39697.2; -; mRNA.
DR EMBL; AL136920; CAB66854.1; -; mRNA.
DR EMBL; AC114956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005295; AAH05295.1; -; mRNA.
DR EMBL; BC015937; AAH15937.1; -; mRNA.
DR EMBL; DB089732; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_006442.2; NM_006451.4.
DR RefSeq; NP_877590.1; NM_182789.3.
DR RefSeq; NP_899152.1; NM_183323.2.
DR RefSeq; XP_005248287.1; XM_005248230.1.
DR UniGene; Hs.482038; -.
DR PDB; 1JH4; NMR; -; B=124-144.
DR PDB; 3NTW; X-ray; 2.60 A; B/D=123-144.
DR PDB; 3RK6; X-ray; 2.00 A; A/B=157-373.
DR PDBsum; 1JH4; -.
DR PDBsum; 3NTW; -.
DR PDBsum; 3RK6; -.
DR ProteinModelPortal; Q9H074; -.
DR SMR; Q9H074; 157-373.
DR IntAct; Q9H074; 7.
DR MINT; MINT-196116; -.
DR STRING; 9606.ENSP00000302768; -.
DR PhosphoSite; Q9H074; -.
DR DMDM; 46397025; -.
DR PaxDb; Q9H074; -.
DR PRIDE; Q9H074; -.
DR DNASU; 10605; -.
DR Ensembl; ENST00000306846; ENSP00000302768; ENSG00000172239.
DR Ensembl; ENST00000338972; ENSP00000339622; ENSG00000172239.
DR Ensembl; ENST00000436644; ENSP00000387729; ENSG00000172239.
DR GeneID; 10605; -.
DR KEGG; hsa:10605; -.
DR UCSC; uc003job.3; human.
DR CTD; 10605; -.
DR GeneCards; GC05M043526; -.
DR HGNC; HGNC:16945; PAIP1.
DR MIM; 605184; gene.
DR neXtProt; NX_Q9H074; -.
DR PharmGKB; PA134941557; -.
DR eggNOG; NOG253454; -.
DR HOGENOM; HOG000285987; -.
DR HOVERGEN; HBG053492; -.
DR InParanoid; Q9H074; -.
DR KO; K14322; -.
DR OMA; EPTFYTE; -.
DR OrthoDB; EOG70CR75; -.
DR PhylomeDB; Q9H074; -.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PAIP1; human.
DR EvolutionaryTrace; Q9H074; -.
DR GeneWiki; PAIP1; -.
DR GenomeRNAi; 10605; -.
DR NextBio; 40270; -.
DR PRO; PR:Q9H074; -.
DR ArrayExpress; Q9H074; -.
DR Bgee; Q9H074; -.
DR CleanEx; HS_PAIP1; -.
DR Genevestigator; Q9H074; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0008494; F:translation activator activity; IDA:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; TAS:UniProtKB.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:ProtInc.
DR Gene3D; 1.25.40.180; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR016021; MIF4-like_typ_1/2/3.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF07145; PAM2; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Reference proteome; Translation regulation.
FT CHAIN 1 479 Polyadenylate-binding protein-interacting
FT protein 1.
FT /FTId=PRO_0000058177.
FT DOMAIN 159 376 MIF4G.
FT REGION 116 143 PABPC1-interacting motif-2 (PAM2).
FT REGION 440 479 PABPC1-interacting motif-1 (PAM1).
FT COMPBIAS 10 36 Gly-rich.
FT COMPBIAS 45 98 Pro-rich.
FT VAR_SEQ 1 112 Missing (in isoform 3).
FT /FTId=VSP_047503.
FT VAR_SEQ 10 88 Missing (in isoform 2).
FT /FTId=VSP_010005.
FT CONFLICT 239 239 R -> C (in Ref. 4; AAH15937).
FT HELIX 158 171
FT HELIX 173 175
FT HELIX 176 190
FT HELIX 194 209
FT HELIX 215 228
FT HELIX 238 250
FT HELIX 253 256
FT HELIX 261 280
FT STRAND 288 291
FT HELIX 294 309
FT HELIX 313 336
FT HELIX 341 355
FT HELIX 360 372
SQ SEQUENCE 479 AA; 53525 MW; A4820607190A3A43 CRC64;
MSDGFDRAPG AGRGRSRGLG RGGGGPEGGG FPNGAGPAER ARHQPPQPKA PGFLQPPPLR
QPRTTPPPGA QCEVPASPQR PSRPGALPEQ TRPLRAPPSS QDKIPQQNSE SAMAKPQVVV
APVLMSKLSV NAPEFYPSGY SSSYTESYED GCEDYPTLSE YVQDFLNHLT EQPGSFETEI
EQFAETLNGC VTTDDALQEL VELIYQQATS IPNFSYMGAR LCNYLSHHLT ISPQSGNFRQ
LLLQRCRTEY EVKDQAAKGD EVTRKRFHAF VLFLGELYLN LEIKGTNGQV TRADILQVGL
RELLNALFSN PMDDNLICAV KLLKLTGSVL EDAWKEKGKM DMEEIIQRIE NVVLDANCSR
DVKQMLLKLV ELRSSNWGRV HATSTYREAT PENDPNYFMN EPTFYTSDGV PFTAADPDYQ
EKYQELLERE DFFPDYEENG TDLSGAGDPY LDDIDDEMDP EIEEAYEKFC LESERKRKQ
//
ID PAIP1_HUMAN Reviewed; 479 AA.
AC Q9H074; A6NKV8; O60455; Q96B61; Q9BS63;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAR-2001, sequence version 1.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Polyadenylate-binding protein-interacting protein 1;
DE Short=PABP-interacting protein 1;
DE Short=PAIP-1;
DE Short=Poly(A)-binding protein-interacting protein 1;
GN Name=PAIP1;
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 [MRNA] (ISOFORM 1), FUNCTION IN TRANSLATION
RP INITIATION STIMULATION, AND INTERACTION WITH PABPC1 AND EIF4A.
RC TISSUE=Placenta;
RX PubMed=9548260; DOI=10.1038/33198;
RA Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.;
RT "Interaction of polyadenylate-binding protein with the eIF4G homologue
RT PAIP enhances translation.";
RL Nature 392:520-523(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-249 (ISOFORM 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, AND IDENTIFICATION
RP IN A COMPLEX WITH HNRPD; SYNCRIP; PABPC1 AND UNR.
RX PubMed=11051545; DOI=10.1016/S0092-8674(00)00102-1;
RA Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H.,
RA Shyu A.-B.;
RT "A mechanism for translationally coupled mRNA turnover: interaction
RT between the poly(A) tail and a c-fos RNA coding determinant via a
RT protein complex.";
RL Cell 103:29-40(2000).
RN [7]
RP INTERACTION WITH PABPC1.
RX PubMed=10970864; DOI=10.1093/emboj/19.17.4723;
RA Gray N.K., Coller J.M., Dickson K.S., Wickens M.;
RT "Multiple portions of poly(A)-binding protein stimulate translation in
RT vivo.";
RL EMBO J. 19:4723-4733(2000).
RN [8]
RP INTERACTION WITH PABPC1.
RX PubMed=11172725; DOI=10.1016/S1097-2765(01)00168-X;
RA Khaleghpour K., Svitkin Y.V., Craig A.W.B., DeMaria C.T., Deo R.C.,
RA Burley S.K., Sonenberg N.;
RT "Translational repression by a novel partner of human poly(A) binding
RT protein, Paip2.";
RL Mol. Cell 7:205-216(2001).
RN [9]
RP INTERACTION WITH PABPC1.
RX PubMed=11997512; DOI=10.1128/MCB.22.11.3769-3782.2002;
RA Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A.,
RA O'Connor-McCourt M., Sonenberg N.;
RT "Paip1 interacts with poly(A) binding protein through two independent
RT binding motifs.";
RL Mol. Cell. Biol. 22:3769-3782(2002).
RN [10]
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).
CC -!- FUNCTION: Acts as a coactivator in the regulation of translation
CC initiation of poly(A)-containing mRNAs. Its stimulatory activity
CC on translation is mediated via its action on PABPC1. Competes with
CC PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1
CC may potentiate contacts between mRNA termini. May also be involved
CC in translationally coupled mRNA turnover. Implicated with other
CC RNA-binding proteins in the cytoplasmic
CC deadenylation/translational and decay interplay of the FOS mRNA
CC mediated by the major coding-region determinant of instability
CC (mCRD) domain.
CC -!- SUBUNIT: Interacts with the RRM1-RRM2 and C-terminus regions of
CC PABPC1 in a 1:1 stoichiometry. Interacts with EIF4A.
CC -!- INTERACTION:
CC P11940:PABPC1; NbExp=11; IntAct=EBI-81519, EBI-81531;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H074-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H074-2; Sequence=VSP_010005;
CC Name=3;
CC IsoId=Q9H074-3; Sequence=VSP_047503;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: Only the PABPC1-interacting motif-1 (PAM1) stimulates
CC translation initiation.
CC -!- SIMILARITY: Contains 1 MIF4G domain.
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DR EMBL; AF013758; AAC39697.2; -; mRNA.
DR EMBL; AL136920; CAB66854.1; -; mRNA.
DR EMBL; AC114956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005295; AAH05295.1; -; mRNA.
DR EMBL; BC015937; AAH15937.1; -; mRNA.
DR EMBL; DB089732; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_006442.2; NM_006451.4.
DR RefSeq; NP_877590.1; NM_182789.3.
DR RefSeq; NP_899152.1; NM_183323.2.
DR RefSeq; XP_005248287.1; XM_005248230.1.
DR UniGene; Hs.482038; -.
DR PDB; 1JH4; NMR; -; B=124-144.
DR PDB; 3NTW; X-ray; 2.60 A; B/D=123-144.
DR PDB; 3RK6; X-ray; 2.00 A; A/B=157-373.
DR PDBsum; 1JH4; -.
DR PDBsum; 3NTW; -.
DR PDBsum; 3RK6; -.
DR ProteinModelPortal; Q9H074; -.
DR SMR; Q9H074; 157-373.
DR IntAct; Q9H074; 7.
DR MINT; MINT-196116; -.
DR STRING; 9606.ENSP00000302768; -.
DR PhosphoSite; Q9H074; -.
DR DMDM; 46397025; -.
DR PaxDb; Q9H074; -.
DR PRIDE; Q9H074; -.
DR DNASU; 10605; -.
DR Ensembl; ENST00000306846; ENSP00000302768; ENSG00000172239.
DR Ensembl; ENST00000338972; ENSP00000339622; ENSG00000172239.
DR Ensembl; ENST00000436644; ENSP00000387729; ENSG00000172239.
DR GeneID; 10605; -.
DR KEGG; hsa:10605; -.
DR UCSC; uc003job.3; human.
DR CTD; 10605; -.
DR GeneCards; GC05M043526; -.
DR HGNC; HGNC:16945; PAIP1.
DR MIM; 605184; gene.
DR neXtProt; NX_Q9H074; -.
DR PharmGKB; PA134941557; -.
DR eggNOG; NOG253454; -.
DR HOGENOM; HOG000285987; -.
DR HOVERGEN; HBG053492; -.
DR InParanoid; Q9H074; -.
DR KO; K14322; -.
DR OMA; EPTFYTE; -.
DR OrthoDB; EOG70CR75; -.
DR PhylomeDB; Q9H074; -.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; PAIP1; human.
DR EvolutionaryTrace; Q9H074; -.
DR GeneWiki; PAIP1; -.
DR GenomeRNAi; 10605; -.
DR NextBio; 40270; -.
DR PRO; PR:Q9H074; -.
DR ArrayExpress; Q9H074; -.
DR Bgee; Q9H074; -.
DR CleanEx; HS_PAIP1; -.
DR Genevestigator; Q9H074; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0008494; F:translation activator activity; IDA:UniProtKB.
DR GO; GO:0048255; P:mRNA stabilization; TAS:UniProtKB.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:ProtInc.
DR Gene3D; 1.25.40.180; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR009818; Ataxin-2_C.
DR InterPro; IPR016021; MIF4-like_typ_1/2/3.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF07145; PAM2; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
KW Reference proteome; Translation regulation.
FT CHAIN 1 479 Polyadenylate-binding protein-interacting
FT protein 1.
FT /FTId=PRO_0000058177.
FT DOMAIN 159 376 MIF4G.
FT REGION 116 143 PABPC1-interacting motif-2 (PAM2).
FT REGION 440 479 PABPC1-interacting motif-1 (PAM1).
FT COMPBIAS 10 36 Gly-rich.
FT COMPBIAS 45 98 Pro-rich.
FT VAR_SEQ 1 112 Missing (in isoform 3).
FT /FTId=VSP_047503.
FT VAR_SEQ 10 88 Missing (in isoform 2).
FT /FTId=VSP_010005.
FT CONFLICT 239 239 R -> C (in Ref. 4; AAH15937).
FT HELIX 158 171
FT HELIX 173 175
FT HELIX 176 190
FT HELIX 194 209
FT HELIX 215 228
FT HELIX 238 250
FT HELIX 253 256
FT HELIX 261 280
FT STRAND 288 291
FT HELIX 294 309
FT HELIX 313 336
FT HELIX 341 355
FT HELIX 360 372
SQ SEQUENCE 479 AA; 53525 MW; A4820607190A3A43 CRC64;
MSDGFDRAPG AGRGRSRGLG RGGGGPEGGG FPNGAGPAER ARHQPPQPKA PGFLQPPPLR
QPRTTPPPGA QCEVPASPQR PSRPGALPEQ TRPLRAPPSS QDKIPQQNSE SAMAKPQVVV
APVLMSKLSV NAPEFYPSGY SSSYTESYED GCEDYPTLSE YVQDFLNHLT EQPGSFETEI
EQFAETLNGC VTTDDALQEL VELIYQQATS IPNFSYMGAR LCNYLSHHLT ISPQSGNFRQ
LLLQRCRTEY EVKDQAAKGD EVTRKRFHAF VLFLGELYLN LEIKGTNGQV TRADILQVGL
RELLNALFSN PMDDNLICAV KLLKLTGSVL EDAWKEKGKM DMEEIIQRIE NVVLDANCSR
DVKQMLLKLV ELRSSNWGRV HATSTYREAT PENDPNYFMN EPTFYTSDGV PFTAADPDYQ
EKYQELLERE DFFPDYEENG TDLSGAGDPY LDDIDDEMDP EIEEAYEKFC LESERKRKQ
//
MIM
605184
*RECORD*
*FIELD* NO
605184
*FIELD* TI
*605184 POLYADENYLATE-BINDING PROTEIN-INTERACTING PROTEIN 1; PAIP1
;;POLY(A)-BINDING PROTEIN-INTERACTING PROTEIN 1;;
read morePABP-INTERACTING PROTEIN 1
*FIELD* TX
DESCRIPTION
In initiation of translation in eukaryotes, binding of the small
ribosomal subunit to mRNA requires recognition of the 5-prime cap
structure by the cap-binding complex eIF4F. eIF4F consists of eIF4E
(133440), eIF4A (see 602641), and eIF4G (see 600495). Translation
initiation is further regulated by the mRNA 3-prime poly(A) tail and the
poly(A)-binding protein (PABC1; 604679). PAIP1 interacts with PABC1 and
some eIF4 complexes.
CLONING
By Far Western blot analysis of HeLa cell extracts and a placenta cDNA
library using a PABC1 probe, Craig et al. (1998) identified a cDNA
encoding PAIP1 (PABC1-interacting protein-1). Sequence analysis of the
deduced 480-amino acid PAIP1 protein predicted that it shares 39% amino
acid similarity with the central portion of eIF4G, which contains an
eIF4A-binding region. PAIP1 also contains a proline-rich N terminus.
SDS-PAGE analysis determined that PAIP1 is expressed as a 70-kD protein.
GENE FUNCTION
Binding analysis by Craig et al. (1998) showed that PAIP1 binds strongly
to poly(A) only in the presence of PABC1. Immunoprecipitation and
Western blot analysis demonstrated that in HeLa extracts, the C terminus
of PAIP1 interacts with PABC1, and PAIP1 interacts with eIF4A but not
eIF4G complexes.
AU-rich elements and protein-coding determinants direct rapid removal of
poly(A) tails as a necessary first step in mRNA decay. Grosset et al.
(2000) determined that 5 proteins form a multiprotein complex associated
with the major protein-coding-region determinant of instability (mCRD)
of the FOS gene (164810): PABP, HNRNPD (601324), PAIP1, NSAP1, and UNR
(191510). Overexpression of these proteins stabilized mCRD-containing
mRNA by impeding deadenylation.
*FIELD* RF
1. Craig, A. W. B.; Haghighat, A.; Yu, A. T. K.; Sonenberg, N.: Interaction
of polyadenylate-binding protein with the eIF4G homologue PAIP enhances
translation. Nature 392: 520-523, 1998.
2. Grosset, C.; Chen, C.-Y. A.; Xu, N.; Sonenberg, N.; Jacquemin-Sablon,
H.; Shyu, A.-B.: A mechanism for translationally coupled mRNA turnover:
interaction between the poly(A) tail and a c-fos RNA coding determinant
via a protein complex. Cell 103: 29-40, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 9/10/2004
*FIELD* CD
Paul J. Converse: 7/31/2000
*FIELD* ED
mgross: 05/10/2007
mgross: 5/10/2007
mgross: 9/10/2004
mgross: 1/30/2001
mgross: 7/31/2000
*RECORD*
*FIELD* NO
605184
*FIELD* TI
*605184 POLYADENYLATE-BINDING PROTEIN-INTERACTING PROTEIN 1; PAIP1
;;POLY(A)-BINDING PROTEIN-INTERACTING PROTEIN 1;;
read morePABP-INTERACTING PROTEIN 1
*FIELD* TX
DESCRIPTION
In initiation of translation in eukaryotes, binding of the small
ribosomal subunit to mRNA requires recognition of the 5-prime cap
structure by the cap-binding complex eIF4F. eIF4F consists of eIF4E
(133440), eIF4A (see 602641), and eIF4G (see 600495). Translation
initiation is further regulated by the mRNA 3-prime poly(A) tail and the
poly(A)-binding protein (PABC1; 604679). PAIP1 interacts with PABC1 and
some eIF4 complexes.
CLONING
By Far Western blot analysis of HeLa cell extracts and a placenta cDNA
library using a PABC1 probe, Craig et al. (1998) identified a cDNA
encoding PAIP1 (PABC1-interacting protein-1). Sequence analysis of the
deduced 480-amino acid PAIP1 protein predicted that it shares 39% amino
acid similarity with the central portion of eIF4G, which contains an
eIF4A-binding region. PAIP1 also contains a proline-rich N terminus.
SDS-PAGE analysis determined that PAIP1 is expressed as a 70-kD protein.
GENE FUNCTION
Binding analysis by Craig et al. (1998) showed that PAIP1 binds strongly
to poly(A) only in the presence of PABC1. Immunoprecipitation and
Western blot analysis demonstrated that in HeLa extracts, the C terminus
of PAIP1 interacts with PABC1, and PAIP1 interacts with eIF4A but not
eIF4G complexes.
AU-rich elements and protein-coding determinants direct rapid removal of
poly(A) tails as a necessary first step in mRNA decay. Grosset et al.
(2000) determined that 5 proteins form a multiprotein complex associated
with the major protein-coding-region determinant of instability (mCRD)
of the FOS gene (164810): PABP, HNRNPD (601324), PAIP1, NSAP1, and UNR
(191510). Overexpression of these proteins stabilized mCRD-containing
mRNA by impeding deadenylation.
*FIELD* RF
1. Craig, A. W. B.; Haghighat, A.; Yu, A. T. K.; Sonenberg, N.: Interaction
of polyadenylate-binding protein with the eIF4G homologue PAIP enhances
translation. Nature 392: 520-523, 1998.
2. Grosset, C.; Chen, C.-Y. A.; Xu, N.; Sonenberg, N.; Jacquemin-Sablon,
H.; Shyu, A.-B.: A mechanism for translationally coupled mRNA turnover:
interaction between the poly(A) tail and a c-fos RNA coding determinant
via a protein complex. Cell 103: 29-40, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 9/10/2004
*FIELD* CD
Paul J. Converse: 7/31/2000
*FIELD* ED
mgross: 05/10/2007
mgross: 5/10/2007
mgross: 9/10/2004
mgross: 1/30/2001
mgross: 7/31/2000