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Polyadenylate-binding protein-interacting protein 1 (PABP-interacting protein 1) (PAIP-1) (Poly(A)-binding protein-interacting protein 1)

 PAIP1_HUMAN             Reviewed;         479 AA.
Q9H074; A6NKV8; O60455; Q96B61; Q9BS63;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
12-SEP-2018, entry version 161.
RecName: Full=Polyadenylate-binding protein-interacting protein 1;
Short=PABP-interacting protein 1;
Short=PAIP-1;
Short=Poly(A)-binding protein-interacting protein 1;
Name=PAIP1;
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), FUNCTION IN TRANSLATION
INITIATION STIMULATION, AND INTERACTION WITH PABPC1 AND EIF4A.
TISSUE=Placenta;
PubMed=9548260; DOI=10.1038/33198;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney, and Skin;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-249 (ISOFORM 3).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, AND IDENTIFICATION
IN A COMPLEX WITH HNRPD; SYNCRIP; PABPC1 AND UNR.
PubMed=11051545; DOI=10.1016/S0092-8674(00)00102-1;
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).
[7]
INTERACTION WITH PABPC1.
PubMed=10970864; DOI=10.1093/emboj/19.17.4723;
Gray N.K., Coller J.M., Dickson K.S., Wickens M.;
"Multiple portions of poly(A)-binding protein stimulate translation in
vivo.";
EMBO J. 19:4723-4733(2000).
[8]
INTERACTION WITH PABPC1.
PubMed=11172725; DOI=10.1016/S1097-2765(01)00168-X;
Khaleghpour K., Svitkin Y.V., Craig A.W.B., DeMaria C.T., Deo R.C.,
Burley S.K., Sonenberg N.;
"Translational repression by a novel partner of human poly(A) binding
protein, Paip2.";
Mol. Cell 7:205-216(2001).
[9]
INTERACTION WITH PABPC1.
PubMed=11997512; DOI=10.1128/MCB.22.11.3769-3782.2002;
Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A.,
O'Connor-McCourt M., Sonenberg N.;
"Paip1 interacts with poly(A) binding protein through two independent
binding motifs.";
Mol. Cell. Biol. 22:3769-3782(2002).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 3), CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 3), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[12]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-21, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Acts as a coactivator in the regulation of translation
initiation of poly(A)-containing mRNAs. Its stimulatory activity
on translation is mediated via its action on PABPC1. Competes with
PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1
may potentiate contacts between mRNA termini. May also be involved
in translationally coupled mRNA turnover. Implicated with other
RNA-binding proteins in the cytoplasmic
deadenylation/translational and decay interplay of the FOS mRNA
mediated by the major coding-region determinant of instability
(mCRD) domain. {ECO:0000269|PubMed:11051545,
ECO:0000269|PubMed:9548260}.
-!- SUBUNIT: Interacts with the RRM1-RRM2 and C-terminus regions of
PABPC1 in a 1:1 stoichiometry. Interacts with EIF4A.
{ECO:0000269|PubMed:10970864, ECO:0000269|PubMed:11051545,
ECO:0000269|PubMed:11172725, ECO:0000269|PubMed:11997512,
ECO:0000269|PubMed:9548260}.
-!- INTERACTION:
P11940:PABPC1; NbExp=13; IntAct=EBI-81519, EBI-81531;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9H074-1; Sequence=Displayed;
Name=2;
IsoId=Q9H074-2; Sequence=VSP_010005;
Name=3;
IsoId=Q9H074-3; Sequence=VSP_047503;
Note=No experimental confirmation available. Initiator Met-1 is
removed. Contains a N-acetylalanine at position 2.
{ECO:0000244|PubMed:22223895};
-!- DOMAIN: Only the PABPC1-interacting motif-1 (PAM1) stimulates
translation initiation.
-----------------------------------------------------------------------
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EMBL; AF013758; AAC39697.2; -; mRNA.
EMBL; AL136920; CAB66854.1; -; mRNA.
EMBL; AC114956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005295; AAH05295.1; -; mRNA.
EMBL; BC015937; AAH15937.1; -; mRNA.
EMBL; DB089732; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS3947.1; -. [Q9H074-1]
CCDS; CCDS3948.1; -. [Q9H074-3]
CCDS; CCDS47204.1; -. [Q9H074-2]
RefSeq; NP_006442.2; NM_006451.4. [Q9H074-1]
RefSeq; NP_877590.1; NM_182789.3. [Q9H074-2]
RefSeq; NP_899152.1; NM_183323.2. [Q9H074-3]
RefSeq; XP_005248287.1; XM_005248230.3. [Q9H074-3]
RefSeq; XP_016864445.1; XM_017008956.1. [Q9H074-3]
UniGene; Hs.482038; -.
PDB; 1JH4; NMR; -; B=123-144.
PDB; 3NTW; X-ray; 2.60 A; B/D=123-144.
PDB; 3RK6; X-ray; 2.00 A; A/B=157-373.
PDBsum; 1JH4; -.
PDBsum; 3NTW; -.
PDBsum; 3RK6; -.
ProteinModelPortal; Q9H074; -.
SMR; Q9H074; -.
BioGrid; 115851; 47.
ComplexPortal; CPX-1076; mCRD-poly(A)-bridging complex.
CORUM; Q9H074; -.
ELM; Q9H074; -.
IntAct; Q9H074; 18.
MINT; Q9H074; -.
STRING; 9606.ENSP00000302768; -.
iPTMnet; Q9H074; -.
PhosphoSitePlus; Q9H074; -.
SwissPalm; Q9H074; -.
BioMuta; PAIP1; -.
DMDM; 46397025; -.
EPD; Q9H074; -.
MaxQB; Q9H074; -.
PaxDb; Q9H074; -.
PeptideAtlas; Q9H074; -.
PRIDE; Q9H074; -.
ProteomicsDB; 80210; -.
ProteomicsDB; 80211; -. [Q9H074-2]
DNASU; 10605; -.
Ensembl; ENST00000306846; ENSP00000302768; ENSG00000172239. [Q9H074-1]
Ensembl; ENST00000338972; ENSP00000339622; ENSG00000172239. [Q9H074-3]
Ensembl; ENST00000436644; ENSP00000387729; ENSG00000172239. [Q9H074-2]
GeneID; 10605; -.
KEGG; hsa:10605; -.
UCSC; uc003joa.4; human. [Q9H074-1]
CTD; 10605; -.
EuPathDB; HostDB:ENSG00000172239.13; -.
GeneCards; PAIP1; -.
HGNC; HGNC:16945; PAIP1.
HPA; HPA073653; -.
HPA; HPA076187; -.
MIM; 605184; gene.
neXtProt; NX_Q9H074; -.
OpenTargets; ENSG00000172239; -.
PharmGKB; PA134941557; -.
eggNOG; ENOG410IPIA; Eukaryota.
eggNOG; ENOG41109D3; LUCA.
GeneTree; ENSGT00630000089897; -.
HOGENOM; HOG000285987; -.
HOVERGEN; HBG053492; -.
InParanoid; Q9H074; -.
KO; K14322; -.
OMA; EPTFYTE; -.
OrthoDB; EOG091G05G0; -.
PhylomeDB; Q9H074; -.
TreeFam; TF325625; -.
Reactome; R-HSA-429947; Deadenylation of mRNA.
ChiTaRS; PAIP1; human.
EvolutionaryTrace; Q9H074; -.
GeneWiki; PAIP1; -.
GenomeRNAi; 10605; -.
PRO; PR:Q9H074; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000172239; Expressed in 211 organ(s), highest expression level in oocyte.
CleanEx; HS_PAIP1; -.
ExpressionAtlas; Q9H074; baseline and differential.
Genevisible; Q9H074; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0003723; F:RNA binding; TAS:ProtInc.
GO; GO:0008494; F:translation activator activity; IDA:UniProtKB.
GO; GO:0048255; P:mRNA stabilization; TAS:UniProtKB.
GO; GO:0006413; P:translational initiation; TAS:ProtInc.
Gene3D; 1.25.40.180; -; 1.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR009818; Ataxin-2_C.
InterPro; IPR016021; MIF4-like_sf.
InterPro; IPR003890; MIF4G-like_typ-3.
Pfam; PF02854; MIF4G; 1.
Pfam; PF07145; PAM2; 1.
SMART; SM00543; MIF4G; 1.
SUPFAM; SSF48371; SSF48371; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Methylation; Reference proteome; Translation regulation.
CHAIN 1 479 Polyadenylate-binding protein-interacting
protein 1.
/FTId=PRO_0000058177.
DOMAIN 159 376 MIF4G.
REGION 116 143 PABPC1-interacting motif-2 (PAM2).
REGION 440 479 PABPC1-interacting motif-1 (PAM1).
COMPBIAS 10 36 Gly-rich.
COMPBIAS 45 98 Pro-rich.
MOD_RES 21 21 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
VAR_SEQ 1 112 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_047503.
VAR_SEQ 10 88 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010005.
CONFLICT 239 239 R -> C (in Ref. 4; AAH15937).
{ECO:0000305}.
HELIX 158 171 {ECO:0000244|PDB:3RK6}.
HELIX 173 175 {ECO:0000244|PDB:3RK6}.
HELIX 176 190 {ECO:0000244|PDB:3RK6}.
HELIX 194 209 {ECO:0000244|PDB:3RK6}.
HELIX 215 228 {ECO:0000244|PDB:3RK6}.
HELIX 238 250 {ECO:0000244|PDB:3RK6}.
HELIX 253 256 {ECO:0000244|PDB:3RK6}.
HELIX 261 280 {ECO:0000244|PDB:3RK6}.
STRAND 288 291 {ECO:0000244|PDB:3RK6}.
HELIX 294 309 {ECO:0000244|PDB:3RK6}.
HELIX 313 336 {ECO:0000244|PDB:3RK6}.
HELIX 341 355 {ECO:0000244|PDB:3RK6}.
HELIX 360 372 {ECO:0000244|PDB:3RK6}.
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


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