ID   PAIP2_HUMAN             Reviewed;         127 AA.
AC   Q9BPZ3; B2RBI1; D3DQC6; Q49A06; Q9H0Y5; Q9P0Q8;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Polyadenylate-binding protein-interacting protein 2;
DE            Short=PABP-interacting protein 2;
DE            Short=PAIP-2;
DE            Short=Poly(A)-binding protein-interacting protein 2;
GN   Name=PAIP2; Synonyms=PAIP2A; ORFNames=HSPC218;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION IN TRANSLATION
RP   INHIBITION, AND INTERACTION WITH PABPC1.
RC   TISSUE=Placenta;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Umbilical cord blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for 300
RT   previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT   cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
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., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Testis;
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   [7]
RP   INTERACTION WITH PABPC1.
RX   PubMed=11438674; DOI=10.1128/mcb.21.15.5200-5213.2001;
RA   Khaleghpour K., Kahvejian A., De Crescenzo G., Roy G., Svitkin Y.V.,
RA   Imataka H., O'Connor-McCourt M., Sonenberg N.;
RT   "Dual interactions of the translational repressor Paip2 with poly(A)
RT   binding protein.";
RL   Mol. Cell. Biol. 21:5200-5213(2001).
RN   [8]
RP   TISSUE SPECIFICITY, AND UBIQUITINATION.
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   [9]
RP   STRUCTURE BY NMR OF 106-127.
RX   PubMed=11287632; DOI=10.1073/pnas.071024998;
RA   Kozlov G., Trempe J.F., Khaleghpour K., Kahvejian A., Ekiel I., Gehring K.;
RT   "Structure and function of the C-terminal PABC domain of human poly(A)-
RT   binding protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4409-4413(2001).
CC   -!- FUNCTION: Acts as a repressor in the regulation of translation
CC       initiation of poly(A)-containing mRNAs. Its inhibitory activity on
CC       translation is mediated via its action on PABPC1. Displaces the
CC       interaction of PABPC1 with poly(A) RNA and competes with PAIP1 for
CC       binding to PABPC1. Its association with PABPC1 results in disruption of
CC       the cytoplasmic poly(A) RNP structure organization.
CC       {ECO:0000269|PubMed:11172725}.
CC   -!- SUBUNIT: Interacts with the second and third RRM domains and C-terminus
CC       regions of PABPC1 in a 2:1 stoichiometry. {ECO:0000269|PubMed:11172725,
CC       ECO:0000269|PubMed:11438674}.
CC   -!- INTERACTION:
CC       Q9BPZ3; O14645: DNALI1; NbExp=3; IntAct=EBI-2957445, EBI-395638;
CC       Q9BPZ3; O14901: KLF11; NbExp=3; IntAct=EBI-2957445, EBI-948266;
CC       Q9BPZ3; Q99608: NDN; NbExp=6; IntAct=EBI-2957445, EBI-718177;
CC       Q9BPZ3; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-2957445, EBI-2811583;
CC       Q9BPZ3; P11940: PABPC1; NbExp=15; IntAct=EBI-2957445, EBI-81531;
CC       Q9BPZ3; Q96DU9: PABPC5; NbExp=3; IntAct=EBI-2957445, EBI-2880076;
CC       Q9BPZ3; O95071: UBR5; NbExp=5; IntAct=EBI-2957445, EBI-358329;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11172725}.
CC   -!- TISSUE SPECIFICITY: Expressed at highest level in testis, but also
CC       abundant in brain, cervix, lung, ovary, placenta, adipose tissue,
CC       thymus and thyroid. {ECO:0000269|PubMed:16804161}.
CC   -!- DOMAIN: Only the PABPC1-interacting motif-1 (PAM1) interferes with the
CC       binding of PABPC1 to poly(A) RNA and translation initiation.
CC   -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC       {ECO:0000269|PubMed:16804161}.
CC   -!- SIMILARITY: Belongs to the PAIP2 family. {ECO:0000305}.
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DR   EMBL; AF317675; AAK11562.1; -; mRNA.
DR   EMBL; AF151052; AAF36138.1; -; mRNA.
DR   EMBL; AL136640; CAB66575.1; -; mRNA.
DR   EMBL; AK314672; BAG37228.1; -; mRNA.
DR   EMBL; CH471062; EAW62107.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW62108.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW62111.1; -; Genomic_DNA.
DR   EMBL; CH471062; EAW62112.1; -; Genomic_DNA.
DR   EMBL; BC001716; AAH01716.1; -; mRNA.
DR   EMBL; BC048106; AAH48106.1; -; mRNA.
DR   EMBL; BC062718; AAH62718.1; -; mRNA.
DR   CCDS; CCDS4211.1; -.
DR   RefSeq; NP_001028284.1; NM_001033112.2.
DR   RefSeq; NP_057564.3; NM_016480.4.
DR   RefSeq; XP_011541730.1; XM_011543428.1.
DR   RefSeq; XP_016865011.1; XM_017009522.1.
DR   RefSeq; XP_016865012.1; XM_017009523.1.
DR   PDB; 1JGN; NMR; -; B=106-127.
DR   PDB; 3KUS; X-ray; 1.40 A; C/D=109-123.
DR   PDB; 3KUT; X-ray; 1.50 A; C/D=109-125.
DR   PDBsum; 1JGN; -.
DR   PDBsum; 3KUS; -.
DR   PDBsum; 3KUT; -.
DR   AlphaFoldDB; Q9BPZ3; -.
DR   BMRB; Q9BPZ3; -.
DR   SMR; Q9BPZ3; -.
DR   BioGRID; 119404; 62.
DR   ELM; Q9BPZ3; -.
DR   IntAct; Q9BPZ3; 19.
DR   MINT; Q9BPZ3; -.
DR   STRING; 9606.ENSP00000378275; -.
DR   MoonDB; Q9BPZ3; Predicted.
DR   iPTMnet; Q9BPZ3; -.
DR   PhosphoSitePlus; Q9BPZ3; -.
DR   BioMuta; PAIP2; -.
DR   DMDM; 46397013; -.
DR   EPD; Q9BPZ3; -.
DR   jPOST; Q9BPZ3; -.
DR   MassIVE; Q9BPZ3; -.
DR   MaxQB; Q9BPZ3; -.
DR   PaxDb; 9606-ENSP00000378275; -.
DR   PeptideAtlas; Q9BPZ3; -.
DR   ProteomicsDB; 78598; -.
DR   Pumba; Q9BPZ3; -.
DR   Antibodypedia; 26731; 206 antibodies from 24 providers.
DR   DNASU; 51247; -.
DR   Ensembl; ENST00000265192.9; ENSP00000265192.4; ENSG00000120727.13.
DR   Ensembl; ENST00000394795.6; ENSP00000378275.2; ENSG00000120727.13.
DR   Ensembl; ENST00000510080.1; ENSP00000422508.1; ENSG00000120727.13.
DR   GeneID; 51247; -.
DR   KEGG; hsa:51247; -.
DR   MANE-Select; ENST00000265192.9; ENSP00000265192.4; NM_016480.5; NP_057564.3.
DR   UCSC; uc003led.5; human.
DR   AGR; HGNC:17970; -.
DR   CTD; 51247; -.
DR   DisGeNET; 51247; -.
DR   GeneCards; PAIP2; -.
DR   HGNC; HGNC:17970; PAIP2.
DR   HPA; ENSG00000120727; Low tissue specificity.
DR   MIM; 605604; gene.
DR   neXtProt; NX_Q9BPZ3; -.
DR   OpenTargets; ENSG00000120727; -.
DR   PharmGKB; PA134897284; -.
DR   VEuPathDB; HostDB:ENSG00000120727; -.
DR   eggNOG; ENOG502RZKX; Eukaryota.
DR   GeneTree; ENSGT00390000017284; -.
DR   HOGENOM; CLU_134152_0_0_1; -.
DR   InParanoid; Q9BPZ3; -.
DR   OMA; MDQLQDQ; -.
DR   OrthoDB; 2910584at2759; -.
DR   PhylomeDB; Q9BPZ3; -.
DR   TreeFam; TF326855; -.
DR   PathwayCommons; Q9BPZ3; -.
DR   SignaLink; Q9BPZ3; -.
DR   SIGNOR; Q9BPZ3; -.
DR   BioGRID-ORCS; 51247; 21 hits in 1145 CRISPR screens.
DR   ChiTaRS; PAIP2; human.
DR   EvolutionaryTrace; Q9BPZ3; -.
DR   GeneWiki; PAIP2; -.
DR   GenomeRNAi; 51247; -.
DR   Pharos; Q9BPZ3; Tbio.
DR   PRO; PR:Q9BPZ3; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9BPZ3; Protein.
DR   Bgee; ENSG00000120727; Expressed in cardiac muscle of right atrium and 197 other cell types or tissues.
DR   ExpressionAtlas; Q9BPZ3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR   GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IEA:InterPro.
DR   GO; GO:0030371; F:translation repressor activity; IDA:UniProtKB.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR   GO; GO:0045947; P:negative regulation of translational initiation; IDA:UniProtKB.
DR   GO; GO:1900271; P:regulation of long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0006412; P:translation; IEA:Ensembl.
DR   IDEAL; IID00582; -.
DR   InterPro; IPR009818; Ataxin-2_C.
DR   InterPro; IPR040396; PAIP2-like.
DR   PANTHER; PTHR13154; POLYADENYLATE-BINDING PROTEIN-INTERACTING PROTEIN 2; 1.
DR   PANTHER; PTHR13154:SF2; POLYADENYLATE-BINDING PROTEIN-INTERACTING PROTEIN 2; 1.
DR   Pfam; PF07145; PAM2; 1.
DR   Genevisible; Q9BPZ3; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Reference proteome; Translation regulation;
KW   Ubl conjugation.
FT   CHAIN           1..127
FT                   /note="Polyadenylate-binding protein-interacting protein 2"
FT                   /id="PRO_0000058179"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          22..75
FT                   /note="PABPC1-interacting motif-1 (PAM1)"
FT   REGION          105..120
FT                   /note="PABPC1-interacting motif-2 (PAM2)"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        98
FT                   /note="D -> E (in Ref. 3; CAB66575)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        116
FT                   /note="K -> T (in Ref. 2; AAF36138)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   127 AA;  14984 MW;  CAC27C537E5C6E22 CRC64;
     MKDPSRSSTS PSIINEDVII NGHSHEDDNP FAEYMWMENE EEFNRQIEEE LWEEEFIERC
     FQEMLEEEEE HEWFIPARDL PQTMDQIQDQ FNDLVISDGS SLEDLVVKSN LNPNAKEFVP
     GVKYGNI
//