PAIP2_HUMAN
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 03-AUG-2022, entry version 145.
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=6; 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; 59.
DR ELM; Q9BPZ3; -.
DR IntAct; Q9BPZ3; 16.
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; Q9BPZ3; -.
DR PeptideAtlas; Q9BPZ3; -.
DR PRIDE; Q9BPZ3; -.
DR ProteomicsDB; 78598; -.
DR Antibodypedia; 26731; 197 antibodies from 25 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 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; NSTAWST; -.
DR OrthoDB; 1624094at2759; -.
DR PhylomeDB; Q9BPZ3; -.
DR TreeFam; TF326855; -.
DR PathwayCommons; Q9BPZ3; -.
DR SignaLink; Q9BPZ3; -.
DR BioGRID-ORCS; 51247; 21 hits in 1069 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 195 other tissues.
DR ExpressionAtlas; Q9BPZ3; baseline and differential.
DR Genevisible; Q9BPZ3; HS.
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; PTHR13154; 1.
DR Pfam; PF07145; PAM2; 1.
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
