ID PWP2_HUMAN Reviewed; 919 AA.
AC Q15269; B2RAG8; Q96A77;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 27-MAR-2024, entry version 207.
DE RecName: Full=Periodic tryptophan protein 2 homolog;
GN Name=PWP2 {ECO:0000312|HGNC:HGNC:9711}; Synonyms=PWP2H;
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 [GENOMIC DNA / MRNA], AND VARIANT ASN-25.
RX PubMed=8661145; DOI=10.1006/geno.1996.0363;
RA Lalioti M.D., Chen H., Rossier C., Reid J.D., Antonarakis S.E.;
RT "Cloning the cDNA of human PWP2, which encodes a protein with WD repeats
RT and maps to 21q22.3.";
RL Genomics 35:321-327(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-25.
RX PubMed=8893822; DOI=10.1159/000134402;
RA Yamakawa K., Gao D.-Q., Korenberg J.R.;
RT "A periodic tryptophan protein 2 gene homologue (PWP2H) in the candidate
RT region of progressive myoclonus epilepsy on 21q22.3.";
RL Cytogenet. Cell Genet. 74:140-145(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANT ASN-25.
RX PubMed=8973917; DOI=10.1101/gr.6.12.1216;
RA Lafreniere R.G., Rochefort D.L., Chretien N., Neville C.E., Korneluk R.G.,
RA Zuo L., Wei Y., Lichter J., Rouleau G.A.;
RT "Isolation and genomic structure of a human homolog of the yeast periodic
RT tryptophan protein 2 (PWP2) gene mapping to 21q22.3.";
RL Genome Res. 6:1216-1226(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9205129; DOI=10.1006/geno.1997.4761;
RA Nagamine K., Kudoh J., Minoshima S., Kawasaki K., Asakawa S., Ito F.,
RA Shimizu N.;
RT "Genomic organization and complete nucleotide sequence of the human PWP2
RT gene on chromosome 21.";
RL Genomics 42:528-531(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-25.
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-25.
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-25 AND ILE-551.
RC TISSUE=Muscle;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-43, AND VARIANT ASN-25.
RX PubMed=9196060; DOI=10.1006/bbrc.1997.6758;
RA Nagamine K., Kudoh J., Kawasaki K., Minoshima S., Asakawa S., Ito F.,
RA Shimizu N.;
RT "Genomic organization and complete nucleotide sequence of the TMEM1 gene on
RT human chromosome 21q22.3.";
RL Biochem. Biophys. Res. Commun. 235:185-190(1997).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [11] {ECO:0007744|PDB:7MQ8, ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=34516797; DOI=10.1126/science.abj5338;
RA Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.;
RT "Nucleolar maturation of the human small subunit processome.";
RL Science 373:eabj5338-eabj5338(2021).
CC -!- FUNCTION: Part of the small subunit (SSU) processome, first precursor
CC of the small eukaryotic ribosomal subunit. During the assembly of the
CC SSU processome in the nucleolus, many ribosome biogenesis factors, an
CC RNA chaperone and ribosomal proteins associate with the nascent pre-
CC rRNA and work in concert to generate RNA folding, modifications,
CC rearrangements and cleavage as well as targeted degradation of pre-
CC ribosomal RNA by the RNA exosome. {ECO:0000269|PubMed:34516797}.
CC -!- SUBUNIT: Part of the small subunit (SSU) processome, composed of more
CC than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3.
CC {ECO:0000269|PubMed:34516797}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:34516797}.
CC -!- SIMILARITY: Belongs to the WD repeat PWP2 family. {ECO:0000305}.
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DR EMBL; X95263; CAA64560.1; -; mRNA.
DR EMBL; X96424; CAA65284.1; -; Genomic_DNA.
DR EMBL; X96425; CAA65285.1; -; Genomic_DNA.
DR EMBL; U53346; AAB08084.1; -; mRNA.
DR EMBL; U56085; AAC50904.1; -; mRNA.
DR EMBL; U56089; AAC50905.1; -; Genomic_DNA.
DR EMBL; U56086; AAC50905.1; JOINED; Genomic_DNA.
DR EMBL; U56087; AAC50905.1; JOINED; Genomic_DNA.
DR EMBL; U56088; AAC50905.1; JOINED; Genomic_DNA.
DR EMBL; AB001517; BAA21137.1; -; Genomic_DNA.
DR EMBL; AK314184; BAG36865.1; -; mRNA.
DR EMBL; AP001753; BAA95553.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09458.1; -; Genomic_DNA.
DR EMBL; BC013309; AAH13309.1; -; mRNA.
DR EMBL; BC014988; AAH14988.1; -; mRNA.
DR EMBL; AB001523; BAA21100.1; -; Genomic_DNA.
DR CCDS; CCDS33579.1; -.
DR RefSeq; NP_005040.2; NM_005049.2.
DR RefSeq; XP_006723973.1; XM_006723910.1.
DR RefSeq; XP_011507205.1; XM_011508903.2.
DR PDB; 7MQ8; EM; 3.60 A; LO=1-919.
DR PDB; 7MQ9; EM; 3.87 A; LO=1-919.
DR PDB; 7MQA; EM; 2.70 A; LO=1-919.
DR PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q15269; -.
DR EMDB; EMD-23936; -.
DR EMDB; EMD-23937; -.
DR EMDB; EMD-23938; -.
DR SMR; Q15269; -.
DR BioGRID; 111780; 176.
DR BioGRID; 3195276; 8.
DR ComplexPortal; CPX-2688; UTP-B complex.
DR IntAct; Q15269; 37.
DR MINT; Q15269; -.
DR STRING; 9606.ENSP00000291576; -.
DR GlyGen; Q15269; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q15269; -.
DR PhosphoSitePlus; Q15269; -.
DR SwissPalm; Q15269; -.
DR BioMuta; PWP2; -.
DR DMDM; 116242740; -.
DR SWISS-2DPAGE; Q15269; -.
DR EPD; Q15269; -.
DR jPOST; Q15269; -.
DR MassIVE; Q15269; -.
DR MaxQB; Q15269; -.
DR PaxDb; 9606-ENSP00000291576; -.
DR PeptideAtlas; Q15269; -.
DR ProteomicsDB; 60506; -.
DR Pumba; Q15269; -.
DR Antibodypedia; 34932; 151 antibodies from 21 providers.
DR DNASU; 5822; -.
DR Ensembl; ENST00000291576.12; ENSP00000291576.6; ENSG00000241945.8.
DR GeneID; 5822; -.
DR KEGG; hsa:5822; -.
DR MANE-Select; ENST00000291576.12; ENSP00000291576.6; NM_005049.3; NP_005040.2.
DR UCSC; uc002zeb.4; human.
DR AGR; HGNC:9711; -.
DR CTD; 5822; -.
DR DisGeNET; 5822; -.
DR GeneCards; PWP2; -.
DR HGNC; HGNC:9711; PWP2.
DR HPA; ENSG00000241945; Low tissue specificity.
DR MIM; 601475; gene.
DR neXtProt; NX_Q15269; -.
DR OpenTargets; ENSG00000241945; -.
DR PharmGKB; PA162400451; -.
DR VEuPathDB; HostDB:ENSG00000241945; -.
DR eggNOG; KOG0291; Eukaryota.
DR GeneTree; ENSGT00550000074981; -.
DR HOGENOM; CLU_010458_0_0_1; -.
DR InParanoid; Q15269; -.
DR OMA; VYEWQSE; -.
DR OrthoDB; 23263at2759; -.
DR PhylomeDB; Q15269; -.
DR TreeFam; TF300853; -.
DR PathwayCommons; Q15269; -.
DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q15269; -.
DR BioGRID-ORCS; 102724159; 0 hits in 6 CRISPR screens.
DR BioGRID-ORCS; 5822; 818 hits in 1131 CRISPR screens.
DR ChiTaRS; PWP2; human.
DR GeneWiki; PWP2; -.
DR Pharos; Q15269; Tbio.
DR PRO; PR:Q15269; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q15269; Protein.
DR Bgee; ENSG00000241945; Expressed in stromal cell of endometrium and 95 other cell types or tissues.
DR ExpressionAtlas; Q15269; baseline and differential.
DR Genevisible; Q15269; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0034388; C:Pwp2p-containing subcomplex of 90S preribosome; IBA:GO_Central.
DR GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR027145; PWP2.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR007148; SSU_processome_Utp12.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR19858:SF0; PERIODIC TRYPTOPHAN PROTEIN 2 HOMOLOG-RELATED; 1.
DR PANTHER; PTHR19858; WD40 REPEAT PROTEIN; 1.
DR Pfam; PF04003; Utp12; 1.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 13.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..919
FT /note="Periodic tryptophan protein 2 homolog"
FT /id="PRO_0000051175"
FT REPEAT 12..50
FT /note="WD 1"
FT REPEAT 53..93
FT /note="WD 2"
FT REPEAT 94..132
FT /note="WD 3"
FT REPEAT 142..181
FT /note="WD 4"
FT REPEAT 186..225
FT /note="WD 5"
FT REPEAT 286..325
FT /note="WD 6"
FT REPEAT 328..368
FT /note="WD 7"
FT REPEAT 371..410
FT /note="WD 8"
FT REPEAT 413..452
FT /note="WD 9"
FT REPEAT 456..498
FT /note="WD 10"
FT REPEAT 499..538
FT /note="WD 11"
FT REPEAT 541..580
FT /note="WD 12"
FT REPEAT 603..642
FT /note="WD 13"
FT REPEAT 700..740
FT /note="WD 14"
FT REGION 238..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BU03"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BU03"
FT VARIANT 25
FT /note="D -> N (in dbSNP:rs2020945)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8661145,
FT ECO:0000269|PubMed:8893822, ECO:0000269|PubMed:8973917,
FT ECO:0000269|PubMed:9196060, ECO:0000269|Ref.7"
FT /id="VAR_028104"
FT VARIANT 174
FT /note="E -> K (in dbSNP:rs35001460)"
FT /id="VAR_053412"
FT VARIANT 551
FT /note="F -> I (in dbSNP:rs17856422)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028105"
FT CONFLICT 719
FT /note="A -> G (in Ref. 1; CAA64560)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 919 AA; 102452 MW; B2A94C5595DF4380 CRC64;
MKFAYRFSNL LGTVYRRGNL NFTCDGNSVI SPVGNRVTVF DLKNNKSDTL PLATRYNVKC
VGLSPDGRLA IIVDEGGDAL LVSLVCRSVL HHFHFKGSVH SVSFSPDGRK FVVTKGNIAQ
MYHAPGKKRE FNAFVLDKTY FGPYDETTCI DWTDDSRCFV VGSKDMSTWV FGAERWDNLI
YYALGGHKDA IVACFFESNS LDLYSLSQDG VLCMWQCDTP PEGLRLKPPA GWKADLLQRE
EEEEEEEDQE GDRETTIRGK ATPAEEEKTG KVKYSRLAKY FFNKEGDFNN LTAAAFHKKS
HLLVTGFASG IFHLHELPEF NLIHSLSISD QSIASVAINS SGDWIAFGCS GLGQLLVWEW
QSESYVLKQQ GHFNSMVALA YSPDGQYIVT GGDDGKVKVW NTLSGFCFVT FTEHSSGVTG
VTFTATGYVV VTSSMDGTVR AFDLHRYRNF RTFTSPRPTQ FSCVAVDASG EIVSAGAQDS
FEIFVWSMQT GRLLDVLSGH EGPISGLCFN PMKSVLASAS WDKTVRLWDM FDSWRTKETL
ALTSDALAVT FRPDGAELAV ATLNSQITFW DPENAVQTGS IEGRHDLKTG RKELDKITAK
HAAKGKAFTA LCYSADGHSI LAGGMSKFVC IYHVREQILM KRFEISCNLS LDAMEEFLNR
RKMTEFGNLA LIDQDAGQED GVAIPLPGVR KGDMSSRHFK PEIRVTSLRF SPTGRCWAAT
TTEGLLIYSL DTRVLFDPFE LDTSVTPGRV REALRQQDFT RAILMALRLN ESKLVQEALE
AVPRGEIEVV TSSLPELYVE KVLEFLASSF EVSRHLEFYL LWTHKLLMLH GQKLKSRAGT
LLPVIQFLQK SIQRHLDDLS KLCSWNHYNM QYALAVSKQR GTKRSLDPLG SEEEAEASED
DSLHLLGGGG RDSEEEMLA
//
