ID PAAF1_HUMAN Reviewed; 392 AA. AC Q9BRP4; A6NDR5; B4DPB0; B7ZAS9; Q4G165; Q53HS9; Q7Z500; Q8TBU6; Q9HAB6; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 2. DT 24-JAN-2024, entry version 177. DE RecName: Full=Proteasomal ATPase-associated factor 1; DE AltName: Full=Protein G-16; DE AltName: Full=WD repeat-containing protein 71; GN Name=PAAF1; Synonyms=WDR71; 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] (ISOFORM 2), AND VARIANT GLY-209. RA Bi A.D., Yu L., Tu Q., Yang J., Dai F.Y., Cui W.C., Zheng L.H., Zhao S.Y.; RT "Cloning of a new human cDNA homology to Xenopus laevis gene 16 mRNA."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT RP GLY-209. RC TISSUE=Embryo, Kidney, and Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-139. RC TISSUE=Adipose tissue; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS RP VAL-53 AND GLY-209. RC TISSUE=Brain, and Lung; 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 FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PSMC1; PSMC2; PSMC3; PSMC4; RP PSMC5 AND PSMC6, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=15831487; DOI=10.1128/mcb.25.9.3842-3853.2005; RA Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.; RT "Proteasomal ATPase-associated factor 1 negatively regulates proteasome RT activity by interacting with proteasomal ATPases."; RL Mol. Cell. Biol. 25:3842-3853(2005). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17323924; DOI=10.1021/bi061994u; RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; RT "Mass spectrometric characterization of the affinity-purified human 26S RT proteasome complex."; RL Biochemistry 46:3553-3565(2007). RN [9] RP FUNCTION, AND INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION). RX PubMed=17289585; DOI=10.1016/j.molcel.2006.12.020; RA Lassot I., Latreille D., Rousset E., Sourisseau M., Linares L.K., RA Chable-Bessia C., Coux O., Benkirane M., Kiernan R.E.; RT "The proteasome regulates HIV-1 transcription by both proteolytic and RT nonproteolytic mechanisms."; RL Mol. Cell 25:369-383(2007). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [11] 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., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [12] RP FUNCTION, AND INTERACTION WITH SUPT6H. RX PubMed=22316138; DOI=10.1186/1742-4690-9-13; RA Nakamura M., Basavarajaiah P., Rousset E., Beraud C., Latreille D., RA Henaoui I.S., Lassot I., Mari B., Kiernan R.; RT "Spt6 levels are modulated by PAAF1 and proteasome to regulate the HIV-1 RT LTR."; RL Retrovirology 9:13-13(2012). CC -!- FUNCTION: Inhibits proteasome 26S assembly and proteolytic activity by CC impairing the association of the 19S regulatory complex with the 20S CC core. In case of HIV-1 infection, recruited by viral Tat to the HIV-1 CC promoter, where it promotes the recruitment of 19S regulatory complex CC through dissociation of the proteasome 26S. This presumably promotes CC provirus transcription efficiency. Protects SUPT6H from proteasomal CC degradation. {ECO:0000269|PubMed:15831487, ECO:0000269|PubMed:17289585, CC ECO:0000269|PubMed:22316138}. CC -!- SUBUNIT: Interacts with PSMC1, PSMC2, PSMC3, PSMC4, PSMC5 and PSMC6. CC Interacts with SUPT6H. {ECO:0000269|PubMed:15831487, CC ECO:0000269|PubMed:22316138}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat. CC {ECO:0000269|PubMed:17289585}. CC -!- INTERACTION: CC Q9BRP4; P62195: PSMC5; NbExp=2; IntAct=EBI-1056358, EBI-357745; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9BRP4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BRP4-2; Sequence=VSP_018477; CC Name=3; CC IsoId=Q9BRP4-3; Sequence=VSP_044699; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in CC kidney, brain and testis. {ECO:0000269|PubMed:15831487}. CC -!- SIMILARITY: Belongs to the WD repeat PAAF1/RPN14 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF087895; AAP97194.1; -; mRNA. DR EMBL; AK021910; BAB13933.1; -; mRNA. DR EMBL; AK222501; BAD96221.1; -; mRNA. DR EMBL; AK298258; BAG60522.1; -; mRNA. DR EMBL; AK316394; BAH14765.1; -; mRNA. DR EMBL; AP002770; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW74917.1; -; Genomic_DNA. DR EMBL; BC006142; AAH06142.2; -; mRNA. DR EMBL; BC021541; AAH21541.1; -; mRNA. DR EMBL; BC028628; AAH28628.1; -; mRNA. DR CCDS; CCDS58157.1; -. [Q9BRP4-2] DR CCDS; CCDS58158.1; -. [Q9BRP4-3] DR CCDS; CCDS8226.1; -. [Q9BRP4-1] DR RefSeq; NP_001254732.1; NM_001267803.1. [Q9BRP4-2] DR RefSeq; NP_001254733.1; NM_001267804.1. [Q9BRP4-2] DR RefSeq; NP_001254734.1; NM_001267805.1. [Q9BRP4-2] DR RefSeq; NP_001254735.1; NM_001267806.1. [Q9BRP4-3] DR RefSeq; NP_079431.1; NM_025155.2. [Q9BRP4-1] DR AlphaFoldDB; Q9BRP4; -. DR SMR; Q9BRP4; -. DR BioGRID; 123191; 79. DR IntAct; Q9BRP4; 14. DR MINT; Q9BRP4; -. DR STRING; 9606.ENSP00000438071; -. DR iPTMnet; Q9BRP4; -. DR MetOSite; Q9BRP4; -. DR PhosphoSitePlus; Q9BRP4; -. DR BioMuta; PAAF1; -. DR DMDM; 97217547; -. DR EPD; Q9BRP4; -. DR jPOST; Q9BRP4; -. DR MassIVE; Q9BRP4; -. DR MaxQB; Q9BRP4; -. DR PaxDb; 9606-ENSP00000311665; -. DR PeptideAtlas; Q9BRP4; -. DR ProteomicsDB; 7085; -. DR ProteomicsDB; 78795; -. [Q9BRP4-1] DR ProteomicsDB; 78796; -. [Q9BRP4-2] DR Pumba; Q9BRP4; -. DR Antibodypedia; 50309; 137 antibodies from 19 providers. DR DNASU; 80227; -. DR Ensembl; ENST00000310571.8; ENSP00000311665.4; ENSG00000175575.13. [Q9BRP4-1] DR Ensembl; ENST00000376384.9; ENSP00000365564.5; ENSG00000175575.13. [Q9BRP4-2] DR Ensembl; ENST00000535604.5; ENSP00000438789.1; ENSG00000175575.13. [Q9BRP4-3] DR Ensembl; ENST00000536003.5; ENSP00000438124.1; ENSG00000175575.13. [Q9BRP4-2] DR Ensembl; ENST00000541951.5; ENSP00000441333.1; ENSG00000175575.13. [Q9BRP4-3] DR Ensembl; ENST00000544552.5; ENSP00000441494.1; ENSG00000175575.13. [Q9BRP4-2] DR GeneID; 80227; -. DR KEGG; hsa:80227; -. DR MANE-Select; ENST00000310571.8; ENSP00000311665.4; NM_025155.3; NP_079431.1. DR UCSC; uc001ouk.3; human. [Q9BRP4-1] DR AGR; HGNC:25687; -. DR CTD; 80227; -. DR GeneCards; PAAF1; -. DR HGNC; HGNC:25687; PAAF1. DR HPA; ENSG00000175575; Tissue enhanced (brain). DR MIM; 619772; gene. DR neXtProt; NX_Q9BRP4; -. DR OpenTargets; ENSG00000175575; -. DR PharmGKB; PA162398551; -. DR VEuPathDB; HostDB:ENSG00000175575; -. DR eggNOG; KOG0266; Eukaryota. DR GeneTree; ENSGT00390000005948; -. DR HOGENOM; CLU_037051_1_0_1; -. DR InParanoid; Q9BRP4; -. DR OMA; IQIIHRS; -. DR OrthoDB; 1466268at2759; -. DR PhylomeDB; Q9BRP4; -. DR TreeFam; TF313690; -. DR PathwayCommons; Q9BRP4; -. DR SignaLink; Q9BRP4; -. DR BioGRID-ORCS; 80227; 9 hits in 1155 CRISPR screens. DR ChiTaRS; PAAF1; human. DR GeneWiki; PAAF1; -. DR GenomeRNAi; 80227; -. DR Pharos; Q9BRP4; Tbio. DR PRO; PR:Q9BRP4; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q9BRP4; Protein. DR Bgee; ENSG00000175575; Expressed in C1 segment of cervical spinal cord and 190 other cell types or tissues. DR ExpressionAtlas; Q9BRP4; baseline and differential. DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB. DR GO; GO:0005669; C:transcription factor TFIID complex; IBA:GO_Central. DR GO; GO:0006367; P:transcription initiation at RNA polymerase II promoter; IBA:GO_Central. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19857:SF19; 26S PROTEASOME REGULATORY SUBUNIT RPN14; 1. DR PANTHER; PTHR19857; MITOCHONDRIAL DIVISION PROTEIN 1-RELATED; 1. DR Pfam; PF00400; WD40; 3. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 3. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q9BRP4; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Host-virus interaction; Proteasome; KW Reference proteome; Repeat; WD repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..392 FT /note="Proteasomal ATPase-associated factor 1" FT /id="PRO_0000235685" FT REPEAT 82..121 FT /note="WD 1" FT REPEAT 125..163 FT /note="WD 2" FT REPEAT 167..205 FT /note="WD 3" FT REPEAT 209..259 FT /note="WD 4" FT REPEAT 270..308 FT /note="WD 5" FT REPEAT 313..349 FT /note="WD 6" FT REPEAT 353..389 FT /note="WD 7" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT VAR_SEQ 1..115 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044699" FT VAR_SEQ 1..30 FT /note="MAAPLRIQSDWAQALRKDEGEAWLSCHPPG -> MLVPCFLYSLQNR (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1" FT /id="VSP_018477" FT VARIANT 53 FT /note="A -> V (in dbSNP:rs17850051)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_026415" FT VARIANT 139 FT /note="C -> S (in dbSNP:rs2067912)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_032082" FT VARIANT 209 FT /note="A -> G (in dbSNP:rs3741138)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1" FT /id="VAR_026416" SQ SEQUENCE 392 AA; 42190 MW; 54ECB1DEC1841B49 CRC64; MAAPLRIQSD WAQALRKDEG EAWLSCHPPG KPSLYGSLTC QGIGLDGIPE VTASEGFTVN EINKKSIHIS CPKENASSKF LAPYTTFSRI HTKSITCLDI SSRGGLGVSS STDGTMKIWQ ASNGELRRVL EGHVFDVNCC RFFPSGLVVL SGGMDAQLKI WSAEDASCVV TFKGHKGGIL DTAIVDRGRN VVSASRDGTA RLWDCGRSAC LGVLADCGSS INGVAVGAAD NSINLGSPEQ MPSEREVGTE AKMLLLARED KKLQCLGLQS RQLVFLFIGS DAFNCCTFLS GFLLLAGTQD GNIYQLDVRS PRAPVQVIHR SGAPVLSLLS VRDGFIASQG DGSCFIVQQD LDYVTELTGA DCDPVYKVAT WEKQIYTCCR DGLVRRYQLS DL //