PAAF1_HUMAN
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 03-AUG-2022, entry version 169.
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}.
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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; 55.
DR IntAct; Q9BRP4; 14.
DR MINT; Q9BRP4; -.
DR STRING; 9606.ENSP00000311665; -.
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; Q9BRP4; -.
DR PeptideAtlas; Q9BRP4; -.
DR PRIDE; Q9BRP4; -.
DR ProteomicsDB; 7085; -.
DR ProteomicsDB; 78795; -. [Q9BRP4-1]
DR ProteomicsDB; 78796; -. [Q9BRP4-2]
DR Antibodypedia; 50309; 126 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 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; QSDWSRA; -.
DR PhylomeDB; Q9BRP4; -.
DR TreeFam; TF313690; -.
DR PathwayCommons; Q9BRP4; -.
DR SignaLink; Q9BRP4; -.
DR BioGRID-ORCS; 80227; 9 hits in 1078 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 188 other tissues.
DR ExpressionAtlas; Q9BRP4; baseline and differential.
DR Genevisible; Q9BRP4; HS.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
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
