ID   PAAF1_HUMAN             Reviewed;         392 AA.
AC   Q9BRP4; A6NDR5; Q4G165; Q53HS9; Q7Z500; Q8TBU6; Q9HAB6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   22-JUL-2008, entry version 52.
DE   RecName: Full=Proteasomal ATPase-associated factor 1;
DE   AltName: Full=WD repeat-containing protein 71;
DE   AltName: Full=Protein G-16;
GN   Name=PAAF1; Synonyms=WDR71;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Zhao S.Y.;
RT   "Cloning of a new human cDNA homology to Xenopus laevis gene 16
RT   mRNA.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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
RP   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.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RP   VARIANTS 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PSMC1; PSMC2; PSMC3;
RP   PSMC4; PSMC5 AND PSMC6, AND 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
RT   proteasome activity by interacting with proteasomal ATPases.";
RL   Mol. Cell. Biol. 25:3842-3853(2005).
RN   [8]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
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
RT   26S proteasome complex.";
RL   Biochemistry 46:3553-3565(2007).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH HIV-1 TAT.
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).
CC   -!- FUNCTION: Inhibits proteasome 26S assembly and proteolytic
CC       activity by impairing the association of the 19S regulatory
CC       complex with the 20S core. In case of HIV-1 infection, recruited
CC       by viral Tat to the HIV-1 promoter, where it promotes the
CC       recruitment of 19S regulatory complex through dissociation of the
CC       proteasome 26S. This presumably promotes provirus transcription
CC       efficiency.
CC   -!- SUBUNIT: Interacts with PSMC1, PSMC2, PSMC3, PSMC4, PSMC5 and
CC       PSMC6. Interacts with HIV-1 Tat.
CC   -!- INTERACTION:
CC       Q8IZ83:ALDH16A1; NbExp=1; IntAct=EBI-1056358, EBI-1044483;
CC       Q9Y315:DERA; NbExp=1; IntAct=EBI-1056358, EBI-1048152;
CC       O60427:DKFZp762M2311; NbExp=1; IntAct=EBI-1056358, EBI-1055473;
CC       P62191:PSMC1; NbExp=1; IntAct=EBI-1056358, EBI-357598;
CC       P35998:PSMC2; NbExp=1; IntAct=EBI-1056358, EBI-359710;
CC       P17980:PSMC3; NbExp=1; IntAct=EBI-1056358, EBI-359720;
CC       P43686:PSMC4; NbExp=1; IntAct=EBI-1056358, EBI-743997;
CC       P62195:PSMC5; NbExp=1; IntAct=EBI-1056358, EBI-357745;
CC       P62333:PSMC6; NbExp=1; IntAct=EBI-1056358, EBI-357669;
CC       Q99460:PSMD1; NbExp=1; IntAct=EBI-1056358, EBI-357874;
CC       O75832:PSMD10; NbExp=1; IntAct=EBI-1056358, EBI-752185;
CC       O00231:PSMD11; NbExp=1; IntAct=EBI-1056358, EBI-357816;
CC       O00232:PSMD12; NbExp=1; IntAct=EBI-1056358, EBI-359733;
CC       O00487:PSMD14; NbExp=1; IntAct=EBI-1056358, EBI-722193;
CC       Q13200:PSMD2; NbExp=1; IntAct=EBI-1056358, EBI-357648;
CC       O43242:PSMD3; NbExp=1; IntAct=EBI-1056358, EBI-357622;
CC       Q15008:PSMD6; NbExp=1; IntAct=EBI-1056358, EBI-359701;
CC       P51665:PSMD7; NbExp=1; IntAct=EBI-1056358, EBI-357659;
CC       P48556:PSMD8; NbExp=1; IntAct=EBI-1056358, EBI-359304;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BRP4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BRP4-2; Sequence=VSP_018477;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC       kidney, brain and testis.
CC   -!- SIMILARITY: Contains 5 WD repeats.
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DR   EMBL; AF087895; AAP97194.1; -; mRNA.
DR   EMBL; AK021910; BAB13933.1; -; mRNA.
DR   EMBL; AK222501; BAD96221.1; -; 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   RefSeq; NP_079431.1; -.
DR   UniGene; Hs.525017; -.
DR   IntAct; Q9BRP4; -.
DR   Ensembl; ENSG00000175575; Homo sapiens.
DR   GeneID; 80227; -.
DR   KEGG; hsa:80227; -.
DR   HGNC; HGNC:25687; PAAF1.
DR   PharmGKB; PA142670604; -.
DR   HOVERGEN; Q9BRP4; -.
DR   ArrayExpress; Q9BRP4; -.
DR   CleanEx; HS_PAAF1; -.
DR   GermOnline; ENSG00000175575; Homo sapiens.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like.
DR   InterPro; IPR001680; WD40_repeat.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   ProDom; PD000018; WD40; 2.
DR   SMART; SM00320; WD40; 6.
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   Alternative splicing; Host-virus interaction; Polymorphism;
KW   Proteasome; Repeat; WD repeat.
FT   CHAIN         1    392       Proteasomal ATPase-associated factor 1.
FT                                /FTId=PRO_0000235685.
FT   REPEAT       90    129       WD 1.
FT   REPEAT      132    171       WD 2.
FT   REPEAT      174    215       WD 3.
FT   REPEAT      278    316       WD 4.
FT   REPEAT      360    392       WD 5.
FT   VAR_SEQ       1     30       MAAPLRIQSDWAQALRKDEGEAWLSCHPPG -> MLVPCFL
FT                                YSLQNR (in isoform 2).
FT                                /FTId=VSP_018477.
FT   VARIANT      53     53       A -> V (in dbSNP:rs17850051).
FT                                /FTId=VAR_026415.
FT   VARIANT     139    139       C -> S (in dbSNP:rs2067912).
FT                                /FTId=VAR_032082.
FT   VARIANT     209    209       A -> G (in dbSNP:rs3741138).
FT                                /FTId=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
//