Full text data of PAAF1
PAAF1
(WDR71)
[Confidence: low (only semi-automatic identification from reviews)]
Proteasomal ATPase-associated factor 1 (Protein G-16; WD repeat-containing protein 71)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Proteasomal ATPase-associated factor 1 (Protein G-16; WD repeat-containing protein 71)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BRP4
ID PAAF1_HUMAN Reviewed; 392 AA.
AC Q9BRP4; A6NDR5; B4DPB0; B7ZAS9; Q4G165; Q53HS9; Q7Z500; Q8TBU6;
read moreAC Q9HAB6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 22-JAN-2014, entry version 107.
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;
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] (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.,
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 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
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).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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
RT HIV-1 LTR.";
RL Retrovirology 9:13-13(2012).
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. Protects SUPT6H from proteasomal degradation.
CC -!- SUBUNIT: Interacts with PSMC1, PSMC2, PSMC3, PSMC4, PSMC5 and
CC PSMC6. Interacts with HIV-1 Tat. Interacts with SUPT6H.
CC -!- INTERACTION:
CC 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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC kidney, brain and testis.
CC -!- SIMILARITY: Belongs to the WD repeat PAAF1/RPN14 family.
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; 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 RefSeq; NP_001254732.1; NM_001267803.1.
DR RefSeq; NP_001254733.1; NM_001267804.1.
DR RefSeq; NP_001254734.1; NM_001267805.1.
DR RefSeq; NP_001254735.1; NM_001267806.1.
DR RefSeq; NP_079431.1; NM_025155.2.
DR UniGene; Hs.525017; -.
DR ProteinModelPortal; Q9BRP4; -.
DR SMR; Q9BRP4; 79-340.
DR IntAct; Q9BRP4; 6.
DR MINT; MINT-3044503; -.
DR STRING; 9606.ENSP00000311665; -.
DR PhosphoSite; Q9BRP4; -.
DR DMDM; 97217547; -.
DR PaxDb; Q9BRP4; -.
DR PRIDE; Q9BRP4; -.
DR DNASU; 80227; -.
DR Ensembl; ENST00000310571; ENSP00000311665; ENSG00000175575.
DR Ensembl; ENST00000376384; ENSP00000365564; ENSG00000175575.
DR Ensembl; ENST00000535604; ENSP00000438789; ENSG00000175575.
DR Ensembl; ENST00000536003; ENSP00000438124; ENSG00000175575.
DR Ensembl; ENST00000541951; ENSP00000441333; ENSG00000175575.
DR Ensembl; ENST00000544552; ENSP00000441494; ENSG00000175575.
DR GeneID; 80227; -.
DR KEGG; hsa:80227; -.
DR UCSC; uc001ouk.2; human.
DR CTD; 80227; -.
DR GeneCards; GC11P073588; -.
DR H-InvDB; HIX0009924; -.
DR HGNC; HGNC:25687; PAAF1.
DR HPA; HPA039952; -.
DR neXtProt; NX_Q9BRP4; -.
DR PharmGKB; PA162398551; -.
DR eggNOG; COG2319; -.
DR HOVERGEN; HBG056033; -.
DR InParanoid; Q9BRP4; -.
DR KO; K11887; -.
DR OMA; IIHRSGA; -.
DR OrthoDB; EOG7Z95MK; -.
DR PhylomeDB; Q9BRP4; -.
DR SignaLink; Q9BRP4; -.
DR GeneWiki; PAAF1; -.
DR GenomeRNAi; 80227; -.
DR NextBio; 70653; -.
DR PRO; PR:Q9BRP4; -.
DR ArrayExpress; Q9BRP4; -.
DR Bgee; Q9BRP4; -.
DR CleanEx; HS_PAAF1; -.
DR Genevestigator; Q9BRP4; -.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
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; Complete proteome;
KW Host-virus interaction; Polymorphism; Proteasome; Reference proteome;
KW Repeat; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 392 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 MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 115 Missing (in isoform 3).
FT /FTId=VSP_044699.
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
//
ID PAAF1_HUMAN Reviewed; 392 AA.
AC Q9BRP4; A6NDR5; B4DPB0; B7ZAS9; Q4G165; Q53HS9; Q7Z500; Q8TBU6;
read moreAC Q9HAB6;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 22-JAN-2014, entry version 107.
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;
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] (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.,
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 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
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).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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.,
RA Buerckstuemmer T., 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
RT HIV-1 LTR.";
RL Retrovirology 9:13-13(2012).
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. Protects SUPT6H from proteasomal degradation.
CC -!- SUBUNIT: Interacts with PSMC1, PSMC2, PSMC3, PSMC4, PSMC5 and
CC PSMC6. Interacts with HIV-1 Tat. Interacts with SUPT6H.
CC -!- INTERACTION:
CC 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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC kidney, brain and testis.
CC -!- SIMILARITY: Belongs to the WD repeat PAAF1/RPN14 family.
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; 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 RefSeq; NP_001254732.1; NM_001267803.1.
DR RefSeq; NP_001254733.1; NM_001267804.1.
DR RefSeq; NP_001254734.1; NM_001267805.1.
DR RefSeq; NP_001254735.1; NM_001267806.1.
DR RefSeq; NP_079431.1; NM_025155.2.
DR UniGene; Hs.525017; -.
DR ProteinModelPortal; Q9BRP4; -.
DR SMR; Q9BRP4; 79-340.
DR IntAct; Q9BRP4; 6.
DR MINT; MINT-3044503; -.
DR STRING; 9606.ENSP00000311665; -.
DR PhosphoSite; Q9BRP4; -.
DR DMDM; 97217547; -.
DR PaxDb; Q9BRP4; -.
DR PRIDE; Q9BRP4; -.
DR DNASU; 80227; -.
DR Ensembl; ENST00000310571; ENSP00000311665; ENSG00000175575.
DR Ensembl; ENST00000376384; ENSP00000365564; ENSG00000175575.
DR Ensembl; ENST00000535604; ENSP00000438789; ENSG00000175575.
DR Ensembl; ENST00000536003; ENSP00000438124; ENSG00000175575.
DR Ensembl; ENST00000541951; ENSP00000441333; ENSG00000175575.
DR Ensembl; ENST00000544552; ENSP00000441494; ENSG00000175575.
DR GeneID; 80227; -.
DR KEGG; hsa:80227; -.
DR UCSC; uc001ouk.2; human.
DR CTD; 80227; -.
DR GeneCards; GC11P073588; -.
DR H-InvDB; HIX0009924; -.
DR HGNC; HGNC:25687; PAAF1.
DR HPA; HPA039952; -.
DR neXtProt; NX_Q9BRP4; -.
DR PharmGKB; PA162398551; -.
DR eggNOG; COG2319; -.
DR HOVERGEN; HBG056033; -.
DR InParanoid; Q9BRP4; -.
DR KO; K11887; -.
DR OMA; IIHRSGA; -.
DR OrthoDB; EOG7Z95MK; -.
DR PhylomeDB; Q9BRP4; -.
DR SignaLink; Q9BRP4; -.
DR GeneWiki; PAAF1; -.
DR GenomeRNAi; 80227; -.
DR NextBio; 70653; -.
DR PRO; PR:Q9BRP4; -.
DR ArrayExpress; Q9BRP4; -.
DR Bgee; Q9BRP4; -.
DR CleanEx; HS_PAAF1; -.
DR Genevestigator; Q9BRP4; -.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR017986; WD40_repeat_dom.
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; Complete proteome;
KW Host-virus interaction; Polymorphism; Proteasome; Reference proteome;
KW Repeat; WD repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 392 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 MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 1 115 Missing (in isoform 3).
FT /FTId=VSP_044699.
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
//