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Q9BRP4 (PAAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proteasomal ATPase-associated factor 1
Alternative name(s):
Protein G-16
WD repeat-containing protein 71
Gene names
Name:PAAF1
Synonyms:WDR71
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length392 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits proteasome 26S assembly and proteolytic activity by impairing the association of the 19S regulatory complex with the 20S core. In case of HIV-1 infection, recruited by viral Tat to the HIV-1 promoter, where it promotes the recruitment of 19S regulatory complex through dissociation of the proteasome 26S. This presumably promotes provirus transcription efficiency. Protects SUPT6H from proteasomal degradation. Ref.7 Ref.9 Ref.12

Subunit structure

Interacts with PSMC1, PSMC2, PSMC3, PSMC4, PSMC5 and PSMC6. Interacts with HIV-1 Tat. Interacts with SUPT6H. Ref.7 Ref.9 Ref.12

Tissue specificity

Ubiquitously expressed, with highest levels in kidney, brain and testis. Ref.7

Sequence similarities

Belongs to the WD repeat PAAF1/RPN14 family.

Contains 5 WD repeats.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentProteasome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
WD repeat
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processviral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentproteasome complex

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PSMC5P621952EBI-1056358,EBI-357745

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BRP4-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BRP4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MAAPLRIQSDWAQALRKDEGEAWLSCHPPG → MLVPCFLYSLQNR
Isoform 3 (identifier: Q9BRP4-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-115: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 392391Proteasomal ATPase-associated factor 1
PRO_0000235685

Regions

Repeat90 – 12940WD 1
Repeat132 – 17140WD 2
Repeat174 – 21542WD 3
Repeat278 – 31639WD 4
Repeat360 – 39233WD 5

Amino acid modifications

Modified residue21N-acetylalanine Ref.10

Natural variations

Alternative sequence1 – 115115Missing in isoform 3.
VSP_044699
Alternative sequence1 – 3030MAAPL…CHPPG → MLVPCFLYSLQNR in isoform 2.
VSP_018477
Natural variant531A → V. Ref.6
Corresponds to variant rs17850051 [ dbSNP | Ensembl ].
VAR_026415
Natural variant1391C → S. Ref.3
Corresponds to variant rs2067912 [ dbSNP | Ensembl ].
VAR_032082
Natural variant2091A → G. Ref.1 Ref.2 Ref.6
Corresponds to variant rs3741138 [ dbSNP | Ensembl ].
VAR_026416

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 16, 2006. Version 2.
Checksum: 54ECB1DEC1841B49

FASTA39242,190
        10         20         30         40         50         60 
MAAPLRIQSD WAQALRKDEG EAWLSCHPPG KPSLYGSLTC QGIGLDGIPE VTASEGFTVN 

        70         80         90        100        110        120 
EINKKSIHIS CPKENASSKF LAPYTTFSRI HTKSITCLDI SSRGGLGVSS STDGTMKIWQ 

       130        140        150        160        170        180 
ASNGELRRVL EGHVFDVNCC RFFPSGLVVL SGGMDAQLKI WSAEDASCVV TFKGHKGGIL 

       190        200        210        220        230        240 
DTAIVDRGRN VVSASRDGTA RLWDCGRSAC LGVLADCGSS INGVAVGAAD NSINLGSPEQ 

       250        260        270        280        290        300 
MPSEREVGTE AKMLLLARED KKLQCLGLQS RQLVFLFIGS DAFNCCTFLS GFLLLAGTQD 

       310        320        330        340        350        360 
GNIYQLDVRS PRAPVQVIHR SGAPVLSLLS VRDGFIASQG DGSCFIVQQD LDYVTELTGA 

       370        380        390 
DCDPVYKVAT WEKQIYTCCR DGLVRRYQLS DL 

« Hide

Isoform 2 [UniParc].

Checksum: C9AAF37840B5F43A
Show »

FASTA37540,439
Isoform 3 [UniParc].

Checksum: 00F78074BBD2F913
Show »

FASTA27729,982

References

« Hide 'large scale' references
[1]"Cloning of a new human cDNA homology to Xenopus laevis gene 16 mRNA."
Bi A.D., Yu L., Tu Q., Yang J., Dai F.Y., Cui W.C., Zheng L.H., Zhao S.Y.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLY-209.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT GLY-209.
Tissue: Embryo, Kidney and Testis.
[3]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-139.
Tissue: Adipose tissue.
[4]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS VAL-53 AND GLY-209.
Tissue: Brain and Lung.
[7]"Proteasomal ATPase-associated factor 1 negatively regulates proteasome activity by interacting with proteasomal ATPases."
Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.
Mol. Cell. Biol. 25:3842-3853(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PSMC1; PSMC2; PSMC3; PSMC4; PSMC5 AND PSMC6, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[9]"The proteasome regulates HIV-1 transcription by both proteolytic and nonproteolytic mechanisms."
Lassot I., Latreille D., Rousset E., Sourisseau M., Linares L.K., Chable-Bessia C., Coux O., Benkirane M., Kiernan R.E.
Mol. Cell 25:369-383(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HIV-1 TAT.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Spt6 levels are modulated by PAAF1 and proteasome to regulate the HIV-1 LTR."
Nakamura M., Basavarajaiah P., Rousset E., Beraud C., Latreille D., Henaoui I.S., Lassot I., Mari B., Kiernan R.
Retrovirology 9:13-13(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SUPT6H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF087895 mRNA. Translation: AAP97194.1.
AK021910 mRNA. Translation: BAB13933.1.
AK222501 mRNA. Translation: BAD96221.1.
AK298258 mRNA. Translation: BAG60522.1.
AK316394 mRNA. Translation: BAH14765.1.
AP002770 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW74917.1.
BC006142 mRNA. Translation: AAH06142.2.
BC021541 mRNA. Translation: AAH21541.1.
BC028628 mRNA. Translation: AAH28628.1.
RefSeqNP_001254732.1. NM_001267803.1.
NP_001254733.1. NM_001267804.1.
NP_001254734.1. NM_001267805.1.
NP_001254735.1. NM_001267806.1.
NP_079431.1. NM_025155.2.
UniGeneHs.525017.

3D structure databases

ProteinModelPortalQ9BRP4.
SMRQ9BRP4. Positions 5-391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123191. 37 interactions.
IntActQ9BRP4. 6 interactions.
MINTMINT-3044503.
STRING9606.ENSP00000311665.

PTM databases

PhosphoSiteQ9BRP4.

Polymorphism databases

DMDM97217547.

Proteomic databases

PaxDbQ9BRP4.
PRIDEQ9BRP4.

Protocols and materials databases

DNASU80227.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310571; ENSP00000311665; ENSG00000175575. [Q9BRP4-1]
ENST00000376384; ENSP00000365564; ENSG00000175575. [Q9BRP4-2]
ENST00000535604; ENSP00000438789; ENSG00000175575. [Q9BRP4-3]
ENST00000536003; ENSP00000438124; ENSG00000175575. [Q9BRP4-2]
ENST00000541951; ENSP00000441333; ENSG00000175575. [Q9BRP4-3]
ENST00000544552; ENSP00000441494; ENSG00000175575. [Q9BRP4-2]
GeneID80227.
KEGGhsa:80227.
UCSCuc001ouk.2. human. [Q9BRP4-1]
uc001oul.2. human. [Q9BRP4-2]

Organism-specific databases

CTD80227.
GeneCardsGC11P073588.
H-InvDBHIX0009924.
HGNCHGNC:25687. PAAF1.
HPAHPA039952.
neXtProtNX_Q9BRP4.
PharmGKBPA162398551.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2319.
HOVERGENHBG056033.
InParanoidQ9BRP4.
KOK11887.
OMAIIHRSGA.
OrthoDBEOG7Z95MK.
PhylomeDBQ9BRP4.
TreeFamTF313690.

Enzyme and pathway databases

SignaLinkQ9BRP4.

Gene expression databases

ArrayExpressQ9BRP4.
BgeeQ9BRP4.
CleanExHS_PAAF1.
GenevestigatorQ9BRP4.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF00400. WD40. 3 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPAAF1.
GenomeRNAi80227.
NextBio70653.
PROQ9BRP4.

Entry information

Entry namePAAF1_HUMAN
AccessionPrimary (citable) accession number: Q9BRP4
Secondary accession number(s): A6NDR5 expand/collapse secondary AC list , B4DPB0, B7ZAS9, Q4G165, Q53HS9, Q7Z500, Q8TBU6, Q9HAB6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: April 16, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM