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Reviewed, UniProtKB/Swiss-Prot P17980 (PRS6A_HUMAN)

Last modified February 9, 2010. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    26S protease regulatory subunit 6A
Alternative name(s):
    Proteasome 26S subunit ATPase 3
    TAT-binding protein 1
      Short name=TBP-1
    Proteasome subunit P50
Gene names
Name: PSMC3
Synonyms: TBP1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex By similarity. In case of HIV-1 infection, suppresses Tat-mediated transactivation.

Subunit structure

May form a heterodimer with a related family member. Interacts with PAAF1. Interacts with HIV-1 Tat. Ref.6 Ref.10

Subcellular location

Cytoplasm Potential. Nucleus Potential.

Post-translational modification

Sumoylated by UBE2I in response to MEKK1-mediated stimuli. Ref.12

Sequence similarities

Belongs to the AAA ATPase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 43943926S protease regulatory subunit 6A
PRO_0000084698

Regions

Nucleotide binding227 – 2348ATP Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11 Ref.14
Modified residue91Phosphoserine Ref.11 Ref.14

Experimental info

Mutagenesis2331K → H: Loss of function.
Mutagenesis2891D → A: Loss of function.
Sequence conflict3561M → T in BAD96205. Ref.5
Sequence conflict4091R → A in AAA36666. Ref.1
Sequence conflict4091R → A Ref.6

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Sequences

Sequence LengthMass (Da)Tools
P17980-1 [UniParc].

Last modified May 10, 2002. Version 3.
Checksum: 0E443465DDDEBB0B

FASTA43949,204
        10         20         30         40         50         60 
MNLLPNIESP VTRQEKMATV WDEAEQDGIG EEVLKMSTEE IIQRTRLLDS EIKIMKSEVL 

        70         80         90        100        110        120 
RVTHELQAMK DKIKENSEKI KVNKTLPYLV SNVIELLDVD PNDQEEDGAN IDLDSQRKGK 

       130        140        150        160        170        180 
CAVIKTSTRQ TYFLPVIGLV DAEKLKPGDL VGVNKDSYLI LETLPTEYDS RVKAMEVDER 

       190        200        210        220        230        240 
PTEQYSDIGG LDKQIQELVE AIVLPMNHKE KFENLGIQPP KGVLMYGPPG TGKTLLARAC 

       250        260        270        280        290        300 
AAQTKATFLK LAGPQLVQMF IGDGAKLVRD AFALAKEKAP SIIFIDELDA IGTKRFDSEK 

       310        320        330        340        350        360 
AGDREVQRTM LELLNQLDGF QPNTQVKVIA ATNRVDILDP ALLRSGRLDR KIEFPMPNEE 

       370        380        390        400        410        420 
ARARIMQIHS RKMNVSPDVN YEELARCTDD FNGAQCKAVC VEAGMIALRR GATELTHEDY 

       430 
MEGILEVQAK KKANLQYYA

« Hide

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References

« Hide 'large scale' references
[1]"The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes."
Ohana B., Moore P.A., Ruben S.M., Southgate C.D., Green M.R., Rosen C.A.
Proc. Natl. Acad. Sci. U.S.A. 90:138-142(1993) [PubMed: 8419915] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney, Lung and Peripheral nerve.
[5]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] OF 16-439.
Tissue: Adipose tissue.
[6]"A cDNA for a protein that interacts with the human immunodeficiency virus Tat transactivator."
Nelbock P., Dillion P.J., Perkins A., Rosen C.A.
Science 248:1650-1653(1990) [PubMed: 2194290] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-439, INTERACTION WITH HIV-1 TAT.
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-439.
[8]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 130-144; 156-171; 174-233; 251-266; 277-294; 309-327; 335-344; 351-362; 372-386 AND 398-409, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[9]"Identification, purification, and characterization of a PA700-dependent activator of the proteasome."
Demartino G.N., Proske R.J., Moomaw C.R., Strong A.A., Song X., Hisamatsu H., Tanaka K., Slaughter C.A.
J. Biol. Chem. 271:3112-3118(1996) [PubMed: 8621709] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[10]"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: 15831487] [Abstract]
Cited for: INTERACTION WITH PAAF1.
[11]"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: 17323924] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, ACETYLATION AT MET-1, MASS SPECTROMETRY.
[12]"Ubc9 fusion-directed SUMOylation identifies constitutive and inducible SUMOylation."
Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.
Nucleic Acids Res. 35:E109-E109(2007) [PubMed: 17709345] [Abstract]
Cited for: SUMOYLATION.
[13]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]"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: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M34079 mRNA. Translation: AAA36666.1.
CH471064 Genomic DNA. Translation: EAW67916.1.
BC008713 mRNA. Translation: AAH08713.4.
BC073165 mRNA. Translation: AAH73165.3.
BC106920 mRNA. Translation: AAI06921.1.
BC107804 mRNA. Translation: AAI07805.1. Different initiation.
AK222485 mRNA. Translation: BAD96205.1.
AK313518 mRNA. Translation: BAG36298.1.
CR456731 mRNA. Translation: CAG33012.1.
IPIIPI00018398.
PIRA34832.
RefSeqNP_002795.2.
UniGeneHs.250758

3D structure databases

SMRP17980. Positions 145-417, 178-422.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-27555N.
IntActP17980. 22 interactions.
STRINGP17980.

PTM databases

PhosphoSiteP17980.

2-D gel databases

REPRODUCTION-2DPAGEIPI00018398.

Proteomic databases

PeptideAtlasP17980.
PRIDEP17980.

Genome annotation databases

EnsemblENST00000298852; ENSP00000298852; ENSG00000165916; Homo sapiens. [Genome view]
GeneID5702.
KEGGhsa:5702.
NMPDRfig|9606.3.peg.5546.
UCSCuc001nfh.2. human.

Organism-specific databases

CTD5702.
GeneCardsGC11M047396.
H-InvDBHIX0035958.
HGNCHGNC:9549. PSMC3.
HPAHPA006065.
MIM186852. gene.
PharmGKBPA33894.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06160.
HOVERGENP17980.
InParanoidP17980.
OMADNEIKIM.
OrthoDBEOG9T4GF5.
PhylomeDBP17980.

Enzyme and pathway databases

ReactomeREACT_11045. Signaling by Wnt.
REACT_13. Metabolism of amino acids.
REACT_13635. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_152. Cell Cycle, Mitotic.
REACT_1538. Cell Cycle Checkpoints.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6185. HIV Infection.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_9035. APC/C:Cdh1-mediated degradation of Skp2.

Gene expression databases

ArrayExpressP17980.
BgeeP17980.
CleanExHS_PSMC3.
GenevestigatorP17980.
GermOnlineENSG00000165916. Homo sapiens.

Family and domain databases

InterProIPR005937. 26S_Psome_P45.
IPR003593. ATPase_AAA+_core.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
[Graphical view]
PfamPF00004. AAA. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
TIGRFAMsTIGR01242. 26Sp45. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio22154.
PMAP-CutDBP17980.
SOURCESearch...

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Entry information

Entry namePRS6A_HUMAN
AccessionPrimary (citable) accession number: P17980
Secondary accession number(s): B2R8V1 expand/collapse secondary AC list , Q3B757, Q3B865, Q53HU5, Q6GPG8, Q6IBS1, Q96HD3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 10, 2002
Last modified: February 9, 2010
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 11

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents