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P28073

- PSB6_RAT

UniProt

P28073 - PSB6_RAT

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Protein
Proteasome subunit beta type-6
Gene
Psmb6, Psmb6l
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei34 – 341Nucleophile By similarity

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_194781. Separation of Sister Chromatids.
REACT_196424. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_198391. Asymmetric localization of PCP proteins.
REACT_199194. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199197. ER-Phagosome pathway.
REACT_199247. Activation of NF-kappaB in B cells.
REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_204983. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_206488. degradation of DVL.
REACT_206997. CDT1 association with the CDC6:ORC:origin complex.
REACT_211117. Orc1 removal from chromatin.
REACT_212486. CDK-mediated phosphorylation and removal of Cdc6.
REACT_220232. Regulation of ornithine decarboxylase (ODC).
REACT_227706. degradation of AXIN.

Protein family/group databases

MEROPSiT01.010.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-6 (EC:3.4.25.1)
Alternative name(s):
Macropain delta chain
Multicatalytic endopeptidase complex delta chain
Proteasome chain 5
Proteasome delta chain
Proteasome subunit Y
Gene namesi
Name:Psmb6
Synonyms:Psmb6l
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi61881. Psmb6.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  3. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Propeptidei2 – 3332Removed in mature form
PRO_0000026617Add
BLAST
Chaini34 – 238205Proteasome subunit beta type-6
PRO_0000026618Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity

Keywords - PTMi

Acetylation, Zymogen

Proteomic databases

PaxDbiP28073.
PRIDEiP28073.

2D gel databases

World-2DPAGE0004:P28073.

Expressioni

Gene expression databases

GenevestigatoriP28073.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. This subunit can be displaced by the equivalent immune-specific subunit PSMB9.

Protein-protein interaction databases

BioGridi248287. 1 interaction.
IntActiP28073. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP28073.
SMRiP28073. Positions 34-235.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
HOVERGENiHBG000123.
InParanoidiP28073.
KOiK02738.
OMAiCIRMCVI.
OrthoDBiEOG79GT80.
PhylomeDBiP28073.
TreeFamiTF106221.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P28073-1 [UniParc]FASTAAdd to Basket

« Hide

MAAALAVRGA VSAPAFGPEA LTPDWENREV STGTTIMAVQ FDGGVVLGAD    50
SRTTTGSYIA NRVTDKLTPI HDHIFCCRSG SAADTQAVAD AVTYQLGFHS 100
IELNEPPLVH TAASLFKEMC YRYREDLMAG IIIAGWDPQE GGQVYSVPMG 150
GMMVRQSFAI GGSGSSYIYG YVDATYREGM TKDECLQFTA NALALAMERD 200
GSSGGVIRLA AIQQSGVERQ VLLGDQIPKV TISTLPPP 238
Length:238
Mass (Da):25,290
Last modified:December 20, 2005 - v3
Checksum:i4B051AF11D78E49B
GO

Sequence cautioni

The sequence BAA01586.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC058451 mRNA. Translation: AAH58451.1.
AABR03076595 Genomic DNA. No translation available.
D10754 mRNA. Translation: BAA01586.1. Different initiation.
BN000325 mRNA. Translation: CAE48380.1.
PIRiJX0228.
S09086.
RefSeqiNP_476440.2. NM_057099.3.
UniGeneiRn.8118.

Genome annotation databases

EnsembliENSRNOT00000015746; ENSRNOP00000015747; ENSRNOG00000011827.
ENSRNOT00000026507; ENSRNOP00000026507; ENSRNOG00000019551.
GeneIDi29666.
KEGGirno:29666.
UCSCiRGD:61881. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC058451 mRNA. Translation: AAH58451.1 .
AABR03076595 Genomic DNA. No translation available.
D10754 mRNA. Translation: BAA01586.1 . Different initiation.
BN000325 mRNA. Translation: CAE48380.1 .
PIRi JX0228.
S09086.
RefSeqi NP_476440.2. NM_057099.3.
UniGenei Rn.8118.

3D structure databases

ProteinModelPortali P28073.
SMRi P28073. Positions 34-235.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 248287. 1 interaction.
IntActi P28073. 1 interaction.

Protein family/group databases

MEROPSi T01.010.

2D gel databases

World-2DPAGE 0004:P28073.

Proteomic databases

PaxDbi P28073.
PRIDEi P28073.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000015746 ; ENSRNOP00000015747 ; ENSRNOG00000011827 .
ENSRNOT00000026507 ; ENSRNOP00000026507 ; ENSRNOG00000019551 .
GeneIDi 29666.
KEGGi rno:29666.
UCSCi RGD:61881. rat.

Organism-specific databases

CTDi 5694.
RGDi 61881. Psmb6.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00510000046484.
HOGENOMi HOG000091079.
HOVERGENi HBG000123.
InParanoidi P28073.
KOi K02738.
OMAi CIRMCVI.
OrthoDBi EOG79GT80.
PhylomeDBi P28073.
TreeFami TF106221.

Enzyme and pathway databases

Reactomei REACT_194781. Separation of Sister Chromatids.
REACT_196424. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_198391. Asymmetric localization of PCP proteins.
REACT_199194. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199197. ER-Phagosome pathway.
REACT_199247. Activation of NF-kappaB in B cells.
REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_204983. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_206488. degradation of DVL.
REACT_206997. CDT1 association with the CDC6:ORC:origin complex.
REACT_211117. Orc1 removal from chromatin.
REACT_212486. CDK-mediated phosphorylation and removal of Cdc6.
REACT_220232. Regulation of ornithine decarboxylase (ODC).
REACT_227706. degradation of AXIN.

Miscellaneous databases

NextBioi 609975.

Gene expression databases

Genevestigatori P28073.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
PRINTSi PR00141. PROTEASOME.
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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].
    Tissue: Pituitary.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Molecular cloning of cDNAs for rat proteasomes: deduced primary structures of four other subunits."
    Tamura T., Shimbara N., Aki M., Ishida N., Bey F., Scherrer K., Tanaka K., Ichihara A.
    J. Biochem. 112:530-534(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-238.
  4. "N-terminal sequence similarities between components of the multicatalytic proteinase complex."
    Lilley K.S., Davison M.D., Rivett A.J.
    FEBS Lett. 262:327-329(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-51.
  5. Lubec G., Diao W.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 67-78 AND 209-229, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  6. "A genomic analysis of rat proteases and protease inhibitors."
    Puente X.S., Lopez-Otin C.
    Genome Res. 14:609-622(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.

Entry informationi

Entry nameiPSB6_RAT
AccessioniPrimary (citable) accession number: P28073
Secondary accession number(s): Q6IE68, Q6PDW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: December 20, 2005
Last modified: September 3, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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