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P53196

- RPN14_YEAST

UniProt

P53196 - RPN14_YEAST

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Protein

26S proteasome regulatory subunit RPN14

Gene

RPN14

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. Is not a genuine component of the 26S proteasome, but an auxiliary factor that interacts with the proteasomal ATPase of 19S regulatory particle (RP). Acts as a chaperone which regulates the highly structured assembly of the 19S regulatory particle. Involved in the substrate specificity of the 26S proteasome and is especially involved in the degradation of ubiquitinated GCN4. May contribute to the stability of the 26S proteasome in some stress conditions.4 Publications

GO - Biological processi

  1. proteasome regulatory particle assembly Source: SGD
  2. ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciYEAST:G3O-30528-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome regulatory subunit RPN14
Alternative name(s):
Proteasome non-ATPase subunit 14
Gene namesi
Name:RPN14
Ordered Locus Names:YGL004C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL004c.
SGDiS000002972. RPN14.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: SGD
  2. nucleus Source: SGD
  3. proteasome complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 41741726S proteasome regulatory subunit RPN14PRO_0000051475Add
BLAST

Proteomic databases

MaxQBiP53196.
PaxDbiP53196.
PeptideAtlasiP53196.

Expressioni

Gene expression databases

GenevestigatoriP53196.

Interactioni

Subunit structurei

Associates with the 19S proteasome regulatory particle (RP). Interacts directly with RPT5 and RPT6.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSM3P383486EBI-23691,EBI-21152
NAS6P500864EBI-23691,EBI-14028
RPT5P332974EBI-23691,EBI-13920
RPT6Q019396EBI-23691,EBI-13914

Protein-protein interaction databases

BioGridi33241. 31 interactions.
DIPiDIP-6617N.
IntActiP53196. 23 interactions.
MINTiMINT-675986.
STRINGi4932.YGL004C.

Structurei

Secondary structure

1
417
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Beta strandi8 – 103Combined sources
Helixi14 – 196Combined sources
Beta strandi27 – 359Combined sources
Beta strandi38 – 458Combined sources
Turni49 – 513Combined sources
Beta strandi60 – 656Combined sources
Beta strandi68 – 736Combined sources
Beta strandi76 – 816Combined sources
Beta strandi84 – 863Combined sources
Turni87 – 904Combined sources
Beta strandi96 – 1027Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi108 – 1136Combined sources
Beta strandi118 – 1214Combined sources
Beta strandi127 – 1315Combined sources
Beta strandi134 – 1374Combined sources
Beta strandi139 – 1446Combined sources
Beta strandi148 – 1558Combined sources
Beta strandi158 – 1647Combined sources
Turni165 – 1673Combined sources
Beta strandi172 – 1754Combined sources
Beta strandi181 – 1877Combined sources
Turni188 – 1914Combined sources
Beta strandi192 – 1976Combined sources
Beta strandi202 – 2065Combined sources
Turni207 – 2104Combined sources
Beta strandi211 – 2166Combined sources
Beta strandi226 – 2338Combined sources
Helixi240 – 2423Combined sources
Beta strandi257 – 2637Combined sources
Beta strandi268 – 2725Combined sources
Turni273 – 2753Combined sources
Beta strandi278 – 2825Combined sources
Beta strandi290 – 2956Combined sources
Beta strandi302 – 3076Combined sources
Beta strandi310 – 3167Combined sources
Beta strandi324 – 3307Combined sources
Beta strandi335 – 3417Combined sources
Beta strandi344 – 3496Combined sources
Turni350 – 3523Combined sources
Beta strandi353 – 3608Combined sources
Beta strandi366 – 3705Combined sources
Beta strandi376 – 3783Combined sources
Beta strandi387 – 3915Combined sources
Beta strandi394 – 3974Combined sources
Beta strandi399 – 4046Combined sources
Turni405 – 4073Combined sources
Beta strandi408 – 4147Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ACPX-ray2.00A1-417[»]
3VL1X-ray1.60A/B1-417[»]
ProteinModelPortaliP53196.
SMRiP53196. Positions 1-417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53196.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati134 – 17340WD 1Add
BLAST
Repeati176 – 21540WD 2Add
BLAST
Repeati242 – 28140WD 3Add
BLAST
Repeati285 – 32541WD 4Add
BLAST
Repeati330 – 37142WD 5Add
BLAST
Repeati380 – 41637WD 6Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat PAAF1/RPN14 family.Curated
Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00390000005948.
HOGENOMiHOG000142386.
InParanoidiP53196.
KOiK11887.
OMAiDESNGEV.
OrthoDBiEOG7TBCBC.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 4 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53196-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTKTITVAHI QYDFKAVLEE NDENDDEFYI NVDKNLNEIK EHKIVVLGNS
60 70 80 90 100
RGVDAGKGNT FEKVGSHLYK ARLDGHDFLF NTIIRDGSKM LKRADYTAVD
110 120 130 140 150
TAKLQMRRFI LGTTEGDIKV LDSNFNLQRE IDQAHVSEIT KLKFFPSGEA
160 170 180 190 200
LISSSQDMQL KIWSVKDGSN PRTLIGHRAT VTDIAIIDRG RNVLSASLDG
210 220 230 240 250
TIRLWECGTG TTIHTFNRKE NPHDGVNSIA LFVGTDRQLH EISTSKKNNL
260 270 280 290 300
EFGTYGKYVI AGHVSGVITV HNVFSKEQTI QLPSKFTCSC NSLTVDGNNA
310 320 330 340 350
NYIYAGYENG MLAQWDLRSP ECPVGEFLIN EGTPINNVYF AAGALFVSSG
360 370 380 390 400
FDTSIKLDII SDPESERPAI EFETPTFLVS NDDEVSQFCY VSDDESNGEV
410
LEVGKNNFCA LYNLSNP
Length:417
Mass (Da):46,383
Last modified:October 1, 1996 - v1
Checksum:i025CAB9A872E1AB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72526 Genomic DNA. Translation: CAA96704.1.
AY692599 Genomic DNA. Translation: AAT92618.1.
BK006941 Genomic DNA. Translation: DAA08095.1.
PIRiS64006.
RefSeqiNP_011511.3. NM_001180869.3.

Genome annotation databases

EnsemblFungiiYGL004C; YGL004C; YGL004C.
GeneIDi852880.
KEGGisce:YGL004C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72526 Genomic DNA. Translation: CAA96704.1 .
AY692599 Genomic DNA. Translation: AAT92618.1 .
BK006941 Genomic DNA. Translation: DAA08095.1 .
PIRi S64006.
RefSeqi NP_011511.3. NM_001180869.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3ACP X-ray 2.00 A 1-417 [» ]
3VL1 X-ray 1.60 A/B 1-417 [» ]
ProteinModelPortali P53196.
SMRi P53196. Positions 1-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33241. 31 interactions.
DIPi DIP-6617N.
IntActi P53196. 23 interactions.
MINTi MINT-675986.
STRINGi 4932.YGL004C.

Proteomic databases

MaxQBi P53196.
PaxDbi P53196.
PeptideAtlasi P53196.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL004C ; YGL004C ; YGL004C .
GeneIDi 852880.
KEGGi sce:YGL004C.

Organism-specific databases

CYGDi YGL004c.
SGDi S000002972. RPN14.

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00390000005948.
HOGENOMi HOG000142386.
InParanoidi P53196.
KOi K11887.
OMAi DESNGEV.
OrthoDBi EOG7TBCBC.

Enzyme and pathway databases

BioCyci YEAST:G3O-30528-MONOMER.

Miscellaneous databases

EvolutionaryTracei P53196.
NextBioi 972523.

Gene expression databases

Genevestigatori P53196.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF00400. WD40. 2 hits.
[Graphical view ]
SMARTi SM00320. WD40. 4 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
PROSITEi PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Rpn13p and Rpn14p are involved in the recognition of ubiquitinated Gcn4p by the 26S proteasome."
    Seong K.M., Baek J.H., Yu M.H., Kim J.
    FEBS Lett. 581:2567-2573(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPT5.
  7. "Chaperone-mediated pathway of proteasome regulatory particle assembly."
    Roelofs J., Park S., Haas W., Tian G., McAllister F.E., Huo Y., Lee B.H., Zhang F., Shi Y., Gygi S.P., Finley D.
    Nature 459:861-865(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH THE PROTEASOME REGULATORY PARTICLE.
  8. "Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base."
    Funakoshi M., Tomko R.J. Jr., Kobayashi H., Hochstrasser M.
    Cell 137:887-899(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH THE 19S REGULATORY PARTICLE OF THE PROTEASOME, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle."
    Saeki Y., Toh-E A., Kudo T., Kawamura H., Tanaka K.
    Cell 137:900-913(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE 19S REGULATORY PARTICLE OF THE PROTEASOME, INTERACTION WITH RPT6.

Entry informationi

Entry nameiRPN14_YEAST
AccessioniPrimary (citable) accession number: P53196
Secondary accession number(s): D6VUD4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2210 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3