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Protein

DNA mismatch repair protein HSM3

Gene

HSM3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in DNA mismatch repair in slow-growing cells. Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the 19S regulatory complex (RC).7 Publications

GO - Biological processi

  • mismatch repair Source: SGD
  • proteasome regulatory particle assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

BioCyciYEAST:G3O-29193-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA mismatch repair protein HSM3
Alternative name(s):
Enhanced spontaneous mutability protein 3
Gene namesi
Name:HSM3
Ordered Locus Names:YBR272C
ORF Names:YBR1740
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR272C.
SGDiS000000476. HSM3.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 480480DNA mismatch repair protein HSM3PRO_0000202532Add
BLAST

Proteomic databases

MaxQBiP38348.
PeptideAtlasiP38348.

PTM databases

iPTMnetiP38348.

Interactioni

Subunit structurei

Interacts with RPT1, RPT2, RPT3, RPT5, RPT6, RPN1 and RPN2. Part of transient complex (BP1) containing HSM3, RPT1, RPT2 and RPT5 formed during the assembly of the 26S proteasome.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NAS6P500866EBI-21152,EBI-14028
RPN14P531966EBI-21152,EBI-23691
RPN8Q087235EBI-21152,EBI-36176
RPT1P332997EBI-21152,EBI-13910
RPT5P332976EBI-21152,EBI-13920
SEM1O947422EBI-21152,EBI-31337

Protein-protein interaction databases

BioGridi32967. 64 interactions.
DIPiDIP-2748N.
IntActiP38348. 39 interactions.
MINTiMINT-545299.

Structurei

Secondary structure

1
480
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2112Combined sources
Beta strandi22 – 243Combined sources
Helixi29 – 4214Combined sources
Helixi52 – 6312Combined sources
Helixi73 – 8614Combined sources
Helixi89 – 957Combined sources
Helixi98 – 1058Combined sources
Helixi110 – 12112Combined sources
Helixi126 – 1294Combined sources
Helixi134 – 1429Combined sources
Helixi150 – 16314Combined sources
Helixi167 – 1748Combined sources
Turni175 – 1773Combined sources
Helixi178 – 18710Combined sources
Helixi190 – 20415Combined sources
Turni209 – 2113Combined sources
Helixi214 – 2174Combined sources
Helixi221 – 2277Combined sources
Helixi231 – 25020Combined sources
Helixi254 – 2563Combined sources
Helixi257 – 2604Combined sources
Helixi261 – 2633Combined sources
Helixi264 – 2729Combined sources
Turni274 – 2763Combined sources
Helixi278 – 2836Combined sources
Helixi285 – 29511Combined sources
Beta strandi301 – 3033Combined sources
Helixi304 – 3129Combined sources
Turni316 – 3183Combined sources
Helixi320 – 3223Combined sources
Helixi323 – 3297Combined sources
Helixi332 – 3387Combined sources
Helixi340 – 3467Combined sources
Helixi351 – 3533Combined sources
Helixi354 – 3607Combined sources
Helixi364 – 3685Combined sources
Helixi371 – 3733Combined sources
Helixi376 – 3805Combined sources
Helixi384 – 39411Combined sources
Helixi398 – 40710Combined sources
Helixi409 – 4168Combined sources
Helixi421 – 4233Combined sources
Helixi427 – 44115Combined sources
Helixi445 – 4484Combined sources
Helixi449 – 4513Combined sources
Helixi452 – 46413Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VLDX-ray2.05A/B1-480[»]
3VLEX-ray2.41A/B1-480[»]
3VLFX-ray3.80A/C1-480[»]
4A3TX-ray2.10A/B2-480[»]
4A3VX-ray3.80A/C2-480[»]
4FP7X-ray2.20A/B1-480[»]
4JPOX-ray5.00A/B1-480[»]
ProteinModelPortaliP38348.
SMRiP38348. Positions 9-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the proteasome subunit S5B/HSM3 family.Curated

Phylogenomic databases

HOGENOMiHOG000112972.
InParanoidiP38348.
OMAiNCENTIM.
OrthoDBiEOG77Q55Z.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

P38348-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEKETNYVE NLLTQLENEL NEDNLPEDIN TLLRKCSLNL VTVVSLPDMD
60 70 80 90 100
VKPLLATIKR FLTSNVSYDS LNYDYLLDVV DKLVPMADFD DVLEVYSAED
110 120 130 140 150
LVKALRSEID PLKVAACRVI ENSQPKGLFA TSNIIDILLD ILFDEKVEND
160 170 180 190 200
KLITAIEKAL ERLSTDELIR RRLFDNNLPY LVSVKGRMET VSFVRLIDFL
210 220 230 240 250
TIEFQFISGP EFKDIIFCFT KEEILKSVED ILVFIELVNY YTKFLLEIRN
260 270 280 290 300
QDKYWALRHV KKILPVFAQL FEDTENYPDV RAFSTNCLLQ LFAEVSRIEE
310 320 330 340 350
DEYSLFKTMD KDSLKIGSEA KLITEWLELI NPQYLVKYHK DVVENYFHVS
360 370 380 390 400
GYSIGMLRNL SADEECFNAI RNKFSAEIVL RLPYLEQMQV VETLTRYEYT
410 420 430 440 450
SKFLLNEMPK VMGSLIGDGS AGAIIDLETV HYRNSALRNL LDKGEEKLSV
460 470 480
WYEPLLREYS KAVNGKNYST GSETKIADCR
Length:480
Mass (Da):55,543
Last modified:October 1, 1994 - v1
Checksum:i8B739BCC9A46A63E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36141 Genomic DNA. Translation: CAA85235.1.
AY692825 Genomic DNA. Translation: AAT92844.1.
BK006936 Genomic DNA. Translation: DAA07388.1.
PIRiS46153.
RefSeqiNP_009831.3. NM_001178620.3.

Genome annotation databases

EnsemblFungiiYBR272C; YBR272C; YBR272C.
GeneIDi852575.
KEGGisce:YBR272C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36141 Genomic DNA. Translation: CAA85235.1.
AY692825 Genomic DNA. Translation: AAT92844.1.
BK006936 Genomic DNA. Translation: DAA07388.1.
PIRiS46153.
RefSeqiNP_009831.3. NM_001178620.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3VLDX-ray2.05A/B1-480[»]
3VLEX-ray2.41A/B1-480[»]
3VLFX-ray3.80A/C1-480[»]
4A3TX-ray2.10A/B2-480[»]
4A3VX-ray3.80A/C2-480[»]
4FP7X-ray2.20A/B1-480[»]
4JPOX-ray5.00A/B1-480[»]
ProteinModelPortaliP38348.
SMRiP38348. Positions 9-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32967. 64 interactions.
DIPiDIP-2748N.
IntActiP38348. 39 interactions.
MINTiMINT-545299.

PTM databases

iPTMnetiP38348.

Proteomic databases

MaxQBiP38348.
PeptideAtlasiP38348.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR272C; YBR272C; YBR272C.
GeneIDi852575.
KEGGisce:YBR272C.

Organism-specific databases

EuPathDBiFungiDB:YBR272C.
SGDiS000000476. HSM3.

Phylogenomic databases

HOGENOMiHOG000112972.
InParanoidiP38348.
OMAiNCENTIM.
OrthoDBiEOG77Q55Z.

Enzyme and pathway databases

BioCyciYEAST:G3O-29193-MONOMER.

Miscellaneous databases

PROiP38348.

Family and domain databases

InterProiIPR016024. ARM-type_fold.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [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. "The yeast HSM3 gene acts in one of the mismatch repair pathways."
    Fedorova I.V., Gracheva L.M., Kovaltzova S.V., Evstuhina T.A., Alekseev S.Y., Korolev V.G.
    Genetics 148:963-973(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "The yeast HSM3 gene is not involved in DNA mismatch repair in rapidly dividing cells."
    Merker J.D., Datta A., Kolodner R.D., Petes T.D.
    Genetics 154:491-493(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The yeast HSM3 gene is involved in DNA mismatch repair in slowly dividing cells."
    Fedorova I.V., Kovaltzova S.V., Korolev V.G.
    Genetics 154:495-496(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Requirement of HSM3 gene for spontaneous mutagenesis in Saccharomyces cerevisiae."
    Fedorova I.V., Kovaltzova S.V., Gracheva L.M., Evstuhina T.A., Korolev V.G.
    Mutat. Res. 554:67-75(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "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 AS PROTEASOME CHAPERONE.
  11. "Hsm3/S5b participates in the assembly pathway of the 19S regulatory particle of the proteasome."
    Le Tallec B., Barrault M.B., Guerois R., Carre T., Peyroche A.
    Mol. Cell 33:389-399(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS PROTEASOME CHAPERONE, INTERACTION WITH RPT1; RPT2; RPT3; RPT5; RPT6; RPN1 AND RPN2.
  12. "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 AS PROTEASOME CHAPERONE, INTERACTION WITH RPT1.
  13. "Hexameric assembly of the proteasomal ATPases is templated through their C termini."
    Park S., Roelofs J., Kim W., Robert J., Schmidt M., Gygi S.P., Finley D.
    Nature 459:866-870(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.

Entry informationi

Entry nameiHSM3_YEAST
AccessioniPrimary (citable) accession number: P38348
Secondary accession number(s): D6VQR8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 8, 2016
This is version 106 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 468 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.