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Protein

ATP-dependent RNA helicase DHH1

Gene

DHH1

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

Functioni

ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping by activating the decapping enzyme DCP1 (PubMed:11780629, PubMed:12032091, PubMed:11696541, PubMed:12730603, PubMed:15703442. PubMed:15706350). Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs (PubMed:15166134). May also have a role in translation and mRNA nuclear export (PubMed:12930949). Required for sporulation (PubMed:12930949). Blocks autophagy in nutrient-rich conditions by, at least partly, binding and repressing the expression of a set of ATG genes, including ATG3, ATG7, ATG8, ATG19, ATG20, ATG22 and SNX4/ATG24 (PubMed:26098573).9 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.Curated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi90 – 978ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: SGD
  • chromatin binding Source: SGD
  • mRNA binding Source: SGD
  • translation regulator activity, nucleic acid binding Source: SGD

GO - Biological processi

  • cytoplasmic mRNA processing body assembly Source: SGD
  • deadenylation-dependent decapping of nuclear-transcribed mRNA Source: SGD
  • mRNA processing Source: UniProtKB-KW
  • mRNA transport Source: UniProtKB-KW
  • negative regulation of translation Source: SGD
  • negative regulation of translational elongation Source: SGD
  • stress granule assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA transport, Translation regulation, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29554-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DHH1Curated (EC:3.6.4.13Curated)
Alternative name(s):
DExD/H-box helicase 11 Publication
Gene namesi
Name:DHH11 Publication
Ordered Locus Names:YDL160CImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL160C.
SGDiS000002319. DHH1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytoplasmic mRNA processing body Source: SGD
  • cytoplasmic stress granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Leads to an increased in autophagy flux (PubMed:26098573). Causes an accumulation of ATG3, ATG7, ATG8, ATG19, ATG20, ATG22 and SNX4/ATG24 transcripts in nutrient-replete conditions (PubMed:26098573).1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi89 – 891R → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius; when associated with A-91. Impairs RNA binding in vitro. 1 Publication
Mutagenesisi91 – 911K → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius; when associated with A-89. Impairs RNA binding in vitro. 1 Publication
Mutagenesisi195 – 1951D → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius. 1 Publication
Mutagenesisi196 – 1961E → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius. 1 Publication
Mutagenesisi345 – 3451R → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius. Impairs RNA binding in vitro. 1 Publication
Mutagenesisi346 – 3461G → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius. Impairs RNA binding in vitro. 1 Publication
Mutagenesisi369 – 3691H → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius. 1 Publication
Mutagenesisi370 – 3701R → A: Leads to mRNA turnover defect and no growth at 37 degrees Celsius. Impairs RNA binding in vitro. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 506506ATP-dependent RNA helicase DHH1PRO_0000055044Add
BLAST

Proteomic databases

MaxQBiP39517.
PeptideAtlasiP39517.

PTM databases

iPTMnetiP39517.

Interactioni

Subunit structurei

Associated with the CCR4-NOT complex and possibly other big complexes (PubMed:9504907, PubMed:12930949). Interacts with CDC39/NOT1 (PubMed:11696541). Interacts with DCP1, LSM1, and POP2 (PubMed:9504907, PubMed:11780629). Interacts with IGO1 (PubMed:20471941). Interacts with PAT1 and with KEM1, the major 5'-3' exonuclease (PubMed:11780629, PubMed:12032091).6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EDC3P399983EBI-158,EBI-22300
LSM1P470173EBI-158,EBI-174
LSM4P400703EBI-158,EBI-188
LSM7P539053EBI-158,EBI-141
PAT1P256444EBI-158,EBI-204
POP2P390083EBI-158,EBI-13629

Protein-protein interaction databases

BioGridi31903. 394 interactions.
DIPiDIP-1243N.
IntActiP39517. 38 interactions.
MINTiMINT-385061.

Structurei

Secondary structure

1
506
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi48 – 514Combined sources
Helixi55 – 639Combined sources
Helixi71 – 8212Combined sources
Beta strandi86 – 894Combined sources
Helixi96 – 10712Combined sources
Beta strandi117 – 1204Combined sources
Helixi124 – 13714Combined sources
Turni138 – 1425Combined sources
Beta strandi145 – 1484Combined sources
Beta strandi150 – 1523Combined sources
Helixi154 – 1607Combined sources
Beta strandi166 – 1705Combined sources
Helixi172 – 1809Combined sources
Beta strandi191 – 1966Combined sources
Helixi197 – 2004Combined sources
Helixi203 – 21311Combined sources
Beta strandi221 – 2277Combined sources
Helixi231 – 24010Combined sources
Beta strandi245 – 2484Combined sources
Beta strandi258 – 2647Combined sources
Helixi267 – 2693Combined sources
Helixi270 – 28011Combined sources
Beta strandi284 – 2896Combined sources
Helixi293 – 30614Combined sources
Beta strandi310 – 3134Combined sources
Helixi319 – 33012Combined sources
Beta strandi333 – 3419Combined sources
Beta strandi343 – 3464Combined sources
Beta strandi352 – 3598Combined sources
Helixi364 – 3718Combined sources
Beta strandi373 – 3753Combined sources
Beta strandi381 – 3877Combined sources
Helixi389 – 3913Combined sources
Helixi392 – 40211Combined sources
Beta strandi406 – 4083Combined sources
Helixi415 – 4173Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S2MX-ray2.10A31-425[»]
4BRUX-ray3.24A46-422[»]
4BRWX-ray2.80A46-422[»]
ProteinModelPortaliP39517.
SMRiP39517. Positions 46-422.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39517.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 247171Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini257 – 417161Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi46 – 7429Q motifAdd
BLAST
Motifi195 – 1984DEAD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi434 – 50572Gln-richAdd
BLAST

Domaini

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00840000129900.
HOGENOMiHOG000268797.
InParanoidiP39517.
KOiK12614.
OMAiGVQVMVT.
OrthoDBiEOG7FNCJ0.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39517-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSINNNFNT NNNSNTDLDR DWKTALNIPK KDTRPQTDDV LNTKGNTFED
60 70 80 90 100
FYLKRELLMG IFEAGFEKPS PIQEEAIPVA ITGRDILARA KNGTGKTAAF
110 120 130 140 150
VIPTLEKVKP KLNKIQALIM VPTRELALQT SQVVRTLGKH CGISCMVTTG
160 170 180 190 200
GTNLRDDILR LNETVHILVG TPGRVLDLAS RKVADLSDCS LFIMDEADKM
210 220 230 240 250
LSRDFKTIIE QILSFLPPTH QSLLFSATFP LTVKEFMVKH LHKPYEINLM
260 270 280 290 300
EELTLKGITQ YYAFVEERQK LHCLNTLFSK LQINQAIIFC NSTNRVELLA
310 320 330 340 350
KKITDLGYSC YYSHARMKQQ ERNKVFHEFR QGKVRTLVCS DLLTRGIDIQ
360 370 380 390 400
AVNVVINFDF PKTAETYLHR IGRSGRFGHL GLAINLINWN DRFNLYKIEQ
410 420 430 440 450
ELGTEIAAIP ATIDKSLYVA ENDETVPVPF PIEQQSYHQQ AIPQQQLPSQ
460 470 480 490 500
QQFAIPPQQH HPQFMVPPSH QQQQAYPPPQ MPSQQGYPPQ QEHFMAMPPG

QSQPQY
Length:506
Mass (Da):57,544
Last modified:February 1, 1995 - v1
Checksum:i062CFA56DF6F2CEE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66057 Genomic DNA. Translation: CAA46853.1.
Z67750 Genomic DNA. Translation: CAA91586.1.
Z74208 Genomic DNA. Translation: CAA98734.1.
BK006938 Genomic DNA. Translation: DAA11700.1.
PIRiS31229.
RefSeqiNP_010121.1. NM_001180220.1.

Genome annotation databases

EnsemblFungiiYDL160C; YDL160C; YDL160C.
GeneIDi851394.
KEGGisce:YDL160C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66057 Genomic DNA. Translation: CAA46853.1.
Z67750 Genomic DNA. Translation: CAA91586.1.
Z74208 Genomic DNA. Translation: CAA98734.1.
BK006938 Genomic DNA. Translation: DAA11700.1.
PIRiS31229.
RefSeqiNP_010121.1. NM_001180220.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S2MX-ray2.10A31-425[»]
4BRUX-ray3.24A46-422[»]
4BRWX-ray2.80A46-422[»]
ProteinModelPortaliP39517.
SMRiP39517. Positions 46-422.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31903. 394 interactions.
DIPiDIP-1243N.
IntActiP39517. 38 interactions.
MINTiMINT-385061.

PTM databases

iPTMnetiP39517.

Proteomic databases

MaxQBiP39517.
PeptideAtlasiP39517.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL160C; YDL160C; YDL160C.
GeneIDi851394.
KEGGisce:YDL160C.

Organism-specific databases

EuPathDBiFungiDB:YDL160C.
SGDiS000002319. DHH1.

Phylogenomic databases

GeneTreeiENSGT00840000129900.
HOGENOMiHOG000268797.
InParanoidiP39517.
KOiK12614.
OMAiGVQVMVT.
OrthoDBiEOG7FNCJ0.

Enzyme and pathway databases

BioCyciYEAST:G3O-29554-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP39517.
NextBioi968552.
PROiP39517.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A yeast gene encoding a putative RNA helicase of the 'DEAD'-box family."
    Strahl-Bolsinger S., Tanner W.
    Yeast 9:429-432(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Dhh1p, a putative RNA helicase, associates with the general transcription factors Pop2p and Ccr4p from Saccharomyces cerevisiae."
    Hata H., Mitsui H., Liu H., Bai Y., Denis C.L., Shimizu Y., Sakai A.
    Genetics 148:571-579(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POP2, ASSOCIATION WITH THE CCR4-NOT COMPLEX.
  5. "The DEAD box helicase, Dhh1p, functions in mRNA decapping and interacts with both the decapping and deadenylase complexes."
    Coller J.M., Tucker M., Sheth U., Valencia-Sanchez M.A., Parker R.
    RNA 7:1717-1727(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DCP1; LSM1; PAT1 AND POP2.
  6. "The DEAD box protein Dhh1 stimulates the decapping enzyme Dcp1."
    Fischer N., Weis K.
    EMBO J. 21:2788-2797(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KEM1 AND PAT1.
  7. "Interaction between Not1p, a component of the Ccr4-not complex, a global regulator of transcription, and Dhh1p, a putative RNA helicase."
    Maillet L., Collart M.A.
    J. Biol. Chem. 277:2835-2842(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDC39.
  8. "Functional conservation of Dhh1p, a cytoplasmic DExD/H-box protein present in large complexes."
    Tseng-Rogenski S.S.-I., Chong J.-L., Thomas C.B., Enomoto S., Berman J., Chang T.-H.
    Nucleic Acids Res. 31:4995-5002(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH LARGE COMPLEXES.
  9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. "Decapping and decay of messenger RNA occur in cytoplasmic processing bodies."
    Sheth U., Parker R.
    Science 300:805-808(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  12. "An essential role for the Saccharomyces cerevisiae DEAD-box helicase DHH1 in G1/S DNA-damage checkpoint recovery."
    Bergkessel M., Reese J.C.
    Genetics 167:21-33(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Processing bodies require RNA for assembly and contain nontranslating mRNAs."
    Teixeira D., Sheth U., Valencia-Sanchez M.A., Brengues M., Parker R.
    RNA 11:371-382(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "The yeast EDC1 mRNA undergoes deadenylation-independent decapping stimulated by Not2p, Not4p, and Not5p."
    Muhlrad D., Parker R.
    EMBO J. 24:1033-1045(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Crystal structure and functional analysis of DEAD-box protein Dhh1p."
    Cheng Z., Coller J.M., Parker R., Song H.
    RNA 11:1258-1270(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 31-425, MUTAGENESIS OF ARG-89; LYS-91; ASP-195; GLU-196; ARG-345; GLY-346; HIS-369 AND ARG-370.
  17. "Initiation of the TORC1-regulated G0 program requires Igo1/2, which license specific mRNAs to evade degradation via the 5'-3' mRNA decay pathway."
    Talarek N., Cameroni E., Jaquenoud M., Luo X., Bontron S., Lippman S., Devgan G., Snyder M., Broach J.R., De Virgilio C.
    Mol. Cell 38:345-355(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGO1.
  18. Cited for: FUNCTION, RNA-BINDING, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiDHH1_YEAST
AccessioniPrimary (citable) accession number: P39517
Secondary accession number(s): D6VRJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 159 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 42900 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.