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Protein

ATP-dependent RNA helicase SUB2

Gene

SUB2

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-binding RNA helicase component of the TREX complex involved in transcription elongation and required for the export of mRNA out of the nucleus. SUB2 plays also a role in pre-mRNA splicing and spliceosome assembly. May be involved in rDNA and telomeric silencing, and maintenance of genome integrity.13 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi106 – 1138ATP

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: SGD
  • RNA binding Source: UniProtKB-KW

GO - Biological processi

  • chromatin silencing at telomere Source: SGD
  • mRNA 3'-end processing Source: SGD
  • mRNA export from nucleus Source: SGD
  • mRNA splicing, via spliceosome Source: SGD
  • RNA secondary structure unwinding Source: GO_Central
  • transcription-coupled nucleotide-excision repair Source: SGD
  • transcription elongation from RNA polymerase II promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29493-MONOMER.

Protein family/group databases

TCDBi3.A.22.1.1. the transcription-coupled trex/tap nuclear mrna export complex (trex) family.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase SUB2 (EC:3.6.4.13)
Alternative name(s):
Suppressor of BRR1 protein 2
Gene namesi
Name:SUB2
Ordered Locus Names:YDL084W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL084W.
SGDiS000002242. SUB2.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: SGD
  • spliceosomal complex Source: SGD
  • transcription export complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81D → G: No growth at 37 degrees Celsius; when associated with DEL-135. 1 Publication
Mutagenesisi22 – 221D → G in SUB2-1; no growth at 16 and 37 degrees Celsius; when associated with G-83; M-142 and T-146. 1 Publication
Mutagenesisi83 – 831E → G in SUB2-1; no growth at 16 and 37 degrees Celsius; when associated with G-22; M-142 and T-146. 1 Publication
Mutagenesisi112 – 1121K → N: Lethal. 1 Publication
Mutagenesisi122 – 1221Q → R in SUB2-201; no growth at 37 degrees Celsius; when associated with G-173 and F-403. 1 Publication
Mutagenesisi135 – 1351Missing : No growth at 37 degrees Celsius; when associated with G-8. 1 Publication
Mutagenesisi142 – 1421L → M in SUB2-1; no growth at 16 and 37 degrees Celsius; when associated with G-22; G-83 and T-146. 1 Publication
Mutagenesisi146 – 1461I → T in SUB2-1; no growth at 16 and 37 degrees Celsius; when associated with G-22; G-83 and M-142. 1 Publication
Mutagenesisi173 – 1731K → G in SUB2-201; no growth at 37 degrees Celsius; when associated with R-122 and F-403. 1 Publication
Mutagenesisi174 – 1741D → G in SUB2-100; no growth at 37 degrees Celsius. 1 Publication
Mutagenesisi215 – 2151D → E: Lethal. 1 Publication
Mutagenesisi217 – 2171C → A: Lethal. 1 Publication
Mutagenesisi247 – 2471S → L: Lethal. 1 Publication
Mutagenesisi308 – 3081Q → R in SUB2-5; no growth at 16 degrees Celsius. 1 Publication
Mutagenesisi403 – 4031K → F in SUB2-201; no growth at 37 degrees Celsius; when associated with R-122 and G-173. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 446445ATP-dependent RNA helicase SUB2PRO_0000055082Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei13 – 131PhosphoserineCombined sources
Modified residuei37 – 371PhosphoserineCombined sources
Modified residuei169 – 1691PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ07478.

PTM databases

iPTMnetiQ07478.

Interactioni

Subunit structurei

Component of the TREX complex composed of at least SUB2, TEX1, YRA1 and the four THO complex components: HPR1, MFT1, THO2 and THP1. Interacts with HPR1, YRA1, and YRA2. SUB2 may mediate the interaction between the THO complex and YRA1. Associates with growing mRNP complexes during transcription. This association requires the presence of HPR1. Interacts also with SAC3.4 Publications

Protein-protein interaction databases

BioGridi31977. 97 interactions.
DIPiDIP-5343N.
IntActiQ07478. 26 interactions.
MINTiMINT-526164.

Structurei

3D structure databases

ProteinModelPortaliQ07478.
SMRiQ07478. Positions 62-444.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini93 – 268176Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini280 – 441162Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi62 – 9029Q motifAdd
BLAST
Motifi215 – 2184DECD box

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

GeneTreeiENSGT00830000128348.
HOGENOMiHOG000268797.
InParanoidiQ07478.
KOiK12812.
OMAiNGAQDKK.
OrthoDBiEOG74J9JF.

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.
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.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q07478-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHEGEEDLL EYSDNEQEIQ IDASKAAEAG ETGAATSATE GDNNNNTAAG
60 70 80 90 100
DKKGSYVGIH STGFKDFLLK PELSRAIIDC GFEHPSEVQQ HTIPQSIHGT
110 120 130 140 150
DVLCQAKSGL GKTAVFVLST LQQLDPVPGE VAVVVICNAR ELAYQIRNEY
160 170 180 190 200
LRFSKYMPDV KTAVFYGGTP ISKDAELLKN KDTAPHIVVA TPGRLKALVR
210 220 230 240 250
EKYIDLSHVK NFVIDECDKV LEELDMRRDV QEIFRATPRD KQVMMFSATL
260 270 280 290 300
SQEIRPICRR FLQNPLEIFV DDEAKLTLHG LQQYYIKLEE REKNRKLAQL
310 320 330 340 350
LDDLEFNQVI IFVKSTTRAN ELTKLLNASN FPAITVHGHM KQEERIARYK
360 370 380 390 400
AFKDFEKRIC VSTDVFGRGI DIERINLAIN YDLTNEADQY LHRVGRAGRF
410 420 430 440
GTKGLAISFV SSKEDEEVLA KIQERFDVKI AEFPEEGIDP STYLNN
Length:446
Mass (Da):50,309
Last modified:November 1, 1996 - v1
Checksum:iAB3605A8C38A560C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74132 Genomic DNA. Translation: CAA98650.1.
AY692907 Genomic DNA. Translation: AAT92926.1.
BK006938 Genomic DNA. Translation: DAA11775.1.
PIRiS67620.
RefSeqiNP_010199.1. NM_001180143.1.

Genome annotation databases

EnsemblFungiiYDL084W; YDL084W; YDL084W.
GeneIDi851475.
KEGGisce:YDL084W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74132 Genomic DNA. Translation: CAA98650.1.
AY692907 Genomic DNA. Translation: AAT92926.1.
BK006938 Genomic DNA. Translation: DAA11775.1.
PIRiS67620.
RefSeqiNP_010199.1. NM_001180143.1.

3D structure databases

ProteinModelPortaliQ07478.
SMRiQ07478. Positions 62-444.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31977. 97 interactions.
DIPiDIP-5343N.
IntActiQ07478. 26 interactions.
MINTiMINT-526164.

Protein family/group databases

TCDBi3.A.22.1.1. the transcription-coupled trex/tap nuclear mrna export complex (trex) family.

PTM databases

iPTMnetiQ07478.

Proteomic databases

MaxQBiQ07478.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL084W; YDL084W; YDL084W.
GeneIDi851475.
KEGGisce:YDL084W.

Organism-specific databases

EuPathDBiFungiDB:YDL084W.
SGDiS000002242. SUB2.

Phylogenomic databases

GeneTreeiENSGT00830000128348.
HOGENOMiHOG000268797.
InParanoidiQ07478.
KOiK12812.
OMAiNGAQDKK.
OrthoDBiEOG74J9JF.

Enzyme and pathway databases

BioCyciYEAST:G3O-29493-MONOMER.

Miscellaneous databases

PROiQ07478.

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.
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.
PROSITEiPS51192. 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. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Systematic identification, classification, and characterization of the open reading frames which encode novel helicase-related proteins in Saccharomyces cerevisiae by gene disruption and Northern analysis."
    Shiratori A., Shibata T., Arisawa M., Hanaoka F., Murakami Y., Eki T.
    Yeast 15:219-253(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "The DECD box putative ATPase Sub2p is an early mRNA export factor."
    Jensen T.H., Boulay J., Rosbash M., Libri D.
    Curr. Biol. 11:1711-1715(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Erratum
    Jensen T.H., Boulay J., Rosbash M., Libri D.
    Curr. Biol. 14:447-447(2004)
  7. "Identification and characterization of yUAP/Sub2p, a yeast homolog of the essential human pre-mRNA splicing factor hUAP56."
    Zhang M., Green M.R.
    Genes Dev. 15:30-35(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-112; ASP-174; ASP-215; CYS-217 AND SER-247.
  8. "Multiple roles for the yeast SUB2/yUAP56 gene in splicing."
    Libri D., Graziani N., Saguez C., Boulay J.
    Genes Dev. 15:36-41(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-8; GLN-122; VAL-135; LYS-173 AND LYS-403.
  9. "Deletion of MUD2, the yeast homolog of U2AF65, can bypass the requirement for sub2, an essential spliceosomal ATPase."
    Kistler A.L., Guthrie C.
    Genes Dev. 15:42-49(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-22; GLU-83; LEU-142; ILE-146 AND GLN-308.
  10. "High-copy-number expression of Sub2p, a member of the RNA helicase superfamily, suppresses hpr1-mediated genomic instability."
    Fan H.-Y., Merker R.J., Klein H.L.
    Mol. Cell. Biol. 21:5459-5470(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Splicing factor Sub2p is required for nuclear mRNA export through its interaction with Yra1p."
    Straesser K., Hurt E.
    Nature 413:648-652(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YRA1.
  12. "The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability."
    Jimeno S., Rondon A.G., Luna R., Aguilera A.
    EMBO J. 21:3526-3535(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores."
    Fischer T., Straesser K., Racz A., Rodriguez-Navarro S., Oppizzi M., Ihrig P., Lechner J., Hurt E.
    EMBO J. 21:5843-5852(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAC3.
  14. "DEAD-box RNA helicase Sub2 is required for expression of lacZ fusions in Saccharomyces cerevisiae and is a dosage-dependent suppressor of RLR1 (THO2)."
    West R.W. Jr., Milgrom E.
    Gene 288:19-27(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Stable mRNP formation and export require cotranscriptional recruitment of the mRNA export factors Yra1p and Sub2p by Hpr1p."
    Zenklusen D., Vinciguerra P., Wyss J.-C., Stutz F.
    Mol. Cell. Biol. 22:8241-8253(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HPR1; YRA1 AND YRA2, ASSOCIATION WITH MRNP COMPLEXES.
  16. Cited for: FUNCTION, IDENTIFICATION IN THE TREX COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "Molecular evidence that the eukaryotic THO/TREX complex is required for efficient transcription elongation."
    Rondon A.G., Jimeno S., Garcia-Rubio M., Aguilera A.
    J. Biol. Chem. 278:39037-39043(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  19. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  20. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  21. "The Saccharomyces cerevisiae Sub2 protein suppresses heterochromatic silencing at telomeres and subtelomeric genes."
    Lahue E., Heckathorn J., Meyer Z., Smith J., Wolfe C.
    Yeast 22:537-551(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  23. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSUB2_YEAST
AccessioniPrimary (citable) accession number: Q07478
Secondary accession number(s): D6VRR5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 163 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 51700 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. 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.