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Protein

RNA polymerase-associated protein CTR9

Gene

CTR9

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

The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. It regulates 3'-end formation of snR47 by modulating the recruitment or stable association of NRD1 and NAB3 with RNA polymerase II. Also has a role in transcription-coupled histone modification. Required for activation of RAD6 ubiquitin conjugate and the BRE1 ubiquitin ligase which ubiquitinate 'Lys-126' histone H2B. Activates the SET1 histone methyltransferase complex for methylation of 'Lys-4' of histone H3 and for methylation of 'Lys-73' of histone H3 by DOT1 and 'Lys-36' of histone H3 by SET2. In complex with PAF1, required for normal CLN1 and CLN2 G1 cyclin expression in late G1. Also has a role in chromosome segregation where it appears to be involved in microtubule placement.4 Publications

GO - Molecular functioni

  • RNA polymerase II core binding Source: SGD
  • RNA polymerase II C-terminal domain phosphoserine binding Source: SGD
  • transcription factor activity, RNA polymerase II transcription factor binding Source: SGD
  • triplex DNA binding Source: SGD

GO - Biological processi

  • DNA-templated transcription, termination Source: SGD
  • histone modification Source: InterPro
  • mRNA 3'-end processing Source: SGD
  • positive regulation of histone H3-K36 trimethylation Source: SGD
  • positive regulation of phosphorylation of RNA polymerase II C-terminal domain serine 2 residues Source: SGD
  • positive regulation of transcription elongation from RNA polymerase I promoter Source: SGD
  • regulation of chromatin silencing at telomere Source: SGD
  • regulation of histone H2B conserved C-terminal lysine ubiquitination Source: SGD
  • regulation of histone H3-K4 methylation Source: SGD
  • regulation of transcription-coupled nucleotide-excision repair Source: SGD
  • regulation of transcription initiation from RNA polymerase II promoter Source: SGD
  • regulation of transcription involved in G1/S transition of mitotic cell cycle Source: SGD
  • snoRNA 3'-end processing Source: SGD
  • snoRNA transcription from an RNA polymerase II promoter Source: SGD
  • transcription elongation from RNA polymerase II promoter Source: SGD
  • transcription elongation from RNA polymerase I promoter Source: SGD
  • transcription from RNA polymerase I promoter Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33535-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA polymerase-associated protein CTR9
Alternative name(s):
Centromere-binding factor 1-dependent protein 1
Cln three-requiring protein 9
Gene namesi
Name:CTR9
Synonyms:CDP1
Ordered Locus Names:YOL145C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOL145C.
SGDiS000005505. CTR9.

Subcellular locationi

GO - Cellular componenti

  • Cdc73/Paf1 complex Source: SGD
  • nucleus Source: SGD
  • transcriptionally active chromatin Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10771077RNA polymerase-associated protein CTR9PRO_0000106280Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki196 – 196Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei1015 – 10151PhosphoserineCombined sources
Modified residuei1017 – 10171PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP89105.

PTM databases

iPTMnetiP89105.

Interactioni

Subunit structurei

Component of the PAF1 complex which consists of at least CDC73, CTR9, LEO1, PAF1 and RTF1. Interacts with SPT6. Interacts with FACT subunits POB3 and SPT16.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LEO1P384396EBI-5283,EBI-10108
PAF1P383516EBI-5283,EBI-12855
RPO21P040504EBI-5283,EBI-15760
RTF1P5306410EBI-5283,EBI-16303
SLT2Q007722EBI-5283,EBI-17372
SPT5P276922EBI-5283,EBI-17937

GO - Molecular functioni

  • RNA polymerase II core binding Source: SGD
  • RNA polymerase II C-terminal domain phosphoserine binding Source: SGD

Protein-protein interaction databases

BioGridi34272. 175 interactions.
DIPiDIP-2814N.
IntActiP89105. 34 interactions.
MINTiMINT-483774.

Structurei

3D structure databases

ProteinModelPortaliP89105.
SMRiP89105. Positions 58-84, 122-162, 213-261, 343-403, 467-529, 682-759.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati56 – 8934TPR 1Add
BLAST
Repeati138 – 17437TPR 2Add
BLAST
Repeati183 – 21634TPR 3Add
BLAST
Repeati218 – 25134TPR 4Add
BLAST
Repeati298 – 33235TPR 5Add
BLAST
Repeati338 – 37134TPR 6Add
BLAST
Repeati373 – 40533TPR 7Add
BLAST
Repeati421 – 45535TPR 8Add
BLAST
Repeati462 – 49534TPR 9Add
BLAST
Repeati501 – 53434TPR 10Add
BLAST
Repeati540 – 57233TPR 11Add
BLAST
Repeati664 – 69734TPR 12Add
BLAST
Repeati699 – 73133TPR 13Add
BLAST
Repeati732 – 76433TPR 14Add
BLAST
Repeati768 – 80134TPR 15Add
BLAST
Repeati830 – 86334TPR 16Add
BLAST

Sequence similaritiesi

Contains 16 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

GeneTreeiENSGT00390000005097.
HOGENOMiHOG000248464.
InParanoidiP89105.
KOiK15176.
OMAiIIFAESK.
OrthoDBiEOG7H4F2V.

Family and domain databases

Gene3Di1.25.40.10. 5 hits.
InterProiIPR031101. Ctr9.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR14027:SF2. PTHR14027:SF2. 1 hit.
PfamiPF13174. TPR_6. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 8 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 8 hits.
PS50293. TPR_REGION. 6 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P89105-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNAMKVEGY PSMEWPTSLD IPLKASEELV GIDLETDLPD DPTDLKTLLV
60 70 80 90 100
EENSEKEHWL TIALAYCNHG KTNEGIKLIE MALDVFQNSE RASLHTFLTW
110 120 130 140 150
AHLNLAKGQS LSVETKEHEL TQAELNLKDA IGFDPTWIGN MLATVELYYQ
160 170 180 190 200
RGHYDKALET SDLFVKSIHA EDHRSGRQSK PNCLFLLLRA KLLYQKKNYM
210 220 230 240 250
ASLKIFQELL VINPVLQPDP RIGIGLCFWQ LKDSKMAIKS WQRALQLNPK
260 270 280 290 300
NTSASILVLL GEFRESFTNS TNDKTFKEAF TKALSDLNNI FSENQHNPVL
310 320 330 340 350
LTLLQTYYYF KGDYQTVLDI YHHRILKMSP MIAKIVLSES SFWCGRAHYA
360 370 380 390 400
LGDYRKSFIM FQESLKKNED NLLAKLGLGQ TQIKNNLLEE SIITFENLYK
410 420 430 440 450
TNESLQELNY ILGMLYAGKA FDAKTAKNTS AKEQSNLNEK ALKYLERYLK
460 470 480 490 500
LTLATKNQLV ISRAYLVISQ LYELQNQYKT SLDYLSKALE EMEFIKKEIP
510 520 530 540 550
LEVLNNLACY HFINGDFIKA DDLFKQAKAK VSDKDESVNI TLEYNIARTN
560 570 580 590 600
EKNDCEKSES IYSQVTSLHP AYIAARIRNL YLKFAQSKIE DSDMSTEMNK
610 620 630 640 650
LLDLNKSDLE IRSFYGWYLK NSKERKNNEK STTHNKETLV KYNSHDAYAL
660 670 680 690 700
ISLANLYVTI ARDGKKSRNP KEQEKSKHSY LKAIQLYQKV LQVDPFNIFA
710 720 730 740 750
AQGLAIIFAE SKRLGPALEI LRKVRDSLDN EDVQLNLAHC YLEMREYGKA
760 770 780 790 800
IENYELVLKK FDNEKTRPHI LNLLGRAWYA RAIKERSVNF YQKALENAKT
810 820 830 840 850
ALDLFVKESS KSKFIHSVKF NIALLHFQIA ETLRRSNPKF RTVQQIKDSL
860 870 880 890 900
EGLKEGLELF RELNDLKEFN MIPKEELEQR IQLGETTMKS ALERSLNEQE
910 920 930 940 950
EFEKEQSAKI DEARKILEEN ELKEQGWMKQ EEEARRLKLE KQAEEYRKLQ
960 970 980 990 1000
DEAQKLIQER EAMAISEHNV KDDSDLSDKD NEYDEEKPRQ KRKRSTKTKN
1010 1020 1030 1040 1050
SGESKRRKAA KKTLSDSDED DDDVVKKPSH NKGKKSQLSN EFIEDSDEEE
1060 1070
AQMSGSEQNK NDDNDENNDN DDNDGLF
Length:1,077
Mass (Da):124,709
Last modified:September 21, 2011 - v3
Checksum:iF794ECBAD26D4820
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971K → E in CAA88282 (PubMed:8553699).Curated
Sequence conflicti197 – 1971K → E in CAA99166 (PubMed:9169874).Curated
Sequence conflicti461 – 4611I → V in AAB81882 (PubMed:8978028).Curated
Sequence conflicti674 – 6741E → G in CAA88282 (PubMed:8553699).Curated
Sequence conflicti674 – 6741E → G in CAA99166 (PubMed:9169874).Curated
Sequence conflicti786 – 7861R → T in CAA88282 (PubMed:8553699).Curated
Sequence conflicti786 – 7861R → T in CAA99166 (PubMed:9169874).Curated
Sequence conflicti903 – 9031E → K in CAA88282 (PubMed:8553699).Curated
Sequence conflicti903 – 9031E → K in CAA99166 (PubMed:9169874).Curated
Sequence conflicti907 – 9071S → R in CAA88282 (PubMed:8553699).Curated
Sequence conflicti907 – 9071S → R in CAA99166 (PubMed:9169874).Curated
Sequence conflicti926 – 9272GW → ER in AAB38704 (Ref. 1) Curated
Sequence conflicti926 – 9272GW → ER in AAB81882 (PubMed:8978028).Curated
Sequence conflicti956 – 9594LIQE → IFQV in CAA88282 (PubMed:8553699).Curated
Sequence conflicti956 – 9594LIQE → IFQV in CAA99166 (PubMed:9169874).Curated
Sequence conflicti987 – 9871K → Q in CAA88282 (PubMed:8553699).Curated
Sequence conflicti987 – 9871K → Q in CAA99166 (PubMed:9169874).Curated
Sequence conflicti1045 – 107733DSDEE…NDGLF → R in CAA88282 (PubMed:8553699).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U69264 Genomic DNA. Translation: AAB38704.1.
U31217 Genomic DNA. Translation: AAB81882.1.
Z48239 Genomic DNA. Translation: CAA88282.1.
Z74887 Genomic DNA. Translation: CAA99166.1.
BK006948 Genomic DNA. Translation: DAA10640.2.
PIRiS66842.
RefSeqiNP_014496.2. NM_001183399.2.

Genome annotation databases

EnsemblFungiiYOL145C; YOL145C; YOL145C.
GeneIDi854020.
KEGGisce:YOL145C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U69264 Genomic DNA. Translation: AAB38704.1.
U31217 Genomic DNA. Translation: AAB81882.1.
Z48239 Genomic DNA. Translation: CAA88282.1.
Z74887 Genomic DNA. Translation: CAA99166.1.
BK006948 Genomic DNA. Translation: DAA10640.2.
PIRiS66842.
RefSeqiNP_014496.2. NM_001183399.2.

3D structure databases

ProteinModelPortaliP89105.
SMRiP89105. Positions 58-84, 122-162, 213-261, 343-403, 467-529, 682-759.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34272. 175 interactions.
DIPiDIP-2814N.
IntActiP89105. 34 interactions.
MINTiMINT-483774.

PTM databases

iPTMnetiP89105.

Proteomic databases

MaxQBiP89105.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOL145C; YOL145C; YOL145C.
GeneIDi854020.
KEGGisce:YOL145C.

Organism-specific databases

EuPathDBiFungiDB:YOL145C.
SGDiS000005505. CTR9.

Phylogenomic databases

GeneTreeiENSGT00390000005097.
HOGENOMiHOG000248464.
InParanoidiP89105.
KOiK15176.
OMAiIIFAESK.
OrthoDBiEOG7H4F2V.

Enzyme and pathway databases

BioCyciYEAST:G3O-33535-MONOMER.

Miscellaneous databases

PROiP89105.

Family and domain databases

Gene3Di1.25.40.10. 5 hits.
InterProiIPR031101. Ctr9.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERiPTHR14027:SF2. PTHR14027:SF2. 1 hit.
PfamiPF13174. TPR_6. 1 hit.
PF13181. TPR_8. 1 hit.
[Graphical view]
SMARTiSM00028. TPR. 8 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS50005. TPR. 8 hits.
PS50293. TPR_REGION. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CTR9 is required for normal CLN1 and CLN2 G1 cyclin expression."
    Arndt K.T., Round E., Hoeppner D.
    Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "CDP1, a novel Saccharomyces cerevisiae gene required for proper nuclear division and chromosome segregation."
    Foreman P.K., Davis R.W.
    Genetics 144:1387-1397(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN CHROMOSOME SEGREGATION.
    Strain: ATCC 200060 / W303.
  3. "DNA sequence analysis of a 13 kbp fragment of the left arm of yeast chromosome XV containing seven new open reading frames."
    Casamayor A., Aldea M., Casas C., Herrero E., Gamo F.-J., Lafuente M.J., Gancedo C., Arino J.
    Yeast 11:1281-1288(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 197; 674; 768; 903; 907; 956-959 AND 987.
    Strain: ATCC 204508 / S288c.
  6. "A role for Ctr9p and Paf1p in the regulation of G1 cyclin expression in yeast."
    Koch C., Wollmann P., Dahl M., Lottspeich F.
    Nucleic Acids Res. 27:2126-2134(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  7. "The yeast CDP1 gene encodes a triple-helical DNA-binding protein."
    Musso M., Bianchi-Scarra G., Van Dyke M.W.
    Nucleic Acids Res. 28:4090-4096(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  8. "Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex."
    Mueller C.L., Jaehning J.A.
    Mol. Cell. Biol. 22:1971-1980(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PAF1 COMPLEX.
  9. "RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach."
    Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A., Shilatifard A., Buratowski S., Greenblatt J.F.
    Mol. Cell. Biol. 22:6979-6992(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POB3 AND SPT16.
  10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  11. Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-196.
    Strain: SUB592.
  12. "Separation of the Saccharomyces cerevisiae Paf1 complex from RNA polymerase II results in changes in its subnuclear localization."
    Porter S.E., Penheiter K.L., Jaehning J.A.
    Eukaryot. Cell 4:209-220(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "Interaction between transcription elongation factors and mRNA 3'-end formation at the Saccharomyces cerevisiae GAL10-GAL7 locus."
    Kaplan C.D., Holland M.J., Winston F.
    J. Biol. Chem. 280:913-922(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPT6.
  14. "A requirement for the Saccharomyces cerevisiae Paf1 complex in snoRNA 3' end formation."
    Sheldon K.E., Mauger D.M., Arndt K.M.
    Mol. Cell 20:225-236(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "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-1015 AND SER-1017, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  16. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1017, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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 SER-1015 AND SER-1017, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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-1015 AND SER-1017, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCTR9_YEAST
AccessioniPrimary (citable) accession number: P89105
Secondary accession number(s): D6W1S4
, O14409, Q07332, Q08292
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 21, 2011
Last modified: July 6, 2016
This is version 162 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 12900 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.