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Protein

Metal resistance protein YCF1

Gene

YCF1

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

Cooperates for the ATP-dependent vacuolar transport of bilirubin and glutathione conjugates.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi663 – 6708ATP 1PROSITE-ProRule annotation
Nucleotide bindingi1306 – 13138ATP 2PROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • bilirubin transmembrane transporter activity Source: SGD
  • glutathione S-conjugate-exporting ATPase activity Source: SGD

GO - Biological processi

  • bilirubin transport Source: SGD
  • cell redox homeostasis Source: SGD
  • glutathione metabolic process Source: SGD
  • response to cadmium ion Source: UniProtKB-KW
  • response to metal ion Source: SGD
  • transmembrane transport Source: SGD
  • vacuole fusion, non-autophagic Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cadmium resistance, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29733-MONOMER.
ReactomeiR-SCE-382556. ABC-family proteins mediated transport.

Protein family/group databases

TCDBi3.A.1.208.11. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Metal resistance protein YCF1
Alternative name(s):
Yeast cadmium factor 1
Gene namesi
Name:YCF1
Ordered Locus Names:YDR135C
ORF Names:YD9302.11C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR135C.
SGDiS000002542. YCF1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3232VacuolarSequence analysisAdd
BLAST
Transmembranei33 – 5321Helical; Name=1PROSITE-ProRule annotationAdd
BLAST
Topological domaini54 – 7320CytoplasmicSequence analysisAdd
BLAST
Transmembranei74 – 9421Helical; Name=2PROSITE-ProRule annotationAdd
BLAST
Topological domaini95 – 995VacuolarSequence analysis
Transmembranei100 – 12021Helical; Name=3PROSITE-ProRule annotationAdd
BLAST
Topological domaini121 – 13010CytoplasmicSequence analysis
Transmembranei131 – 15121Helical; Name=4PROSITE-ProRule annotationAdd
BLAST
Topological domaini152 – 16918VacuolarSequence analysisAdd
BLAST
Transmembranei170 – 19021Helical; Name=5PROSITE-ProRule annotationAdd
BLAST
Topological domaini191 – 27888CytoplasmicSequence analysisAdd
BLAST
Transmembranei279 – 29921Helical; Name=6PROSITE-ProRule annotationAdd
BLAST
Topological domaini300 – 34546VacuolarSequence analysisAdd
BLAST
Transmembranei346 – 36621Helical; Name=7PROSITE-ProRule annotationAdd
BLAST
Topological domaini367 – 42256CytoplasmicSequence analysisAdd
BLAST
Transmembranei423 – 44321Helical; Name=8PROSITE-ProRule annotationAdd
BLAST
Topological domaini444 – 4463VacuolarSequence analysis
Transmembranei447 – 46721Helical; Name=9PROSITE-ProRule annotationAdd
BLAST
Topological domaini468 – 53063CytoplasmicSequence analysisAdd
BLAST
Transmembranei531 – 55121Helical; Name=10PROSITE-ProRule annotationAdd
BLAST
Topological domaini552 – 57221VacuolarSequence analysisAdd
BLAST
Transmembranei573 – 59321Helical; Name=11PROSITE-ProRule annotationAdd
BLAST
Topological domaini594 – 943350CytoplasmicSequence analysisAdd
BLAST
Transmembranei944 – 96421Helical; Name=12PROSITE-ProRule annotationAdd
BLAST
Topological domaini965 – 100137VacuolarSequence analysisAdd
BLAST
Transmembranei1002 – 102322Helical; Name=13PROSITE-ProRule annotationAdd
BLAST
Topological domaini1024 – 106643CytoplasmicSequence analysisAdd
BLAST
Transmembranei1067 – 108721Helical; Name=14PROSITE-ProRule annotationAdd
BLAST
Topological domaini1088 – 10881VacuolarSequence analysis
Transmembranei1089 – 110921Helical; Name=15PROSITE-ProRule annotationAdd
BLAST
Topological domaini1110 – 118071CytoplasmicSequence analysisAdd
BLAST
Transmembranei1181 – 120121Helical; Name=16PROSITE-ProRule annotationAdd
BLAST
Topological domaini1202 – 12054VacuolarSequence analysis
Transmembranei1206 – 122621Helical; Name=17PROSITE-ProRule annotationAdd
BLAST
Topological domaini1227 – 1515289CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • fungal-type vacuole membrane Source: SGD
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi713 – 7131Missing : Loss of function.
Mutagenesisi908 – 9081S → A: Loss of function.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15151515Metal resistance protein YCF1PRO_0000093449Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei251 – 2511PhosphoserineCombined sources
Modified residuei873 – 8731PhosphoserineCombined sources
Modified residuei903 – 9031PhosphoserineCombined sources
Modified residuei908 – 9081PhosphoserineCombined sources
Modified residuei911 – 9111PhosphothreonineCombined sources
Modified residuei914 – 9141PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39109.
PeptideAtlasiP39109.

PTM databases

iPTMnetiP39109.

Interactioni

Protein-protein interaction databases

BioGridi32190. 62 interactions.
DIPiDIP-2612N.
IntActiP39109. 4 interactions.
MINTiMINT-424452.

Structurei

3D structure databases

ProteinModelPortaliP39109.
SMRiP39109. Positions 363-890, 936-1514.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini287 – 590304ABC transmembrane type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini626 – 853228ABC transporter 1PROSITE-ProRule annotationAdd
BLAST
Domaini951 – 1235285ABC transmembrane type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini1272 – 1507236ABC transporter 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 ABC transmembrane type-1 domains.PROSITE-ProRule annotation
Contains 2 ABC transporter domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00840000129727.
InParanoidiP39109.
OMAiVDQTLPH.
OrthoDBiEOG75XGV5.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF90123. SSF90123. 2 hits.
PROSITEiPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39109-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGNLVSWAC KLCRSPEGFG PISFYGDFTQ CFIDGVILNL SAIFMITFGI
60 70 80 90 100
RDLVNLCKKK HSGIKYRRNW IIVSRMALVL LEIAFVSLAS LNISKEEAEN
110 120 130 140 150
FTIVSQYAST MLSLFVALAL HWIEYDRSVV ANTVLLFYWL FETFGNFAKL
160 170 180 190 200
INILIRHTYE GIWYSGQTGF ILTLFQVITC ASILLLEALP KKPLMPHQHI
210 220 230 240 250
HQTLTRRKPN PYDSANIFSR ITFSWMSGLM KTGYEKYLVE ADLYKLPRNF
260 270 280 290 300
SSEELSQKLE KNWENELKQK SNPSLSWAIC RTFGSKMLLA AFFKAIHDVL
310 320 330 340 350
AFTQPQLLRI LIKFVTDYNS ERQDDHSSLQ GFENNHPQKL PIVRGFLIAF
360 370 380 390 400
AMFLVGFTQT SVLHQYFLNV FNTGMYIKSA LTALIYQKSL VLSNEASGLS
410 420 430 440 450
STGDIVNLMS VDVQKLQDLT QWLNLIWSGP FQIIICLYSL YKLLGNSMWV
460 470 480 490 500
GVIILVIMMP LNSFLMRIQK KLQKSQMKYK DERTRVISEI LNNIKSLKLY
510 520 530 540 550
AWEKPYREKL EEVRNNKELK NLTKLGCYMA VTSFQFNIVP FLVSCCTFAV
560 570 580 590 600
FVYTEDRALT TDLVFPALTL FNLLSFPLMI IPMVLNSFIE ASVSIGRLFT
610 620 630 640 650
FFTNEELQPD SVQRLPKVKN IGDVAINIGD DATFLWQRKP EYKVALKNIN
660 670 680 690 700
FQAKKGNLTC IVGKVGSGKT ALLSCMLGDL FRVKGFATVH GSVAYVSQVP
710 720 730 740 750
WIMNGTVKEN ILFGHRYDAE FYEKTIKACA LTIDLAILMD GDKTLVGEKG
760 770 780 790 800
ISLSGGQKAR LSLARAVYAR ADTYLLDDPL AAVDEHVARH LIEHVLGPNG
810 820 830 840 850
LLHTKTKVLA TNKVSALSIA DSIALLDNGE ITQQGTYDEI TKDADSPLWK
860 870 880 890 900
LLNNYGKKNN GKSNEFGDSS ESSVRESSIP VEGELEQLQK LNDLDFGNSD
910 920 930 940 950
AISLRRASDA TLGSIDFGDD ENIAKREHRE QGKVKWNIYL EYAKACNPKS
960 970 980 990 1000
VCVFILFIVI SMFLSVMGNV WLKHWSEVNS RYGSNPNAAR YLAIYFALGI
1010 1020 1030 1040 1050
GSALATLIQT IVLWVFCTIH ASKYLHNLMT NSVLRAPMTF FETTPIGRIL
1060 1070 1080 1090 1100
NRFSNDIYKV DALLGRTFSQ FFVNAVKVTF TITVICATTW QFIFIIIPLS
1110 1120 1130 1140 1150
VFYIYYQQYY LRTSRELRRL DSITRSPIYS HFQETLGGLA TVRGYSQQKR
1160 1170 1180 1190 1200
FSHINQCRID NNMSAFYPSI NANRWLAYRL ELIGSIIILG AATLSVFRLK
1210 1220 1230 1240 1250
QGTLTAGMVG LSLSYALQIT QTLNWIVRMT VEVETNIVSV ERIKEYADLK
1260 1270 1280 1290 1300
SEAPLIVEGH RPPKEWPSQG DIKFNNYSTR YRPELDLVLK HINIHIKPNE
1310 1320 1330 1340 1350
KVGIVGRTGA GKSSLTLALF RMIEASEGNI VIDNIAINEI GLYDLRHKLS
1360 1370 1380 1390 1400
IIPQDSQVFE GTVRENIDPI NQYTDEAIWR ALELSHLKEH VLSMSNDGLD
1410 1420 1430 1440 1450
AQLTEGGGNL SVGQRQLLCL ARAMLVPSKI LVLDEATAAV DVETDKVVQE
1460 1470 1480 1490 1500
TIRTAFKDRT ILTIAHRLNT IMDSDRIIVL DNGKVAEFDS PGQLLSDNKS
1510
LFYSLCMEAG LVNEN
Length:1,515
Mass (Da):171,121
Last modified:May 30, 2000 - v2
Checksum:i30F92FDDBAF60431
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti680 – 6801L → R in AAA50353 (PubMed:7521334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35237 Genomic DNA. Translation: AAA50353.1.
Z48179 Genomic DNA. Translation: CAA88217.1.
BK006938 Genomic DNA. Translation: DAA11979.1.
PIRiS51863.
RefSeqiNP_010419.3. NM_001180442.3.

Genome annotation databases

EnsemblFungiiYDR135C; YDR135C; YDR135C.
GeneIDi851713.
KEGGisce:YDR135C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L35237 Genomic DNA. Translation: AAA50353.1.
Z48179 Genomic DNA. Translation: CAA88217.1.
BK006938 Genomic DNA. Translation: DAA11979.1.
PIRiS51863.
RefSeqiNP_010419.3. NM_001180442.3.

3D structure databases

ProteinModelPortaliP39109.
SMRiP39109. Positions 363-890, 936-1514.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32190. 62 interactions.
DIPiDIP-2612N.
IntActiP39109. 4 interactions.
MINTiMINT-424452.

Protein family/group databases

TCDBi3.A.1.208.11. the atp-binding cassette (abc) superfamily.

PTM databases

iPTMnetiP39109.

Proteomic databases

MaxQBiP39109.
PeptideAtlasiP39109.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR135C; YDR135C; YDR135C.
GeneIDi851713.
KEGGisce:YDR135C.

Organism-specific databases

EuPathDBiFungiDB:YDR135C.
SGDiS000002542. YCF1.

Phylogenomic databases

GeneTreeiENSGT00840000129727.
InParanoidiP39109.
OMAiVDQTLPH.
OrthoDBiEOG75XGV5.

Enzyme and pathway databases

BioCyciYEAST:G3O-29733-MONOMER.
ReactomeiR-SCE-382556. ABC-family proteins mediated transport.

Miscellaneous databases

NextBioi969406.
PROiP39109.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR011527. ABC1_TM_dom.
IPR003439. ABC_transporter-like.
IPR017871. ABC_transporter_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00664. ABC_membrane. 2 hits.
PF00005. ABC_tran. 2 hits.
[Graphical view]
SMARTiSM00382. AAA. 2 hits.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF90123. SSF90123. 2 hits.
PROSITEiPS50929. ABC_TM1F. 2 hits.
PS00211. ABC_TRANSPORTER_1. 2 hits.
PS50893. ABC_TRANSPORTER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A yeast metal resistance protein similar to human cystic fibrosis transmembrane conductance regulator (CFTR) and multidrug resistance-associated protein."
    Szczypka M.S., Wemmie J.A., Moye-Rowley S.W., Thiele D.J.
    J. Biol. Chem. 269:22853-22857(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: H9.
  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. "The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugate pump."
    Li Z.S., Szczypka M., Lu Y.P., Thiele D.J., Rea P.A.
    J. Biol. Chem. 271:6509-6517(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "The products of YCF1 and YLL015w (BPT1) cooperate for the ATP-dependent vacuolar transport of unconjugated bilirubin in Saccharomyces cerevisiae."
    Petrovic S., Pascolo L., Gallo R., Cupelli F., Ostrow J.D., Goffeau A., Tiribelli C., Bruschi C.V.
    Yeast 16:561-571(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  8. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
    Kim H., Melen K., Oesterberg M., von Heijne G.
    Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
    Strain: ATCC 208353 / W303-1A.
  9. "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-903; SER-908 AND THR-911, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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].
  11. "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-903 AND SER-914, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-251; SER-873; SER-903 AND SER-908, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiYCFI_YEAST
AccessioniPrimary (citable) accession number: P39109
Secondary accession number(s): D6VSB9, Q03905
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 30, 2000
Last modified: May 11, 2016
This is version 169 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 396 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.