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Protein

Protein ZRG17

Gene

ZRG17

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. zinc ion transmembrane transporter activity Source: SGD

GO - Biological processi

  1. zinc ion transmembrane transport Source: GOC
  2. zinc ion transport Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-33349-MONOMER.

Protein family/group databases

TCDBi2.A.4.4.1. the cation diffusion facilitator (cdf) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ZRG17
Alternative name(s):
Zinc-regulated gene 17 protein
Gene namesi
Name:ZRG17
Ordered Locus Names:YNR039C
ORF Names:N3403
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XIV

Organism-specific databases

CYGDiYNR039c.
SGDiS000005322. ZRG17.

Subcellular locationi

Endoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 225225CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei226 – 24621HelicalSequence AnalysisAdd
BLAST
Topological domaini247 – 2548LumenalSequence Analysis
Transmembranei255 – 27521HelicalSequence AnalysisAdd
BLAST
Topological domaini276 – 28712CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei288 – 30821HelicalSequence AnalysisAdd
BLAST
Topological domaini309 – 3091LumenalSequence Analysis
Transmembranei310 – 33021HelicalSequence AnalysisAdd
BLAST
Topological domaini331 – 36333CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei364 – 38421HelicalSequence AnalysisAdd
BLAST
Topological domaini385 – 39915LumenalSequence AnalysisAdd
BLAST
Transmembranei400 – 42021HelicalSequence AnalysisAdd
BLAST
Topological domaini421 – 4222CytoplasmicSequence Analysis
Transmembranei423 – 44321HelicalSequence AnalysisAdd
BLAST
Topological domaini444 – 545102LumenalSequence AnalysisAdd
BLAST
Transmembranei546 – 56621HelicalSequence AnalysisAdd
BLAST
Topological domaini567 – 60539CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: SGD
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 605605Protein ZRG17PRO_0000203477Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Phosphoserine1 Publication
Modified residuei131 – 1311Phosphoserine1 Publication
Modified residuei498 – 4981Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53735.
PaxDbiP53735.

Expressioni

Gene expression databases

GenevestigatoriP53735.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MSC2Q034553EBI-28507,EBI-34990

Protein-protein interaction databases

BioGridi35865. 28 interactions.
DIPiDIP-5210N.
IntActiP53735. 5 interactions.
MINTiMINT-493060.
STRINGi4932.YNR039C.

Structurei

3D structure databases

ProteinModelPortaliP53735.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG80215.
HOGENOMiHOG000057080.
InParanoidiP53735.
OMAiHRKGHKY.
OrthoDBiEOG7V1G0C.

Family and domain databases

InterProiIPR002524. Cation_efflux.
[Graphical view]
PANTHERiPTHR11562. PTHR11562. 1 hit.
PfamiPF01545. Cation_efflux. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53735-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METPQMNAIQ EEDNLSPEVA FQTPKLNDSD ASSFSLSNMN AVGNVDGIPS
60 70 80 90 100
QNRTFFASPR PSSLFYSAKE GNNSSSSIIY NPSFTFGENA SSNANINEAA
110 120 130 140 150
LMKGKGNEGR RQSLKYIPAP KLVPPPPRTR SPVRGISPDA GSSKRSSMTL
160 170 180 190 200
DSPFNFTTST LQPHQQTPPS SAASRTSFRK GHRYKHSSVS MNFFQEPEVK
210 220 230 240 250
IPLNIAKSLP IPDFNDLLSN LPWPKAYIQL SIAALQIFAC LITFQVGHLY
260 270 280 290 300
SWSNFITLSH FITYDIIGSL VIIFVENLSQ FQVWFTGTIT FPFGLNRIDV
310 320 330 340 350
LLSFALAVSL CFVGLDLLFH IIEEFIVLFV ESGSSLTNNH DHDEINEQIP
360 370 380 390 400
HSHIANANDS QNENITLWYS ILMINLVLST LSLYKTFYAN KYSNLKTKNP
410 420 430 440 450
IITITYTAYL FIYPLLLDLL SSISDYLATL VISSLILWHG LTIARWTSTV
460 470 480 490 500
LLMGFSTTSL SNSALFNNND STDTTAHTQQ VESKAAKEKP SVRPRSMSSL
510 520 530 540 550
PIATKNTKIR KTGFLNSAGF TENPTTIKNM IKDQIERLSE FKSRYILNYD
560 570 580 590 600
DIVISKVNFT LYVVLIKITM KGGSDDDELM LRLAIDKCIQ TSIPTCETTI

DIDRI
Length:605
Mass (Da):67,461
Last modified:October 1, 1996 - v1
Checksum:i299A89B0E4FCDBC8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391A → V in AAT93124 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71654 Genomic DNA. Translation: CAA96319.1.
AY693105 Genomic DNA. Translation: AAT93124.1.
BK006947 Genomic DNA. Translation: DAA10581.1.
PIRiS63370.
RefSeqiNP_014437.1. NM_001183216.1.

Genome annotation databases

EnsemblFungiiYNR039C; YNR039C; YNR039C.
GeneIDi855775.
KEGGisce:YNR039C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71654 Genomic DNA. Translation: CAA96319.1.
AY693105 Genomic DNA. Translation: AAT93124.1.
BK006947 Genomic DNA. Translation: DAA10581.1.
PIRiS63370.
RefSeqiNP_014437.1. NM_001183216.1.

3D structure databases

ProteinModelPortaliP53735.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35865. 28 interactions.
DIPiDIP-5210N.
IntActiP53735. 5 interactions.
MINTiMINT-493060.
STRINGi4932.YNR039C.

Protein family/group databases

TCDBi2.A.4.4.1. the cation diffusion facilitator (cdf) family.

Proteomic databases

MaxQBiP53735.
PaxDbiP53735.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNR039C; YNR039C; YNR039C.
GeneIDi855775.
KEGGisce:YNR039C.

Organism-specific databases

CYGDiYNR039c.
SGDiS000005322. ZRG17.

Phylogenomic databases

eggNOGiNOG80215.
HOGENOMiHOG000057080.
InParanoidiP53735.
OMAiHRKGHKY.
OrthoDBiEOG7V1G0C.

Enzyme and pathway databases

BioCyciYEAST:G3O-33349-MONOMER.

Miscellaneous databases

NextBioi980235.

Gene expression databases

GenevestigatoriP53735.

Family and domain databases

InterProiIPR002524. Cation_efflux.
[Graphical view]
PANTHERiPTHR11562. PTHR11562. 1 hit.
PfamiPF01545. Cation_efflux. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. "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.
  6. "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-498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "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-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-498, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiZRG17_YEAST
AccessioniPrimary (citable) accession number: P53735
Secondary accession number(s): D6W1L5, E9P919
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 4, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

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 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.