Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Mannosyl phosphorylinositol ceramide synthase SUR1

Gene

SUR1

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

Involved in the synthesis of mannosyl phosphorylinositol ceramide. Catalyzes the addition of mannosyl to phosphorylinositol ceramide. Suppressor of RVS161 mutation.1 Publication

GO - Molecular functioni

  • mannosyltransferase activity Source: SGD
  • transferase activity, transferring glycosyl groups Source: SGD

GO - Biological processi

  • glycosphingolipid biosynthetic process Source: SGD
  • mannosylation Source: GOC
  • mannosyl-inositol phosphorylceramide metabolic process Source: SGD
  • sphingolipid biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-703.
YEAST:MONOMER3O-703.

Protein family/group databases

CAZyiGT32. Glycosyltransferase Family 32.

Names & Taxonomyi

Protein namesi
Recommended name:
Mannosyl phosphorylinositol ceramide synthase SUR1 (EC:2.4.-.-)
Gene namesi
Name:SUR1
Synonyms:BCL21, CSG1, LPE15
Ordered Locus Names:YPL057C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL057C.
SGDiS000005978. SUR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 2721HelicalSequence analysisAdd
BLAST
Topological domaini28 – 269242ExtracellularSequence analysisAdd
BLAST
Transmembranei270 – 29021HelicalSequence analysisAdd
BLAST
Topological domaini291 – 38292CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intracellular Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 382382Mannosyl phosphorylinositol ceramide synthase SUR1PRO_0000072314Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei349 – 3491PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP33300.

PTM databases

iPTMnetiP33300.

Interactioni

Subunit structurei

Heterodimer of SUR1 and CSG2.1 Publication

Protein-protein interaction databases

BioGridi36123. 365 interactions.
DIPiDIP-4557N.
IntActiP33300. 3 interactions.
MINTiMINT-485923.

Structurei

3D structure databases

ProteinModelPortaliP33300.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 32 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000007232.
HOGENOMiHOG000200927.
InParanoidiP33300.
OMAiDDGCERK.
OrthoDBiEOG7D8665.

Family and domain databases

InterProiIPR007577. GlycoTrfase_DXD_sugar-bd_CS.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF04488. Gly_transf_sug. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

P33300-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKELKYLIC FNILLLLSII YYTFDLLTLC IDDTVKDAIL EEDLNPDAPP
60 70 80 90 100
KPQLIPKIIH QTYKTEDIPE HWKEGRQKCL DLHPDYKYIL WTDEMAYEFI
110 120 130 140 150
KEEYPWFLDT FENYKYPIER ADAIRYFILS HYGGVYIDLD DGCERKLDPL
160 170 180 190 200
LAFPAFLRKT SPLGVSNDVM GSVPRHPFFL KALKSLKHYD KYWFIPYMTI
210 220 230 240 250
MGSTGPLFLS VIWKQYKRWR IPKNGTVRIL QPAYYKMHSY SFFSITKGSS
260 270 280 290 300
WHLDDAKLMK ALENHILSCV VTGFIFGFFI LYGEFTFYCW LCSKNFSNLT
310 320 330 340 350
KNWKLNAIKV RFVTILNSLG LRLKLSKSTS DTASATLLAR QQKRLRKDSN
360 370 380
TNIVLLKSSR KSDVYDLEKN DSSKYSLGNN SS
Length:382
Mass (Da):44,808
Last modified:February 1, 1994 - v1
Checksum:i5A9AAB5F9A4069E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96648 Genomic DNA. Translation: AAA68909.1.
D26581 Genomic DNA. Translation: BAA05628.1.
U39205 Genomic DNA. Translation: AAB68308.1.
BK006949 Genomic DNA. Translation: DAA11373.1.
PIRiS41798.
RefSeqiNP_015268.1. NM_001183871.1.

Genome annotation databases

EnsemblFungiiYPL057C; YPL057C; YPL057C.
GeneIDi856050.
KEGGisce:YPL057C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M96648 Genomic DNA. Translation: AAA68909.1.
D26581 Genomic DNA. Translation: BAA05628.1.
U39205 Genomic DNA. Translation: AAB68308.1.
BK006949 Genomic DNA. Translation: DAA11373.1.
PIRiS41798.
RefSeqiNP_015268.1. NM_001183871.1.

3D structure databases

ProteinModelPortaliP33300.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36123. 365 interactions.
DIPiDIP-4557N.
IntActiP33300. 3 interactions.
MINTiMINT-485923.

Protein family/group databases

CAZyiGT32. Glycosyltransferase Family 32.

PTM databases

iPTMnetiP33300.

Proteomic databases

MaxQBiP33300.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL057C; YPL057C; YPL057C.
GeneIDi856050.
KEGGisce:YPL057C.

Organism-specific databases

EuPathDBiFungiDB:YPL057C.
SGDiS000005978. SUR1.

Phylogenomic databases

GeneTreeiENSGT00390000007232.
HOGENOMiHOG000200927.
InParanoidiP33300.
OMAiDDGCERK.
OrthoDBiEOG7D8665.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-703.
YEAST:MONOMER3O-703.

Miscellaneous databases

PROiP33300.

Family and domain databases

InterProiIPR007577. GlycoTrfase_DXD_sugar-bd_CS.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF04488. Gly_transf_sug. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Yeast mutants affected in viability upon starvation have a modified phospholipid composition."
    Desfarges L., Durrens P., Juguelin H., Cassagne C., Bonneu M., Aigle M.
    Yeast 9:267-277(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 44827 / SKQ2N.
  2. "The CLS2 gene encodes a protein with multiple membrane-spanning domains that is important Ca2+ tolerance in yeast."
    Takita Y., Ohya Y., Anraku Y.
    Mol. Gen. Genet. 246:269-281(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26786 / X2180-1A.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Csg1p and newly identified Csh1p function in mannosylinositol phosphorylceramide synthesis by interacting with Csg2p."
    Uemura S., Kihara A., Inokuchi J., Igarashi Y.
    J. Biol. Chem. 278:45049-45055(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  6. "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.
  7. "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-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "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-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSUR1_YEAST
AccessioniPrimary (citable) accession number: P33300
Secondary accession number(s): D6W3V7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: June 8, 2016
This is version 134 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. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: 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.