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Protein

Suppressor of yeast profilin deletion

Gene

SYP1

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

Multi-functional protein that contributes to the endocytic process, but also to events that occur at the neck during budding and/or cytokinesis. Plays a role as an endocytic adapters with membrane-tubulation activity that associates with transmembrane cargo proteins and initiates the formation of endocytic sites. Contributes to the stabilization of the nascent clathrin-coated pit. Plays also a role in late endocytosis by mediating vesiculation. Involved in the regulation of cell cycle-dependent dynamics of the septin cytoskeleton by promoting septin turnover in different cell cycle stages. May act through the RHO2 signaling pathway to repolarize cortical actin patches in profilin-deficient cells.4 Publications

GO - Molecular functioni

  • enzyme inhibitor activity Source: SGD
  • identical protein binding Source: IntAct

GO - Biological processi

  • actin cortical patch assembly Source: SGD
  • cell cycle Source: UniProtKB-KW
  • endocytosis Source: UniProtKB-KW
  • negative regulation of catalytic activity Source: SGD
  • septin cytoskeleton organization Source: SGD
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Endocytosis

Enzyme and pathway databases

BioCyciYEAST:G3O-29344-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Suppressor of yeast profilin deletion
Gene namesi
Name:SYP1
Ordered Locus Names:YCR030C
ORF Names:YCR30C/YCR29C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCR030C.
SGDiS000000626. SYP1.

Subcellular locationi

GO - Cellular componenti

  • cellular bud neck Source: UniProtKB
  • cellular bud neck septin ring Source: SGD
  • cellular bud tip Source: UniProtKB
  • endocytic patch Source: SGD
  • mating projection base Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 870870Suppressor of yeast profilin deletionPRO_0000072390Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki256 – 256Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei264 – 2641PhosphoserineCombined sources
Modified residuei331 – 3311PhosphoserineCombined sources
Modified residuei416 – 4161PhosphothreonineCombined sources
Modified residuei496 – 4961PhosphoserineCombined sources
Modified residuei500 – 5001PhosphoserineCombined sources
Modified residuei577 – 5771PhosphothreonineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP25623.

PTM databases

iPTMnetiP25623.

Interactioni

Subunit structurei

Interacts with CDC3, CDC10, CDC11, CDC12, EDE1 and EPS15.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-21900,EBI-21900
EDE1P342167EBI-21900,EBI-21243
MID2P360272EBI-21900,EBI-10901
SLA1P327903EBI-21900,EBI-17313

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi31013. 61 interactions.
DIPiDIP-1758N.
IntActiP25623. 32 interactions.
MINTiMINT-402640.

Structurei

Secondary structure

1
870
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 115Combined sources
Turni12 – 154Combined sources
Helixi18 – 6447Combined sources
Helixi67 – 7711Combined sources
Helixi83 – 886Combined sources
Helixi97 – 12529Combined sources
Helixi127 – 1315Combined sources
Beta strandi133 – 1364Combined sources
Helixi138 – 15922Combined sources
Helixi168 – 23063Combined sources
Helixi233 – 24614Combined sources
Beta strandi611 – 62515Combined sources
Beta strandi628 – 64316Combined sources
Beta strandi646 – 6483Combined sources
Beta strandi654 – 6618Combined sources
Helixi663 – 6653Combined sources
Beta strandi666 – 6716Combined sources
Turni673 – 6753Combined sources
Beta strandi676 – 6805Combined sources
Beta strandi683 – 6864Combined sources
Turni688 – 6914Combined sources
Beta strandi695 – 70511Combined sources
Beta strandi709 – 71810Combined sources
Beta strandi720 – 73112Combined sources
Beta strandi741 – 75313Combined sources
Beta strandi758 – 7669Combined sources
Beta strandi771 – 7733Combined sources
Beta strandi775 – 7795Combined sources
Beta strandi784 – 7874Combined sources
Beta strandi793 – 80311Combined sources
Beta strandi812 – 8187Combined sources
Turni827 – 8304Combined sources
Beta strandi836 – 84510Combined sources
Beta strandi856 – 86914Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G9GX-ray2.40A1-264[»]
3G9HX-ray2.80A566-870[»]
ProteinModelPortaliP25623.
SMRiP25623. Positions 1-250, 609-870.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25623.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini609 – 869261MHDPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi308 – 40598Ser-richAdd
BLAST
Compositional biasi417 – 528112Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the SYP1 family.Curated
Contains 1 MHD (mu homology) domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000057127.
InParanoidiP25623.
KOiK20042.
OMAiQPIFEDE.
OrthoDBiEOG76HQ90.

Family and domain databases

InterProiIPR028565. MHD.
IPR018808. Muniscin_C.
[Graphical view]
PfamiPF10291. muHD. 1 hit.
[Graphical view]
PROSITEiPS51072. MHD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25623-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEQRTKYAD SILTTKSPYE ATETIRIRLS QVKLLNKDFY LLFKELANLK
60 70 80 90 100
RNYAQQLRKI IAENEDITKI LNAQMIESNV LTPQEMSAFR FNSLGELRNV
110 120 130 140 150
WDTVIEELKS DLKSSTEYYN TLDQQVVREL KESVENNTSW RESKDLHSKL
160 170 180 190 200
SKNAASIEHY SKNNENSSHL EEARRQWDQQ SPYLFELFET IDYNRLDTLK
210 220 230 240 250
NCMLRFQTSF SDYLLNTTKE CETVMTKFLA FEPQSEIDRF AKDASQYNFQ
260 270 280 290 300
LSSSSKEVVP NNASPASATG ARPVSVSNGA ANTEREKKSP QKDKRKSAFG
310 320 330 340 350
NIGHRLASAS SSLTHNDLMN NEFSDSTNNS SLKSKKSSHT LRSKVGSIFG
360 370 380 390 400
RNKTKNKRQQ QSSSNSHIQA SITETPNNSS TRVSSTATSS IYQKQRRPTY
410 420 430 440 450
SSSKSNNWTP GEASDTPPLP PHATPKNVDA PVTADTPPAQ TFTPSEVPPS
460 470 480 490 500
TPQQSSPPTA KEPDSSNLPK TVPISISQPP LQPQSKTKPL PVEPASPSIS
510 520 530 540 550
LPTATVDNQP SGQVDSRPLH IRAPALPPSR KQNFIHNRDS QLYDSLPNHG
560 570 580 590 600
SGATPTSSSL SSIPQERPVS TLSSQITGEL RELNPQATGS STSLVGQSLF
610 620 630 640 650
QHSSLDTSQF GLNASIAEVL NASFKDGMLQ NSQLIGEIAL NYLPNSVMNS
660 670 680 690 700
PLPIGINLRI NNGAKFEKVI LNQAFIERVA PEEFKVNPSF IDSRTLGAIK
710 720 730 740 750
YSIKEPIAPI VIHPVWRFES HQASVVLTVK MSPSLPDEIS QIVIEDLVVF
760 770 780 790 800
VNIDGANATS ALSKPQGSFS KEKKRITWRF KEPVVLTRNG EGQRLIARFI
810 820 830 840 850
TDGLAHESAK GVITKFTISE TDNVALPHSG AGSGITLTCQ ELDENNPFGG
860 870
EWLDVNTKRT LTTGNYHGLA
Length:870
Mass (Da):96,137
Last modified:October 24, 2003 - v3
Checksum:i6F35C8F1562E41CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAC42980.1.
BK006937 Genomic DNA. Translation: DAA07509.1.
PIRiS74291.
RefSeqiNP_009959.2. NM_001178744.1.

Genome annotation databases

EnsemblFungiiCAC42980; CAC42980; CAC42980.
YCR030C; YCR030C; YCR030C.
GeneIDi850396.
KEGGisce:YCR030C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAC42980.1.
BK006937 Genomic DNA. Translation: DAA07509.1.
PIRiS74291.
RefSeqiNP_009959.2. NM_001178744.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G9GX-ray2.40A1-264[»]
3G9HX-ray2.80A566-870[»]
ProteinModelPortaliP25623.
SMRiP25623. Positions 1-250, 609-870.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31013. 61 interactions.
DIPiDIP-1758N.
IntActiP25623. 32 interactions.
MINTiMINT-402640.

PTM databases

iPTMnetiP25623.

Proteomic databases

MaxQBiP25623.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAC42980; CAC42980; CAC42980.
YCR030C; YCR030C; YCR030C.
GeneIDi850396.
KEGGisce:YCR030C.

Organism-specific databases

EuPathDBiFungiDB:YCR030C.
SGDiS000000626. SYP1.

Phylogenomic databases

HOGENOMiHOG000057127.
InParanoidiP25623.
KOiK20042.
OMAiQPIFEDE.
OrthoDBiEOG76HQ90.

Enzyme and pathway databases

BioCyciYEAST:G3O-29344-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP25623.
PROiP25623.

Family and domain databases

InterProiIPR028565. MHD.
IPR018808. Muniscin_C.
[Graphical view]
PfamiPF10291. muHD. 1 hit.
[Graphical view]
PROSITEiPS51072. MHD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Gromadka R.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. Valles G., Volckaerts G.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 824 AND 831.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Suppression of the profilin-deficient phenotype by the RHO2 signaling pathway in Saccharomyces cerevisiae."
    Marcoux N., Cloutier S., Zakrzewska E., Charest P.-M., Bourbonnais Y., Pallotta D.
    Genetics 156:579-592(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  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-264; SER-496 AND SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "A novel septin-associated protein, Syp1p, is required for normal cell cycle-dependent septin cytoskeleton dynamics in yeast."
    Qiu W., Neo S.P., Yu X., Cai M.
    Genetics 180:1445-1457(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDC3; CDC10; CDC11 AND CDC12.
  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 THR-577, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Early-arriving Syp1p and Ede1p function in endocytic site placement and formation in budding yeast."
    Stimpson H.E., Toret C.P., Cheng A.T., Pauly B.S., Drubin D.G.
    Mol. Biol. Cell 20:4640-4651(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  11. "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-264; SER-331; THR-416 AND SER-496, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation."
    Reider A., Barker S.L., Mishra S.K., Im Y.J., Maldonado-Baez L., Hurley J.H., Traub L.M., Wendland B.
    EMBO J. 28:3103-3116(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-264 AND 566-870, INTERACTION WITH EDE1, SUBCELLULAR LOCATION, FUNCTION.

Entry informationi

Entry nameiSYP1_YEAST
AccessioniPrimary (citable) accession number: P25623
Secondary accession number(s): D6VR40, P25622, Q96VH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 24, 2003
Last modified: July 6, 2016
This is version 133 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 4280 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: 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.