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Protein

Coronin-like protein

Gene

CRN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • actin filament binding Source: SGD
  • microtubule binding Source: SGD
  • protein binding, bridging Source: SGD

GO - Biological processi

  • actin cortical patch localization Source: SGD
  • actin filament organization Source: SGD
  • microtubule-based process Source: SGD
  • negative regulation of Arp2/3 complex-mediated actin nucleation Source: SGD
  • positive regulation of Arp2/3 complex-mediated actin nucleation Source: SGD
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32488-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Coronin-like protein
Gene namesi
Name:CRN1
Ordered Locus Names:YLR429W
ORF Names:L9576.2
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR429W.
SGDiS000004421. CRN1.

Subcellular locationi

GO - Cellular componenti

  • actin cortical patch Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Coronin-like proteinPRO_0000050940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei441 – 4411PhosphoserineCombined sources
Modified residuei454 – 4541PhosphoserineCombined sources
Modified residuei456 – 4561PhosphoserineCombined sources
Modified residuei517 – 5171PhosphothreonineCombined sources
Modified residuei529 – 5291PhosphothreonineCombined sources
Modified residuei573 – 5731PhosphoserineCombined sources
Modified residuei579 – 5791PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ06440.
PeptideAtlasiQ06440.

PTM databases

iPTMnetiQ06440.

Interactioni

Subunit structurei

Binds to F-actin.By similarity

GO - Molecular functioni

  • actin filament binding Source: SGD
  • microtubule binding Source: SGD
  • protein binding, bridging Source: SGD

Protein-protein interaction databases

BioGridi31688. 123 interactions.
DIPiDIP-2722N.
IntActiQ06440. 16 interactions.
MINTiMINT-405323.

Structurei

3D structure databases

ProteinModelPortaliQ06440.
SMRiQ06440. Positions 9-401.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati79 – 11032WD 1Add
BLAST
Repeati138 – 16932WD 2Add
BLAST
Repeati180 – 21031WD 3Add
BLAST
Repeati226 – 25732WD 4Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili618 – 65033Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the WD repeat coronin family.Curated
Contains 4 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

GeneTreeiENSGT00760000119195.
HOGENOMiHOG000166356.
InParanoidiQ06440.
KOiK13886.
OMAiSMEALYE.
OrthoDBiEOG7VX94P.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015505. Coronin.
IPR015048. DUF1899.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR10856. PTHR10856. 2 hits.
PfamiPF08953. DUF1899. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM01166. DUF1899. 1 hit.
SM00320. WD40. 4 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q06440-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGKFVRASK YRHVFGQAAK KELQYEKLKV TNNAWDSNLL KTNGKFIAVN
60 70 80 90 100
WNASGGGAFA VIPIEEVGKA PDQVPLFRGH TAQVLDTDFD PFNDHRIASG
110 120 130 140 150
SDDSKIGIWD IPENYKFHDH VDEDGEPIDI KPVKFLTGHA RKVGHVLYHP
160 170 180 190 200
VAENVLASSS GDYTVKLWNV ETGKDMITLK HPDMVTSMSF SYDGNYLATV
210 220 230 240 250
ARDKKLRVWN IREEKIVSEG PAHTGAKNQR VVWLGNSDRL ATTGFSKLSD
260 270 280 290 300
RQIGIWDAFN IEKGDLGGFY TVDQSSGILM PFYDEGNKIL YLVGKGDGNI
310 320 330 340 350
RYYEFQNDEL FELSEFQSTE AQRGFAVAPK RMVNVKENEV LKGFKTVVDQ
360 370 380 390 400
RIEPVSFFVP RRSEEFQEDI YPDAPSNKPA LTAEEWFSGK SVEGPILVSM
410 420 430 440 450
RSIYDGSAPS FHEAKRPQQP TTQETALEEK KEQPKVEKPI SESEKEVKQE
460 470 480 490 500
APKSPSPLKS ASSSSTINHV LKEDNSINKL LKKSSDIDQV NNAEDPSRDT
510 520 530 540 550
SGWEEADDEP APIKIETPVT PTETKKDRTP KVEPSKELKP EPVSIATDRK
560 570 580 590 600
QEQSLPQEEK SSEKTKSPEQ EKSATPPSSI TAAKTAITAS SKEEPSAART
610 620 630 640 650
SPKSLGLKKS VEKLSTLVLQ LEDVVDKLTK ANLDKDERLL KLEQKIGELS

K
Length:651
Mass (Da):72,553
Last modified:November 1, 1996 - v1
Checksum:iE4A3AC8CF5112001
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20939 Genomic DNA. Translation: AAB67503.1.
AY693023 Genomic DNA. Translation: AAT93042.1.
BK006945 Genomic DNA. Translation: DAA09730.1.
PIRiS53415.
RefSeqiNP_013533.1. NM_001182317.1.

Genome annotation databases

EnsemblFungiiYLR429W; YLR429W; YLR429W.
GeneIDi851148.
KEGGisce:YLR429W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20939 Genomic DNA. Translation: AAB67503.1.
AY693023 Genomic DNA. Translation: AAT93042.1.
BK006945 Genomic DNA. Translation: DAA09730.1.
PIRiS53415.
RefSeqiNP_013533.1. NM_001182317.1.

3D structure databases

ProteinModelPortaliQ06440.
SMRiQ06440. Positions 9-401.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31688. 123 interactions.
DIPiDIP-2722N.
IntActiQ06440. 16 interactions.
MINTiMINT-405323.

PTM databases

iPTMnetiQ06440.

Proteomic databases

MaxQBiQ06440.
PeptideAtlasiQ06440.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR429W; YLR429W; YLR429W.
GeneIDi851148.
KEGGisce:YLR429W.

Organism-specific databases

EuPathDBiFungiDB:YLR429W.
SGDiS000004421. CRN1.

Phylogenomic databases

GeneTreeiENSGT00760000119195.
HOGENOMiHOG000166356.
InParanoidiQ06440.
KOiK13886.
OMAiSMEALYE.
OrthoDBiEOG7VX94P.

Enzyme and pathway databases

BioCyciYEAST:G3O-32488-MONOMER.

Miscellaneous databases

PROiQ06440.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015505. Coronin.
IPR015048. DUF1899.
IPR020472. G-protein_beta_WD-40_rep.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR10856. PTHR10856. 2 hits.
PfamiPF08953. DUF1899. 1 hit.
PF00400. WD40. 3 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM01166. DUF1899. 1 hit.
SM00320. WD40. 4 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(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: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "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 THR-517, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "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-441; SER-454 AND THR-529, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-454 AND SER-456, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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-454; SER-456; THR-517; SER-573 AND SER-579, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCORO_YEAST
AccessioniPrimary (citable) accession number: Q06440
Secondary accession number(s): D6VZ64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2900 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.