Cell wall assembly regulator SMI1 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P32566 (SMI1_YEAST)

Last modified November 24, 2009. Version 83. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Cell wall assembly regulator SMI1
Alternative name(s):
Killer toxin-resistance protein 4

Gene names

Name:	SMI1
Synonyms:	KNR4, KTR4
Ordered Locus Names:	YGR229C
ORF Names:	G8553

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Protein involved in the regulation of cell wall assembly and 1,3-beta-glucan synthesis, possibly through the transcriptional regulation of cell wall glucan and chitin synthesis. Ref.2 Ref.6
Subunit structure	Interacts with TYS1. Ref.7
Subcellular location	Nucleus.
Miscellaneous	Present with 5680 molecules/cell in log phase SD medium. Ref.9
Sequence similarities	Belongs to the KNR4/SMI1 family.

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Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall biogenesis Inferred from electronic annotation. Source: InterPro cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW regulation of fungal-type cell wall biogenesis Ref.6 Inferred from genetic interaction. Source: SGD regulation of mitotic cell cycle Ref.7 Inferred from mutant phenotype. Source: SGD regulation of transcription Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cellular bud neck Ref.6 Inferred from direct assay. Source: SGD incipient cellular bud site Ref.6 Inferred from direct assay. Source: SGD mating projection tip Inferred from direct assay. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
CHS5	Q12114	1	EBI-17452,EBI-4640
CIN5	P40917	2	EBI-17452,EBI-4680
CYS4	P32582	1	EBI-17452,EBI-4167
DNF1	P32660	1	EBI-17452,EBI-3121
DRS2	P39524	1	EBI-17452,EBI-3106
FLC2	P39719	1	EBI-17452,EBI-20703
GAP1	P19145	1	EBI-17452,EBI-7314
GGA2	P38817	1	EBI-17452,EBI-7569
GLN1	P32288	1	EBI-17452,EBI-7665
IPP1	P00817	1	EBI-17452,EBI-9338
KEX1	P09620	1	EBI-17452,EBI-9653
MID2	P36027	1	EBI-17452,EBI-10901
PIN2	Q12057	1	EBI-17452,EBI-29838
RNR2	P09938	1	EBI-17452,EBI-15240
SEC26	P41810	1	EBI-17452,EBI-4869
SEC27	P41811	1	EBI-17452,EBI-4898
SEC7	P11075	1	EBI-17452,EBI-16882
TYS1	P36421	3	EBI-17452,EBI-18843
VAS1	P07806-1	1	EBI-17452,EBI-1009942
VMA4	P22203	1	EBI-17452,EBI-20268

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 505

505

Cell wall assembly regulator SMI1

PRO_0000209870

Amino acid modifications

Modified residue

198

Phosphothreonine Ref.13

Modified residue

200

Phosphoserine Ref.13 Ref.8 Ref.11

Modified residue

201

Phosphoserine Ref.11

Modified residue

202

Phosphoserine Ref.13 Ref.10

Modified residue

203

Phosphoserine Ref.13 Ref.8 Ref.11 Ref.10 Ref.12

Modified residue

381

Phosphoserine Ref.13 Ref.10

Modified residue

389

Phosphoserine Ref.13 Ref.12

Modified residue

394

Phosphoserine Ref.13 Ref.10 Ref.12

Modified residue

400

Phosphoserine Ref.13 Ref.10 Ref.12

Modified residue

409

Phosphoserine Ref.12

Modified residue

420

Phosphoserine Ref.13 Ref.12

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Sequences

Sequence

Length

Mass (Da)

Tools

P32566-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: E1A4AE086C5137D7
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FASTA

505

57,079

        10         20         30         40         50         60 
MDLFKRKVKE WVYSLSTDDH YAEYNPDETP TFNMGKRLNS NNGQVNPSQM HLNSVDEEMS 

        70         80         90        100        110        120 
MGFQNGVPSN EDINIDEFTS TESNDGVSET LLAWRHIDFW TSEHNPDLNA TLSDPCTQND 

       130        140        150        160        170        180 
ITHAEEDLEV SFPNPVKASF KIHDGQEDLE SMTGTSGLFY GFQLMTLDQV VAMTQAWRNV 

       190        200        210        220        230        240 
AKNLNKRSQQ GLSHVTSTGS SSSMERLNGN KFKLPNIPDQ KSIPPNAVQP VYAHPAWIPL 

       250        260        270        280        290        300 
ITDNAGNHIG VDLAPGPNGK YAQIITFGRD FDTKFVIAEN WGEFLLSFAN DLEAGNWYLV 

       310        320        330        340        350        360 
DDNDDYFSGD GELVFRDKKS NGPIQDYFEV LKRRTWIKYQ ENLRSQQQKS QPDTSLQEQK 

       370        380        390        400        410        420 
YVPASQKKVA AEQPSTLNAE SIKGEDSGSA DVQSVQDHES VKIVKTEPSE AETTTVNTES 

       430        440        450        460        470        480 
LGQAEHEIKA DNVDIKQESE RKEDEKQPKV EEKEHVENEH VTESAKKDDD VNKQTEEMNK 

       490        500 
KEENEIRSDD AKVEEAREEF ENIAL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast calmodulin and a conserved nuclear protein participate in the in vivo binding of a matrix association region." Fishel B.R., Sperry A.O., Garrard W.T. Proc. Natl. Acad. Sci. U.S.A. 90:5623-5627(1993) [PubMed: 8516310] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 208353 / W303-1A.
[2]	"Cloning and characterization of KNR4, a yeast gene involved in (1,3)-beta-glucan synthesis." Hong Z., Mann P., Brown N.H., Tran L.E., Shaw K.J., Didomenico B.J. Mol. Cell. Biol. 14:1017-1025(1994) [PubMed: 8289782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[3]	"Sequence analysis of the 43 kb CRM1-YLM9-PET54-DIE2-SMI1-PHO81-YHB4-PFK1 region from the right arm of Saccharomyces cerevisiae chromosome VII." van der Aart Q.J.M., Kleine K., Steensma H.Y. Yeast 12:385-390(1996) [PubMed: 8701610] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"KNR4, a suppressor of Saccharomyces cerevisiae cwh mutants, is involved in the transcriptional control of chitin synthase genes." Martin H., Dagkessamanskaia A., Satchanska G., Dallies N., Francois J. Microbiology 145:249-258(1999) [PubMed: 10206705] [Abstract] Cited for: FUNCTION.
[7]	"Interaction of Knr4 protein, a protein involved in cell wall synthesis, with tyrosine tRNA synthetase encoded by TYS1 in Saccharomyces cerevisiae." Dagkessamanskaia A., Martin-Yken H., Basmaji F., Briza P., Francois J. FEMS Microbiol. Lett. 200:53-58(2001) [PubMed: 11410349] [Abstract] Cited for: INTERACTION WITH TYS1.
[8]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed: 11875433] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND SER-203, MASS SPECTROMETRY.
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-203; SER-381; SER-394 AND SER-400, MASS SPECTROMETRY.
[11]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-201 AND SER-203, MASS SPECTROMETRY.
[12]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-389; SER-394; SER-400; SER-409 AND SER-420, MASS SPECTROMETRY.
[13]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198; SER-200; SER-202; SER-203; SER-381; SER-389; SER-394; SER-400 AND SER-420, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	L15423 Genomic DNA. Translation: AAA35053.1. L13164 Genomic DNA. Translation: AAA67469.1. X87941 Genomic DNA. Translation: CAA61178.1. Z73013 Genomic DNA. Translation: CAA97257.1. AY723820 Genomic DNA. Translation: AAU09737.1.
PIR	A55923.
RefSeq	NP_011745.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1635N.
IntAct	P32566. 88 interactions.
STRING	P32566.
Proteomic databases
PeptideAtlas	P32566.
Genome annotation databases
Ensembl	YGR229C; YGR229C; YGR229C; Saccharomyces cerevisiae. [Genome view]
GeneID	853144.
KEGG	sce:YGR229C.
NMPDR	fig\|4932.3.peg.2873.
Organism-specific databases
CYGD	YGR229c.
SGD	S000003461. SMI1.
Phylogenomic databases
HOGENOM	P32566.
OMA	NAVENTE
OrthoDB	EOG9KSR23
Gene expression databases
ArrayExpress	P32566.
Genevestigator	P32566.
GermOnline	YGR229C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR009203. Cell_wall_assmbl/prolif_KNR4. IPR018958. Cell_wall_assmbl_KNR4-like. [Graphical view]
Pfam	PF09346. SMI1_KNR4. 1 hit. [Graphical view]
PIRSF	PIRSF017023. KNR4. 1 hit.
SMART	SM00860. SMI1_KNR4. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	973216.

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Entry information

Entry name

SMI1_YEAST

Accession

Primary (citable) accession number: P32566

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 24, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome VII

Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents