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P14180 (CHS2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chitin synthase 2
EC=2.4.1.16
Alternative name(s):
Chitin-UDP acetyl-glucosaminyl transferase 2
Gene names
Name:CHS2
Ordered Locus Names:YBR038W
ORF Names:YBR0407
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length963 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for septum formation and cell division. CHS2 is required for maintaining normal cell morphology.

Catalytic activity

UDP-N-acetyl-D-glucosamine + (1,4-(N-acetyl-beta-D-glucosaminyl))(n) = UDP + (1,4-(N-acetyl-beta-D-glucosaminyl))(n+1).

Enzyme regulation

Requires proteolytic activation.

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the chitin synthase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ISR1Q060981EBI-4624,EBI-38581

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 963963Chitin synthase 2
PRO_0000193728

Regions

Topological domain1 – 643643Extracellular Potential
Transmembrane644 – 66421Helical; Potential
Topological domain665 – 67713Cytoplasmic Potential
Transmembrane678 – 69821Helical; Potential
Topological domain699 – 71113Extracellular Potential
Transmembrane712 – 73221Helical; Potential
Topological domain733 – 74311Cytoplasmic Potential
Transmembrane744 – 76421Helical; Potential
Topological domain765 – 77511Extracellular Potential
Transmembrane776 – 79621Helical; Potential
Topological domain797 – 87579Cytoplasmic Potential
Transmembrane876 – 89621Helical; Potential
Topological domain897 – 9059Extracellular Potential
Transmembrane906 – 92621Helical; Potential
Topological domain927 – 96337Cytoplasmic Potential

Amino acid modifications

Modified residue111Phosphoserine Ref.9
Modified residue141Phosphoserine Ref.7
Modified residue691Phosphoserine Ref.8
Modified residue821Phosphoserine Ref.5 Ref.8 Ref.9
Modified residue861Phosphoserine Ref.5 Ref.8 Ref.9
Modified residue1001Phosphoserine Ref.8
Modified residue1331Phosphoserine Ref.8 Ref.9
Modified residue2171Phosphoserine Ref.7
Glycosylation221N-linked (GlcNAc...) Potential
Glycosylation1971N-linked (GlcNAc...) Potential
Glycosylation4471N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis1971N → A: 30% decrease of activity.
Mutagenesis3121S → A: 20% increase of activity.
Mutagenesis3551D → A: 10% decrease of activity.
Mutagenesis3931D → A: 5% decrease of activity.
Mutagenesis4411D → A: Loss of activity.
Mutagenesis4411D → E: Loss of activity.
Mutagenesis4471N → A: 80% decrease of activity.
Mutagenesis4901Q → A: 70% decrease of activity.
Mutagenesis4921F → A: 80% decrease of activity.
Mutagenesis4931E → A: 90% decrease of activity.
Mutagenesis4941Y → A: 95% decrease of activity.
Mutagenesis4971S → A: 95% decrease of activity.
Mutagenesis5021K → A: 90% decrease of activity.
Mutagenesis5051E → A: 80% decrease of activity.
Mutagenesis5061S → A: 20% increase of activity.
Mutagenesis5081F → A: 60% decrease of activity.
Mutagenesis5091G → A: 70% decrease of activity.
Mutagenesis5141L → A: 80% decrease of activity.
Mutagenesis5151P → A: 90% decrease of activity.
Mutagenesis5161G → A: 95% decrease of activity.
Mutagenesis5211Y → A: Loss of activity.
Mutagenesis5221R → A: 60% decrease of activity.
Mutagenesis5371R → A: No change in activity.
Mutagenesis5501H → A: 85% decrease of activity.
Mutagenesis5561N → A: 95% decrease of activity.
Mutagenesis5591L → A: 95% decrease of activity.
Mutagenesis5611E → A: Loss of activity.
Mutagenesis5611E → D: 65% decrease of activity.
Mutagenesis5611E → Q: Loss of activity.
Mutagenesis5621D → A: Loss of activity.
Mutagenesis5621D → E: Loss of activity.
Mutagenesis5621D → N: Loss of activity.
Mutagenesis5631R → A: Loss of activity.
Mutagenesis5631R → K: 94% decrease of activity.
Mutagenesis5651L → A: 95% decrease of activity.
Mutagenesis5891T → A: 70% decrease of activity.
Mutagenesis5921P → A: 70% decrease of activity.
Mutagenesis6011Q → A: Loss of activity.
Mutagenesis6011Q → N: Loss of activity.
Mutagenesis602 – 6032RR → KK: Loss of activity.
Mutagenesis6021R → A: Loss of activity.
Mutagenesis6021R → K: 95% decrease of activity.
Mutagenesis6031R → A: Loss of activity.
Mutagenesis6031R → K: 57% decrease of activity.
Mutagenesis6041R → A: Loss of activity.
Mutagenesis6041R → K: Loss of activity.
Mutagenesis6051W → A: Loss of activity.
Mutagenesis6051W → Y: Loss of activity.
Mutagenesis6071N → A: 95% decrease of activity.

Sequences

Sequence LengthMass (Da)Tools
P14180 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 4D44A287C0B65B5B

FASTA963109,882
        10         20         30         40         50         60 
MTRNPFMVEP SNGSPNRRGA SNLSKFYANA NSNSRWANPS EESLEDSYDQ SNVFQGLPAS 

        70         80         90        100        110        120 
PSRAALRYSP DRRHRTQFYR DSAHNSPVAP NRYAANLQES PKRAGEAVIH LSEGSNLYPR 

       130        140        150        160        170        180 
DNADLPVDPY HLSPQQQPSN NLFGSGRLYS QSSKYTMSTT STTAPSLAEA DDEKEKYLTS 

       190        200        210        220        230        240 
TTSYDDQSTI FSADTFNETK FELNHPTRQQ YVRRANSESK RRMVSDLPPP SKKKALLKLD 

       250        260        270        280        290        300 
NPIPKGLLDT LPRRNSPEFT EMRYTACTVE PDDFLREGYT LRFAEMNREC QIAICITMYN 

       310        320        330        340        350        360 
EDKYSLARTI HSIMKNVAHL CKREKSHVWG PNGWKKVSVI LISDGRAKVN QGSLDYLAAL 

       370        380        390        400        410        420 
GVYQEDMAKA SVNGDPVKAH IFELTTQVSI NADLDYVSKD IVPVQLVFCL KEENKKKINS 

       430        440        450        460        470        480 
HRWLFNAFCP VLQPTVVTLV DVGTRLNNTA IYRLWKVFDM DSNVAGAAGQ IKTMKGKWGL 

       490        500        510        520        530        540 
KLFNPLVASQ NFEYKISNIL DKPLESVFGY ISVLPGALSA YRYRALKNHE DGTGPLRSYF 

       550        560        570        580        590        600 
LGETQEGRDH DVFTANMYLA EDRILCWELV AKRDAKWVLK YVKEATGETD VPEDVSEFIS 

       610        620        630        640        650        660 
QRRRWLNGAM FAAIYAQLHF YQIWKTKHSV VRKFFLHVEF LYQFIQMLFS WFSIANFVLT 

       670        680        690        700        710        720 
FYYLAGSMNL VIKHGEALFI FFKYLIFCDL ASLFIISMGN RPQGAKHLFI TSMVILSICA 

       730        740        750        760        770        780 
TYSLICGFVF AFKSLASGTE SHKIFVDIVI SLLSTYGLYF FSSLMYLDPW HMFTSSIQYF 

       790        800        810        820        830        840 
LTLPAFTCTL QIFAFCNTHD VSWGTKGSTQ ESKQLSKAIV VQGPDGKQIV ETDWPQEVDK 

       850        860        870        880        890        900 
KFLEIKSRLK EPEFEESSGN EKQSKNDYYR DIRTRIVMIW MLSNLILIMS IIQVFTPQDT 

       910        920        930        940        950        960 
DNGYLIFILW SVAALAAFRV VGSMAFLFMK YLRIIVSYRN KVEGSGSWEV SKLDLPNVFH 


KKG

« Hide

References

« Hide 'large scale' references
[1]"Similar and different domains of chitin synthases 1 and 2 of S. cerevisiae: two isozymes with distinct functions."
Silverman S.J.
Yeast 5:459-467(1989) [PubMed: 2533436] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed: 7813418] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Characterization of chitin synthase 2 of Saccharomyces cerevisiae. Implication of two highly conserved domains as possible catalytic sites."
Nagahashi S., Sudoh M., Ono N., Sawada R., Yamaguchi E., Uchida Y., Mio T., Takagi M., Arisawa M., Yamada-Okabe H.
J. Biol. Chem. 270:13961-13967(1995) [PubMed: 7775457] [Abstract]
Cited for: MUTAGENESIS.
[5]"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-82 AND SER-86, MASS SPECTROMETRY.
Strain: 2124.
[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: 16847258] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
[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: 17287358] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-217, MASS SPECTROMETRY.
[8]"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-69; SER-82; SER-86; SER-100 AND SER-133, MASS SPECTROMETRY.
[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: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-82; SER-86 AND SER-133, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M23865 Genomic DNA. Translation: AAA34493.1.
Z35907 Genomic DNA. Translation: CAA84980.1.
BK006936 Genomic DNA. Translation: DAA07158.1.
PIRS45167.
RefSeqNP_009594.1. NM_001178386.1.

3D structure databases

ProteinModelPortalP14180.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-3819N.
IntActP14180. 17 interactions.
MINTMINT-532106.
STRINGP14180.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR038W; YBR038W; YBR038W.
GeneID852326.
KEGGsce:YBR038W.
NMPDRfig|4932.3.peg.289.

Organism-specific databases

CYGDYBR038w.
SGDS000000242. CHS2.

Phylogenomic databases

eggNOGfuNOG04531.
GeneTreeEFGT00050000001909.
HOGENOMHBG327157.
OMAWLFNAFC.
OrthoDBEOG4WHCTW.

Gene expression databases

ArrayExpressP14180.
GenevestigatorP14180.
GermOnlineYBR038W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR004834. Chitin_synth.
IPR013616. Chitin_synth_N.
[Graphical view]
KOK00698.
PfamPF01644. Chitin_synth_1. 1 hit.
PF08407. Chitin_synth_1N. 1 hit.
[Graphical view]
ProDomPD002998. Chitin_synth. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other

NextBio971032.

Entry information

Entry nameCHS2_YEAST
AccessionPrimary (citable) accession number: P14180
Secondary accession number(s): D6VQ38
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: December 14, 2011
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome II

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents