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Protein

Chitin synthase 2

Gene

CHS2

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

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

Catalytic activityi

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

Enzyme regulationi

Requires proteolytic activation.

GO - Molecular functioni

  • chitin synthase activity Source: SGD

GO - Biological processi

  • actomyosin contractile ring contraction Source: SGD
  • cell wall organization Source: UniProtKB-KW
  • chitin biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17132.
YEAST:YBR038W-MONOMER.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitin synthase 2 (EC:2.4.1.16)
Alternative name(s):
Chitin-UDP acetyl-glucosaminyl transferase 2
Gene namesi
Name:CHS2
Ordered Locus Names:YBR038W
ORF Names:YBR0407
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR038W.
SGDiS000000242. CHS2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 643643ExtracellularSequence analysisAdd
BLAST
Transmembranei644 – 66421HelicalSequence analysisAdd
BLAST
Topological domaini665 – 67713CytoplasmicSequence analysisAdd
BLAST
Transmembranei678 – 69821HelicalSequence analysisAdd
BLAST
Topological domaini699 – 71113ExtracellularSequence analysisAdd
BLAST
Transmembranei712 – 73221HelicalSequence analysisAdd
BLAST
Topological domaini733 – 74311CytoplasmicSequence analysisAdd
BLAST
Transmembranei744 – 76421HelicalSequence analysisAdd
BLAST
Topological domaini765 – 77511ExtracellularSequence analysisAdd
BLAST
Transmembranei776 – 79621HelicalSequence analysisAdd
BLAST
Topological domaini797 – 87579CytoplasmicSequence analysisAdd
BLAST
Transmembranei876 – 89621HelicalSequence analysisAdd
BLAST
Topological domaini897 – 9059ExtracellularSequence analysis
Transmembranei906 – 92621HelicalSequence analysisAdd
BLAST
Topological domaini927 – 96337CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cellular bud neck Source: SGD
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi197 – 1971N → A: 30% decrease of activity. 1 Publication
Mutagenesisi312 – 3121S → A: 20% increase of activity. 1 Publication
Mutagenesisi355 – 3551D → A: 10% decrease of activity. 1 Publication
Mutagenesisi393 – 3931D → A: 5% decrease of activity. 1 Publication
Mutagenesisi441 – 4411D → A: Loss of activity. 1 Publication
Mutagenesisi441 – 4411D → E: Loss of activity. 1 Publication
Mutagenesisi447 – 4471N → A: 80% decrease of activity. 1 Publication
Mutagenesisi490 – 4901Q → A: 70% decrease of activity. 1 Publication
Mutagenesisi492 – 4921F → A: 80% decrease of activity. 1 Publication
Mutagenesisi493 – 4931E → A: 90% decrease of activity. 1 Publication
Mutagenesisi494 – 4941Y → A: 95% decrease of activity. 1 Publication
Mutagenesisi497 – 4971S → A: 95% decrease of activity. 1 Publication
Mutagenesisi502 – 5021K → A: 90% decrease of activity. 1 Publication
Mutagenesisi505 – 5051E → A: 80% decrease of activity. 1 Publication
Mutagenesisi506 – 5061S → A: 20% increase of activity. 1 Publication
Mutagenesisi508 – 5081F → A: 60% decrease of activity. 1 Publication
Mutagenesisi509 – 5091G → A: 70% decrease of activity. 1 Publication
Mutagenesisi514 – 5141L → A: 80% decrease of activity. 1 Publication
Mutagenesisi515 – 5151P → A: 90% decrease of activity. 1 Publication
Mutagenesisi516 – 5161G → A: 95% decrease of activity. 1 Publication
Mutagenesisi521 – 5211Y → A: Loss of activity. 1 Publication
Mutagenesisi522 – 5221R → A: 60% decrease of activity. 1 Publication
Mutagenesisi537 – 5371R → A: No change in activity. 1 Publication
Mutagenesisi550 – 5501H → A: 85% decrease of activity. 1 Publication
Mutagenesisi556 – 5561N → A: 95% decrease of activity. 1 Publication
Mutagenesisi559 – 5591L → A: 95% decrease of activity. 1 Publication
Mutagenesisi561 – 5611E → A: Loss of activity. 1 Publication
Mutagenesisi561 – 5611E → D: 65% decrease of activity. 1 Publication
Mutagenesisi561 – 5611E → Q: Loss of activity. 1 Publication
Mutagenesisi562 – 5621D → A: Loss of activity. 1 Publication
Mutagenesisi562 – 5621D → E: Loss of activity. 1 Publication
Mutagenesisi562 – 5621D → N: Loss of activity. 1 Publication
Mutagenesisi563 – 5631R → A: Loss of activity. 1 Publication
Mutagenesisi563 – 5631R → K: 94% decrease of activity. 1 Publication
Mutagenesisi565 – 5651L → A: 95% decrease of activity. 1 Publication
Mutagenesisi589 – 5891T → A: 70% decrease of activity. 1 Publication
Mutagenesisi592 – 5921P → A: 70% decrease of activity. 1 Publication
Mutagenesisi601 – 6011Q → A: Loss of activity. 1 Publication
Mutagenesisi601 – 6011Q → N: Loss of activity. 1 Publication
Mutagenesisi602 – 6032RR → KK: Loss of activity. 1 Publication
Mutagenesisi602 – 6021R → A: Loss of activity. 1 Publication
Mutagenesisi602 – 6021R → K: 95% decrease of activity. 1 Publication
Mutagenesisi603 – 6031R → A: Loss of activity. 1 Publication
Mutagenesisi603 – 6031R → K: 57% decrease of activity. 1 Publication
Mutagenesisi604 – 6041R → A: Loss of activity. 1 Publication
Mutagenesisi604 – 6041R → K: Loss of activity. 1 Publication
Mutagenesisi605 – 6051W → A: Loss of activity. 1 Publication
Mutagenesisi605 – 6051W → Y: Loss of activity. 1 Publication
Mutagenesisi607 – 6071N → A: 95% decrease of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 963963Chitin synthase 2PRO_0000193728Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi22 – 221N-linked (GlcNAc...)Sequence analysis
Modified residuei40 – 401PhosphoserineCombined sources
Modified residuei82 – 821PhosphoserineCombined sources
Modified residuei86 – 861PhosphoserineCombined sources
Modified residuei100 – 1001PhosphoserineCombined sources
Modified residuei133 – 1331PhosphoserineCombined sources
Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence analysis
Modified residuei217 – 2171PhosphoserineCombined sources
Glycosylationi447 – 4471N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP14180.
PRIDEiP14180.

PTM databases

iPTMnetiP14180.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ISR1Q060981EBI-4624,EBI-38581

Protein-protein interaction databases

BioGridi32739. 48 interactions.
DIPiDIP-3819N.
IntActiP14180. 17 interactions.
MINTiMINT-532106.

Structurei

3D structure databases

ProteinModelPortaliP14180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the chitin synthase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00730000113171.
HOGENOMiHOG000162144.
InParanoidiP14180.
KOiK00698.
OMAiANSESKR.
OrthoDBiEOG7W6WV3.

Family and domain databases

InterProiIPR004835. Chitin_synth.
IPR004834. Chitin_synth_fun.
IPR013616. Chitin_synth_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR22914. PTHR22914. 1 hit.
PfamiPF01644. Chitin_synth_1. 1 hit.
PF08407. Chitin_synth_1N. 1 hit.
[Graphical view]
ProDomiPD002998. Chitin_synth. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53448. SSF53448. 3 hits.

Sequencei

Sequence statusi: Complete.

P14180-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRNPFMVEP SNGSPNRRGA SNLSKFYANA NSNSRWANPS EESLEDSYDQ
60 70 80 90 100
SNVFQGLPAS PSRAALRYSP DRRHRTQFYR DSAHNSPVAP NRYAANLQES
110 120 130 140 150
PKRAGEAVIH LSEGSNLYPR DNADLPVDPY HLSPQQQPSN NLFGSGRLYS
160 170 180 190 200
QSSKYTMSTT STTAPSLAEA DDEKEKYLTS TTSYDDQSTI FSADTFNETK
210 220 230 240 250
FELNHPTRQQ YVRRANSESK RRMVSDLPPP SKKKALLKLD NPIPKGLLDT
260 270 280 290 300
LPRRNSPEFT EMRYTACTVE PDDFLREGYT LRFAEMNREC QIAICITMYN
310 320 330 340 350
EDKYSLARTI HSIMKNVAHL CKREKSHVWG PNGWKKVSVI LISDGRAKVN
360 370 380 390 400
QGSLDYLAAL GVYQEDMAKA SVNGDPVKAH IFELTTQVSI NADLDYVSKD
410 420 430 440 450
IVPVQLVFCL KEENKKKINS HRWLFNAFCP VLQPTVVTLV DVGTRLNNTA
460 470 480 490 500
IYRLWKVFDM DSNVAGAAGQ IKTMKGKWGL KLFNPLVASQ NFEYKISNIL
510 520 530 540 550
DKPLESVFGY ISVLPGALSA YRYRALKNHE DGTGPLRSYF LGETQEGRDH
560 570 580 590 600
DVFTANMYLA EDRILCWELV AKRDAKWVLK YVKEATGETD VPEDVSEFIS
610 620 630 640 650
QRRRWLNGAM FAAIYAQLHF YQIWKTKHSV VRKFFLHVEF LYQFIQMLFS
660 670 680 690 700
WFSIANFVLT FYYLAGSMNL VIKHGEALFI FFKYLIFCDL ASLFIISMGN
710 720 730 740 750
RPQGAKHLFI TSMVILSICA TYSLICGFVF AFKSLASGTE SHKIFVDIVI
760 770 780 790 800
SLLSTYGLYF FSSLMYLDPW HMFTSSIQYF LTLPAFTCTL QIFAFCNTHD
810 820 830 840 850
VSWGTKGSTQ ESKQLSKAIV VQGPDGKQIV ETDWPQEVDK KFLEIKSRLK
860 870 880 890 900
EPEFEESSGN EKQSKNDYYR DIRTRIVMIW MLSNLILIMS IIQVFTPQDT
910 920 930 940 950
DNGYLIFILW SVAALAAFRV VGSMAFLFMK YLRIIVSYRN KVEGSGSWEV
960
SKLDLPNVFH KKG
Length:963
Mass (Da):109,882
Last modified:January 1, 1990 - v1
Checksum:i4D44A287C0B65B5B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23865 Genomic DNA. Translation: AAA34493.1.
Z35907 Genomic DNA. Translation: CAA84980.1.
BK006936 Genomic DNA. Translation: DAA07158.1.
PIRiS45167.
RefSeqiNP_009594.1. NM_001178386.1.

Genome annotation databases

EnsemblFungiiYBR038W; YBR038W; YBR038W.
GeneIDi852326.
KEGGisce:YBR038W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23865 Genomic DNA. Translation: AAA34493.1.
Z35907 Genomic DNA. Translation: CAA84980.1.
BK006936 Genomic DNA. Translation: DAA07158.1.
PIRiS45167.
RefSeqiNP_009594.1. NM_001178386.1.

3D structure databases

ProteinModelPortaliP14180.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32739. 48 interactions.
DIPiDIP-3819N.
IntActiP14180. 17 interactions.
MINTiMINT-532106.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

PTM databases

iPTMnetiP14180.

Proteomic databases

MaxQBiP14180.
PRIDEiP14180.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR038W; YBR038W; YBR038W.
GeneIDi852326.
KEGGisce:YBR038W.

Organism-specific databases

EuPathDBiFungiDB:YBR038W.
SGDiS000000242. CHS2.

Phylogenomic databases

GeneTreeiENSGT00730000113171.
HOGENOMiHOG000162144.
InParanoidiP14180.
KOiK00698.
OMAiANSESKR.
OrthoDBiEOG7W6WV3.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17132.
YEAST:YBR038W-MONOMER.

Miscellaneous databases

PROiP14180.

Family and domain databases

InterProiIPR004835. Chitin_synth.
IPR004834. Chitin_synth_fun.
IPR013616. Chitin_synth_N.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR22914. PTHR22914. 1 hit.
PfamiPF01644. Chitin_synth_1. 1 hit.
PF08407. Chitin_synth_1N. 1 hit.
[Graphical view]
ProDomiPD002998. Chitin_synth. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF53448. SSF53448. 3 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  5. "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.
  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-217, 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-86 AND SER-133, 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-40; SER-82; SER-86; SER-100 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCHS2_YEAST
AccessioniPrimary (citable) accession number: P14180
Secondary accession number(s): D6VQ38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 8, 2016
This is version 156 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.