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Protein

Chitin synthase 1

Gene

CHS1

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

Septum formation and repair, especially under certain adverse conditions.

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

  • cell separation after cytokinesis Source: SGD
  • cell wall organization Source: UniProtKB-KW
  • chitin biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciYEAST:YNL192W-MONOMER.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Names & Taxonomyi

Protein namesi
Recommended name:
Chitin synthase 1 (EC:2.4.1.16)
Alternative name(s):
Chitin-UDP acetyl-glucosaminyl transferase 1
Gene namesi
Name:CHS1
Ordered Locus Names:YNL192W
ORF Names:N1404
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL192W.
SGDiS000005136. CHS1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei795 – 81521HelicalSequence analysisAdd
BLAST
Transmembranei833 – 85321HelicalSequence analysisAdd
BLAST
Transmembranei866 – 88621HelicalSequence analysisAdd
BLAST
Transmembranei914 – 93421HelicalSequence analysisAdd
BLAST
Transmembranei942 – 96221HelicalSequence analysisAdd
BLAST
Transmembranei1042 – 106221HelicalSequence analysisAdd
BLAST
Transmembranei1101 – 112121HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

  • chitosome Source: SGD
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3827.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11311131Chitin synthase 1PRO_0000193727Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341PhosphoserineCombined sources
Modified residuei35 – 351PhosphoserineCombined sources
Modified residuei270 – 2701PhosphoserineCombined sources
Modified residuei299 – 2991PhosphoserineCombined sources
Modified residuei318 – 3181PhosphoserineCombined sources
Modified residuei328 – 3281PhosphothreonineCombined sources
Modified residuei358 – 3581PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP08004.
PeptideAtlasiP08004.

PTM databases

iPTMnetiP08004.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CAN1P048171EBI-4618,EBI-3993
COX20Q049351EBI-4618,EBI-36910
GAP1P191451EBI-4618,EBI-7314
PMP2P409751EBI-4618,EBI-2043041
PMP3P872841EBI-4618,EBI-13555

Protein-protein interaction databases

BioGridi35641. 122 interactions.
DIPiDIP-4680N.
IntActiP08004. 7 interactions.
MINTiMINT-557753.

Structurei

3D structure databases

ProteinModelPortaliP08004.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the chitin synthase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00730000113171.
HOGENOMiHOG000162144.
InParanoidiP08004.
KOiK00698.
OMAiCGEIRTD.
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. 1 hit.

Sequencei

Sequence statusi: Complete.

P08004-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDQNNRSRN EYHSNRKNEP SYELQNAHSG LFHSSNEELT NRNQRYTNQN
60 70 80 90 100
ASMGSFTPVQ SLQFPEQSQQ TNMLYNGDDG NNNTINDNER DIYGGFVNHH
110 120 130 140 150
RQRPPPATAE YNDVFNTNSQ QLPSEHQYNN VPSYPLPSIN VIQTTPELIH
160 170 180 190 200
NGSQTMATPI ERPFFNENDY YYNNRNSRTS PSIASSSDGY ADQEARPILE
210 220 230 240 250
QPNNNMNSGN IPQYHDQPFG YNNGYHGLQA KDYYDDPEGG YIDQRGDDYQ
260 270 280 290 300
INSYLGRNGE MVDPYDYENS LRHMTPMERR EYLHDDSRPV NDGKEELDSV
310 320 330 340 350
KSGYSHRDLG EYDKDDFSRD DEYDDLNTID KLQFQANGVP ASSSVSSIGS
360 370 380 390 400
KESDIIVSND NLTANRALKR SGTEIRKFKL WNGNFVFDSP ISKTLLDQYA
410 420 430 440 450
TTTENANTLP NEFKFMRYQA VTCEPNQLAE KNFTVRQLKY LTPRETELML
460 470 480 490 500
VVTMYNEDHI LLGRTLKGIM DNVKYMVKKK NSSTWGPDAW KKIVVCIISD
510 520 530 540 550
GRSKINERSL ALLSSLGCYQ DGFAKDEINE KKVAMHVYEH TTMINITNIS
560 570 580 590 600
ESEVSLECNQ GTVPIQLLFC LKEQNQKKIN SHRWAFEGFA ELLRPNIVTL
610 620 630 640 650
LDAGTMPGKD SIYQLWREFR NPNVGGACGE IRTDLGKRFV KLLNPLVASQ
660 670 680 690 700
NFEYKMSNIL DKTTESNFGF ITVLPGAFSA YRFEAVRGQP LQKYFYGEIM
710 720 730 740 750
ENEGFHFFSS NMYLAEDRIL CFEVVTKKNC NWILKYCRSS YASTDVPERV
760 770 780 790 800
PEFILQRRRW LNGSFFASVY SFCHFYRVWS SGHNIGRKLL LTVEFFYLFF
810 820 830 840 850
NTLISWFSLS SFFLVFRILT VSIALAYHSA FNVLSVIFLW LYGICTLSTF
860 870 880 890 900
ILSLGNKPKS TEKFYVLTCV IFAVMMIYMI FCSIFMSVKS FQNILKNDTI
910 920 930 940 950
SFEGLITTEA FRDIVISLGS TYCLYLISSI IYLQPWHMLT SFIQYILLSP
960 970 980 990 1000
SYINVLNIYA FCNVHDLSWG TKGAMANPLG KINTTEDGTF KMEVLVSSSE
1010 1020 1030 1040 1050
IQANYDKYLK VLNDFDPKSE SRPTEPSYDE KKTGYYANVR SLVIIFWVIT
1060 1070 1080 1090 1100
NFIIVAVVLE TGGIADYIAM KSISTDDTLE TAKKAEIPLM TSKASIYFNV
1110 1120 1130
ILWLVALSAL IRFIGCSIYM IVRFFKKVTF R
Length:1,131
Mass (Da):129,871
Last modified:September 21, 2011 - v2
Checksum:iC1856F3C0C857E07
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti815 – 8151V → F in AAA34491 (PubMed:2941152).Curated
Sequence conflicti815 – 8151V → F in CAA96086 (PubMed:9169873).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14045 Genomic DNA. Translation: AAA34491.1.
Z71468 Genomic DNA. Translation: CAA96086.1.
BK006947 Genomic DNA. Translation: DAA10361.2.
PIRiA23944.
RefSeqiNP_014207.2. NM_001183030.2.

Genome annotation databases

EnsemblFungiiYNL192W; YNL192W; YNL192W.
GeneIDi855529.
KEGGisce:YNL192W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14045 Genomic DNA. Translation: AAA34491.1.
Z71468 Genomic DNA. Translation: CAA96086.1.
BK006947 Genomic DNA. Translation: DAA10361.2.
PIRiA23944.
RefSeqiNP_014207.2. NM_001183030.2.

3D structure databases

ProteinModelPortaliP08004.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35641. 122 interactions.
DIPiDIP-4680N.
IntActiP08004. 7 interactions.
MINTiMINT-557753.

Chemistry

ChEMBLiCHEMBL3827.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

PTM databases

iPTMnetiP08004.

Proteomic databases

MaxQBiP08004.
PeptideAtlasiP08004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL192W; YNL192W; YNL192W.
GeneIDi855529.
KEGGisce:YNL192W.

Organism-specific databases

EuPathDBiFungiDB:YNL192W.
SGDiS000005136. CHS1.

Phylogenomic databases

GeneTreeiENSGT00730000113171.
HOGENOMiHOG000162144.
InParanoidiP08004.
KOiK00698.
OMAiCGEIRTD.
OrthoDBiEOG7W6WV3.

Enzyme and pathway databases

BioCyciYEAST:YNL192W-MONOMER.

Miscellaneous databases

NextBioi979574.
PROiP08004.

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. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The S. cerevisiae structural gene for chitin synthase is not required for chitin synthesis in vivo."
    Bulawa C.E., Slater M., Cabib E., Au-Young J., Sburlati A., Adair W.L. Jr., Robbins P.W.
    Cell 46:213-225(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 815.
    Strain: ATCC 204508 / S288c.
  4. "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-34; SER-270; SER-299; SER-318 AND THR-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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-270 AND SER-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-34; SER-35 AND SER-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCHS1_YEAST
AccessioniPrimary (citable) accession number: P08004
Secondary accession number(s): D6W0Z5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: September 21, 2011
Last modified: May 11, 2016
This is version 153 of the entry and version 2 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.