Reviewed, UniProtKB/Swiss-Prot P14180 (CHS2_YEAST)

Names and origin

Protein names

Recommended 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

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	963 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Membrane
Domain	Transmembrane
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW chitin biosynthetic process Inferred from electronic annotation. Source: InterPro contractile ring contraction involved in cytokinesis during cell cycle Inferred from direct assay. Source: SGD
Cellular component	cellular bud neck Inferred from direct assay. Source: SGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chitin synthase activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ISR1	Q06098	1	EBI-4624,EBI-38581

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 963	963	Chitin synthase 2		PRO_0000193728
Regions
	Topological domain	1 – 643	643	Extracellular Potential
	Transmembrane	644 – 664	21	Potential
	Topological domain	665 – 677	13	Cytoplasmic Potential
	Transmembrane	678 – 698	21	Potential
	Topological domain	699 – 711	13	Extracellular Potential
	Transmembrane	712 – 732	21	Potential
	Topological domain	733 – 743	11	Cytoplasmic Potential
	Transmembrane	744 – 764	21	Potential
	Topological domain	765 – 775	11	Extracellular Potential
	Transmembrane	776 – 796	21	Potential
	Topological domain	797 – 875	79	Cytoplasmic Potential
	Transmembrane	876 – 896	21	Potential
	Topological domain	897 – 905	9	Extracellular Potential
	Transmembrane	906 – 926	21	Potential
	Topological domain	927 – 963	37	Cytoplasmic Potential
Amino acid modifications
	Modified residue	11	1	Phosphoserine Ref.8
	Modified residue	14	1	Phosphoserine Ref.6
	Modified residue	69	1	Phosphoserine Ref.7
	Modified residue	82	1	Phosphoserine Ref.8 Ref.7 Ref.4
	Modified residue	86	1	Phosphoserine Ref.8 Ref.7 Ref.4
	Modified residue	100	1	Phosphoserine Ref.7
	Modified residue	133	1	Phosphoserine Ref.8 Ref.7
	Modified residue	217	1	Phosphoserine Ref.6
	Glycosylation	22	1	N-linked (GlcNAc...) Potential
	Glycosylation	197	1	N-linked (GlcNAc...) Potential
	Glycosylation	447	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	197	1	N → A: 30% decrease of activity.
	Mutagenesis	312	1	S → A: 20% increase of activity.
	Mutagenesis	355	1	D → A: 10% decrease of activity.
	Mutagenesis	393	1	D → A: 5% decrease of activity.
	Mutagenesis	441	1	D → A: Loss of activity.
	Mutagenesis	441	1	D → E: Loss of activity.
	Mutagenesis	447	1	N → A: 80% decrease of activity.
	Mutagenesis	490	1	Q → A: 70% decrease of activity.
	Mutagenesis	492	1	F → A: 80% decrease of activity.
	Mutagenesis	493	1	E → A: 90% decrease of activity.
	Mutagenesis	494	1	Y → A: 95% decrease of activity.
	Mutagenesis	497	1	S → A: 95% decrease of activity.
	Mutagenesis	502	1	K → A: 90% decrease of activity.
	Mutagenesis	505	1	E → A: 80% decrease of activity.
	Mutagenesis	506	1	S → A: 20% increase of activity.
	Mutagenesis	508	1	F → A: 60% decrease of activity.
	Mutagenesis	509	1	G → A: 70% decrease of activity.
	Mutagenesis	514	1	L → A: 80% decrease of activity.
	Mutagenesis	515	1	P → A: 90% decrease of activity.
	Mutagenesis	516	1	G → A: 95% decrease of activity.
	Mutagenesis	521	1	Y → A: Loss of activity.
	Mutagenesis	522	1	R → A: 60% decrease of activity.
	Mutagenesis	537	1	R → A: No change in activity.
	Mutagenesis	550	1	H → A: 85% decrease of activity.
	Mutagenesis	556	1	N → A: 95% decrease of activity.
	Mutagenesis	559	1	L → A: 95% decrease of activity.
	Mutagenesis	561	1	E → A: Loss of activity.
	Mutagenesis	561	1	E → D: 65% decrease of activity.
	Mutagenesis	561	1	E → Q: Loss of activity.
	Mutagenesis	562	1	D → A: Loss of activity.
	Mutagenesis	562	1	D → E: Loss of activity.
	Mutagenesis	562	1	D → N: Loss of activity.
	Mutagenesis	563	1	R → A: Loss of activity.
	Mutagenesis	563	1	R → K: 94% decrease of activity.
	Mutagenesis	565	1	L → A: 95% decrease of activity.
	Mutagenesis	589	1	T → A: 70% decrease of activity.
	Mutagenesis	592	1	P → A: 70% decrease of activity.
	Mutagenesis	601	1	Q → A: Loss of activity.
	Mutagenesis	601	1	Q → N: Loss of activity.
	Mutagenesis	602 – 603	2	RR → KK: Loss of activity.
	Mutagenesis	602	1	R → A: Loss of activity.
	Mutagenesis	602	1	R → K: 95% decrease of activity.
	Mutagenesis	603	1	R → A: Loss of activity.
	Mutagenesis	603	1	R → K: 57% decrease of activity.
	Mutagenesis	604	1	R → A: Loss of activity.
	Mutagenesis	604	1	R → K: Loss of activity.
	Mutagenesis	605	1	W → A: Loss of activity.
	Mutagenesis	605	1	W → Y: Loss of activity.
	Mutagenesis	607	1	N → A: 95% decrease of activity.

Sequences

	Sequence		Length	Mass (Da)
	P14180-1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 4D44A287C0B65B5B	FASTA	963	109,882
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[4]	"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.
[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: 16847258] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
[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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-217, MASS SPECTROMETRY.
[7]	"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.
[8]	"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
EMBLGenBankDDBJ	M23865 Genomic DNA. Translation: AAA34493.1. Z35907 Genomic DNA. Translation: CAA84980.1.
PIR	S45167.
RefSeq	NP_009594.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:3819N.
IntAct	P14180. 19 interactions.
STRING	P14180.
Protein family/group databases
CAZy	GT2. Glycosyltransferase Family 2.
Proteomic databases
PRIDE	P14180.
Genome annotation databases
Ensembl	YBR038W; YBR038W; YBR038W; Saccharomyces cerevisiae. [Genome view]
GeneID	852326.
GenomeReviews	Gene locus YBR038W in contig Y13134_GR.
KEGG	sce:YBR038W.
NMPDR	fig|4932.3.peg.289.
Organism-specific databases
CYGD	YBR038w.
SGD	S000000242. CHS2.
Phylogenomic databases
HOGENOM	P14180.
OMA	WLFNAFC.
Enzyme and pathway databases
BRENDA	2.4.1.16. 250.
Gene expression databases
ArrayExpress	P14180.
Genevestigator	P14180.
GermOnline	YBR038W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004834. Chitin_synth. IPR013616. Chitin_synth_N. [Graphical view]
Pfam	PF01644. Chitin_synth_1. 1 hit. PF08407. Chitin_synth_1N. 1 hit. [Graphical view]
ProDom	PD002998. Chitin_synth. 1 hit. [Graphical view] [Entries sharing at least one domain]
ProtoNet	Search...
Other Resources
NextBio	971032.

Entry information

Entry name

CHS2_YEAST

Accession

Primary (citable) accession number: P14180

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	November 3, 2009
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)