Reviewed, UniProtKB/Swiss-Prot P34237 (CASP_YEAST)

Names and origin

Protein names

Recommended name:
    Protein CASP

Gene names

Name:	COY1
Ordered Locus Names:	YKL179C

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

General annotation (Comments)

Function	May be involved in intra-Golgi transport. Ref.4
Subcellular location	Golgi apparatus membrane; Single-pass type IV membrane protein.
Miscellaneous	Present with 2650 molecules/cell in log phase SD medium. Ref.5
Sequence similarities	Belongs to the CASP family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Golgi apparatus Membrane
Domain	Coiled coil Transmembrane
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	intra-Golgi vesicle-mediated transport Inferred from electronic annotation. Source: InterPro
Cellular component	integral to Golgi membrane Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 679	679	Protein CASP		PRO_0000071795
Regions
	Topological domain	1 – 614	614	Cytoplasmic Potential
	Transmembrane	615 – 635	21	Anchor for type IV membrane protein Potential
	Topological domain	636 – 679	44	Lumenal Potential
	Coiled coil	14 – 90	77	Potential
	Coiled coil	178 – 341	164	Potential
	Coiled coil	385 – 444	60	Potential
	Coiled coil	492 – 540	49	Potential
Amino acid modifications
	Modified residue	364	1	Phosphoserine Ref.6 Ref.7 Ref.9
	Modified residue	450	1	Phosphoserine Ref.6 Ref.9
	Modified residue	463	1	Phosphothreonine Ref.9 Ref.8
	Modified residue	468	1	Phosphoserine Ref.9
	Modified residue	470	1	Phosphothreonine Ref.9
	Modified residue	471	1	Phosphoserine Ref.9
	Modified residue	555	1	Phosphoserine Ref.9
Experimental info
	Mutagenesis	619	1	Y → L: Retained in the endoplasmic reticulum. Ref.4
	Mutagenesis	624	1	H → L: No effect on subcellular location. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P34237-1 [UniParc]. Last modified June 1, 1994. Version 2. Checksum: CA849F6F4C88A4A9	FASTA	679	77,514
	10 20 30 40 50 60 MDTSVYSHAL DIWAKADLTN LQRELDADVI EIKDKETLSL NSRKSLATET KKFKKLEPEE 70 80 90 100 110 120 KLNNVNKIIK QYQREIDNLT QRSKFSEKVL FDVYEKLSEA PDPQPLLQSS LEKLGKIDDS 130 140 150 160 170 180 KELKEKISYL EDKLAKYADY ETLKSRLLDL EQSSAKTLAK RLTAKTQEIN STWEEKGRNW 190 200 210 220 230 240 KEREADLLKQ LTNVQEQNKA LEAKISKNID IEGNGNEDGD QENNQKEVST RIAEYNLVTQ 250 260 270 280 290 300 ELETTQARIY QLEKRNEELS GALAKATSEA EKETELHAKE LKLNQLESEN ALLSASYEQE 310 320 330 340 350 360 RKSTSHAINE LKEQLNSVVA ESESYKSELE TVRRKLNNYS DYNKIKEELS ALKKIEFGVN 370 380 390 400 410 420 EDDSDNDIRS EDKNDNTFES SLLSANKKLQ ATLAEYRSKS TAQEEERNEL KKSVDQLKQQ 430 440 450 460 470 480 IATLKEANEK LETDLEKVEN VSPHFNETAS MMSGVTRQMN NRTSHKMSPT SSIIGIPEDG 490 500 510 520 530 540 ELSGNQSTIL PIVTKQRDRF RSRNMDLEKQ LRQGNSEKGK LKLEISKLKG DNTKLYERIR 550 560 570 580 590 600 YLQSYNNNNA PVNQSTERID VESQYSRVYD ESLHPMANFR QNELNHYKNK KLSALEKLFS 610 620 630 640 650 660 SFAKVILQNK MTRMVFLFYC IGLHGLVFMM SMYVINISGY MTPEVGIVQS AKSSSNLNGG 670 LGGAEKVAAG VGSVHGINR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI from Saccharomyces cerevisiae reveals 23 open reading frames including the FAS1 gene." Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J., Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W. Yeast 9:1343-1348(1993) [PubMed: 8154185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Complete DNA sequence of yeast chromosome XI." Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION. Strain: ATCC 96604 / S288c / FY1679.
[3]	"CASP, a novel, highly conserved alternative-splicing product of the CDP/cut/cux gene, lacks cut-repeat and homeo DNA-binding domains, and interacts with full-length CDP in vitro." Lievens P.M.-J., Tufarelli C., Donady J.J., Stagg A., Neufeld E.J. Gene 197:73-81(1997) [PubMed: 9332351] [Abstract] Cited for: IDENTIFICATION.
[4]	"CASP, the alternatively spliced product of the gene encoding the CCAAT-displacement protein transcription factor, is a Golgi membrane protein related to giantin." Gillingham A.K., Pfeifer A.C., Munro S. Mol. Biol. Cell 13:3761-3774(2002) [PubMed: 12429822] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-619 AND HIS-624.
[5]	"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].
[6]	"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-364 AND SER-450, MASS SPECTROMETRY.
[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-364, 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 THR-463, 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-364; SER-450; THR-463; SER-468; THR-470; SER-471 AND SER-555, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X74151 Genomic DNA. Translation: CAA52259.1. Z28179 Genomic DNA. Translation: CAA82021.1.
PIR	S38011.
RefSeq	NP_012742.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2851N.
IntAct	P34237. 2 interactions.
STRING	P34237.
Genome annotation databases
Ensembl	YKL179C; YKL179C; YKL179C; Saccharomyces cerevisiae. [Genome view]
GeneID	853675.
KEGG	sce:YKL179C.
NMPDR	fig|4932.3.peg.3720.
Organism-specific databases
CYGD	YKL179c.
SGD	S000001662. COY1.
Phylogenomic databases
HOGENOM	P34237.
OMA	KQRDRFR
OrthoDB	EOG9X9914
Gene expression databases
ArrayExpress	P34237.
Genevestigator	P34237.
GermOnline	YKL179C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR012955. CASP_C. [Graphical view]
Pfam	PF08172. CASP_C. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	974628.

Entry information

Entry name

CASP_YEAST

Accession

Primary (citable) accession number: P34237
Secondary accession number(s): P34236

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 24, 2009
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)