Reviewed, UniProtKB/Swiss-Prot P21827 (RCC1_YEAST)

Names and origin

Protein names

Recommended name:
    Regulator of chromosome condensation
Alternative name(s):
    Protein PRP20
    Pheromone response pathway component SRM1

Gene names

Name:	PRP20
Synonyms:	MTR1, SRM1
Ordered Locus Names:	YGL097W

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

General annotation (Comments)

Function	Promotes the exchange of GSP1/GSP2-bound GDP by GTP. Involved in yeast pheromone response pathway and in mRNA metabolism. Probably involved in the control of nuclear organization.
Subcellular location	Nucleus. Ref.5
Induction	By pheromone.
Post-translational modification	Phosphorylated; possibly by KSP1. Ref.6 Ref.8 Ref.9 Ref.10
Miscellaneous	Present with 12100 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Contains 7 RCC1 repeats.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Pheromone response
Cellular component	Nucleus
Domain	Repeat
Molecular function	Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW rRNA export from nucleus Inferred from mutant phenotype. Source: SGD response to pheromone Inferred from electronic annotation. Source: UniProtKB-KW ribosome export from nucleus Inferred from mutant phenotype. Source: SGD
Cellular component	nuclear chromatin Inferred from direct assay. Source: SGD
Molecular function	guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct signal transducer activity Ref.1 Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BOI1	P38041	1	EBI-14866,EBI-3719

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 482	482	Regulator of chromosome condensation		PRO_0000206634
Regions
	Repeat	45 – 101	57	RCC1 1
	Repeat	103 – 152	50	RCC1 2
	Repeat	183 – 238	56	RCC1 3
	Repeat	239 – 291	53	RCC1 4
	Repeat	292 – 347	56	RCC1 5
	Repeat	349 – 411	63	RCC1 6
	Repeat	412 – 466	55	RCC1 7
Amino acid modifications
	Modified residue	135	1	Phosphoserine Ref.8 Ref.9 Ref.10
	Modified residue	136	1	Phosphoserine Ref.8 Ref.9 Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P21827-1 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 04FFC7B9DC7DE535	FASTA	482	53,014
	10 20 30 40 50 60 MVKRTVATNG DASGAHRAKK MSKTHASHII NAQEDYKHMY LSVQPLDIFC WGTGSMCELG 70 80 90 100 110 120 LGPLAKNKEV KRPRLNPFLP RDEAKIISFA VGGMHTLALD EESNVWSWGC NDVGALGRDT 130 140 150 160 170 180 SNAKEQLKDM DADDSSDDED GDLNELESTP AKIPRESFPP LAEGHKVVQL AATDNMSCAL 190 200 210 220 230 240 FSNGEVYAWG TFRCNEGILG FYQDKIKIQK TPWKVPTFSK YNIVQLAPGK DHILFLDEEG 250 260 270 280 290 300 MVFAWGNGQQ NQLGRKVMER FRLKTLDPRP FGLRHVKYIA SGENHCFALT KDNKLVSWGL 310 320 330 340 350 360 NQFGQCGVSE DVEDGALVTK PKRLALPDNV VIRSIAAGEH HSLILSQDGD LYSCGRLDMF 370 380 390 400 410 420 EVGIPKDNLP EYTYKDVHGK ARAVPLPTKL NNVPKFKSVA AGSHHSVAVA QNGIAYSWGF 430 440 450 460 470 480 GETYAVGLGP FEDDTEVPTR IKNTATQDHN IILVGCGGQF SVSGGVKLSD EDAEKRADEM DD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Yeast pheromone response pathway: characterization of a suppressor that restores mating to receptorless mutants." Clark K.L., Sprague G.F. Jr. Mol. Cell. Biol. 9:2682-2694(1989) [PubMed: 2548085] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A yeast mutant, PRP20, altered in mRNA metabolism and maintenance of the nuclear structure, is defective in a gene homologous to the human gene RCC1 which is involved in the control of chromosome condensation." Aebi M., Clark M.W., Vijayraghavan U., Abelson J. Mol. Gen. Genet. 224:72-80(1990) [PubMed: 2277633] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII." Rieger M., Brueckner M., Schaefer M., Mueller-Auer S. Yeast 13:1077-1090(1997) [PubMed: 9290212] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	"Mutation of the hamster cell cycle gene RCC1 is complemented by the homologous genes of Drosophila and S.cerevisiae." Ohtsubo M., Yoshida T., Seino H., Nishitani H., Clark K.L., Sprague G.F. Jr., Frasch M., Nishimoto T. EMBO J. 10:1265-1273(1991) [PubMed: 2022190] [Abstract] Cited for: CHARACTERIZATION, SUBCELLULAR LOCATION.
[6]	"Allele-specific suppression of a Saccharomyces cerevisiae prp20 mutation by overexpression of a nuclear serine/threonine protein kinase." Fleischmann M., Stagljar I., Aebi M. Mol. Gen. Genet. 250:614-625(1996) [PubMed: 8676864] [Abstract] Cited for: PHOSPHORYLATION.
[7]	"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].
[8]	"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-135 AND SER-136, MASS SPECTROMETRY.
[9]	"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-135 AND SER-136, MASS SPECTROMETRY.
[10]	"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-135 AND SER-136, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M27013 Genomic DNA. Translation: AAA62268.1. Z72619 Genomic DNA. Translation: CAA96803.1.
PIR	RGBYM1. A32320.
RefSeq	NP_011418.1.
3D structure databases
HSSP	HSSP built from PDB template 1I2M based on UniProtKB P18754.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2315N.
IntAct	P21827. 5 interactions.
STRING	P21827.
Proteomic databases
PeptideAtlas	P21827.
PRIDE	P21827.
Genome annotation databases
Ensembl	YGL097W; YGL097W; YGL097W; Saccharomyces cerevisiae. [Genome view]
GeneID	852782.
GenomeReviews	Gene locus YGL097W in contig Y13135_GR.
KEGG	sce:YGL097W.
NMPDR	fig|4932.3.peg.2523.
Organism-specific databases
CYGD	YGL097w.
SGD	S000003065. SRM1.
Phylogenomic databases
HOGENOM	P21827.
OMA	RCNEGIL.
Gene expression databases
ArrayExpress	P21827.
Genevestigator	P21827.
GermOnline	YGL097W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR000408. Reg_chr_condens. IPR009091. Reg_csome_cond/b-lactamase_inh. [Graphical view]
Gene3D	G3DSA:2.130.10.30. Reg_csome_cond/b-lactamase_inh. 1 hit.
PRINTS	PR00633. RCCNDNSATION.
PROSITE	PS00625. RCC1_1. 1 hit. PS00626. RCC1_2. 1 hit. PS50012. RCC1_3. 7 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	972265.

Entry information

Entry name

RCC1_YEAST

Accession

Primary (citable) accession number: P21827

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	November 3, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)