P21827 (RCC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide exchange factor SRM1

Alternative name(s):
Pheromone response pathway component SRM1
Pre-mRNA-processing protein 20
Regulator of chromosome condensation
Suppressor of receptor mutations 1
mRNA transport protein 1

Gene names

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

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Guanine nucleotide exchange factor that promotes the exchange of GSP1/GSP2-bound GDP by GTP and controls RNA metabolism and transport. Involved in yeast pheromone response pathway and in mRNA metabolism. Involved in nuclear pore complex (NPC) assembly and required for mRNA and ribosome nuclear export. Binds chromatin and is involved NPC-mediated transcriptional control. Ref.1 Ref.2 Ref.7 Ref.9 Ref.10 Ref.11 Ref.13 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22 Ref.23 Ref.25
Subunit structure	Component of a multicomponent complex composed of six to seven proteins, which has a collective molecular mass greater than 150 kDa. Interacts with GSP1 and YRB2. Ref.12 Ref.15 Ref.20 Ref.21
Subcellular location	Nucleus Ref.6 Ref.7 Ref.9 Ref.21 Ref.25.
Induction	By pheromone.
Post-translational modification	Phosphorylated; possibly by KSP1. Ref.8 Ref.24 Ref.26 Ref.27
Miscellaneous	Present with 12100 molecules/cell in log phase SD medium. Ref.14
Sequence similarities	Contains 7 RCC1 repeats.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis Pheromone response Transport
Cellular component	Nucleus
Domain	Repeat
Molecular function	Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference 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 ribosomal subunit export from nucleus Inferred from mutant phenotype. Source: SGD
Cellular component	nuclear chromatin Inferred from direct assay Ref.25. Source: SGD
Molecular function	guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: UniProtKB-KW signal transducer activity Inferred from mutant phenotype Ref.1. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 482

482

Guanine nucleotide exchange factor SRM1

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

Motif

15 – 26

12

Nuclear localization signal Ref.21

Amino acid modifications

Modified residue

135

1

Phosphoserine Ref.24 Ref.26 Ref.27

Modified residue

136

1

Phosphoserine Ref.24 Ref.26 Ref.27

Experimental info

Mutagenesis

19

1

K → T: Impairs correct nuclear localization; when associated with T-20 and T-23. Ref.21

Mutagenesis

20

1

K → A or Q: Impairs activity. Ref.21

Mutagenesis

20

1

K → T: Impairs correct nuclear localization; when associated with T-19 and T-23. Ref.21

Mutagenesis

23

1

K → T: Impairs correct nuclear localization; when associated with T-19 and T-20. Ref.21

Mutagenesis

282

1

G → S: Leads to temperature-dependent mislocalization of nucleoporins (nups) and the pore-membrane protein POM152. Ref.23

Secondary structure

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482

Helix Strand Turn

Details...

Helix

33 – 36

4

Helix

37 – 40

4

Beta strand

49 – 51

3

Helix

65 – 68

4

Turn

81 – 83

3

Beta strand

86 – 90

5

Beta strand

96 – 100

5

Beta strand

105 – 108

4

Helix

145 – 148

4

Helix

155 – 157

3

Helix

159 – 162

4

Beta strand

167 – 172

6

Beta strand

177 – 181

5

Beta strand

186 – 189

4

Turn

203 – 205

3

Beta strand

223 – 227

5

Beta strand

233 – 237

5

Beta strand

241 – 245

5

Helix

259 – 261

3

Turn

262 – 265

4

Beta strand

269 – 271

3

Beta strand

273 – 280

8

Beta strand

286 – 290

5

Beta strand

295 – 298

4

Beta strand

332 – 336

5

Beta strand

342 – 346

5

Beta strand

351 – 354

4

Helix

366 – 368

3

Beta strand

381 – 383

3

Beta strand

396 – 400

5

Beta strand

406 – 410

5

Beta strand

415 – 418

4

Turn

444 – 448

5

Beta strand

461 – 463

3

Helix

471 – 481

11

Sequences

	Sequence		Length	Mass (Da)
	P21827 [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], FUNCTION.
[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], FUNCTION.
[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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"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.
[7]	"The yeast SRM1 protein and human RCC1 protein share analogous functions." Clark K.L., Ohtsubo M., Nishimoto T., Goebl M., Sprague G.F. Jr. Cell Regul. 2:781-792(1991) [PubMed: 1666302] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]	"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.
[9]	"Analysis of yeast prp20 mutations and functional complementation by the human homologue RCC1, a protein involved in the control of chromosome condensation." Fleischmann M., Clark M.W., Forrester W., Wickens M., Nishimoto T., Aebi M. Mol. Gen. Genet. 227:417-423(1991) [PubMed: 1865879] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]	"Defects in mRNA 3'-end formation, transcription initiation, and mRNA transport associated with the yeast mutation prp20: possible coupling of mRNA processing and chromatin structure." Forrester W., Stutz F., Rosbash M., Wickens M. Genes Dev. 6:1914-1926(1992) [PubMed: 1398069] [Abstract] Cited for: FUNCTION.
[11]	"Nuclear PRP20 protein is required for mRNA export." Amberg D.C., Fleischmann M., Stagljar I., Cole C.N., Aebi M. EMBO J. 12:233-241(1993) [PubMed: 7679070] [Abstract] Cited for: FUNCTION.
[12]	"Prp20, the Saccharomyces cerevisiae homolog of the regulator of chromosome condensation, RCC1, interacts with double-stranded DNA through a multi-component complex containing GTP-binding proteins." Lee A., Tam R., Belhumeur P., DiPaolo T., Clark M.W. J. Cell Sci. 106:287-298(1993) [PubMed: 8270631] [Abstract] Cited for: DNA-BINDING, SUBUNIT.
[13]	"Overexpression of yeast homologs of the mammalian checkpoint gene RCC1 suppresses the class of alpha-tubulin mutations that arrest with excess microtubules." Kirkpatrick D., Solomon F. Genetics 137:381-392(1994) [PubMed: 8070652] [Abstract] Cited for: FUNCTION.
[14]	"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].
[15]	"Yrb2p is a nuclear protein that interacts with Prp20p, a yeast Rcc1 homologue." Taura T., Schlenstedt G., Silver P.A. J. Biol. Chem. 272:31877-31884(1997) [PubMed: 9395535] [Abstract] Cited for: INTERACTION WITH YRB2.
[16]	"A novel in vivo assay reveals inhibition of ribosomal nuclear export in ran-cycle and nucleoporin mutants." Hurt E.C., Hannus S., Schmelzl B., Lau D.M., Tollervey D., Simos G. J. Cell Biol. 144:389-401(1999) [PubMed: 9971735] [Abstract] Cited for: FUNCTION.
[17]	"Factors affecting nuclear export of the 60S ribosomal subunit in vivo." Stage-Zimmermann T., Schmidt U., Silver P.A. Mol. Biol. Cell 11:3777-3789(2000) [PubMed: 11071906] [Abstract] Cited for: FUNCTION.
[18]	"Pre-mRNA processing factors are required for nuclear export." Brodsky A.S., Silver P.A. RNA 6:1737-1749(2000) [PubMed: 11142374] [Abstract] Cited for: FUNCTION.
[19]	"Interaction between Ran and Mog1 is required for efficient nuclear protein import." Baker R.P., Harreman M.T., Eccleston J.F., Corbett A.H., Stewart M. J. Biol. Chem. 276:41255-41262(2001) [PubMed: 11509570] [Abstract] Cited for: FUNCTION.
[20]	"The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex." Denning D.P., Mykytka B., Allen N.P., Huang L., Burlingame A., Rexach M. J. Cell Biol. 154:937-950(2001) [PubMed: 11535617] [Abstract] Cited for: INTERACTION WITH NUP60.
[21]	"Functional analysis of the yeast Ran exchange factor Prp20p: in vivo evidence for the RanGTP gradient model." Akhtar N., Hagan H., Lopilato J.E., Corbett A.H. Mol. Genet. Genomics 265:851-864(2001) [PubMed: 11523802] [Abstract] Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF LYS-19; LYS-20 AND LYS-23, INTERACTION WITH GSP1.
[22]	"Overexpression of Bud5p can suppress mutations in the Gsp1p guanine nucleotide exchange factor Prp20p in Saccharomyces cerevisiae." Clement M., Lavallee F., Barbes-Morin G., de Repentigny L., Belhumeur P. Mol. Genet. Genomics 266:20-27(2001) [PubMed: 11589573] [Abstract] Cited for: FUNCTION.
[23]	"The Ran GTPase cycle is required for yeast nuclear pore complex assembly." Ryan K.J., McCaffery J.M., Wente S.R. J. Cell Biol. 160:1041-1053(2003) [PubMed: 12654904] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-282.
[24]	"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. Strain: ADR376.
[25]	"The mobile nucleoporin Nup2p and chromatin-bound Prp20p function in endogenous NPC-mediated transcriptional control." Dilworth D.J., Tackett A.J., Rogers R.S., Yi E.C., Christmas R.H., Smith J.J., Siegel A.F., Chait B.T., Wozniak R.W., Aitchison J.D. J. Cell Biol. 171:955-965(2005) [PubMed: 16365162] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, CHROMATIN-BINDING.
[26]	"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.
[27]	"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

EMBL
GenBank
DDBJ

M27013 Genomic DNA. Translation: AAA62268.1.
Z72619 Genomic DNA. Translation: CAA96803.1.
BK006941 Genomic DNA. Translation: DAA08009.1.

PIR

RGBYM1. A32320.

RefSeq

NP_011418.1. NM_001180962.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3OF7	X-ray	1.90	A	27-482	[»]

ProteinModelPortal

P21827.

SMR

P21827. Positions 27-482.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2315N.

IntAct

P21827. 4 interactions.

MINT

MINT-561451.

STRING

P21827.

Proteomic databases

PeptideAtlas

P21827.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YGL097W; YGL097W; YGL097W.

GeneID

852782.

KEGG

sce:YGL097W.

NMPDR

fig|4932.3.peg.2523.

Organism-specific databases

CYGD

YGL097w.

SGD

S000003065. SRM1.

Phylogenomic databases

eggNOG

fuNOG04785.

GeneTree

EFGT00050000001144.

HOGENOM

HBG593714.

OMA

KNKEVKR.

OrthoDB

EOG466ZVF.

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.

Pfam

PF00415. RCC1. 6 hits.
[Graphical view]

PRINTS

PR00633. RCCNDNSATION.

SUPFAM

SSF50985. RCC1/BLIP-II. 1 hit.

PROSITE

PS00625. RCC1_1. 1 hit.
PS00626. RCC1_2. 1 hit.
PS50012. RCC1_3. 7 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

972265.

Entry information

Entry name

RCC1_YEAST

Accession

Primary (citable) accession number: P21827
Secondary accession number(s): D6VU48

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	December 14, 2011
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program