Q01855 (RS15_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
40S ribosomal protein S15

Alternative name(s):
RIG protein
RP52
S21
YS21

Gene names

Name:	RPS15
Synonyms:	RPS21
Ordered Locus Names:	YOL040C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	142 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the nuclear export of the small ribosomal subunit. Has a role in the late stage of the assembly of pre-40S particles within the nucleus and controls their export to the cytoplasm. Ref.7
Subunit structure	Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains 32 different proteins (encoded by 56 genes) and 1 molecule of RNA (18S). The 60S subunit contains 46 different proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S and 5S). Ref.5
Subcellular location	Cytoplasm By similarity HAMAP-Rule MF_00531.
Sequence similarities	Belongs to the ribosomal protein S19P family.

Ontologies

Keywords
Biological process	Ribosome biogenesis
Cellular component	Cytoplasm
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytoplasmic translation Non-traceable author statement Ref.5. Source: SGD rRNA export from nucleus Inferred from mutant phenotype Ref.7PubMed 16246728. Source: SGD
Cellular_component	cytosolic small ribosomal subunit Non-traceable author statement Ref.5. Source: SGD
Molecular_function	RNA binding Inferred from electronic annotation. Source: InterPro structural constituent of ribosome Non-traceable author statement Ref.5. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 142

141

40S ribosomal protein S15 HAMAP-Rule MF_00531

PRO_0000130051

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.6

Modified residue

16

1

Phosphoserine Ref.8

Modified residue

124

1

Phosphothreonine Ref.9

Secondary structure

1

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142

Helix Strand Turn

Details...

Beta strand

16 – 19

4

Helix

22 – 26

5

Helix

30 – 36

7

Helix

39 – 46

8

Helix

54 – 66

13

Beta strand

69 – 71

3

Beta strand

76 – 78

3

Helix

87 – 89

3

Beta strand

93 – 106

14

Helix

109 – 111

3

Helix

116 – 119

4

Sequences

	Sequence		Length	Mass (Da)
	Q01855 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 06B564FD68051CD2	FASTA	142	16,002
	10 20 30 40 50 60 MSQAVNAKKR VFKTHSYRGV DLEKLLEMST EDFVKLAPAR VRRRFARGMT SKPAGFMKKL 70 80 90 100 110 120 RAAKLAAPEN EKPAPVRTHM RNMIIVPEMI GSVVGIYNGK AFNQVEIRPE MLGHYLGEFS 130 140 ITYTPVRHGR AGATTSRFIP LK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural determination of Saccharomyces cerevisiae rig gene and identification of its product as ribosomal protein S21." Takasawa S., Tohgo A., Unno M., Yonekura H., Okamoto H. FEBS Lett. 307:318-323(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K. Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae." Planta R.J., Mager W.H. Yeast 14:471-477(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE, SUBUNIT.
[6]	"The action of N-terminal acetyltransferases on yeast ribosomal proteins." Arnold R.J., Polevoda B., Reilly J.P., Sherman F. J. Biol. Chem. 274:37035-37040(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2 BY NATA.
[7]	"The ribosomal protein Rps15p is required for nuclear exit of the 40S subunit precursors in yeast." Leger-Silvestre I., Milkereit P., Ferreira-Cerca S., Saveanu C., Rousselle J.-C., Choesmel V., Guinefoleau C., Gas N., Gleizes P.-E. EMBO J. 23:2336-2347(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-124, MASS SPECTROMETRY.
[10]	"Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions." Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J. Cell 107:373-386(2001) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 47-126, ELECTRON MICROSCOPY.
[11]	"Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation." Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J. EMBO J. 23:1008-1019(2004) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 47-126, ELECTRON MICROSCOPY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D11386 mRNA. Translation: BAA01982.1.
D11387 Genomic DNA. Translation: BAA01983.1.
Z74782 Genomic DNA. Translation: CAA99042.1.
AY558426 Genomic DNA. Translation: AAS56752.1.
BK006948 Genomic DNA. Translation: DAA10742.1.

PIR

S24053.

RefSeq

NP_014602.1. NM_001183294.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K5X	model	-	S	47-126	[»]
1S1H	electron microscopy	11.70	S	47-126	[»]
3IZB	electron microscopy	-	R	1-142	[»]
3O2Z	X-ray	4.00	I	1-142	[»]
3O30	X-ray	4.00	I	1-142	[»]
3U5C	X-ray	3.00	P	1-142	[»]
3U5G	X-ray	3.00	P	1-142	[»]

ProteinModelPortal

Q01855.

SMR

Q01855. Positions 4-138.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q01855. 3 interactions.

MINT

MINT-4986189.

STRING

4932.YOL040C.

Proteomic databases

PaxDb

Q01855.

PeptideAtlas

Q01855.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YOL040C; YOL040C; YOL040C.

GeneID

854117.

KEGG

sce:YOL040C.

Organism-specific databases

CYGD

YOL040c.

SGD

S000005400. RPS15.

Phylogenomic databases

eggNOG

COG0185.

GeneTree

ENSGT00390000000475.

HOGENOM

HOG000111561.

KO

K02958.

OMA

VIRTHCR.

OrthoDB

EOG4HHSBV.

Enzyme and pathway databases

BioCyc

YEAST:G3O-33454-MONOMER.

Gene expression databases

Genevestigator

Q01855.

GermOnline

YOL040C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.30.860.10. 1 hit.

HAMAP

MF_00531. Ribosomal_S19.

InterPro

IPR002222. Ribosomal_S19.
IPR020934. Ribosomal_S19_CS.
IPR023575. Ribosomal_S19_SF.
IPR005713. Ribosomal_S19A/S15e.
[Graphical view]

PANTHER

PTHR11880. PTHR11880. 1 hit.

Pfam

PF00203. Ribosomal_S19. 1 hit.
[Graphical view]

PIRSF

PIRSF002144. Ribosomal_S19. 1 hit.

PRINTS

PR00975. RIBOSOMALS19.

SUPFAM

SSF54570. Ribosomal_S19. 1 hit.

TIGRFAMs

TIGR01025. rpsS_arch. 1 hit.

PROSITE

PS00323. RIBOSOMAL_S19. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q01855.

NextBio

975816.

Entry information

Entry name

RS15_YEAST

Accession

Primary (citable) accession number: Q01855
Secondary accession number(s): D6W226

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	May 29, 2013
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program