P06367 (RS14A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
40S ribosomal protein S14-A

Alternative name(s):
RP59A

Gene names

Name:	RPS14A
Synonyms:	CRY1, RPL59
Ordered Locus Names:	YCR031C
ORF Names:	YCR31C

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	137 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 nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Ref.9
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). Interacts with snoRNA U3. Interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3. Ref.6 Ref.9
Subcellular location	Cytoplasm By similarity. Nucleus › nucleolus Ref.9.
Post-translational modification	N-terminally acetylated by acetyltransferase NatA. HAMAP-Rule MF_01310
Miscellaneous	Present with 29600 molecules/cell in log phase SD medium. HAMAP-Rule MF_01310 There are 2 genes for S14 in yeast. HAMAP-Rule MF_01310
Sequence similarities	Belongs to the ribosomal protein S11P family.

Ontologies

Keywords
Biological process	Ribosome biogenesis rRNA processing
Cellular component	Cytoplasm Nucleus
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.6. Source: SGD maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from mutant phenotype PubMed 15125836. Source: SGD ribosomal small subunit assembly Inferred from mutant phenotype PubMed 2277060PubMed 8293976. Source: SGD
Cellular_component	90S preribosome Inferred from direct assay PubMed 12150911. Source: SGD cytosolic small ribosomal subunit Non-traceable author statement Ref.6. Source: SGD nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell small-subunit processome Inferred from direct assay Ref.9. Source: SGD
Molecular_function	mRNA binding Inferred from direct assay PubMed 9858605. Source: SGD structural constituent of ribosome Non-traceable author statement Ref.6. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ESS1	P22696	1	EBI-14460,EBI-6679
PRP40	P33203	1	EBI-14460,EBI-701
SET2	P46995	1	EBI-14460,EBI-16985
URN1	Q06525	1	EBI-14460,EBI-35138
YFL010C	P43582	1	EBI-14460,EBI-22766

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 137

136

40S ribosomal protein S14-A HAMAP-Rule MF_01310

PRO_0000123359

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.5 Ref.7 Ref.10

Modified residue

2

1

Phosphoserine Ref.10

Modified residue

11

1

Phosphoserine Ref.11 Ref.12

Modified residue

125

1

Phosphoserine Ref.12

Experimental info

Sequence conflict

72

1

K → R in AAA34530. Ref.1

Sequence conflict

123

1

S → C in AAA34530. Ref.1

Secondary structure

1

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137

Helix Strand Turn

Details...

Beta strand

14 – 16

3

Beta strand

19 – 22

4

Beta strand

25 – 28

4

Beta strand

35 – 37

3

Turn

44 – 47

4

Turn

52 – 55

4

Helix

57 – 74

18

Beta strand

78 – 80

3

Beta strand

82 – 84

3

Helix

96 – 98

3

Helix

99 – 106

8

Turn

107 – 109

3

Beta strand

111 – 117

7

Sequences

	Sequence		Length	Mass (Da)
	P06367 [UniParc]. Last modified January 23, 2007. Version 5. Checksum: 65A9212E10340A95	FASTA	137	14,537
	10 20 30 40 50 60 MSNVVQARDN SQVFGVARIY ASFNDTFVHV TDLSGKETIA RVTGGMKVKA DRDESSPYAA 70 80 90 100 110 120 MLAAQDVAAK CKEVGITAVH VKIRATGGTR TKTPGPGGQA ALRALARSGL RIGRIEDVTP 130 VPSDSTRKKG GRRGRRL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and expression of the Saccharomyces cerevisiae CRY1 gene: a highly conserved ribosomal protein gene." Larkin J.C., Thompson J.R., Woolford J.L. Jr. Mol. Cell. Biol. 7:1764-1775(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete DNA sequence of yeast chromosome III." Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G. Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Valles G., Volckaerts G. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 72 AND 123.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae." Takakura H., Tsunasawa S., Miyagi M., Warner J.R. J. Biol. Chem. 267:5442-5445(1992) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT SER-2 BY NATA.
[6]	"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.
[7]	"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.
[8]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"The small-subunit processome is a ribosome assembly intermediate." Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S., Baserga S.J. Eukaryot. Cell 3:1619-1626(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU PROCESSOME, SUBCELLULAR LOCATION.
[10]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2, MASS SPECTROMETRY. Strain: YAL6B.
[11]	"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-11, MASS SPECTROMETRY.
[12]	"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 SER-11 AND SER-125, MASS SPECTROMETRY.
[13]	"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 9-133, ELECTRON MICROSCOPY.
[14]	"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, ELECTRON MICROSCOPY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16126 Genomic DNA. Translation: AAA34530.1.
X59720 Genomic DNA. Translation: CAC42981.1.
BK006937 Genomic DNA. Translation: DAA07510.1.

PIR

R5BY59. A02726.

RefSeq

NP_009960.2. NM_001178745.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K5X	model	-	K	9-133	[»]
1S1H	electron microscopy	11.70	K	2-137	[»]
3IZB	electron microscopy	-	K	1-137	[»]
3O2Z	X-ray	4.00	H	1-137	[»]
3O30	X-ray	4.00	H	1-137	[»]
3U5C	X-ray	3.00	O	1-137	[»]
3U5G	X-ray	3.00	O	1-137	[»]

ProteinModelPortal

P06367.

SMR

P06367. Positions 10-126.

ModBase

Search...

Protein-protein interaction databases

IntAct

P06367. 22 interactions.

MINT

MINT-4083975.

STRING

4932.YCR031C.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YCR031C; YCR031C; YCR031C.

GeneID

850397.

KEGG

sce:YCR031C.

Organism-specific databases

SGD

S000000627. RPS14A.

Phylogenomic databases

GeneTree

ENSGT00390000000703.

HOGENOM

HOG000111598.

KO

K02955.

OMA

VANIFAS.

OrthoDB

EOG4M0JBD.

Gene expression databases

Genevestigator

P06367.

GermOnline

YCR031C. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.30.420.80. 1 hit.

HAMAP

MF_01310. Ribosomal_S11.

InterPro

IPR001971. Ribosomal_S11.
IPR018102. Ribosomal_S11_CS.
[Graphical view]

PANTHER

PTHR11759. PTHR11759. 1 hit.

Pfam

PF00411. Ribosomal_S11. 1 hit.
[Graphical view]

PIRSF

PIRSF002131. Ribosomal_S11. 1 hit.

PROSITE

PS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P06367.

NextBio

965926.

Entry information

Entry name

RS14A_YEAST

Accession

Primary (citable) accession number: P06367
Secondary accession number(s): D6VR41, Q96VG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 131 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program