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Protein

40S ribosomal protein S4, X isoform

Gene

Rps4x

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S4, X isoform
Gene namesi
Name:Rps4x
Synonyms:Rps4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:98158. Rps4x.

Subcellular locationi

  • Cytoplasm By similarity

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 26326240S ribosomal protein S4, X isoformPRO_0000130809Add
BLAST

Proteomic databases

MaxQBiP62702.
PaxDbiP62702.
PRIDEiP62702.

PTM databases

PhosphoSiteiP62702.

Expressioni

Gene expression databases

BgeeiP62702.
CleanExiMM_RPS4X.
ExpressionAtlasiP62702. baseline and differential.
GenevestigatoriP62702.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.By similarity

Protein-protein interaction databases

BioGridi203011. 3 interactions.
IntActiP62702. 8 interactions.
MINTiMINT-1845743.

Structurei

3D structure databases

ProteinModelPortaliP62702.
SMRiP62702. Positions 1-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 10463S4 RNA-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S4e family.Curated
Contains 1 S4 RNA-binding domain.Curated

Phylogenomic databases

eggNOGiCOG1471.
HOVERGENiHBG000935.
InParanoidiP62702.
KOiK02987.
OMAiHIQLNLH.
OrthoDBiEOG77WWD1.
PhylomeDBiP62702.
TreeFamiTF300612.

Family and domain databases

HAMAPiMF_00485. Ribosomal_S4e.
InterProiIPR005824. KOW.
IPR000876. Ribosomal_S4e.
IPR013845. Ribosomal_S4e_central_region.
IPR013843. Ribosomal_S4e_N.
IPR018199. Ribosomal_S4e_N_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERiPTHR11581. PTHR11581. 1 hit.
PfamiPF00467. KOW. 1 hit.
PF00900. Ribosomal_S4e. 1 hit.
PF08071. RS4NT. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
PIRSFiPIRSF002116. Ribosomal_S4. 1 hit.
ProDomiPD002667. Ribosomal_S4e_central. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00363. S4. 1 hit.
[Graphical view]
PROSITEiPS00528. RIBOSOMAL_S4E. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62702-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARGPKKHLK RVAAPKHWML DKLTGVFAPR PSTGPHKLRE CLPLIIFLRN
60 70 80 90 100
RLKYALTGDE VKKICMQRFI KIDGKVRTDI TYPAGFMDVI SIDKTGENFR
110 120 130 140 150
LIYDTKGRFA VHRITPEEAK YKLCKVRKIF VGTKGIPHLV THDARTIRYP
160 170 180 190 200
DPLIKVNDTI QIDLETGKIT DFIKFDTGNL CMVTGGANLG RIGVITNRER
210 220 230 240 250
HPGSFDVVHV KDANGNSFAT RLSNIFVIGK GNKPWISLPR GKGIRLTIAE
260
ERDKRLAAKQ SSG
Length:263
Mass (Da):29,598
Last modified:January 23, 2007 - v2
Checksum:i87200E545A8958B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91L → M in BAB29207 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73436 mRNA. Translation: AAA40075.1.
AK014210 mRNA. Translation: BAB29207.1.
BC009100 mRNA. Translation: AAH09100.1.
M77296 Genomic DNA. Translation: AAA40072.1.
CCDSiCCDS41083.1.
RefSeqiNP_033120.1. NM_009094.1.
UniGeneiMm.66.

Genome annotation databases

EnsembliENSMUST00000033683; ENSMUSP00000033683; ENSMUSG00000031320.
GeneIDi20102.
KEGGimmu:20102.
UCSCiuc009tyl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73436 mRNA. Translation: AAA40075.1.
AK014210 mRNA. Translation: BAB29207.1.
BC009100 mRNA. Translation: AAH09100.1.
M77296 Genomic DNA. Translation: AAA40072.1.
CCDSiCCDS41083.1.
RefSeqiNP_033120.1. NM_009094.1.
UniGeneiMm.66.

3D structure databases

ProteinModelPortaliP62702.
SMRiP62702. Positions 1-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203011. 3 interactions.
IntActiP62702. 8 interactions.
MINTiMINT-1845743.

PTM databases

PhosphoSiteiP62702.

Proteomic databases

MaxQBiP62702.
PaxDbiP62702.
PRIDEiP62702.

Protocols and materials databases

DNASUi20102.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033683; ENSMUSP00000033683; ENSMUSG00000031320.
GeneIDi20102.
KEGGimmu:20102.
UCSCiuc009tyl.1. mouse.

Organism-specific databases

CTDi6191.
MGIiMGI:98158. Rps4x.

Phylogenomic databases

eggNOGiCOG1471.
HOVERGENiHBG000935.
InParanoidiP62702.
KOiK02987.
OMAiHIQLNLH.
OrthoDBiEOG77WWD1.
PhylomeDBiP62702.
TreeFamiTF300612.

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

ChiTaRSiRps4x. mouse.
NextBioi297599.
PROiP62702.
SOURCEiSearch...

Gene expression databases

BgeeiP62702.
CleanExiMM_RPS4X.
ExpressionAtlasiP62702. baseline and differential.
GenevestigatoriP62702.

Family and domain databases

HAMAPiMF_00485. Ribosomal_S4e.
InterProiIPR005824. KOW.
IPR000876. Ribosomal_S4e.
IPR013845. Ribosomal_S4e_central_region.
IPR013843. Ribosomal_S4e_N.
IPR018199. Ribosomal_S4e_N_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERiPTHR11581. PTHR11581. 1 hit.
PfamiPF00467. KOW. 1 hit.
PF00900. Ribosomal_S4e. 1 hit.
PF08071. RS4NT. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
PIRSFiPIRSF002116. Ribosomal_S4. 1 hit.
ProDomiPD002667. Ribosomal_S4e_central. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00363. S4. 1 hit.
[Graphical view]
PROSITEiPS00528. RIBOSOMAL_S4E. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  4. "Rps4 maps near the inactivation center on the mouse X chromosome."
    Hamvas R.M., Zinn A.R., Keer J.T., Fisher E.M., Beer-Romero P., Brown S.D., Page D.C.
    Genomics 12:363-367(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 219-237.

Entry informationi

Entry nameiRS4X_MOUSE
AccessioniPrimary (citable) accession number: P62702
Secondary accession number(s): P12631
, P12750, P27576, P55831, Q14727, Q9CXN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.