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Protein

40S ribosomal protein S28

Gene

Rps28

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S28
Gene namesi
Name:Rps28
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1859516. Rps28.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 696940S ribosomal protein S28PRO_0000136823Add
BLAST

Proteomic databases

EPDiP62858.
PaxDbiP62858.
PRIDEiP62858.

PTM databases

iPTMnetiP62858.
PhosphoSiteiP62858.

Expressioni

Gene expression databases

BgeeiP62858.
CleanExiMM_RPS28.
ExpressionAtlasiP62858. baseline and differential.
GenevisibleiP62858. MM.

Interactioni

Protein-protein interaction databases

BioGridi207567. 1 interaction.
IntActiP62858. 4 interactions.
MINTiMINT-1855217.
STRINGi10090.ENSMUSP00000110013.

Structurei

3D structure databases

ProteinModelPortaliP62858.
SMRiP62858. Positions 8-68.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S28e family.Curated

Phylogenomic databases

eggNOGiKOG3502. Eukaryota.
COG2053. LUCA.
HOVERGENiHBG000219.
InParanoidiP62858.
KOiK02979.
OMAiILCLLET.
OrthoDBiEOG7SN8GQ.
PhylomeDBiP62858.
TreeFamiTF300136.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00292. Ribosomal_S28e.
InterProiIPR012340. NA-bd_OB-fold.
IPR000289. Ribosomal_S28e.
IPR028626. Ribosomal_S28e_CS.
[Graphical view]
PANTHERiPTHR10769. PTHR10769. 1 hit.
PfamiPF01200. Ribosomal_S28e. 1 hit.
[Graphical view]
ProDomiPD005541. Ribosomal_S28e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiPS00961. RIBOSOMAL_S28E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P62858-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDTSRVQPIK LARVTKVLGR TGSQGQCTQV RVEFMDDTSR SIIRNVKGPV
60
REGDVLTLLE SEREARRLR
Length:69
Mass (Da):7,841
Last modified:August 16, 2004 - v1
Checksum:i49902FE9376EB74F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11248 mRNA. Translation: AAA19605.1.
AK002919 mRNA. Translation: BAB22456.1.
AF110520 Genomic DNA. Translation: AAC97967.1.
AF528162 Genomic DNA. Translation: AAO17375.1.
BC010987 mRNA. Translation: AAH10987.1.
BC090982 mRNA. Translation: AAH90982.1.
CCDSiCCDS37571.1.
RefSeqiNP_058540.1. NM_016844.2.
XP_006524687.1. XM_006524624.2.
XP_006525478.1. XM_006525415.2.
XP_006536723.1. XM_006536660.2.
XP_006537454.1. XM_006537391.2.
UniGeneiMm.352374.
Mm.353967.
Mm.371603.
Mm.393918.

Genome annotation databases

EnsembliENSMUST00000087342; ENSMUSP00000110013; ENSMUSG00000067288.
ENSMUST00000166693; ENSMUSP00000133642; ENSMUSG00000067288.
ENSMUST00000173019; ENSMUSP00000134615; ENSMUSG00000067288.
ENSMUST00000173844; ENSMUSP00000133357; ENSMUSG00000067288.
GeneIDi54127.
KEGGimmu:54127.
UCSCiuc008bzs.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11248 mRNA. Translation: AAA19605.1.
AK002919 mRNA. Translation: BAB22456.1.
AF110520 Genomic DNA. Translation: AAC97967.1.
AF528162 Genomic DNA. Translation: AAO17375.1.
BC010987 mRNA. Translation: AAH10987.1.
BC090982 mRNA. Translation: AAH90982.1.
CCDSiCCDS37571.1.
RefSeqiNP_058540.1. NM_016844.2.
XP_006524687.1. XM_006524624.2.
XP_006525478.1. XM_006525415.2.
XP_006536723.1. XM_006536660.2.
XP_006537454.1. XM_006537391.2.
UniGeneiMm.352374.
Mm.353967.
Mm.371603.
Mm.393918.

3D structure databases

ProteinModelPortaliP62858.
SMRiP62858. Positions 8-68.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207567. 1 interaction.
IntActiP62858. 4 interactions.
MINTiMINT-1855217.
STRINGi10090.ENSMUSP00000110013.

PTM databases

iPTMnetiP62858.
PhosphoSiteiP62858.

Proteomic databases

EPDiP62858.
PaxDbiP62858.
PRIDEiP62858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087342; ENSMUSP00000110013; ENSMUSG00000067288.
ENSMUST00000166693; ENSMUSP00000133642; ENSMUSG00000067288.
ENSMUST00000173019; ENSMUSP00000134615; ENSMUSG00000067288.
ENSMUST00000173844; ENSMUSP00000133357; ENSMUSG00000067288.
GeneIDi54127.
KEGGimmu:54127.
UCSCiuc008bzs.2. mouse.

Organism-specific databases

CTDi6234.
MGIiMGI:1859516. Rps28.

Phylogenomic databases

eggNOGiKOG3502. Eukaryota.
COG2053. LUCA.
HOVERGENiHBG000219.
InParanoidiP62858.
KOiK02979.
OMAiILCLLET.
OrthoDBiEOG7SN8GQ.
PhylomeDBiP62858.
TreeFamiTF300136.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiP62858.
SOURCEiSearch...

Gene expression databases

BgeeiP62858.
CleanExiMM_RPS28.
ExpressionAtlasiP62858. baseline and differential.
GenevisibleiP62858. MM.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_00292. Ribosomal_S28e.
InterProiIPR012340. NA-bd_OB-fold.
IPR000289. Ribosomal_S28e.
IPR028626. Ribosomal_S28e_CS.
[Graphical view]
PANTHERiPTHR10769. PTHR10769. 1 hit.
PfamiPF01200. Ribosomal_S28e. 1 hit.
[Graphical view]
ProDomiPD005541. Ribosomal_S28e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
PROSITEiPS00961. RIBOSOMAL_S28E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of mouse cDNA for ribosomal protein S28."
    Yotov W.V., St Arnaud R.
    Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  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: Kidney.
  3. "Sequence of the mouse major histocompatibility complex class II region."
    Rowen L., Qin S., Madan A., Loretz C., Hall J., James R., Dors M., Shaffer T., Abbasi N., Ratcliffe A., Dickhoff R., Lasky S., Hood L.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 129.
  4. "Genomic sequence analysis in the mouse T-complex region."
    Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D., Nagaraja R.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 129/Sv.
  5. "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].
    Tissue: Colon and Testis.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRS28_MOUSE
AccessioniPrimary (citable) accession number: P62858
Secondary accession number(s): P25112, Q5BKQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: June 8, 2016
This is version 108 of the entry and version 1 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

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 one 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.