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P62301 (RS13_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S13
Gene names
Name:Rps13
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein S15P family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 15115040S ribosomal protein S13 HAMAP-Rule MF_01343_A
PRO_0000115662

Amino acid modifications

Modified residue271N6-acetyllysine; alternate By similarity
Modified residue271N6-succinyllysine; alternate Ref.2
Modified residue341N6-succinyllysine Ref.2
Modified residue381Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P62301 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 23F94D38F87B8D53

FASTA15117,222
        10         20         30         40         50         60 
MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI GVILRDSHGV 

        70         80         90        100        110        120 
AQVRFVTGNK ILRILKSKGL APDLPEDLYH LIKKAVAVRK HLERNRKDKD AKFRLILIES 

       130        140        150 
RIHRLARYYK TKRVLPPNWK YESSTASALV A 

« Hide

References

[1]"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. expand/collapse author list , 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.
[2]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-34, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK012479 mRNA. Translation: BAB28268.1.
AK018703 mRNA. Translation: BAB31354.1.
AK076060 mRNA. Translation: BAC36154.1.
CCDSCCDS52370.1.
RefSeqNP_080809.1. NM_026533.3.
XP_006544804.1. XM_006544741.1.
UniGeneMm.14798.
Mm.345443.
Mm.425541.

3D structure databases

ProteinModelPortalP62301.
SMRP62301. Positions 2-151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212630. 4 interactions.
DIPDIP-59976N.
MINTMINT-1863201.
STRING10090.ENSMUSP00000082124.

PTM databases

PhosphoSiteP62301.

Proteomic databases

MaxQBP62301.
PaxDbP62301.
PRIDEP62301.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000170953; ENSMUSP00000126294; ENSMUSG00000090862.
GeneID102642137.
68052.
KEGGmmu:102642137.
mmu:68052.
UCSCuc009jje.2. mouse.

Organism-specific databases

CTD6207.
MGIMGI:1915302. Rps13.

Phylogenomic databases

eggNOGCOG0184.
HOGENOMHOG000180723.
HOVERGENHBG000938.
InParanoidP62301.
KOK02953.
OMANWKYESA.
OrthoDBEOG7KH9MB.
PhylomeDBP62301.
TreeFamTF300190.

Gene expression databases

BgeeP62301.
CleanExMM_RPS13.
GenevestigatorP62301.

Family and domain databases

HAMAPMF_01343_A. Ribosomal_S15_A.
InterProIPR012606. Ribosomal_S13/S15_N.
IPR000589. Ribosomal_S15.
IPR023029. Ribosomal_S15P.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamPF08069. Ribosomal_S13_N. 1 hit.
PF00312. Ribosomal_S15. 1 hit.
[Graphical view]
SUPFAMSSF47060. SSF47060. 1 hit.
PROSITEPS00362. RIBOSOMAL_S15. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio326320.
PROP62301.
SOURCESearch...

Entry information

Entry nameRS13_MOUSE
AccessionPrimary (citable) accession number: P62301
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot