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Protein

60S ribosomal protein L24

Gene

Rpl24

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

  • exit from mitosis Source: MGI
  • mitotic cell cycle checkpoint Source: MGI
  • optic nerve development Source: MGI
  • retina development in camera-type eye Source: MGI
  • retinal ganglion cell axon guidance Source: MGI
  • ribosomal large subunit assembly Source: MGI
  • translation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L24
Gene namesi
Name:Rpl24
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1915443. Rpl24.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15715760S ribosomal protein L24PRO_0000136869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271N6-acetyllysine1 Publication
Modified residuei77 – 771N6-acetyllysineBy similarity
Modified residuei83 – 831PhosphothreonineBy similarity
Modified residuei86 – 861PhosphoserineBy similarity
Modified residuei93 – 931N6-acetyllysineBy similarity
Modified residuei131 – 1311N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BP67.
PaxDbiQ8BP67.
PRIDEiQ8BP67.

PTM databases

PhosphoSiteiQ8BP67.

Expressioni

Gene expression databases

BgeeiQ8BP67.
CleanExiMM_RPL24.
ExpressionAtlasiQ8BP67. baseline and differential.
GenevisibleiQ8BP67. MM.

Interactioni

Protein-protein interaction databases

BioGridi212718. 2 interactions.
IntActiQ8BP67. 5 interactions.
MINTiMINT-1857981.

Structurei

3D structure databases

ProteinModelPortaliQ8BP67.
SMRiQ8BP67. Positions 1-56.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L24e family.Curated

Phylogenomic databases

eggNOGiCOG2075.
GeneTreeiENSGT00550000074809.
HOVERGENiHBG001066.
InParanoidiQ8BP67.
KOiK02896.
OMAiFRVELCS.
TreeFamiTF312933.

Family and domain databases

Gene3Di2.30.170.20. 1 hit.
InterProiIPR000988. Ribosomal_L24e-rel.
IPR023442. Ribosomal_L24e_CS.
IPR023441. Ribosomal_L24e_dom.
IPR011017. TRASH_dom.
[Graphical view]
PANTHERiPTHR10792. PTHR10792. 1 hit.
PfamiPF01246. Ribosomal_L24e. 1 hit.
[Graphical view]
SMARTiSM00746. TRASH. 1 hit.
[Graphical view]
PROSITEiPS01073. RIBOSOMAL_L24E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BP67-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVELCSFSG YKIYPGHGRR YARTDGKVFQ FLNAKCESAF LSKRNPRQIN
60 70 80 90 100
WTVLYRRKHK KGQSEEIQKK RTRRAVKFQR AITGASLADI MAKRNQKPEV
110 120 130 140 150
RKAQREQAIR AAKEAKKAKQ ASKKTAMAAA KAPTKAAPKQ KIVKPVKVSA

PRVGGKR
Length:157
Mass (Da):17,779
Last modified:January 16, 2004 - v2
Checksum:i1D48EEB7C0652574
GO

Sequence cautioni

The sequence AAH02110.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141Y → N in BAC36903 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK018731 mRNA. Translation: BAB31374.1.
AK077617 mRNA. Translation: BAC36903.1.
BC002110 mRNA. Translation: AAH02110.2. Different initiation.
BC053377 mRNA. Translation: AAH53377.1.
BC058114 mRNA. Translation: AAH58114.1.
BC092008 mRNA. Translation: AAH92008.1.
CCDSiCCDS28218.1.
RefSeqiNP_077180.1. NM_024218.4.
UniGeneiMm.29221.
Mm.482104.

Genome annotation databases

EnsembliENSMUST00000023269; ENSMUSP00000023269; ENSMUSG00000098274.
GeneIDi68193.
KEGGimmu:68193.
UCSCiuc007zlv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK018731 mRNA. Translation: BAB31374.1.
AK077617 mRNA. Translation: BAC36903.1.
BC002110 mRNA. Translation: AAH02110.2. Different initiation.
BC053377 mRNA. Translation: AAH53377.1.
BC058114 mRNA. Translation: AAH58114.1.
BC092008 mRNA. Translation: AAH92008.1.
CCDSiCCDS28218.1.
RefSeqiNP_077180.1. NM_024218.4.
UniGeneiMm.29221.
Mm.482104.

3D structure databases

ProteinModelPortaliQ8BP67.
SMRiQ8BP67. Positions 1-56.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212718. 2 interactions.
IntActiQ8BP67. 5 interactions.
MINTiMINT-1857981.

PTM databases

PhosphoSiteiQ8BP67.

Proteomic databases

MaxQBiQ8BP67.
PaxDbiQ8BP67.
PRIDEiQ8BP67.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023269; ENSMUSP00000023269; ENSMUSG00000098274.
GeneIDi68193.
KEGGimmu:68193.
UCSCiuc007zlv.2. mouse.

Organism-specific databases

CTDi6152.
MGIiMGI:1915443. Rpl24.

Phylogenomic databases

eggNOGiCOG2075.
GeneTreeiENSGT00550000074809.
HOVERGENiHBG001066.
InParanoidiQ8BP67.
KOiK02896.
OMAiFRVELCS.
TreeFamiTF312933.

Miscellaneous databases

NextBioi326666.
PROiQ8BP67.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BP67.
CleanExiMM_RPL24.
ExpressionAtlasiQ8BP67. baseline and differential.
GenevisibleiQ8BP67. MM.

Family and domain databases

Gene3Di2.30.170.20. 1 hit.
InterProiIPR000988. Ribosomal_L24e-rel.
IPR023442. Ribosomal_L24e_CS.
IPR023441. Ribosomal_L24e_dom.
IPR011017. TRASH_dom.
[Graphical view]
PANTHERiPTHR10792. PTHR10792. 1 hit.
PfamiPF01246. Ribosomal_L24e. 1 hit.
[Graphical view]
SMARTiSM00746. TRASH. 1 hit.
[Graphical view]
PROSITEiPS01073. RIBOSOMAL_L24E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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: Embryo and Kidney.
  2. "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 and FVB/N.
    Tissue: Brain, Colon, Eye and Mammary gland.
  3. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRL24_MOUSE
AccessioniPrimary (citable) accession number: Q8BP67
Secondary accession number(s): P38663, Q58EA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: July 22, 2015
This is version 104 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.