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Protein

39S ribosomal protein L24, mitochondrial

Gene

Mrpl24

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

Functioni

GO - Molecular functioni

  1. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_292710. Mitochondrial translation elongation.
REACT_344470. Mitochondrial translation termination.
REACT_350780. Mitochondrial translation initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L24, mitochondrial
Short name:
L24mt
Short name:
MRP-L24
Gene namesi
Name:Mrpl24
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1914957. Mrpl24.

Subcellular locationi

  1. Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: MGI
  2. ribosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 99MitochondrionBy similarity
Chaini10 – 21620739S ribosomal protein L24, mitochondrialPRO_0000270489Add
BLAST

Proteomic databases

MaxQBiQ9CQ06.
PaxDbiQ9CQ06.
PRIDEiQ9CQ06.

PTM databases

PhosphoSiteiQ9CQ06.

Expressioni

Gene expression databases

BgeeiQ9CQ06.
CleanExiMM_MRPL24.
GenevestigatoriQ9CQ06.

Structurei

3D structure databases

ProteinModelPortaliQ9CQ06.
SMRiQ9CQ06. Positions 53-155.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 8934KOWAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein L24P family.Curated
Contains 1 KOW domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG325647.
GeneTreeiENSGT00390000014542.
HOGENOMiHOG000031326.
HOVERGENiHBG093899.
InParanoidiQ9CQ06.
KOiK02895.
OMAiGIQETRR.
OrthoDBiEOG7JQBP1.
PhylomeDBiQ9CQ06.
TreeFamiTF105984.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
HAMAPiMF_01326_B. Ribosomal_L24_B.
InterProiIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR003256. Ribosomal_L24.
IPR005825. Ribosomal_L24/26_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR12903. PTHR12903. 1 hit.
PfamiPF00467. KOW. 1 hit.
[Graphical view]
SMARTiSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
TIGRFAMsiTIGR01079. rplX_bact. 1 hit.
PROSITEiPS01108. RIBOSOMAL_L24. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9CQ06-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLSALLALA SKATSSPFYR YGMSRPGSIA DKRKNPPWSR RRPVVVEPIS
60 70 80 90 100
DEDWHLFCGD MVEILEGKDA GKQGKVVQVV RQRNWVVLEG LNTHYRYIGR
110 120 130 140 150
TKDHRGTMIA SEAPLLHHQV KLVDPVDRKP TEIQWRFTEA GERVRVSTRS
160 170 180 190 200
GRIIPKPEFP RADGIVPETW TDGPKDTSVE DALERTYVPR LKTLEEDVME
210
AMGIQETRRF KKVYWY
Length:216
Mass (Da):24,945
Last modified:June 1, 2001 - v1
Checksum:iDE869E7630AF599F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 93LAL → FAS in BAB25991 (PubMed:16141072).Curated
Sequence conflicti14 – 152TS → IC in BAB25991 (PubMed:16141072).Curated
Sequence conflicti26 – 272PG → RS in BAB25991 (PubMed:16141072).Curated
Sequence conflicti30 – 301A → G in BAB25991 (PubMed:16141072).Curated
Sequence conflicti34 – 341K → Q in BAB25991 (PubMed:16141072).Curated
Sequence conflicti42 – 421R → L in BAB22737 (PubMed:16141072).Curated
Sequence conflicti48 – 481P → A in BAB25991 (PubMed:16141072).Curated
Sequence conflicti116 – 1161L → F in BAB32014 (PubMed:16141072).Curated
Sequence conflicti143 – 1431R → L in BAB22737 (PubMed:16141072).Curated
Sequence conflicti177 – 1771T → I in BAB32014 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003362 mRNA. Translation: BAB22737.1.
AK008117 mRNA. Translation: BAB25472.1.
AK008961 mRNA. Translation: BAB25991.1.
AK013394 mRNA. Translation: BAB28828.1.
AK019976 mRNA. Translation: BAB31945.1.
AK020157 mRNA. Translation: BAB32014.1.
AK167623 mRNA. Translation: BAE39675.1.
BC004736 mRNA. Translation: AAH04736.1.
BC025506 mRNA. Translation: AAH25506.1.
BC031730 mRNA. Translation: AAH31730.1.
CCDSiCCDS38477.1.
RefSeqiNP_080867.2. NM_026591.3.
XP_006502002.1. XM_006501939.1.
XP_006502003.1. XM_006501940.1.
XP_006502004.1. XM_006501941.2.
XP_006502005.1. XM_006501942.2.
UniGeneiMm.393802.

Genome annotation databases

EnsembliENSMUST00000019854; ENSMUSP00000019854; ENSMUSG00000019710.
ENSMUST00000119968; ENSMUSP00000114111; ENSMUSG00000019710.
ENSMUST00000121048; ENSMUSP00000113959; ENSMUSG00000019710.
ENSMUST00000121920; ENSMUSP00000112885; ENSMUSG00000019710.
GeneIDi67707.
KEGGimmu:67707.
UCSCiuc008ptd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK003362 mRNA. Translation: BAB22737.1.
AK008117 mRNA. Translation: BAB25472.1.
AK008961 mRNA. Translation: BAB25991.1.
AK013394 mRNA. Translation: BAB28828.1.
AK019976 mRNA. Translation: BAB31945.1.
AK020157 mRNA. Translation: BAB32014.1.
AK167623 mRNA. Translation: BAE39675.1.
BC004736 mRNA. Translation: AAH04736.1.
BC025506 mRNA. Translation: AAH25506.1.
BC031730 mRNA. Translation: AAH31730.1.
CCDSiCCDS38477.1.
RefSeqiNP_080867.2. NM_026591.3.
XP_006502002.1. XM_006501939.1.
XP_006502003.1. XM_006501940.1.
XP_006502004.1. XM_006501941.2.
XP_006502005.1. XM_006501942.2.
UniGeneiMm.393802.

3D structure databases

ProteinModelPortaliQ9CQ06.
SMRiQ9CQ06. Positions 53-155.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9CQ06.

Proteomic databases

MaxQBiQ9CQ06.
PaxDbiQ9CQ06.
PRIDEiQ9CQ06.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000019854; ENSMUSP00000019854; ENSMUSG00000019710.
ENSMUST00000119968; ENSMUSP00000114111; ENSMUSG00000019710.
ENSMUST00000121048; ENSMUSP00000113959; ENSMUSG00000019710.
ENSMUST00000121920; ENSMUSP00000112885; ENSMUSG00000019710.
GeneIDi67707.
KEGGimmu:67707.
UCSCiuc008ptd.1. mouse.

Organism-specific databases

CTDi79590.
MGIiMGI:1914957. Mrpl24.

Phylogenomic databases

eggNOGiNOG325647.
GeneTreeiENSGT00390000014542.
HOGENOMiHOG000031326.
HOVERGENiHBG093899.
InParanoidiQ9CQ06.
KOiK02895.
OMAiGIQETRR.
OrthoDBiEOG7JQBP1.
PhylomeDBiQ9CQ06.
TreeFamiTF105984.

Enzyme and pathway databases

ReactomeiREACT_292710. Mitochondrial translation elongation.
REACT_344470. Mitochondrial translation termination.
REACT_350780. Mitochondrial translation initiation.

Miscellaneous databases

NextBioi325321.
PROiQ9CQ06.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQ06.
CleanExiMM_MRPL24.
GenevestigatoriQ9CQ06.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
HAMAPiMF_01326_B. Ribosomal_L24_B.
InterProiIPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR003256. Ribosomal_L24.
IPR005825. Ribosomal_L24/26_CS.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR12903. PTHR12903. 1 hit.
PfamiPF00467. KOW. 1 hit.
[Graphical view]
SMARTiSM00739. KOW. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
TIGRFAMsiTIGR01079. rplX_bact. 1 hit.
PROSITEiPS01108. RIBOSOMAL_L24. 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: Placenta, Small intestine, Stomach and Wolffian duct.
  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: Czech II and FVB/N.
    Tissue: Mammary gland.

Entry informationi

Entry nameiRM24_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ06
Secondary accession number(s): Q9CX51, Q9D1L7, Q9D7R6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 103 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

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.