Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

39S ribosomal protein L49, mitochondrial

Gene

Mrpl49

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-5389840. Mitochondrial translation elongation.
R-MMU-5419276. Mitochondrial translation termination.

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L49, mitochondrial
Short name:
L49mt
Short name:
MRP-L49
Gene namesi
Name:Mrpl49
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:108180. Mrpl49.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial ribosome Source: UniProtKB
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16616639S ribosomal protein L49, mitochondrialPRO_0000207666Add
BLAST

Proteomic databases

EPDiQ9CQ40.
MaxQBiQ9CQ40.
PaxDbiQ9CQ40.
PRIDEiQ9CQ40.

PTM databases

PhosphoSiteiQ9CQ40.

Expressioni

Gene expression databases

BgeeiQ9CQ40.
CleanExiMM_MRPL49.
GenevisibleiQ9CQ40. MM.

Interactioni

Subunit structurei

Interacts with OXA1L.By similarity

Protein-protein interaction databases

BioGridi201802. 1 interaction.
STRINGi10090.ENSMUSP00000007482.

Structurei

3D structure databases

ProteinModelPortaliQ9CQ40.
SMRiQ9CQ40. Positions 38-166.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L49em family.Curated

Phylogenomic databases

eggNOGiKOG4034. Eukaryota.
ENOG4111N34. LUCA.
GeneTreeiENSGT00390000017253.
HOGENOMiHOG000044600.
HOVERGENiHBG023124.
InParanoidiQ9CQ40.
KOiK17430.
OMAiKPPKHEH.
OrthoDBiEOG7G1V7M.
PhylomeDBiQ9CQ40.
TreeFamiTF317750.

Family and domain databases

InterProiIPR007740. Ribosomal_L49/IMG2.
[Graphical view]
PANTHERiPTHR13477. PTHR13477. 1 hit.
PfamiPF05046. Img2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CQ40-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAVLRAAL QDWRSCLGRS YGRRKLSQTQ GPPDNPGFVE SVDEYQFVER
60 70 80 90 100
LLPPTKIPEP PKHKHYPTPS GWQPPRDPLP SLPYFVRRSR MHNIPVYKEI
110 120 130 140 150
THGNRQMTLI RKVEGDIWAL QKDVEEFLSP LLGKTPITQV NEVTGTLRIK
160
GYFDEQLKAW LLEKGF
Length:166
Mass (Da):19,133
Last modified:June 1, 2001 - v1
Checksum:iCCF652F8403DA229
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521Y → N in BAC33922 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007712 mRNA. Translation: BAB25205.1.
AK014723 mRNA. Translation: BAB29520.1.
AK027949 mRNA. Translation: BAC25678.1.
AK049794 mRNA. Translation: BAC33922.1.
AK077397 mRNA. Translation: BAC36782.1.
AK150572 mRNA. Translation: BAE29667.1.
AK150715 mRNA. Translation: BAE29793.1.
BC028956 mRNA. Translation: AAH28956.1.
CCDSiCCDS29488.1.
RefSeqiNP_080522.1. NM_026246.3.
UniGeneiMm.181290.

Genome annotation databases

EnsembliENSMUST00000007482; ENSMUSP00000007482; ENSMUSG00000007338.
GeneIDi18120.
KEGGimmu:18120.
UCSCiuc008ggq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007712 mRNA. Translation: BAB25205.1.
AK014723 mRNA. Translation: BAB29520.1.
AK027949 mRNA. Translation: BAC25678.1.
AK049794 mRNA. Translation: BAC33922.1.
AK077397 mRNA. Translation: BAC36782.1.
AK150572 mRNA. Translation: BAE29667.1.
AK150715 mRNA. Translation: BAE29793.1.
BC028956 mRNA. Translation: AAH28956.1.
CCDSiCCDS29488.1.
RefSeqiNP_080522.1. NM_026246.3.
UniGeneiMm.181290.

3D structure databases

ProteinModelPortaliQ9CQ40.
SMRiQ9CQ40. Positions 38-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201802. 1 interaction.
STRINGi10090.ENSMUSP00000007482.

PTM databases

PhosphoSiteiQ9CQ40.

Proteomic databases

EPDiQ9CQ40.
MaxQBiQ9CQ40.
PaxDbiQ9CQ40.
PRIDEiQ9CQ40.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000007482; ENSMUSP00000007482; ENSMUSG00000007338.
GeneIDi18120.
KEGGimmu:18120.
UCSCiuc008ggq.1. mouse.

Organism-specific databases

CTDi740.
MGIiMGI:108180. Mrpl49.

Phylogenomic databases

eggNOGiKOG4034. Eukaryota.
ENOG4111N34. LUCA.
GeneTreeiENSGT00390000017253.
HOGENOMiHOG000044600.
HOVERGENiHBG023124.
InParanoidiQ9CQ40.
KOiK17430.
OMAiKPPKHEH.
OrthoDBiEOG7G1V7M.
PhylomeDBiQ9CQ40.
TreeFamiTF317750.

Enzyme and pathway databases

ReactomeiR-MMU-5389840. Mitochondrial translation elongation.
R-MMU-5419276. Mitochondrial translation termination.

Miscellaneous databases

NextBioi293332.
PROiQ9CQ40.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQ40.
CleanExiMM_MRPL49.
GenevisibleiQ9CQ40. MM.

Family and domain databases

InterProiIPR007740. Ribosomal_L49/IMG2.
[Graphical view]
PANTHERiPTHR13477. PTHR13477. 1 hit.
PfamiPF05046. Img2. 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: Bone marrow, Head and Pancreas.
  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].
    Tissue: Eye.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Spleen and Testis.

Entry informationi

Entry nameiRM49_MOUSE
AccessioniPrimary (citable) accession number: Q9CQ40
Secondary accession number(s): Q3UC21, Q8C5R0, Q8C7P3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 99 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.