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Protein

39S ribosomal protein L1, mitochondrial

Gene

Mrpl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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

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

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L1, mitochondrial
Short name:
L1mt
Short name:
MRP-L1
Gene namesi
Name:Mrpl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2137202. Mrpl1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial large ribosomal subunit Source: MGI
  • mitochondrion Source: MGI
  • nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5050MitochondrionSequence AnalysisAdd
BLAST
Chaini51 – 33628639S ribosomal protein L1, mitochondrialPRO_0000252441Add
BLAST

Proteomic databases

MaxQBiQ99N96.
PaxDbiQ99N96.
PRIDEiQ99N96.

PTM databases

PhosphoSiteiQ99N96.

Expressioni

Gene expression databases

BgeeiQ99N96.
CleanExiMM_MRPL1.
ExpressionAtlasiQ99N96. baseline and differential.
GenevisibleiQ99N96. MM.

Interactioni

Protein-protein interaction databases

BioGridi220433. 1 interaction.
IntActiQ99N96. 1 interaction.
MINTiMINT-4124547.
STRINGi10090.ENSMUSP00000037046.

Structurei

3D structure databases

ProteinModelPortaliQ99N96.
SMRiQ99N96. Positions 93-288.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi44 – 507Poly-Ala

Sequence similaritiesi

Belongs to the ribosomal protein L1P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0081.
GeneTreeiENSGT00390000003587.
HOGENOMiHOG000293225.
HOVERGENiHBG061212.
InParanoidiQ99N96.
KOiK02863.
OMAiLVPLKNK.
OrthoDBiEOG73BVDN.
PhylomeDBiQ99N96.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
InterProiIPR023674. Ribosomal_L1-like.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR024663. Ribosomal_L1_chr.
IPR005879. Ribosomal_L1_mit.
[Graphical view]
PfamiPF13003. MRL1. 1 hit.
[Graphical view]
SUPFAMiSSF56808. SSF56808. 1 hit.
TIGRFAMsiTIGR01170. rplA_mito. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q99N96-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAVRCLRR VLIHHQRHCL CKMASQASLY PCSVNSLLHN RHFAAAAAAA
60 70 80 90 100
TKPARKIKKG AKEKTSDEKP VDDIEKIKSY TYMESDPEDD VYLKRLYPRR
110 120 130 140 150
IYEVEKAIHL LKKFQVLDFT NPKQGVYLDL TLDMALGKKK TVEPFASVIA
160 170 180 190 200
LPHLFSSEVN KVAVFTANAS EIKIAEENGA AFAGGTDLVK KIMDDEVVVD
210 220 230 240 250
FYVAVPEIMG ELNPLRKKLK KRFPKATRNS IGRDIPKMLE LFKTAHEIMV
260 270 280 290 300
DEERQNFLST KIATLDMPSD QIAANLQAVI NEVCKHRPLN LGPFVVRAFL
310 320 330
RSSTSEGLLL KTDSLLPKEA KTTEAETEET QTAEAA
Length:336
Mass (Da):37,597
Last modified:June 16, 2009 - v2
Checksum:i328783081296B824
GO

Sequence cautioni

The sequence AAH61042.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB26866.1 differs from that shown. Reason: Frameshift at position 7. Curated
The sequence BAB26866.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB40837.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561K → E in BAB26866 (PubMed:15489334).Curated
Sequence conflicti94 – 941K → R in BAB26866 (PubMed:15489334).Curated
Sequence conflicti118 – 1181D → G in BAB26866 (PubMed:15489334).Curated
Sequence conflicti131 – 1311T → R in BAB26866 (PubMed:15489334).Curated
Sequence conflicti140 – 1401K → R in BAB26866 (PubMed:15489334).Curated
Sequence conflicti180 – 1801A → V in BAB26866 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010343 mRNA. Translation: BAB26866.1. Sequence problems.
AK142249 mRNA. Translation: BAE24994.1.
BC028774 mRNA. Translation: AAH28774.1.
BC061042 mRNA. Translation: AAH61042.1. Different initiation.
AB049632 mRNA. Translation: BAB40837.1. Different initiation.
CCDSiCCDS19449.1.
RefSeqiNP_444388.2. NM_053158.3.
XP_006535355.1. XM_006535292.1.
UniGeneiMm.295499.

Genome annotation databases

EnsembliENSMUST00000036437; ENSMUSP00000037046; ENSMUSG00000029486.
ENSMUST00000117766; ENSMUSP00000112977; ENSMUSG00000029486.
GeneIDi94061.
KEGGimmu:94061.
UCSCiuc008yfi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010343 mRNA. Translation: BAB26866.1. Sequence problems.
AK142249 mRNA. Translation: BAE24994.1.
BC028774 mRNA. Translation: AAH28774.1.
BC061042 mRNA. Translation: AAH61042.1. Different initiation.
AB049632 mRNA. Translation: BAB40837.1. Different initiation.
CCDSiCCDS19449.1.
RefSeqiNP_444388.2. NM_053158.3.
XP_006535355.1. XM_006535292.1.
UniGeneiMm.295499.

3D structure databases

ProteinModelPortaliQ99N96.
SMRiQ99N96. Positions 93-288.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220433. 1 interaction.
IntActiQ99N96. 1 interaction.
MINTiMINT-4124547.
STRINGi10090.ENSMUSP00000037046.

PTM databases

PhosphoSiteiQ99N96.

Proteomic databases

MaxQBiQ99N96.
PaxDbiQ99N96.
PRIDEiQ99N96.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036437; ENSMUSP00000037046; ENSMUSG00000029486.
ENSMUST00000117766; ENSMUSP00000112977; ENSMUSG00000029486.
GeneIDi94061.
KEGGimmu:94061.
UCSCiuc008yfi.1. mouse.

Organism-specific databases

CTDi65008.
MGIiMGI:2137202. Mrpl1.

Phylogenomic databases

eggNOGiCOG0081.
GeneTreeiENSGT00390000003587.
HOGENOMiHOG000293225.
HOVERGENiHBG061212.
InParanoidiQ99N96.
KOiK02863.
OMAiLVPLKNK.
OrthoDBiEOG73BVDN.
PhylomeDBiQ99N96.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi352027.
PROiQ99N96.
SOURCEiSearch...

Gene expression databases

BgeeiQ99N96.
CleanExiMM_MRPL1.
ExpressionAtlasiQ99N96. baseline and differential.
GenevisibleiQ99N96. MM.

Family and domain databases

Gene3Di3.30.190.20. 2 hits.
3.40.50.790. 1 hit.
InterProiIPR023674. Ribosomal_L1-like.
IPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR024663. Ribosomal_L1_chr.
IPR005879. Ribosomal_L1_mit.
[Graphical view]
PfamiPF13003. MRL1. 1 hit.
[Graphical view]
SUPFAMiSSF56808. SSF56808. 1 hit.
TIGRFAMsiTIGR01170. rplA_mito. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: Embryonic stem cell and Heart.
  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.
    Tissue: Mammary gland and Testis.
  3. "Structural compensation for the deficit of rRNA with proteins in the mammalian mitochondrial ribosome. Systematic analysis of protein components of the large ribosomal subunit from mammalian mitochondria."
    Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A., Watanabe K.
    J. Biol. Chem. 276:21724-21736(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-336.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiRM01_MOUSE
AccessioniPrimary (citable) accession number: Q99N96
Secondary accession number(s): Q3UQP5, Q8K351, Q9CWW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: June 16, 2009
Last modified: June 24, 2015
This is version 93 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.