Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q99N96 (RM01_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 66. 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
39S ribosomal protein L1, mitochondrial
Short name=L1mt
Short name=MRP-L1
Gene names
Name:Mrpl1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Mitochondrion By similarity.

Sequence similarities

Belongs to the ribosomal protein L1P family.

Sequence caution

The sequence AAH61042.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB26866.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAB26866.1 differs from that shown. Reason: Frameshift at position 7.

The sequence BAB40837.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: InterPro

   Cellular componentlarge ribosomal subunit

Inferred from electronic annotation. Source: InterPro

mitochondrion

Inferred from direct assay. Source: MGI

   Molecular functionRNA binding

Inferred from electronic annotation. Source: InterPro

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5050Mitochondrion Potential
Chain51 – 33628639S ribosomal protein L1, mitochondrial
PRO_0000252441

Regions

Compositional bias44 – 507Poly-Ala

Amino acid modifications

Modified residue851Phosphoserine Ref.4

Experimental info

Sequence conflict561K → E in BAB26866. Ref.2
Sequence conflict941K → R in BAB26866. Ref.2
Sequence conflict1181D → G in BAB26866. Ref.2
Sequence conflict1311T → R in BAB26866. Ref.2
Sequence conflict1401K → R in BAB26866. Ref.2
Sequence conflict1801A → V in BAB26866. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q99N96 [UniParc].

Last modified June 16, 2009. Version 2.
Checksum: 328783081296B824

FASTA33637,597
        10         20         30         40         50         60 
MAAAVRCLRR VLIHHQRHCL CKMASQASLY PCSVNSLLHN RHFAAAAAAA TKPARKIKKG 

        70         80         90        100        110        120 
AKEKTSDEKP VDDIEKIKSY TYMESDPEDD VYLKRLYPRR IYEVEKAIHL LKKFQVLDFT 

       130        140        150        160        170        180 
NPKQGVYLDL TLDMALGKKK TVEPFASVIA LPHLFSSEVN KVAVFTANAS EIKIAEENGA 

       190        200        210        220        230        240 
AFAGGTDLVK KIMDDEVVVD FYVAVPEIMG ELNPLRKKLK KRFPKATRNS IGRDIPKMLE 

       250        260        270        280        290        300 
LFKTAHEIMV DEERQNFLST KIATLDMPSD QIAANLQAVI NEVCKHRPLN LGPFVVRAFL 

       310        320        330 
RSSTSEGLLL KTDSLLPKEA KTTEAETEET QTAEAA

« Hide

References

« Hide 'large scale' 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: 16141072] [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: 15489334] [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: 11279069] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-336.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00118237.
RefSeqNP_444388.2. NM_053158.2.
UniGeneMm.295499.

3D structure databases

ProteinModelPortalQ99N96.
SMRQ99N96. Positions 95-313.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ99N96.

PTM databases

PhosphoSiteQ99N96.

Proteomic databases

PRIDEQ99N96.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000036437; ENSMUSP00000037046; ENSMUSG00000029486.
ENSMUST00000117766; ENSMUSP00000112977; ENSMUSG00000029486.
GeneID94061.
KEGGmmu:94061.
UCSCuc008yfi.1. mouse.

Organism-specific databases

CTD65008.
MGIMGI:2137202. Mrpl1.

Phylogenomic databases

eggNOGroNOG09550.
HOGENOMHBG713326.
HOVERGENHBG061212.
InParanoidQ99N96.
OMAFEDYIEK.
OrthoDBEOG4K6G54.

Gene expression databases

ArrayExpressQ99N96.
BgeeQ99N96.
CleanExMM_MRPL1.
GenevestigatorQ99N96.
GermOnlineENSMUSG00000029486. Mus musculus.

Family and domain databases

InterProIPR016094. Ribosomal_L1_2-a/b-sand.
IPR016095. Ribosomal_L1_3-a/b-sand.
IPR024663. Ribosomal_L1_chr.
IPR005879. Ribosomal_L1_mit.
IPR023674. Ribosomal_L1_SF.
[Graphical view]
Gene3DG3DSA:3.30.190.20. Ribosomal_L1_2-a/b-sand. 2 hits.
G3DSA:3.40.50.790. Ribosomal_L1_3-a/b-sand. 1 hit.
PfamPF13003. MRL1. 1 hit.
[Graphical view]
SUPFAMSSF56808. Ribosomal_L1. 1 hit.
TIGRFAMsTIGR01170. RplA_mito. 1 hit.
ProtoNetSearch...

Other

NextBio352027.
SOURCESearch...

Entry information

Entry nameRM01_MOUSE
AccessionPrimary (citable) accession number: Q99N96
Secondary accession number(s): Q3UQP5, Q8K351, Q9CWW4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: June 16, 2009
Last modified: October 19, 2011
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents