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Protein

39S ribosomal protein L40, mitochondrial

Gene

Mrpl40

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: MGI
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 L40, mitochondrial
Short name:
L40mt
Short name:
MRP-L40
Alternative name(s):
Nuclear localization signal-containing protein deleted in velocardiofacial syndrome homolog
Gene namesi
Name:Mrpl40
Synonyms:Nlvcf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1332635. Mrpl40.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrial ribosome Source: UniProtKB
  2. mitochondrion Source: MGI
  3. nucleolus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646MitochondrionBy similarityAdd
BLAST
Chaini47 – 20616039S ribosomal protein L40, mitochondrialPRO_0000030559Add
BLAST

Proteomic databases

MaxQBiQ9Z2Q5.
PaxDbiQ9Z2Q5.
PRIDEiQ9Z2Q5.

PTM databases

PhosphoSiteiQ9Z2Q5.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9Z2Q5.
CleanExiMM_MRPL40.
ExpressionAtlasiQ9Z2Q5. baseline and differential.
GenevestigatoriQ9Z2Q5.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2Q5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiNOG331446.
GeneTreeiENSGT00390000010239.
HOGENOMiHOG000015976.
HOVERGENiHBG044505.
InParanoidiQ9Z2Q5.
KOiK17421.
OMAiLYKQQEH.
OrthoDBiEOG71VSVJ.
PhylomeDBiQ9Z2Q5.
TreeFamiTF105982.

Family and domain databases

InterProiIPR019192. Ribosomal_L28/L40_mit.
[Graphical view]
PfamiPF09812. MRP-L28. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9Z2Q5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATGVMLCAA RALRPRSWIP GTCQAHVRHT HQRASLLAFW DLIPMRAEPL
60 70 80 90 100
RKKKKVDPRK DQAAKDRLKK RIRKLEKASQ ELIPIEDFIT PVRFLDKSRQ
110 120 130 140 150
RPQEEHSPEE SERRALLLKR WALFKQQEHE MERDAIRSML EAQQEALEEL
160 170 180 190 200
KLESAELYAE AIKRDTSLFP FEKEGPHYTP PISNYQAPEG RYNDITKVYT

QVEFKR
Length:206
Mass (Da):24,301
Last modified:May 26, 2002 - v2
Checksum:i9AF9D8095D7B28D2
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti200 – 2001T → K.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF034092 mRNA. Translation: AAC70905.1.
BC028436 mRNA. Translation: AAH28436.1.
AK018757 mRNA. Translation: BAB31389.1.
CCDSiCCDS28030.1.
RefSeqiNP_035052.2. NM_010922.2.
UniGeneiMm.20918.

Genome annotation databases

EnsembliENSMUST00000023391; ENSMUSP00000023391; ENSMUSG00000022706.
GeneIDi18100.
KEGGimmu:18100.
UCSCiuc007yop.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF034092 mRNA. Translation: AAC70905.1.
BC028436 mRNA. Translation: AAH28436.1.
AK018757 mRNA. Translation: BAB31389.1.
CCDSiCCDS28030.1.
RefSeqiNP_035052.2. NM_010922.2.
UniGeneiMm.20918.

3D structure databases

ProteinModelPortaliQ9Z2Q5.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9Z2Q5.

Proteomic databases

MaxQBiQ9Z2Q5.
PaxDbiQ9Z2Q5.
PRIDEiQ9Z2Q5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023391; ENSMUSP00000023391; ENSMUSG00000022706.
GeneIDi18100.
KEGGimmu:18100.
UCSCiuc007yop.2. mouse.

Organism-specific databases

CTDi64976.
MGIiMGI:1332635. Mrpl40.

Phylogenomic databases

eggNOGiNOG331446.
GeneTreeiENSGT00390000010239.
HOGENOMiHOG000015976.
HOVERGENiHBG044505.
InParanoidiQ9Z2Q5.
KOiK17421.
OMAiLYKQQEH.
OrthoDBiEOG71VSVJ.
PhylomeDBiQ9Z2Q5.
TreeFamiTF105982.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi293263.
PROiQ9Z2Q5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z2Q5.
CleanExiMM_MRPL40.
ExpressionAtlasiQ9Z2Q5. baseline and differential.
GenevestigatoriQ9Z2Q5.

Family and domain databases

InterProiIPR019192. Ribosomal_L28/L40_mit.
[Graphical view]
PfamiPF09812. MRP-L28. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a human gene containing a nuclear localization signal from the critical region for velo-cardio-facial syndrome on 22q11."
    Funke B., Puech A., Saint-Jore B., Pandita R., Skoultchi A., Morrow B.
    Genomics 53:146-154(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT LYS-200.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  3. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-206.
    Strain: C57BL/6J.
    Tissue: Embryo.

Entry informationi

Entry nameiRM40_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2Q5
Secondary accession number(s): Q9CS52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 26, 2002
Last sequence update: May 26, 2002
Last modified: March 31, 2015
This is version 94 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

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.