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Protein

60S ribosomal protein L38

Gene

Rpl38

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

GO - Molecular functioni

GO - Biological processi

  • 90S preribosome assembly Source: MGI
  • axial mesoderm development Source: MGI
  • middle ear morphogenesis Source: MGI
  • ossification Source: MGI
  • regulation of translation Source: MGI
  • sensory perception of sound Source: MGI
  • skeletal system development Source: MGI
  • translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L38
Gene namesi
Name:Rpl38
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1914921. Rpl38.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 706960S ribosomal protein L38PRO_0000215436Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91N6-acetyllysineBy similarity
Modified residuei67 – 671N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9JJI8.
PaxDbiQ9JJI8.
PRIDEiQ9JJI8.

PTM databases

PhosphoSiteiQ9JJI8.

Expressioni

Gene expression databases

BgeeiQ9JJI8.
CleanExiMM_RPL38.
ExpressionAtlasiQ9JJI8. baseline and differential.
GenevestigatoriQ9JJI8.

Interactioni

Protein-protein interaction databases

BioGridi212354. 5 interactions.
IntActiQ9JJI8. 5 interactions.
MINTiMINT-1858856.

Structurei

3D structure databases

ProteinModelPortaliQ9JJI8.
SMRiQ9JJI8. Positions 2-70.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L38e family.Curated

Phylogenomic databases

eggNOGiNOG323549.
GeneTreeiENSGT00390000003718.
HOGENOMiHOG000188979.
HOVERGENiHBG001013.
InParanoidiQ9JJI8.
KOiK02923.
OMAiLYTLVIQ.
OrthoDBiEOG79W98H.
PhylomeDBiQ9JJI8.
TreeFamiTF300215.

Family and domain databases

InterProiIPR002675. Ribosomal_L38e.
[Graphical view]
PANTHERiPTHR10965. PTHR10965. 1 hit.
PfamiPF01781. Ribosomal_L38e. 1 hit.
[Graphical view]
ProDomiPD010361. Ribosomal_L38e. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

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

Q9JJI8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRKIEEIKD FLLTARRKDA KSVKIKKNKD NVKFKVRCSR YLYTLVITDK
60 70
EKAEKLKQSL PPGLAVKDLK
Length:70
Mass (Da):8,204
Last modified:January 23, 2007 - v3
Checksum:iFDD9A0B7BC98DBBA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037665 mRNA. Translation: BAB03500.1.
AK002659 mRNA. Translation: BAB22266.1.
AK010277 mRNA. Translation: BAB26814.1.
AK010518 mRNA. Translation: BAB27000.1.
AK012391 mRNA. Translation: BAB28208.1.
BC055346 mRNA. Translation: AAH55346.1.
CCDSiCCDS36365.1.
RefSeqiNP_001041522.1. NM_001048057.1.
NP_001041523.1. NM_001048058.1.
NP_075861.1. NM_023372.2.
XP_006534072.1. XM_006534009.2.
UniGeneiMm.238817.
Mm.371629.

Genome annotation databases

EnsembliENSMUST00000077915; ENSMUSP00000102211; ENSMUSG00000057322.
ENSMUST00000082092; ENSMUSP00000080741; ENSMUSG00000057322.
ENSMUST00000106599; ENSMUSP00000102209; ENSMUSG00000057322.
ENSMUST00000106602; ENSMUSP00000102213; ENSMUSG00000057322.
GeneIDi67671.
KEGGimmu:67671.
UCSCiuc007mfk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB037665 mRNA. Translation: BAB03500.1.
AK002659 mRNA. Translation: BAB22266.1.
AK010277 mRNA. Translation: BAB26814.1.
AK010518 mRNA. Translation: BAB27000.1.
AK012391 mRNA. Translation: BAB28208.1.
BC055346 mRNA. Translation: AAH55346.1.
CCDSiCCDS36365.1.
RefSeqiNP_001041522.1. NM_001048057.1.
NP_001041523.1. NM_001048058.1.
NP_075861.1. NM_023372.2.
XP_006534072.1. XM_006534009.2.
UniGeneiMm.238817.
Mm.371629.

3D structure databases

ProteinModelPortaliQ9JJI8.
SMRiQ9JJI8. Positions 2-70.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212354. 5 interactions.
IntActiQ9JJI8. 5 interactions.
MINTiMINT-1858856.

PTM databases

PhosphoSiteiQ9JJI8.

Proteomic databases

MaxQBiQ9JJI8.
PaxDbiQ9JJI8.
PRIDEiQ9JJI8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000077915; ENSMUSP00000102211; ENSMUSG00000057322.
ENSMUST00000082092; ENSMUSP00000080741; ENSMUSG00000057322.
ENSMUST00000106599; ENSMUSP00000102209; ENSMUSG00000057322.
ENSMUST00000106602; ENSMUSP00000102213; ENSMUSG00000057322.
GeneIDi67671.
KEGGimmu:67671.
UCSCiuc007mfk.1. mouse.

Organism-specific databases

CTDi6169.
MGIiMGI:1914921. Rpl38.

Phylogenomic databases

eggNOGiNOG323549.
GeneTreeiENSGT00390000003718.
HOGENOMiHOG000188979.
HOVERGENiHBG001013.
InParanoidiQ9JJI8.
KOiK02923.
OMAiLYTLVIQ.
OrthoDBiEOG79W98H.
PhylomeDBiQ9JJI8.
TreeFamiTF300215.

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

ChiTaRSiRpl38. mouse.
NextBioi325203.
PROiQ9JJI8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJI8.
CleanExiMM_RPL38.
ExpressionAtlasiQ9JJI8. baseline and differential.
GenevestigatoriQ9JJI8.

Family and domain databases

InterProiIPR002675. Ribosomal_L38e.
[Graphical view]
PANTHERiPTHR10965. PTHR10965. 1 hit.
PfamiPF01781. Ribosomal_L38e. 1 hit.
[Graphical view]
ProDomiPD010361. Ribosomal_L38e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Positional cloning of tail-short gene."
    Shimizu K.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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: Embryo, Embryonic stem cell and Kidney.
  3. "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: FVB/N-3.
    Tissue: Mammary gland.

Entry informationi

Entry nameiRL38_MOUSE
AccessioniPrimary (citable) accession number: Q9JJI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 107 of the entry and version 3 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.