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Protein

60S ribosomal protein L14

Gene

Rpl14

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: MGI
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. ribosomal large subunit biogenesis Source: MGI
  2. rRNA processing Source: MGI
  3. 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 L14
Gene namesi
Name:Rpl14
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1914365. Rpl14.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosolic large ribosomal subunit Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. membrane Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 21721660S ribosomal protein L14PRO_0000132032Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei79 – 791N6-acetyllysineBy similarity
Modified residuei85 – 851N6-acetyllysine; alternate1 Publication
Modified residuei85 – 851N6-succinyllysine; alternate1 Publication
Modified residuei139 – 1391PhosphoserineBy similarity
Modified residuei206 – 2061N6-succinyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9CR57.
PaxDbiQ9CR57.
PRIDEiQ9CR57.

PTM databases

PhosphoSiteiQ9CR57.

Expressioni

Gene expression databases

BgeeiQ9CR57.
CleanExiMM_RPL14.
ExpressionAtlasiQ9CR57. baseline and differential.
GenevestigatoriQ9CR57.

Interactioni

Protein-protein interaction databases

BioGridi211949. 11 interactions.
IntActiQ9CR57. 5 interactions.
MINTiMINT-4132595.

Structurei

3D structure databases

ProteinModelPortaliQ9CR57.
SMRiQ9CR57. Positions 1-139.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati173 – 17751-1; approximate
Repeati178 – 18251-2
Repeati183 – 18751-3
Repeati188 – 19251-4
Repeati195 – 19732-1
Repeati198 – 20032-2

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni173 – 192204 X 5 AA tandem repeats of Q-K-A-[APS]-XAdd
BLAST
Regioni195 – 20062 X 3 AA tandem repeats of K-G-Q

Sequence similaritiesi

Belongs to the ribosomal protein L14e family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG2163.
GeneTreeiENSGT00390000007888.
HOGENOMiHOG000201693.
HOVERGENiHBG005187.
InParanoidiQ9CR57.
KOiK02875.
OMAiYVRAAWE.
OrthoDBiEOG7MD4S6.
TreeFamiTF314356.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR014722. Rib_L2_dom2.
IPR002784. Ribosomal_L14.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF01929. Ribosomal_L14e. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9CR57-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVFRRYVEVG RVAYISFGPH AGKLVAIVDV IDQNRALVDG PCTRVRRQAM
60 70 80 90 100
PFKCMQLTDF ILKFPHSARQ KYVRKAWEKA DINTKWAATR WAKKIDARER
110 120 130 140 150
KAKMTDFDRF KVMKAKKMRN RIIKTEVKKL QRAAILKASP KKAAVAKAAI
160 170 180 190 200
AAAAAAAAAK AKVPAKKATG PGKKAAGQKA PAQKAAGQKA APPAKGQKGQ
210
KTPAQKAPAP KAAGKKA
Length:217
Mass (Da):23,564
Last modified:January 22, 2007 - v3
Checksum:i1DB57CAA155D05A9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261A → T in BAB25272 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007807 mRNA. Translation: BAB25272.1.
AK012277 mRNA. Translation: BAB28136.1.
AK013912 mRNA. Translation: BAB29051.1.
CCDSiCCDS40809.1.
RefSeqiNP_080250.1. NM_025974.2.
UniGeneiMm.289810.

Genome annotation databases

EnsembliENSMUST00000165532; ENSMUSP00000131489; ENSMUSG00000025794.
GeneIDi67115.
KEGGimmu:67115.
UCSCiuc009scr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007807 mRNA. Translation: BAB25272.1.
AK012277 mRNA. Translation: BAB28136.1.
AK013912 mRNA. Translation: BAB29051.1.
CCDSiCCDS40809.1.
RefSeqiNP_080250.1. NM_025974.2.
UniGeneiMm.289810.

3D structure databases

ProteinModelPortaliQ9CR57.
SMRiQ9CR57. Positions 1-139.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211949. 11 interactions.
IntActiQ9CR57. 5 interactions.
MINTiMINT-4132595.

PTM databases

PhosphoSiteiQ9CR57.

Proteomic databases

MaxQBiQ9CR57.
PaxDbiQ9CR57.
PRIDEiQ9CR57.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000165532; ENSMUSP00000131489; ENSMUSG00000025794.
GeneIDi67115.
KEGGimmu:67115.
UCSCiuc009scr.1. mouse.

Organism-specific databases

CTDi9045.
MGIiMGI:1914365. Rpl14.

Phylogenomic databases

eggNOGiCOG2163.
GeneTreeiENSGT00390000007888.
HOGENOMiHOG000201693.
HOVERGENiHBG005187.
InParanoidiQ9CR57.
KOiK02875.
OMAiYVRAAWE.
OrthoDBiEOG7MD4S6.
TreeFamiTF314356.

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

NextBioi323609.
PROiQ9CR57.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CR57.
CleanExiMM_RPL14.
ExpressionAtlasiQ9CR57. baseline and differential.
GenevestigatoriQ9CR57.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiIPR014722. Rib_L2_dom2.
IPR002784. Ribosomal_L14.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamiPF01929. Ribosomal_L14e. 1 hit.
[Graphical view]
SUPFAMiSSF50104. SSF50104. 1 hit.
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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head and Pancreas.
  2. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-85, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-85 AND LYS-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRL14_MOUSE
AccessioniPrimary (citable) accession number: Q9CR57
Secondary accession number(s): Q9D8Q1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2004
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 91 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.