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Q9CR57 (RL14_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 80. 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

Names and origin

Protein namesRecommended name:
60S ribosomal protein L14
Gene names
Name:Rpl14
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein L14e family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 21721660S ribosomal protein L14
PRO_0000132032

Regions

Repeat173 – 17751-1; approximate
Repeat178 – 18251-2
Repeat183 – 18751-3
Repeat188 – 19251-4
Repeat195 – 19732-1
Repeat198 – 20032-2
Region173 – 192204 X 5 AA tandem repeats of Q-K-A-[APS]-X
Region195 – 20062 X 3 AA tandem repeats of K-G-Q

Amino acid modifications

Modified residue791N6-acetyllysine By similarity
Modified residue851N6-acetyllysine; alternate Ref.2
Modified residue851N6-succinyllysine; alternate Ref.2
Modified residue1391Phosphoserine By similarity
Modified residue2061N6-succinyllysine Ref.2

Experimental info

Sequence conflict261A → T in BAB25272. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CR57 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 1DB57CAA155D05A9

FASTA21723,564
        10         20         30         40         50         60 
MVFRRYVEVG RVAYISFGPH AGKLVAIVDV IDQNRALVDG PCTRVRRQAM PFKCMQLTDF 

        70         80         90        100        110        120 
ILKFPHSARQ KYVRKAWEKA DINTKWAATR WAKKIDARER KAKMTDFDRF KVMKAKKMRN 

       130        140        150        160        170        180 
RIIKTEVKKL QRAAILKASP KKAAVAKAAI AAAAAAAAAK AKVPAKKATG PGKKAAGQKA 

       190        200        210 
PAQKAAGQKA APPAKGQKGQ KTPAQKAPAP KAAGKKA 

« Hide

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] [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(2013) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK007807 mRNA. Translation: BAB25272.1.
AK012277 mRNA. Translation: BAB28136.1.
AK013912 mRNA. Translation: BAB29051.1.
RefSeqNP_080250.1. NM_025974.2.
UniGeneMm.289810.

3D structure databases

ProteinModelPortalQ9CR57.
SMRQ9CR57. Positions 1-139.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211949. 10 interactions.
IntActQ9CR57. 5 interactions.
MINTMINT-4132595.

PTM databases

PhosphoSiteQ9CR57.

Proteomic databases

PaxDbQ9CR57.
PRIDEQ9CR57.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000165532; ENSMUSP00000131489; ENSMUSG00000025794.
GeneID67115.
KEGGmmu:67115.
UCSCuc009scr.1. mouse.

Organism-specific databases

CTD9045.
MGIMGI:1914365. Rpl14.

Phylogenomic databases

eggNOGCOG2163.
GeneTreeENSGT00390000007888.
HOGENOMHOG000201693.
HOVERGENHBG005187.
InParanoidQ9CR57.
KOK02875.
OMAYVRAAWE.
OrthoDBEOG7MD4S6.
TreeFamTF314356.

Gene expression databases

ArrayExpressQ9CR57.
BgeeQ9CR57.
CleanExMM_RPL14.
GenevestigatorQ9CR57.

Family and domain databases

Gene3D2.30.30.30. 1 hit.
InterProIPR014722. Rib_L2_dom2.
IPR002784. Ribosomal_L14.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PfamPF01929. Ribosomal_L14e. 1 hit.
[Graphical view]
SUPFAMSSF50104. SSF50104. 1 hit.
ProtoNetSearch...

Other

NextBio323609.
PROQ9CR57.
SOURCESearch...

Entry information

Entry nameRL14_MOUSE
AccessionPrimary (citable) accession number: Q9CR57
Secondary accession number(s): Q9D8Q1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 80 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

MGD cross-references

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