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Protein

60S ribosomal protein L35a

Gene

Rpl35a

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

Functioni

Required for the proliferation and viability of hematopoietic cells. Plays a role in 60S ribosomal subunit formation. The protein was found to bind to both initiator and elongator tRNAs and consequently was assigned to the P site or P and A site.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-6791226. Major pathway of rRNA processing in the nucleolus.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L35a
Gene namesi
Name:Rpl35a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:1928894. Rpl35a.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: MGI
  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11011060S ribosomal protein L35aPRO_0000192798Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81N6-acetyllysineBy similarity
Modified residuei63 – 631N6-acetyllysine; alternateCombined sources
Modified residuei63 – 631N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO55142.
PaxDbiO55142.
PRIDEiO55142.
TopDownProteomicsiO55142.

PTM databases

iPTMnetiO55142.
PhosphoSiteiO55142.

Expressioni

Gene expression databases

BgeeiO55142.
CleanExiMM_RPL35A.
ExpressionAtlasiO55142. baseline and differential.
GenevisibleiO55142. MM.

Interactioni

Protein-protein interaction databases

BioGridi208332. 2 interactions.
IntActiO55142. 2 interactions.
MINTiMINT-1870227.
STRINGi10090.ENSMUSP00000077857.

Structurei

3D structure databases

ProteinModelPortaliO55142.
SMRiO55142. Positions 8-105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L35Ae family.Curated

Phylogenomic databases

eggNOGiKOG0887. Eukaryota.
COG2451. LUCA.
HOGENOMiHOG000195636.
HOVERGENiHBG054581.
InParanoidiO55142.
KOiK02917.
OMAiSTRLYSK.
OrthoDBiEOG741Z4R.
PhylomeDBiO55142.
TreeFamiTF300104.

Family and domain databases

InterProiIPR001780. Ribosomal_L35A.
IPR018266. Ribosomal_L35Ae_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PANTHERiPTHR10902. PTHR10902. 1 hit.
PfamiPF01247. Ribosomal_L35Ae. 1 hit.
[Graphical view]
ProDomiPD012670. Ribosomal_L35Ae. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50447. SSF50447. 1 hit.
PROSITEiPS01105. RIBOSOMAL_L35AE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O55142-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGRLWCKAI FAGYKRGLRN QREHTALLKI EGVYARDETE FYLGKRCAYV
60 70 80 90 100
YKAKNNTVTP GGKPNKTRVI WGKVTRAHGN SGMVRAKFRS NLPAKAIGHR
110
IRVMLYPSRI
Length:110
Mass (Da):12,554
Last modified:March 29, 2004 - v2
Checksum:i126B5E77E75F29F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16430 mRNA. Translation: CAA76215.2.
AK028214 mRNA. Translation: BAC25818.1.
CCDSiCCDS28126.1.
RefSeqiNP_001123956.1. NM_001130484.1.
NP_001123957.1. NM_001130485.1.
NP_067313.2. NM_021338.3.
UniGeneiMm.19355.

Genome annotation databases

EnsembliENSMUST00000078804; ENSMUSP00000077857; ENSMUSG00000060636.
ENSMUST00000115075; ENSMUSP00000110727; ENSMUSG00000060636.
ENSMUST00000115076; ENSMUSP00000110728; ENSMUSG00000060636.
ENSMUST00000115078; ENSMUSP00000110730; ENSMUSG00000060636.
ENSMUST00000115079; ENSMUSP00000110731; ENSMUSG00000060636.
GeneIDi57808.
KEGGimmu:57808.
UCSCiuc007yzu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y16430 mRNA. Translation: CAA76215.2.
AK028214 mRNA. Translation: BAC25818.1.
CCDSiCCDS28126.1.
RefSeqiNP_001123956.1. NM_001130484.1.
NP_001123957.1. NM_001130485.1.
NP_067313.2. NM_021338.3.
UniGeneiMm.19355.

3D structure databases

ProteinModelPortaliO55142.
SMRiO55142. Positions 8-105.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208332. 2 interactions.
IntActiO55142. 2 interactions.
MINTiMINT-1870227.
STRINGi10090.ENSMUSP00000077857.

PTM databases

iPTMnetiO55142.
PhosphoSiteiO55142.

Proteomic databases

EPDiO55142.
PaxDbiO55142.
PRIDEiO55142.
TopDownProteomicsiO55142.

Protocols and materials databases

DNASUi100505110.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000078804; ENSMUSP00000077857; ENSMUSG00000060636.
ENSMUST00000115075; ENSMUSP00000110727; ENSMUSG00000060636.
ENSMUST00000115076; ENSMUSP00000110728; ENSMUSG00000060636.
ENSMUST00000115078; ENSMUSP00000110730; ENSMUSG00000060636.
ENSMUST00000115079; ENSMUSP00000110731; ENSMUSG00000060636.
GeneIDi57808.
KEGGimmu:57808.
UCSCiuc007yzu.2. mouse.

Organism-specific databases

CTDi6165.
MGIiMGI:1928894. Rpl35a.

Phylogenomic databases

eggNOGiKOG0887. Eukaryota.
COG2451. LUCA.
HOGENOMiHOG000195636.
HOVERGENiHBG054581.
InParanoidiO55142.
KOiK02917.
OMAiSTRLYSK.
OrthoDBiEOG741Z4R.
PhylomeDBiO55142.
TreeFamiTF300104.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-6791226. Major pathway of rRNA processing in the nucleolus.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiO55142.
SOURCEiSearch...

Gene expression databases

BgeeiO55142.
CleanExiMM_RPL35A.
ExpressionAtlasiO55142. baseline and differential.
GenevisibleiO55142. MM.

Family and domain databases

InterProiIPR001780. Ribosomal_L35A.
IPR018266. Ribosomal_L35Ae_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PANTHERiPTHR10902. PTHR10902. 1 hit.
PfamiPF01247. Ribosomal_L35Ae. 1 hit.
[Graphical view]
ProDomiPD012670. Ribosomal_L35Ae. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50447. SSF50447. 1 hit.
PROSITEiPS01105. RIBOSOMAL_L35AE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing and expression of a cDNA encoding the mouse L35a ribosomal protein during differentiation of murine erythroleukemia (MEL) cells."
    Pappas I.S., Vizirianakis I.S., Tsiftsoglou A.S.
    Cell Biol. Int. 25:629-634(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: DBA/2J.
    Tissue: Erythroid cell.
  2. Vizirianakis I.S.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 53.
  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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pancreas and Spleen.
  5. "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-63, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRL35A_MOUSE
AccessioniPrimary (citable) accession number: O55142
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: March 29, 2004
Last modified: June 8, 2016
This is version 132 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
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.