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Protein

28S ribosomal protein S35, mitochondrial

Gene

Mrps35

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

Functioni

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Names & Taxonomyi

Protein namesi
Recommended name:
28S ribosomal protein S35, mitochondrial
Short name:
MRP-S35
Short name:
S35mt
Gene namesi
Name:Mrps35Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2385255. Mrps35.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • mitochondrial small ribosomal subunit Source: UniProtKB
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 32028S ribosomal protein S35, mitochondrialPRO_0000046056
Transit peptidei1 – ?MitochondrionCurated

Proteomic databases

EPDiQ8BJZ4.
MaxQBiQ8BJZ4.
PaxDbiQ8BJZ4.
PeptideAtlasiQ8BJZ4.
PRIDEiQ8BJZ4.

PTM databases

iPTMnetiQ8BJZ4.
PhosphoSiteiQ8BJZ4.

Expressioni

Gene expression databases

BgeeiQ8BJZ4.
CleanExiMM_MRPS35.

Interactioni

Subunit structurei

Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000048348.

Structurei

3D structure databases

ProteinModelPortaliQ8BJZ4.
SMRiQ8BJZ4. Positions 46-320.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3933. Eukaryota.
ENOG410ZX0Y. LUCA.
HOGENOMiHOG000045127.
HOVERGENiHBG082941.
InParanoidiQ8BJZ4.
KOiK17413.
OrthoDBiEOG7QG44D.
PhylomeDBiQ8BJZ4.
TreeFamiTF318686.

Family and domain databases

InterProiIPR019349. Ribosomal_S24/S35_mit.
[Graphical view]
PfamiPF10213. MRP-S28. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8BJZ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAALQLRQ SLCPGPRVLR TFSSVASPAA PRAGPRTASR SERPMRRKAL
60 70 80 90 100
PPRTEKMDTD QDWPSVYPTA APFKPSAVPL PVRMGYPVKK GVPMAKEGNL
110 120 130 140 150
ELLKIPNFLH LTPVAIKRHC AALKDFCTEW PAALDSDEKC EEHFPVEIDT
160 170 180 190 200
ADYVSSGPSI RNPKARAVTL RVKLSSLNLD NHAKKKLIKL VGERYCKATD
210 220 230 240 250
VLTITTDRCP LKRQNYDYAV YLLTVLYHES WKTEDWENSK TEEDMDEYVW
260 270 280 290 300
AKSSSENSVL QTLLQMRAAE SSVAPSREEL LGTKEVEDYQ KCVVRLKNEG
310 320
ENEASLAQYK ESVKRLLNLA
Length:320
Mass (Da):35,975
Last modified:February 7, 2006 - v2
Checksum:i83A35D706DFB806E
GO

Sequence cautioni

The sequence AAH19964.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111S → T in BAC36950 (PubMed:16141072).Curated
Sequence conflicti11 – 111S → T in BAE41824 (PubMed:16141072).Curated
Sequence conflicti16 – 161P → A in BAC36950 (PubMed:16141072).Curated
Sequence conflicti16 – 161P → A in BAE41824 (PubMed:16141072).Curated
Sequence conflicti216 – 2161Y → C in BAC36950 (PubMed:16141072).Curated
Sequence conflicti216 – 2161Y → C in BAE41824 (PubMed:16141072).Curated
Sequence conflicti293 – 2931V → I in BAC36950 (PubMed:16141072).Curated
Sequence conflicti293 – 2931V → I in BAE41824 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077677 mRNA. Translation: BAC36950.1.
AK170480 mRNA. Translation: BAE41824.1.
CU207396 Genomic DNA. Translation: CAQ51866.1.
BC019964 mRNA. Translation: AAH19964.1. Different initiation.
CCDSiCCDS51959.1.
RefSeqiNP_663548.2. NM_145573.2.
UniGeneiMm.46656.

Genome annotation databases

GeneIDi232536.
KEGGimmu:232536.
UCSCiuc009ess.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK077677 mRNA. Translation: BAC36950.1.
AK170480 mRNA. Translation: BAE41824.1.
CU207396 Genomic DNA. Translation: CAQ51866.1.
BC019964 mRNA. Translation: AAH19964.1. Different initiation.
CCDSiCCDS51959.1.
RefSeqiNP_663548.2. NM_145573.2.
UniGeneiMm.46656.

3D structure databases

ProteinModelPortaliQ8BJZ4.
SMRiQ8BJZ4. Positions 46-320.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000048348.

PTM databases

iPTMnetiQ8BJZ4.
PhosphoSiteiQ8BJZ4.

Proteomic databases

EPDiQ8BJZ4.
MaxQBiQ8BJZ4.
PaxDbiQ8BJZ4.
PeptideAtlasiQ8BJZ4.
PRIDEiQ8BJZ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi232536.
KEGGimmu:232536.
UCSCiuc009ess.1. mouse.

Organism-specific databases

CTDi60488.
MGIiMGI:2385255. Mrps35.

Phylogenomic databases

eggNOGiKOG3933. Eukaryota.
ENOG410ZX0Y. LUCA.
HOGENOMiHOG000045127.
HOVERGENiHBG082941.
InParanoidiQ8BJZ4.
KOiK17413.
OrthoDBiEOG7QG44D.
PhylomeDBiQ8BJZ4.
TreeFamiTF318686.

Miscellaneous databases

PROiQ8BJZ4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BJZ4.
CleanExiMM_MRPS35.

Family and domain databases

InterProiIPR019349. Ribosomal_S24/S35_mit.
[Graphical view]
PfamiPF10213. MRP-S28. 1 hit.
[Graphical view]
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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported and NODImported.
    Tissue: EmbryoImported.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] OF 4-320.
    Strain: FVB/NImported.
    Tissue: LiverImported.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiRT35_MOUSE
AccessioniPrimary (citable) accession number: Q8BJZ4
Secondary accession number(s): B2KFS5, Q8VCG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 7, 2006
Last modified: July 6, 2016
This is version 90 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

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.