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Protein

28S ribosomal protein S30, mitochondrial

Gene

Mrps30

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

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_292710. Mitochondrial translation elongation.
REACT_344470. Mitochondrial translation termination.
REACT_350780. Mitochondrial translation initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
28S ribosomal protein S30, mitochondrial
Short name:
MRP-S30
Short name:
S30mt
Gene namesi
Name:Mrps30
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1926237. Mrps30.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
  • ribosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 44244228S ribosomal protein S30, mitochondrialPRO_0000087721Add
BLAST

Proteomic databases

MaxQBiQ9D0G0.
PaxDbiQ9D0G0.
PRIDEiQ9D0G0.

PTM databases

PhosphoSiteiQ9D0G0.

Expressioni

Gene expression databases

BgeeiQ9D0G0.
CleanExiMM_MRPS30.
GenevisibleiQ9D0G0. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022245.

Structurei

3D structure databases

ProteinModelPortaliQ9D0G0.
SMRiQ9D0G0. Positions 40-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S30/L37 family.Curated

Phylogenomic databases

eggNOGiNOG241777.
GeneTreeiENSGT00390000001442.
HOGENOMiHOG000059255.
HOVERGENiHBG036127.
InParanoidiQ9D0G0.
KOiK17409.
OMAiKYVVYPQ.
OrthoDBiEOG7SR4M3.
PhylomeDBiQ9D0G0.
TreeFamiTF320686.

Family and domain databases

InterProiIPR010793. Ribosomal_L37/S30.
[Graphical view]
PfamiPF07147. PDCD9. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D0G0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAARYWKLV PRGRGLSQNA AAKASATAPE VRDLEVVATP VARYPPIVAS
60 70 80 90 100
MTADSKAARQ RRVQRWQATV HAAPSVDEKI RILTKMQFKK YVVHPQISAL
110 120 130 140 150
NADRWYQSFT KTVFVSGLPP APALSPPPPS LDLAALRAAV CDCILQEQVY
160 170 180 190 200
VRRRRPRSLF DRRQALASSI LDQVVRTLVN LLAPLNPVLS TAALDCKRSV
210 220 230 240 250
DFYWLRGEER IPAGHRKGHI DALRYQINDK PHNQIRISKQ LPEFVPLDYS
260 270 280 290 300
IPTEIPVMKC KPDKLPLFRR QYENSIFTGS KTADPCCYGH TQFHLIPDRL
310 320 330 340 350
KRERLIRQNQ AEQVEAVFRA NAIASLFAWT GAQAMYQGFW SEADVTRPFV
360 370 380 390 400
SQAVITDGKY FSFFCYQLNT LALTVQADQN NPRKNLCWGS QSQPLYETVE
410 420 430 440
DNDVKGFDDG TLLQIVHFLL NKPREDGAQL LASQEKELDL GP
Length:442
Mass (Da):49,939
Last modified:June 1, 2001 - v1
Checksum:iC35A540D3A524BCC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti121 – 1211A → T in AAH29784 (PubMed:15489334).Curated
Sequence conflicti127 – 1271P → SPS in AAH29784 (PubMed:15489334).Curated
Sequence conflicti155 – 1573RPR → QPG in AAH29784 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011476 mRNA. Translation: BAB27644.1.
AK151642 mRNA. Translation: BAE30572.1.
CT030257 Genomic DNA. Translation: CAQ51573.1.
BC029784 mRNA. Translation: AAH29784.1.
AL355719 mRNA. Translation: CAB90812.1.
CCDSiCCDS26794.1.
RefSeqiNP_067531.1. NM_021556.3.
UniGeneiMm.143810.

Genome annotation databases

EnsembliENSMUST00000022245; ENSMUSP00000022245; ENSMUSG00000021731.
GeneIDi59054.
KEGGimmu:59054.
UCSCiuc007ryr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011476 mRNA. Translation: BAB27644.1.
AK151642 mRNA. Translation: BAE30572.1.
CT030257 Genomic DNA. Translation: CAQ51573.1.
BC029784 mRNA. Translation: AAH29784.1.
AL355719 mRNA. Translation: CAB90812.1.
CCDSiCCDS26794.1.
RefSeqiNP_067531.1. NM_021556.3.
UniGeneiMm.143810.

3D structure databases

ProteinModelPortaliQ9D0G0.
SMRiQ9D0G0. Positions 40-426.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022245.

PTM databases

PhosphoSiteiQ9D0G0.

Proteomic databases

MaxQBiQ9D0G0.
PaxDbiQ9D0G0.
PRIDEiQ9D0G0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022245; ENSMUSP00000022245; ENSMUSG00000021731.
GeneIDi59054.
KEGGimmu:59054.
UCSCiuc007ryr.1. mouse.

Organism-specific databases

CTDi10884.
MGIiMGI:1926237. Mrps30.

Phylogenomic databases

eggNOGiNOG241777.
GeneTreeiENSGT00390000001442.
HOGENOMiHOG000059255.
HOVERGENiHBG036127.
InParanoidiQ9D0G0.
KOiK17409.
OMAiKYVVYPQ.
OrthoDBiEOG7SR4M3.
PhylomeDBiQ9D0G0.
TreeFamiTF320686.

Enzyme and pathway databases

ReactomeiREACT_292710. Mitochondrial translation elongation.
REACT_344470. Mitochondrial translation termination.
REACT_350780. Mitochondrial translation initiation.

Miscellaneous databases

ChiTaRSiMrps30. mouse.
NextBioi314698.
PROiQ9D0G0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0G0.
CleanExiMM_MRPS30.
GenevisibleiQ9D0G0. MM.

Family and domain databases

InterProiIPR010793. Ribosomal_L37/S30.
[Graphical view]
PfamiPF07147. PDCD9. 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/6J.
    Tissue: Bone marrow and Embryo.
  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].
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. The European IMAGE consortium
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 283-442.

Entry informationi

Entry nameiRT30_MOUSE
AccessioniPrimary (citable) accession number: Q9D0G0
Secondary accession number(s): B2KF79
, Q3U9U4, Q9CYS8, Q9JJQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 94 of the entry and version 1 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.