Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P35980

- RL18_MOUSE

UniProt

P35980 - RL18_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

60S ribosomal protein L18

Gene

Rpl18

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

Functioni

GO - Molecular functioni

  1. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L18
Gene namesi
Name:Rpl18
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:98003. Rpl18.

Subcellular locationi

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: Ensembl
  2. nucleolus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 18818760S ribosomal protein L18PRO_0000132770Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301PhosphoserineBy similarity
Modified residuei158 – 1581PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP35980.
PaxDbiP35980.
PRIDEiP35980.

PTM databases

PhosphoSiteiP35980.

Expressioni

Gene expression databases

BgeeiP35980.
CleanExiMM_RPL18.
ExpressionAtlasiP35980. baseline and differential.
GenevestigatoriP35980.

Interactioni

Protein-protein interaction databases

BioGridi202968. 10 interactions.
IntActiP35980. 4 interactions.
MINTiMINT-1857698.

Structurei

3D structure databases

ProteinModelPortaliP35980.
SMRiP35980. Positions 20-140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18e family.Curated

Phylogenomic databases

eggNOGiCOG1727.
HOGENOMiHOG000213425.
HOVERGENiHBG000875.
InParanoidiP35980.
KOiK02883.
OMAiKVRRTEP.
OrthoDBiEOG7PS1GP.
PhylomeDBiP35980.
TreeFamiTF300202.

Family and domain databases

InterProiIPR000039. Ribosomal_L18e.
IPR021131. Ribosomal_L18e/L15P.
IPR021132. Ribosomal_L18e_CS.
[Graphical view]
PANTHERiPTHR10934. PTHR10934. 1 hit.
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiPS01106. RIBOSOMAL_L18E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P35980 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGVDIRHNKD RKVRRKEPKS QDIYLRLLVK LYRFLARRTN STFNQVVLKR
60 70 80 90 100
LFMSRTNRPP LSLSRMIRKM KLPGRENKTA VVVGTVTDDV RILEVPKLKV
110 120 130 140 150
CALRVSSRAR SRILKAGGKI LTFDQLALES PKGRGTVLLS GPRKGREVYR
160 170 180
HFGKAPGTPH SHTKPYVRSK GRKFERARGR RASRGYKN
Length:188
Mass (Da):21,645
Last modified:January 23, 2007 - v3
Checksum:i9489EFE201ABF7A1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 591P → S in AAA40067. (PubMed:8359697)Curated
Sequence conflicti109 – 1091A → V in AAA40067. (PubMed:8359697)Curated
Sequence conflicti115 – 1151K → R in BAB24923. (PubMed:16141072)Curated
Sequence conflicti116 – 1161A → G in AAA40067. (PubMed:8359697)Curated
Sequence conflicti147 – 1504EVYR → DVFP in AAA40067. (PubMed:8359697)Curated
Sequence conflicti155 – 1551A → V in AAA40067. (PubMed:8359697)Curated
Sequence conflicti160 – 1623HSH → YSQ in AAA40067. (PubMed:8359697)Curated
Sequence conflicti173 – 1742KF → RL in AAA40067. (PubMed:8359697)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04128 mRNA. Translation: AAA40067.1.
AK007263 mRNA. Translation: BAB24923.1.
AK009044 mRNA. Translation: BAB26043.1.
AK010510 mRNA. Translation: BAB26993.1.
AK012580 mRNA. Translation: BAB28332.1.
BC082290 mRNA. Translation: AAH82290.1.
CCDSiCCDS39958.1.
PIRiJN0779.
RefSeqiNP_033103.2. NM_009077.2.
XP_006540783.1. XM_006540720.1.
UniGeneiMm.3459.
Mm.422997.

Genome annotation databases

EnsembliENSMUST00000072503; ENSMUSP00000072320; ENSMUSG00000059070.
ENSMUST00000075178; ENSMUSP00000103365; ENSMUSG00000059070.
GeneIDi19899.
KEGGimmu:19899.
UCSCiuc009gww.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L04128 mRNA. Translation: AAA40067.1 .
AK007263 mRNA. Translation: BAB24923.1 .
AK009044 mRNA. Translation: BAB26043.1 .
AK010510 mRNA. Translation: BAB26993.1 .
AK012580 mRNA. Translation: BAB28332.1 .
BC082290 mRNA. Translation: AAH82290.1 .
CCDSi CCDS39958.1.
PIRi JN0779.
RefSeqi NP_033103.2. NM_009077.2.
XP_006540783.1. XM_006540720.1.
UniGenei Mm.3459.
Mm.422997.

3D structure databases

ProteinModelPortali P35980.
SMRi P35980. Positions 20-140.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202968. 10 interactions.
IntActi P35980. 4 interactions.
MINTi MINT-1857698.

PTM databases

PhosphoSitei P35980.

Proteomic databases

MaxQBi P35980.
PaxDbi P35980.
PRIDEi P35980.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000072503 ; ENSMUSP00000072320 ; ENSMUSG00000059070 .
ENSMUST00000075178 ; ENSMUSP00000103365 ; ENSMUSG00000059070 .
GeneIDi 19899.
KEGGi mmu:19899.
UCSCi uc009gww.1. mouse.

Organism-specific databases

CTDi 6141.
MGIi MGI:98003. Rpl18.

Phylogenomic databases

eggNOGi COG1727.
HOGENOMi HOG000213425.
HOVERGENi HBG000875.
InParanoidi P35980.
KOi K02883.
OMAi KVRRTEP.
OrthoDBi EOG7PS1GP.
PhylomeDBi P35980.
TreeFami TF300202.

Enzyme and pathway databases

Reactomei REACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

NextBioi 297433.
PROi P35980.
SOURCEi Search...

Gene expression databases

Bgeei P35980.
CleanExi MM_RPL18.
ExpressionAtlasi P35980. baseline and differential.
Genevestigatori P35980.

Family and domain databases

InterProi IPR000039. Ribosomal_L18e.
IPR021131. Ribosomal_L18e/L15P.
IPR021132. Ribosomal_L18e_CS.
[Graphical view ]
PANTHERi PTHR10934. PTHR10934. 1 hit.
Pfami PF00828. Ribosomal_L18e. 1 hit.
[Graphical view ]
SUPFAMi SSF52080. SSF52080. 1 hit.
PROSITEi PS01106. RIBOSOMAL_L18E. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of mouse cDNAs encoding ribosomal proteins L12 and L18."
    Hou E.W., Li S.S.L.
    Gene 130:287-290(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
    Tissue: Lung.
  2. "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: Embryo, Testis and Tongue.
  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-3.
    Tissue: Mammary gland.

Entry informationi

Entry nameiRL18_MOUSE
AccessioniPrimary (citable) accession number: P35980
Secondary accession number(s): Q9CQF1, Q9D987
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 111 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