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Protein

40S ribosomal protein S27-like

Gene

Rps27l

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

Functioni

Cofactori

Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri38 – 6023C4-typeSequence analysisAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S27-like
Gene namesi
Name:Rps27lImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1915191. Rps27l.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 848340S ribosomal protein S27-likePRO_0000149055Add
BLAST

Proteomic databases

EPDiQ6ZWY3.
MaxQBiQ6ZWY3.
PaxDbiQ6ZWY3.
PRIDEiQ6ZWY3.
TopDownProteomicsiQ6ZWY3.

PTM databases

iPTMnetiQ6ZWY3.
PhosphoSiteiQ6ZWY3.
SwissPalmiQ6ZWY3.

Expressioni

Gene expression databases

BgeeiQ6ZWY3.
CleanExiMM_RPS27L.
ExpressionAtlasiQ6ZWY3. baseline and differential.
GenevisibleiQ6ZWY3. MM.

Interactioni

Protein-protein interaction databases

BioGridi212553. 4 interactions.
IntActiQ6ZWY3. 3 interactions.
MINTiMINT-1858537.
STRINGi10090.ENSMUSP00000046016.

Structurei

3D structure databases

ProteinModelPortaliQ6ZWY3.
SMRiQ6ZWY3. Positions 2-83.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S27e family.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri38 – 6023C4-typeSequence analysisAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG1779. Eukaryota.
COG2051. LUCA.
GeneTreeiENSGT00390000013514.
HOVERGENiHBG000252.
InParanoidiQ6ZWY3.
OrthoDBiEOG78SQM9.
PhylomeDBiQ6ZWY3.
TreeFamiTF300265.

Family and domain databases

Gene3Di2.20.25.100. 1 hit.
HAMAPiMF_00371. Ribosomal_S27e.
InterProiIPR000592. Ribosomal_S27e.
IPR023407. Ribosomal_S27e_Zn-bd_dom.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PANTHERiPTHR11594. PTHR11594. 1 hit.
PfamiPF01667. Ribosomal_S27e. 1 hit.
[Graphical view]
ProDomiPD004466. Ribosomal_S27e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01168. RIBOSOMAL_S27E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q6ZWY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPLARDLLHP SLEEEKKKHK KKRLVQSPNS YFMDVKCPGC YKITTVFSHA
60 70 80
QTVVLCVGCS TVLCQPTGGK ARLTEGCSFR RKQH
Length:84
Mass (Da):9,477
Last modified:January 23, 2007 - v3
Checksum:i271CCACFBB269E38
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007689 mRNA. Translation: BAB25192.1.
AK011262 mRNA. Translation: BAB27503.1.
AK151083 mRNA. Translation: BAE30096.1.
BC058115 mRNA. Translation: AAH58115.1.
CCDSiCCDS40673.1.
RefSeqiNP_080743.1. NM_026467.4.
UniGeneiMm.30120.

Genome annotation databases

EnsembliENSMUST00000040917; ENSMUSP00000046016; ENSMUSG00000036781.
GeneIDi67941.
UCSCiuc009qfm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK007689 mRNA. Translation: BAB25192.1.
AK011262 mRNA. Translation: BAB27503.1.
AK151083 mRNA. Translation: BAE30096.1.
BC058115 mRNA. Translation: AAH58115.1.
CCDSiCCDS40673.1.
RefSeqiNP_080743.1. NM_026467.4.
UniGeneiMm.30120.

3D structure databases

ProteinModelPortaliQ6ZWY3.
SMRiQ6ZWY3. Positions 2-83.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212553. 4 interactions.
IntActiQ6ZWY3. 3 interactions.
MINTiMINT-1858537.
STRINGi10090.ENSMUSP00000046016.

PTM databases

iPTMnetiQ6ZWY3.
PhosphoSiteiQ6ZWY3.
SwissPalmiQ6ZWY3.

Proteomic databases

EPDiQ6ZWY3.
MaxQBiQ6ZWY3.
PaxDbiQ6ZWY3.
PRIDEiQ6ZWY3.
TopDownProteomicsiQ6ZWY3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040917; ENSMUSP00000046016; ENSMUSG00000036781.
GeneIDi67941.
UCSCiuc009qfm.1. mouse.

Organism-specific databases

CTDi51065.
MGIiMGI:1915191. Rps27l.

Phylogenomic databases

eggNOGiKOG1779. Eukaryota.
COG2051. LUCA.
GeneTreeiENSGT00390000013514.
HOVERGENiHBG000252.
InParanoidiQ6ZWY3.
OrthoDBiEOG78SQM9.
PhylomeDBiQ6ZWY3.
TreeFamiTF300265.

Miscellaneous databases

PROiQ6ZWY3.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZWY3.
CleanExiMM_RPS27L.
ExpressionAtlasiQ6ZWY3. baseline and differential.
GenevisibleiQ6ZWY3. MM.

Family and domain databases

Gene3Di2.20.25.100. 1 hit.
HAMAPiMF_00371. Ribosomal_S27e.
InterProiIPR000592. Ribosomal_S27e.
IPR023407. Ribosomal_S27e_Zn-bd_dom.
IPR011332. Ribosomal_zn-bd.
[Graphical view]
PANTHERiPTHR11594. PTHR11594. 1 hit.
PfamiPF01667. Ribosomal_S27e. 1 hit.
[Graphical view]
ProDomiPD004466. Ribosomal_S27e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiPS01168. RIBOSOMAL_S27E. 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 Pancreas.
  2. "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: C57BL/6JImported.
    Tissue: BrainImported.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Pancreas and Spleen.

Entry informationi

Entry nameiRS27L_MOUSE
AccessioniPrimary (citable) accession number: Q6ZWY3
Secondary accession number(s): Q3UB68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 101 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

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.