Skip Header

Contribute Send feedback
Read comments (?) or add your own

P62983 (RS27A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-40S ribosomal protein S27a
Alternative name(s):
Ubiquitin carboxyl extension protein 80

Cleaved into the following 2 chains:

  1. Ubiquitin
  2. 40S ribosomal protein S27a
Gene names
Name:Rps27a
Synonyms:Uba80, Ubcep1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length156 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. Ref.4

Ribosomal protein S27a is a component of the 40S subunit of the ribosome. Ref.4

Subunit structure

Ribosomal protein S27a is part of the 40S ribosomal subunit By similarity.

Subcellular location

Ubiquitin: Cytoplasm By similarity. Nucleus By similarity.

Miscellaneous

Ubiquitin is encoded by 4 different genes. Uba52 and Rps27a genes code for a single copy of ubiquitin fused to the ribosomal proteins L40 and S27a, respectively. UBB and UBC genes code for a polyubiquitin precursor with exact head to tail repeats, the number of repeats differ between species and strains.

Sequence similarities

In the N-terminal section; belongs to the ubiquitin family.

In the C-terminal section; belongs to the ribosomal protein S27Ae family.

Contains 1 ubiquitin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7676Ubiquitin
PRO_0000396479
Chain77 – 1568040S ribosomal protein S27a
PRO_0000137663

Regions

Domain1 – 7676Ubiquitin-like
Zinc finger121 – 14424C4-type
Compositional bias77 – 9923Lys-rich (highly basic)
Compositional bias78 – 10730Lys-rich

Sites

Binding site541Activating enzyme
Binding site721Activating enzyme
Site681Essential for function

Amino acid modifications

Modified residue571Phosphoserine Ref.3
Modified residue1041N6-acetyllysine By similarity
Modified residue1131N6-acetyllysine By similarity
Cross-link6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity

Sequences

Sequence LengthMass (Da)Tools
P62983 [UniParc].

Last modified August 10, 2010. Version 2.
Checksum: C11DC63DF3A904F3

FASTA15617,951
        10         20         30         40         50         60 
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 

        70         80         90        100        110        120 
IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL AVLKYYKVDE NGKISRLRRE 

       130        140        150 
CPSDECGAGV FMGSHFDRHY CGKCCLTYCF NKPEDK

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: Head and Kidney.
[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/6J and FVB/N.
Tissue: Liver and Mammary tumor.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, MASS SPECTROMETRY.
Tissue: Liver.
[4]"The emerging complexity of protein ubiquitination."
Komander D.
Biochem. Soc. Trans. 37:937-953(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK018706 mRNA. Translation: BAB31357.1.
BC002108 mRNA. Translation: AAH02108.1.
IPIIPI00470152.
RefSeqNP_001029037.1. NM_001033865.1.
NP_077239.1. NM_024277.2.
UniGeneMm.180003.
Mm.458088.

3D structure databases

ProteinModelPortalP62983.
SMRP62983. Positions 1-76, 102-150.
ModBaseSearch...

Protein-protein interaction databases

IntActP62983. 1 interaction.

PTM databases

PhosphoSiteP62983.

2D gel databases

REPRODUCTION-2DPAGEP62991.

Proteomic databases

PaxDbP62983.
PRIDEP62983.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102844; ENSMUSP00000099908; ENSMUSG00000020460.
ENSMUST00000102845; ENSMUSP00000099909; ENSMUSG00000020460.
GeneID78294.
KEGGmmu:78294.

Organism-specific databases

CTD6233.
MGIMGI:1925544. Rps27a.

Phylogenomic databases

eggNOGCOG5272.
HOVERGENHBG079153.
InParanoidP62983.
KOK02977.
OMAKKVYTTP.
OrthoDBEOG4PZJ82.

Enzyme and pathway databases

ReactomeREACT_109335. Circadian Clock.
REACT_115202. Signal Transduction.
REACT_24972. Circadian Clock (mouse).

Gene expression databases

ArrayExpressP62983.
BgeeP62983.
CleanExMM_RPS27A.
GenevestigatorP62991.
GermOnlineENSMUSG00000008348. Mus musculus.
ENSMUSG00000019505. Mus musculus.
ENSMUSG00000020460. Mus musculus.
ENSMUSG00000044285. Mus musculus.
ENSMUSG00000058838. Mus musculus.
ENSMUSG00000061390. Mus musculus.
ENSMUSG00000063789. Mus musculus.

Family and domain databases

InterProIPR002906. Ribosomal_S27a.
IPR000626. Ubiquitin.
IPR019954. Ubiquitin_CS.
IPR019956. Ubiquitin_subgr.
IPR019955. Ubiquitin_supergroup.
[Graphical view]
PfamPF01599. Ribosomal_S27. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PRINTSPR00348. UBIQUITIN.
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
PROSITEPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio348635.
SOURCESearch...

Entry information

Entry nameRS27A_MOUSE
AccessionPrimary (citable) accession number: P62983
Secondary accession number(s): P02248 expand/collapse secondary AC list , P02249, P02250, P49664, P62991, Q29120, Q62317, Q64223, Q8VCH1, Q91887, Q91888, Q9CXY4, Q9CZM0, Q9D1R5, Q9D2W3, Q9D8D9, Q9ET23, Q9ET24, Q9Z0H9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 10, 2010
Last modified: May 1, 2013
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents