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Protein

Ubiquitin-40S ribosomal protein S27a

Gene

Rps27a

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity
40S Ribosomal protein S27a: Component of the 40S subunit of the ribosome.

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei54Activating enzyme1
Sitei68Essential for function1
Binding sitei72Activating enzyme1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri121 – 144C4-typeAdd BLAST24

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-40S ribosomal protein S27a
Alternative name(s):
Ubiquitin carboxyl extension protein 80
Cleaved into the following 2 chains:
Gene namesi
Name:Rps27a
Synonyms:Uba80, Ubcep1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componentsi: Chromosome 14, Chromosome 5

Organism-specific databases

RGDi6489478. Rps27a.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003964801 – 76UbiquitinAdd BLAST76
ChainiPRO_000013766477 – 15640S ribosomal protein S27aAdd BLAST80

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei65Phosphoserine; by PINK1By similarity1
Cross-linki76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
Modified residuei104N6-acetyllysineBy similarity1
Modified residuei113N6-acetyllysineBy similarity1
Modified residuei152N6-acetyllysineBy similarity1

Post-translational modificationi

Ubiquitin: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP62982.
PRIDEiP62982.

PTM databases

iPTMnetiP62982.
PhosphoSitePlusiP62982.

Expressioni

Gene expression databases

BgeeiENSRNOG00000004426.
ExpressionAtlasiP62982. baseline and differential.
GenevisibleiP62982. RN.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi249649. 1 interactor.
IntActiP62982. 2 interactors.
MINTiMINT-4575200.
STRINGi10116.ENSRNOP00000048664.

Structurei

3D structure databases

ProteinModelPortaliP62982.
SMRiP62982.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 76Ubiquitin-likePROSITE-ProRule annotationAdd BLAST76

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi77 – 99Lys-rich (highly basic)Add BLAST23
Compositional biasi78 – 107Lys-richAdd BLAST30

Sequence similaritiesi

In the N-terminal section; belongs to the ubiquitin family.Curated
In the C-terminal section; belongs to the eukaryotic ribosomal protein eS31 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri121 – 144C4-typeAdd BLAST24

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0004. Eukaryota.
COG5272. LUCA.
GeneTreeiENSGT00900000140945.
HOVERGENiHBG079153.
InParanoidiP62982.
KOiK02977.
OMAiMSILKYY.
OrthoDBiEOG091G178I.
PhylomeDBiP62982.
TreeFamiTF300036.

Family and domain databases

InterProiView protein in InterPro
IPR002906. Ribosomal_S27a.
IPR011332. Ribosomal_zn-bd.
IPR019956. Ubiquitin.
IPR029071. Ubiquitin-like_domsf.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
PfamiView protein in Pfam
PF01599. Ribosomal_S27. 1 hit.
PF00240. ubiquitin. 1 hit.
PRINTSiPR00348. UBIQUITIN.
SMARTiView protein in SMART
SM01402. Ribosomal_S27. 1 hit.
SM00213. UBQ. 1 hit.
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF57829. SSF57829. 1 hit.
PROSITEiView protein in PROSITE
PS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P62982-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL
110 120 130 140 150
AVLKYYKVDE NGKISRLRRE CPSDECGAGV FMGSHFDRHY CGKCCLTYCF

NKPEDK
Length:156
Mass (Da):17,951
Last modified:August 10, 2010 - v2
Checksum:iC11DC63DF3A904F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81839 mRNA. Translation: CAA57432.1.
PIRiI52328.
RefSeqiNP_001292372.1. NM_001305443.1.
NP_112375.1. NM_031113.2.
UniGeneiRn.106034.
Rn.144605.

Genome annotation databases

EnsembliENSRNOT00000005872; ENSRNOP00000005872; ENSRNOG00000004426.
ENSRNOT00000049535; ENSRNOP00000048664; ENSRNOG00000034246.
GeneIDi100912032.
KEGGirno:100912032.

Similar proteinsi

Entry informationi

Entry nameiRS27A_RAT
AccessioniPrimary (citable) accession number: P62982
Secondary accession number(s): P02248
, P02249, P02250, P49664, P62989, Q29120, Q63446, Q91887, Q91888, Q9D2W3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 10, 2010
Last modified: November 22, 2017
This is version 113 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families