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Protein

Ubiquitin-40S ribosomal protein S27a

Gene

ubi3

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed-Annotation score: Annotation score: 4 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, and DNA-damage responses. 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
Ribosomal protein S27a is a component of the 40S subunit of the ribosome.

Miscellaneous

Ubiquitin is encoded by several different genes. Ubi3 genes code for a single copy of ubiquitin fused to the ribosomal proteins S27a. Ubi4 is synthesized as a polyubiquitin precursor with 5 exact head to tail repeats.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri121 – 142C4-typeAdd BLAST22

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
Cleaved into the following 2 chains:
Gene namesi
Name:ubi3
Ordered Locus Names:KLLA0D18304g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
Proteomesi
  • UP000000598 Componenti: Chromosome D

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole 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_00001148571 – 76UbiquitinAdd BLAST76
ChainiPRO_000013768577 – 15040S ribosomal protein S27aAdd BLAST74

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
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)
Cross-linki76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PRIDEiP69061.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi284590.XP_453871.1.

Structurei

Secondary structure

1150
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi105 – 107Combined sources3
Beta strandi110 – 112Combined sources3
Beta strandi122 – 124Combined sources3
Beta strandi133 – 135Combined sources3
Beta strandi140 – 142Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J80electron microscopy3.75f1-150[»]
3J81electron microscopy4.00f1-150[»]
3JAMelectron microscopy3.46f1-150[»]
3JAPelectron microscopy4.90f1-150[»]
3JAQelectron microscopy6.00f1-150[»]
5IT7electron microscopy3.60f82-150[»]
5IT9electron microscopy3.80f82-150[»]
ProteinModelPortaliP69061.
SMRiP69061.
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

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 – 142C4-typeAdd BLAST22

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0004. Eukaryota.
COG5272. LUCA.
HOGENOMiHOG000233943.
InParanoidiP69061.
KOiK02977.
OMAiMSILKYY.
OrthoDBiEOG092C5P9Y.

Family and domain databases

InterProiView protein in InterPro
IPR002906. Ribosomal_S27a.
IPR011332. Ribosomal_zn-bd.
IPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
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.

P69061-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGGKKR KKKVYTTPKK IRHKHKKVKL
110 120 130 140 150
AVLNYYKVDD EGKVAKLRKE CPNCGPGIFL ANHGDRFYCG KCHSTFATQK
Length:150
Mass (Da):17,074
Last modified:August 10, 2010 - v2
Checksum:i4D7C82E923721474
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243802 Genomic DNA. Translation: CAB50894.1.
CR382124 Genomic DNA. Translation: CAH00967.1.
RefSeqiXP_453871.1. XM_453871.1.

Genome annotation databases

EnsemblFungiiCAH00967; CAH00967; KLLA0_D18304g.
GeneIDi2893475.
KEGGikla:KLLA0D18304g.

Similar proteinsi

Entry informationi

Entry nameiRS27A_KLULA
AccessioniPrimary (citable) accession number: P69061
Secondary accession number(s): Q6CQ09
, Q6CQB8, Q9Y848, Q9Y852
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: August 10, 2010
Last modified: September 27, 2017
This is version 68 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families