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Entry version 122 (02 Jun 2021)
Sequence version 2 (10 Aug 2010)
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Protein

Ubiquitin-40S ribosomal protein S27a

Gene

ubqC

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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-48-linked is involved in protein degradation via the proteasome. 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 synthesized as a polyubiquitin precursor with exact head to tail repeats. Some ubiquitin genes contain a single copy of ubiquitin fused to a ribosomal protein. In D.discoideum there are 9 genes: ubqA: 5 copies of Ub and a final Asn; ubqB: 1 copy of Ub and ribosomal protein L40; ubqC: 1 copy of Ub and ribosomal protein S27A; ubqD: 3 copies of Ub and a final Leu; ubqF: 7 copies of Ub and a final Asn; ubqG: 5 copies of Ub and a final Leu; ubqH: 5 copies of Ub and a final Asn; ubqI: 4 copies of Ub and a final Asn; ubqJ: 4 copies of Ub and a final Asn.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri122 – 145C4-typeAdd BLAST24

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DDI-1169408, ISG15 antiviral mechanism
R-DDI-1358803, Downregulation of ERBB2:ERBB3 signaling
R-DDI-156827, L13a-mediated translational silencing of Ceruloplasmin expression
R-DDI-174048, APC/C:Cdc20 mediated degradation of Cyclin B
R-DDI-174084, Autodegradation of Cdh1 by Cdh1:APC/C
R-DDI-174113, SCF-beta-TrCP mediated degradation of Emi1
R-DDI-174154, APC/C:Cdc20 mediated degradation of Securin
R-DDI-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-DDI-174184, Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-DDI-179409, APC-Cdc20 mediated degradation of Nek2A
R-DDI-1799339, SRP-dependent cotranslational protein targeting to membrane
R-DDI-187577, SCF(Skp2)-mediated degradation of p27/p21
R-DDI-2467813, Separation of Sister Chromatids
R-DDI-2559582, Senescence-Associated Secretory Phenotype (SASP)
R-DDI-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-DDI-382556, ABC-family proteins mediated transport
R-DDI-450408, AUF1 (hnRNP D0) binds and destabilizes mRNA
R-DDI-4641258, Degradation of DVL
R-DDI-532668, N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-DDI-5358346, Hedgehog ligand biogenesis
R-DDI-5632684, Hedgehog 'on' state
R-DDI-5658442, Regulation of RAS by GAPs
R-DDI-5687128, MAPK6/MAPK4 signaling
R-DDI-5689603, UCH proteinases
R-DDI-5689877, Josephin domain DUBs
R-DDI-5689880, Ub-specific processing proteases
R-DDI-5689901, Metalloprotease DUBs
R-DDI-5696394, DNA Damage Recognition in GG-NER
R-DDI-5696395, Formation of Incision Complex in GG-NER
R-DDI-6781823, Formation of TC-NER Pre-Incision Complex
R-DDI-6782135, Dual incision in TC-NER
R-DDI-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-DDI-68949, Orc1 removal from chromatin
R-DDI-69017, CDK-mediated phosphorylation and removal of Cdc6
R-DDI-69231, Cyclin D associated events in G1
R-DDI-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-DDI-72649, Translation initiation complex formation
R-DDI-72689, Formation of a pool of free 40S subunits
R-DDI-72695, Formation of the ternary complex, and subsequently, the 43S complex
R-DDI-72702, Ribosomal scanning and start codon recognition
R-DDI-72706, GTP hydrolysis and joining of the 60S ribosomal subunit
R-DDI-8854050, FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-DDI-8866652, Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-DDI-8866654, E3 ubiquitin ligases ubiquitinate target proteins
R-DDI-8948751, Regulation of PTEN stability and activity
R-DDI-901032, ER Quality Control Compartment (ERQC)
R-DDI-9020702, Interleukin-1 signaling
R-DDI-9033241, Peroxisomal protein import
R-DDI-917729, Endosomal Sorting Complex Required For Transport (ESCRT)
R-DDI-917937, Iron uptake and transport
R-DDI-936440, Negative regulators of DDX58/IFIH1 signaling
R-DDI-937042, IRAK2 mediated activation of TAK1 complex
R-DDI-937072, TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-DDI-9646399, Aggrephagy
R-DDI-975163, IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-DDI-975956, Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-DDI-975957, Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
R-DDI-983168, Antigen processing: Ubiquitination & Proteasome degradation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ubiquitin-40S ribosomal protein S27a
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ubqC
ORF Names:DDB_G0276765
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiDictyostelium discoideum (Slime mold)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri44689 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaAmoebozoaEvoseaEumycetozoaDictyosteliaDictyostelialesDictyosteliaceaeDictyostelium
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002195 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componentsi: Chromosome 2, Unassembled WGS sequence

Organism-specific databases

Dictyostelium discoideum online informatics resource

More...
dictyBasei
DDB_G0276765, ubqC

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003964841 – 76UbiquitinAdd BLAST76
ChainiPRO_000013766977 – 15440S ribosomal protein S27aAdd BLAST78

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P14797

PRoteomics IDEntifications database

More...
PRIDEi
P14797

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
44689.DDB0191355

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P14797

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 75Ubiquitin-likePROSITE-ProRule annotationAdd BLAST75

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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 fingeri122 – 145C4-typeAdd BLAST24

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0004, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_010412_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P14797

Identification of Orthologs from Complete Genome Data

More...
OMAi
FMAQHAN

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P14797

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.20.25.660, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002906, Ribosomal_S27a
IPR011332, Ribosomal_zn-bd
IPR038582, S27a-like_sf
IPR000626, Ubiquitin-like_dom
IPR029071, Ubiquitin-like_domsf
IPR019954, Ubiquitin_CS
IPR019956, Ubiquitin_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01599, Ribosomal_S27, 1 hit
PF00240, ubiquitin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00348, UBIQUITIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01402, Ribosomal_S27, 1 hit
SM00213, UBQ, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54236, SSF54236, 1 hit
SSF57829, SSF57829, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00299, UBIQUITIN_1, 1 hit
PS50053, UBIQUITIN_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P14797-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQIFIKTLTG KTITLEVEGS DNIENVKAKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGGGKK KKKKTYATPK VLKRKLRKVK
110 120 130 140 150
LAVLKYYKFD ENGKIKRVLR ECPAETCGAG VFMAQHANRQ YCGKCHSTLV

KKSK
Length:154
Mass (Da):17,449
Last modified:August 10, 2010 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i99A0ECB5F1BC010F
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AAFI02000019 Genomic DNA Translation: EAL68884.1
M23750 mRNA Translation: AAA33264.1

Protein sequence database of the Protein Information Resource

More...
PIRi
E34080, UQDOR7

NCBI Reference Sequences

More...
RefSeqi
XP_642815.1, XM_637723.1

Genome annotation databases

Ensembl protists genome annotation project

More...
EnsemblProtistsi
EAL68884; EAL68884; DDB_G0276765

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8620678

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ddi:DDB_G0276765

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAFI02000019 Genomic DNA Translation: EAL68884.1
M23750 mRNA Translation: AAA33264.1
PIRiE34080, UQDOR7
RefSeqiXP_642815.1, XM_637723.1

3D structure databases

SMRiP14797
ModBaseiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0191355

Proteomic databases

PaxDbiP14797
PRIDEiP14797

Genome annotation databases

EnsemblProtistsiEAL68884; EAL68884; DDB_G0276765
GeneIDi8620678
KEGGiddi:DDB_G0276765

Organism-specific databases

dictyBaseiDDB_G0276765, ubqC

Phylogenomic databases

eggNOGiKOG0004, Eukaryota
HOGENOMiCLU_010412_2_0_1
InParanoidiP14797
OMAiFMAQHAN
PhylomeDBiP14797

Enzyme and pathway databases

ReactomeiR-DDI-1169408, ISG15 antiviral mechanism
R-DDI-1358803, Downregulation of ERBB2:ERBB3 signaling
R-DDI-156827, L13a-mediated translational silencing of Ceruloplasmin expression
R-DDI-174048, APC/C:Cdc20 mediated degradation of Cyclin B
R-DDI-174084, Autodegradation of Cdh1 by Cdh1:APC/C
R-DDI-174113, SCF-beta-TrCP mediated degradation of Emi1
R-DDI-174154, APC/C:Cdc20 mediated degradation of Securin
R-DDI-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-DDI-174184, Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-DDI-179409, APC-Cdc20 mediated degradation of Nek2A
R-DDI-1799339, SRP-dependent cotranslational protein targeting to membrane
R-DDI-187577, SCF(Skp2)-mediated degradation of p27/p21
R-DDI-2467813, Separation of Sister Chromatids
R-DDI-2559582, Senescence-Associated Secretory Phenotype (SASP)
R-DDI-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-DDI-382556, ABC-family proteins mediated transport
R-DDI-450408, AUF1 (hnRNP D0) binds and destabilizes mRNA
R-DDI-4641258, Degradation of DVL
R-DDI-532668, N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-DDI-5358346, Hedgehog ligand biogenesis
R-DDI-5632684, Hedgehog 'on' state
R-DDI-5658442, Regulation of RAS by GAPs
R-DDI-5687128, MAPK6/MAPK4 signaling
R-DDI-5689603, UCH proteinases
R-DDI-5689877, Josephin domain DUBs
R-DDI-5689880, Ub-specific processing proteases
R-DDI-5689901, Metalloprotease DUBs
R-DDI-5696394, DNA Damage Recognition in GG-NER
R-DDI-5696395, Formation of Incision Complex in GG-NER
R-DDI-6781823, Formation of TC-NER Pre-Incision Complex
R-DDI-6782135, Dual incision in TC-NER
R-DDI-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-DDI-68949, Orc1 removal from chromatin
R-DDI-69017, CDK-mediated phosphorylation and removal of Cdc6
R-DDI-69231, Cyclin D associated events in G1
R-DDI-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-DDI-72649, Translation initiation complex formation
R-DDI-72689, Formation of a pool of free 40S subunits
R-DDI-72695, Formation of the ternary complex, and subsequently, the 43S complex
R-DDI-72702, Ribosomal scanning and start codon recognition
R-DDI-72706, GTP hydrolysis and joining of the 60S ribosomal subunit
R-DDI-8854050, FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-DDI-8866652, Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-DDI-8866654, E3 ubiquitin ligases ubiquitinate target proteins
R-DDI-8948751, Regulation of PTEN stability and activity
R-DDI-901032, ER Quality Control Compartment (ERQC)
R-DDI-9020702, Interleukin-1 signaling
R-DDI-9033241, Peroxisomal protein import
R-DDI-917729, Endosomal Sorting Complex Required For Transport (ESCRT)
R-DDI-917937, Iron uptake and transport
R-DDI-936440, Negative regulators of DDX58/IFIH1 signaling
R-DDI-937042, IRAK2 mediated activation of TAK1 complex
R-DDI-937072, TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-DDI-9646399, Aggrephagy
R-DDI-975163, IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-DDI-975956, Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-DDI-975957, Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
R-DDI-983168, Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P14797

Family and domain databases

Gene3Di2.20.25.660, 1 hit
InterProiView protein in InterPro
IPR002906, Ribosomal_S27a
IPR011332, Ribosomal_zn-bd
IPR038582, S27a-like_sf
IPR000626, Ubiquitin-like_dom
IPR029071, Ubiquitin-like_domsf
IPR019954, Ubiquitin_CS
IPR019956, 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

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRS27A_DICDI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P14797
Secondary accession number(s): P08618
, Q54HH5, Q54L38, Q54SE1, Q54SP3, Q54UW7, Q54WJ3, Q550W7, Q55DZ5, Q86KQ4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: August 10, 2010
Last modified: June 2, 2021
This is version 122 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  3. SIMILARITY comments
    Index of protein domains and families
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