Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P62983 (RS27A_MOUSE)

Entry version 144 (16 Oct 2019)
Sequence version 2 (10 Aug 2010)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Ubiquitin-40S ribosomal protein S27a

Gene

Rps27a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 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-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.1 Publication
40S Ribosomal protein S27a: Component of the 40S subunit of the ribosome.1 Publication

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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei54Activating enzyme1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei68Essential for function1
Binding sitei72Activating enzyme1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 fingeri121 – 144C4-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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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-MMU-110312 Translesion synthesis by REV1
R-MMU-110314 Recognition of DNA damage by PCNA-containing replication complex
R-MMU-110320 Translesion Synthesis by POLH
R-MMU-1169091 Activation of NF-kappaB in B cells
R-MMU-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-MMU-1253288 Downregulation of ERBB4 signaling
R-MMU-1295596 Spry regulation of FGF signaling
R-MMU-1358803 Downregulation of ERBB2:ERBB3 signaling
R-MMU-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-MMU-168638 NOD1/2 Signaling Pathway
R-MMU-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-MMU-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-MMU-174154 APC/C:Cdc20 mediated degradation of Securin
R-MMU-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-MMU-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-MMU-179409 APC-Cdc20 mediated degradation of Nek2A
R-MMU-1799339 SRP-dependent cotranslational protein targeting to membrane
R-MMU-182971 EGFR downregulation
R-MMU-187577 SCF(Skp2)-mediated degradation of p27/p21
R-MMU-195253 Degradation of beta-catenin by the destruction complex
R-MMU-201681 TCF dependent signaling in response to WNT
R-MMU-202424 Downstream TCR signaling
R-MMU-205043 NRIF signals cell death from the nucleus
R-MMU-209543 p75NTR recruits signalling complexes
R-MMU-209560 NF-kB is activated and signals survival
R-MMU-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-MMU-2173788 Downregulation of TGF-beta receptor signaling
R-MMU-2173791 TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-MMU-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-MMU-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-2559585 Oncogene Induced Senescence
R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-2672351 Stimuli-sensing channels
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-3134975 Regulation of innate immune responses to cytosolic DNA
R-MMU-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-MMU-3769402 Deactivation of the beta-catenin transactivating complex
R-MMU-382556 ABC-family proteins mediated transport
R-MMU-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-MMU-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-MMU-4608870 Asymmetric localization of PCP proteins
R-MMU-4641257 Degradation of AXIN
R-MMU-4641258 Degradation of DVL
R-MMU-4641263 Regulation of FZD by ubiquitination
R-MMU-5205685 Pink/Parkin Mediated Mitophagy
R-MMU-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-MMU-5357905 Regulation of TNFR1 signaling
R-MMU-5357956 TNFR1-induced NFkappaB signaling pathway
R-MMU-5358346 Hedgehog ligand biogenesis
R-MMU-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5610780 Degradation of GLI1 by the proteasome
R-MMU-5610785 GLI3 is processed to GLI3R by the proteasome
R-MMU-5632684 Hedgehog 'on' state
R-MMU-5654726 Negative regulation of FGFR1 signaling
R-MMU-5654727 Negative regulation of FGFR2 signaling
R-MMU-5654732 Negative regulation of FGFR3 signaling
R-MMU-5654733 Negative regulation of FGFR4 signaling
R-MMU-5655862 Translesion synthesis by POLK
R-MMU-5656121 Translesion synthesis by POLI
R-MMU-5656169 Termination of translesion DNA synthesis
R-MMU-5658442 Regulation of RAS by GAPs
R-MMU-5668541 TNFR2 non-canonical NF-kB pathway
R-MMU-5675221 Negative regulation of MAPK pathway
R-MMU-5675482 Regulation of necroptotic cell death
R-MMU-5676590 NIK-->noncanonical NF-kB signaling
R-MMU-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-MMU-5685942 HDR through Homologous Recombination (HRR)
R-MMU-5687128 MAPK6/MAPK4 signaling
R-MMU-5689603 UCH proteinases
R-MMU-5689877 Josephin domain DUBs
R-MMU-5689880 Ub-specific processing proteases
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-5689901 Metalloprotease DUBs
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693607 Processing of DNA double-strand break ends
R-MMU-5696394 DNA Damage Recognition in GG-NER
R-MMU-5696395 Formation of Incision Complex in GG-NER
R-MMU-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-MMU-5696400 Dual Incision in GG-NER
R-MMU-6781823 Formation of TC-NER Pre-Incision Complex
R-MMU-6782135 Dual incision in TC-NER
R-MMU-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-MMU-6783310 Fanconi Anemia Pathway
R-MMU-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-6804757 Regulation of TP53 Degradation
R-MMU-6804760 Regulation of TP53 Activity through Methylation
R-MMU-6807004 Negative regulation of MET activity
R-MMU-68827 CDT1 association with the CDC6:ORC:origin complex
R-MMU-68949 Orc1 removal from chromatin
R-MMU-69017 CDK-mediated phosphorylation and removal of Cdc6
R-MMU-69231 Cyclin D associated events in G1
R-MMU-69481 G2/M Checkpoints
R-MMU-69541 Stabilization of p53
R-MMU-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-MMU-72649 Translation initiation complex formation
R-MMU-72689 Formation of a pool of free 40S subunits
R-MMU-72695 Formation of the ternary complex, and subsequently, the 43S complex
R-MMU-72702 Ribosomal scanning and start codon recognition
R-MMU-72706 GTP hydrolysis and joining of the 60S ribosomal subunit
R-MMU-75815 Ubiquitin-dependent degradation of Cyclin D
R-MMU-8849469 PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-MMU-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis
R-MMU-8863795 Downregulation of ERBB2 signaling
R-MMU-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-MMU-8866654 E3 ubiquitin ligases ubiquitinate target proteins
R-MMU-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-8939902 Regulation of RUNX2 expression and activity
R-MMU-8941858 Regulation of RUNX3 expression and activity
R-MMU-8948747 Regulation of PTEN localization
R-MMU-8948751 Regulation of PTEN stability and activity
R-MMU-8951664 Neddylation
R-MMU-901032 ER Quality Control Compartment (ERQC)
R-MMU-9010553 Regulation of expression of SLITs and ROBOs
R-MMU-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus
R-MMU-9020702 Interleukin-1 signaling
R-MMU-9033241 Peroxisomal protein import
R-MMU-912631 Regulation of signaling by CBL
R-MMU-917729 Endosomal Sorting Complex Required For Transport (ESCRT)
R-MMU-917937 Iron uptake and transport
R-MMU-936440 Negative regulators of DDX58/IFIH1 signaling
R-MMU-936964 Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon
R-MMU-937041 IKK complex recruitment mediated by RIP1
R-MMU-937042 IRAK2 mediated activation of TAK1 complex
R-MMU-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-MMU-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-MMU-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-MMU-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
R-MMU-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_and_taxonomy_section">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
Alternative name(s):
Ubiquitin carboxyl extension protein 80
Cleaved into the following 2 chains:
Ubiquitin
40S ribosomal protein S27a
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Rps27a
Synonyms:Uba80, Ubcep1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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> Componenti: Chromosome 11

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:1925544 Rps27a

<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

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

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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003964791 – 76UbiquitinAdd BLAST76
ChainiPRO_000013766377 – 15640S ribosomal protein S27aAdd BLAST80

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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-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-linki27Glycyl 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
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei65Phosphoserine; by PINK1By similarity1
Modified residuei76ADP-ribosylglycineBy similarity1
Cross-linki76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation
Modified residuei104N6-acetyllysineBy similarity1
Modified residuei113N6-acetyllysineBy similarity1
Modified residuei152N6-acetyllysineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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
Ubiquitin: Mono-ADP-ribosylated at the C-terminus by PARP9, a component of the PPAR9-DTX3L complex. ADP-ribosylation requires processing by E1 and E2 enzymes and prevents ubiquitin conjugation to substrates such as histones.By similarity

Keywords - PTMi

Acetylation, ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P62983

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P62983

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

More...PaxDbi		P62983

PeptideAtlas

More...PeptideAtlasi		P62983

PRoteomics IDEntifications database

More...PRIDEi		P62983

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P62983

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		P62991

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P62983

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P62983

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P62983

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000020460 Expressed in 19 organ(s), highest expression level in female gonad

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P62983 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P62983 MM

<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_section">'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_section">'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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		219309, 19 interactors

Protein interaction database and analysis system

More...IntActi		P62983, 5 interactors

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000099909

<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

Secondary structure

1156
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P62983

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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_and_domains_section">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 – 76Ubiquitin-likePROSITE-ProRule annotationAdd BLAST76

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi77 – 99Lys-rich (highly basic)Add BLAST23
Compositional biasi78 – 107Lys-richAdd BLAST30

<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 fingeri121 – 144C4-typeAdd BLAST24

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0004 Eukaryota
COG5272 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00910000144152

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P62983

KEGG Orthology (KO)

More...KOi		K02977

Identification of Orthologs from Complete Genome Data

More...OMAi		GIFMANM

Database of Orthologous Groups

More...OrthoDBi		1536766at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P62983

TreeFam database of animal gene trees

More...TreeFami		TF300036

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
IPR019956 Ubiquitin
IPR029071 Ubiquitin-like_domsf
IPR019954 Ubiquitin_CS
IPR000626 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P62983-1 [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
<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:iC11DC63DF3A904F3
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
AK018706 mRNA Translation: BAB31357.1
BC002108 mRNA Translation: AAH02108.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS24497.1

NCBI Reference Sequences

More...RefSeqi		NP_001029037.1, NM_001033865.1
NP_077239.1, NM_024277.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000102844; ENSMUSP00000099908; ENSMUSG00000020460
ENSMUST00000102845; ENSMUSP00000099909; ENSMUSG00000020460

Database of genes from NCBI RefSeq genomes

More...GeneIDi		78294

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:78294

UCSC genome browser

More...UCSCi		uc007ihg.1 mouse

<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
AK018706 mRNA Translation: BAB31357.1
BC002108 mRNA Translation: AAH02108.1
CCDSiCCDS24497.1
RefSeqiNP_001029037.1, NM_001033865.1
NP_077239.1, NM_024277.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GVIX-ray1.87B1-76[»]
C1-72[»]
5XISX-ray1.78B/C/E/F1-76[»]
5XITX-ray2.25B/D/F/H1-76[»]
5XIUX-ray1.80B1-76[»]
SMRiP62983
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi219309, 19 interactors
IntActiP62983, 5 interactors
STRINGi10090.ENSMUSP00000099909

PTM databases

iPTMnetiP62983
PhosphoSitePlusiP62983
SwissPalmiP62983

2D gel databases

REPRODUCTION-2DPAGEiP62991

Proteomic databases

EPDiP62983
jPOSTiP62983
PaxDbiP62983
PeptideAtlasiP62983
PRIDEiP62983
TopDownProteomicsiP62983

Genome annotation databases

EnsembliENSMUST00000102844; ENSMUSP00000099908; ENSMUSG00000020460
ENSMUST00000102845; ENSMUSP00000099909; ENSMUSG00000020460
GeneIDi78294
KEGGimmu:78294
UCSCiuc007ihg.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		6233
MGIiMGI:1925544 Rps27a

Phylogenomic databases

eggNOGiKOG0004 Eukaryota
COG5272 LUCA
GeneTreeiENSGT00910000144152
InParanoidiP62983
KOiK02977
OMAiGIFMANM
OrthoDBi1536766at2759
PhylomeDBiP62983
TreeFamiTF300036

Enzyme and pathway databases

ReactomeiR-MMU-110312 Translesion synthesis by REV1
R-MMU-110314 Recognition of DNA damage by PCNA-containing replication complex
R-MMU-110320 Translesion Synthesis by POLH
R-MMU-1169091 Activation of NF-kappaB in B cells
R-MMU-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-MMU-1253288 Downregulation of ERBB4 signaling
R-MMU-1295596 Spry regulation of FGF signaling
R-MMU-1358803 Downregulation of ERBB2:ERBB3 signaling
R-MMU-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-MMU-168638 NOD1/2 Signaling Pathway
R-MMU-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-MMU-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-MMU-174154 APC/C:Cdc20 mediated degradation of Securin
R-MMU-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-MMU-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-MMU-179409 APC-Cdc20 mediated degradation of Nek2A
R-MMU-1799339 SRP-dependent cotranslational protein targeting to membrane
R-MMU-182971 EGFR downregulation
R-MMU-187577 SCF(Skp2)-mediated degradation of p27/p21
R-MMU-195253 Degradation of beta-catenin by the destruction complex
R-MMU-201681 TCF dependent signaling in response to WNT
R-MMU-202424 Downstream TCR signaling
R-MMU-205043 NRIF signals cell death from the nucleus
R-MMU-209543 p75NTR recruits signalling complexes
R-MMU-209560 NF-kB is activated and signals survival
R-MMU-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-MMU-2173788 Downregulation of TGF-beta receptor signaling
R-MMU-2173791 TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-MMU-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-MMU-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-2559585 Oncogene Induced Senescence
R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-2672351 Stimuli-sensing channels
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-3134975 Regulation of innate immune responses to cytosolic DNA
R-MMU-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-MMU-3769402 Deactivation of the beta-catenin transactivating complex
R-MMU-382556 ABC-family proteins mediated transport
R-MMU-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-MMU-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-MMU-4608870 Asymmetric localization of PCP proteins
R-MMU-4641257 Degradation of AXIN
R-MMU-4641258 Degradation of DVL
R-MMU-4641263 Regulation of FZD by ubiquitination
R-MMU-5205685 Pink/Parkin Mediated Mitophagy
R-MMU-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-MMU-5357905 Regulation of TNFR1 signaling
R-MMU-5357956 TNFR1-induced NFkappaB signaling pathway
R-MMU-5358346 Hedgehog ligand biogenesis
R-MMU-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5610780 Degradation of GLI1 by the proteasome
R-MMU-5610785 GLI3 is processed to GLI3R by the proteasome
R-MMU-5632684 Hedgehog 'on' state
R-MMU-5654726 Negative regulation of FGFR1 signaling
R-MMU-5654727 Negative regulation of FGFR2 signaling
R-MMU-5654732 Negative regulation of FGFR3 signaling
R-MMU-5654733 Negative regulation of FGFR4 signaling
R-MMU-5655862 Translesion synthesis by POLK
R-MMU-5656121 Translesion synthesis by POLI
R-MMU-5656169 Termination of translesion DNA synthesis
R-MMU-5658442 Regulation of RAS by GAPs
R-MMU-5668541 TNFR2 non-canonical NF-kB pathway
R-MMU-5675221 Negative regulation of MAPK pathway
R-MMU-5675482 Regulation of necroptotic cell death
R-MMU-5676590 NIK-->noncanonical NF-kB signaling
R-MMU-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-MMU-5685942 HDR through Homologous Recombination (HRR)
R-MMU-5687128 MAPK6/MAPK4 signaling
R-MMU-5689603 UCH proteinases
R-MMU-5689877 Josephin domain DUBs
R-MMU-5689880 Ub-specific processing proteases
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-5689901 Metalloprotease DUBs
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693607 Processing of DNA double-strand break ends
R-MMU-5696394 DNA Damage Recognition in GG-NER
R-MMU-5696395 Formation of Incision Complex in GG-NER
R-MMU-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-MMU-5696400 Dual Incision in GG-NER
R-MMU-6781823 Formation of TC-NER Pre-Incision Complex
R-MMU-6782135 Dual incision in TC-NER
R-MMU-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-MMU-6783310 Fanconi Anemia Pathway
R-MMU-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-6804757 Regulation of TP53 Degradation
R-MMU-6804760 Regulation of TP53 Activity through Methylation
R-MMU-6807004 Negative regulation of MET activity
R-MMU-68827 CDT1 association with the CDC6:ORC:origin complex
R-MMU-68949 Orc1 removal from chromatin
R-MMU-69017 CDK-mediated phosphorylation and removal of Cdc6
R-MMU-69231 Cyclin D associated events in G1
R-MMU-69481 G2/M Checkpoints
R-MMU-69541 Stabilization of p53
R-MMU-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-MMU-72649 Translation initiation complex formation
R-MMU-72689 Formation of a pool of free 40S subunits
R-MMU-72695 Formation of the ternary complex, and subsequently, the 43S complex
R-MMU-72702 Ribosomal scanning and start codon recognition
R-MMU-72706 GTP hydrolysis and joining of the 60S ribosomal subunit
R-MMU-75815 Ubiquitin-dependent degradation of Cyclin D
R-MMU-8849469 PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-MMU-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis
R-MMU-8863795 Downregulation of ERBB2 signaling
R-MMU-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-MMU-8866654 E3 ubiquitin ligases ubiquitinate target proteins
R-MMU-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-8939902 Regulation of RUNX2 expression and activity
R-MMU-8941858 Regulation of RUNX3 expression and activity
R-MMU-8948747 Regulation of PTEN localization
R-MMU-8948751 Regulation of PTEN stability and activity
R-MMU-8951664 Neddylation
R-MMU-901032 ER Quality Control Compartment (ERQC)
R-MMU-9010553 Regulation of expression of SLITs and ROBOs
R-MMU-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus
R-MMU-9020702 Interleukin-1 signaling
R-MMU-9033241 Peroxisomal protein import
R-MMU-912631 Regulation of signaling by CBL
R-MMU-917729 Endosomal Sorting Complex Required For Transport (ESCRT)
R-MMU-917937 Iron uptake and transport
R-MMU-936440 Negative regulators of DDX58/IFIH1 signaling
R-MMU-936964 Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon
R-MMU-937041 IKK complex recruitment mediated by RIP1
R-MMU-937042 IRAK2 mediated activation of TAK1 complex
R-MMU-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-MMU-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-MMU-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-MMU-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		Rps27a mouse

Protein Ontology

More...PROi		PR:P62983

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000020460 Expressed in 19 organ(s), highest expression level in female gonad
ExpressionAtlasiP62983 baseline and differential
GenevisibleiP62983 MM

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
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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<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_MOUSE
<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: P62983
Secondary accession number(s): P02248
, P02249, P02250, P49664, P62991, Q29120, Q62317, Q64223, Q8VCH1, Q91887, Q91888, Q9CXY4, Q9CZM0, Q9D1R5, Q9D2W3, Q9D8D9, Q9ET23, Q9ET24, Q9Z0H9
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 10, 2010
Last modified: October 16, 2019
This is version 144 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)
Annotation programChordata Protein Annotation Program

<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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again