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UniProtKB - P39940 (RSP5_YEAST)

Entry version 207 (12 Aug 2020)
Sequence version 1 (01 Feb 1995)
Previous versions | rss
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Protein

E3 ubiquitin-protein ligase RSP5

Gene

RSP5

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Component of a RSP5 ubiquitin ligase complex which specifies polyubiquitination and intracellular trafficking of the general amino acid permease GAP1 as well as other cell surface proteins like GAP1, FUR4, MAL61, PMA1 and STE2. The RSP5-BUL1/2 complex is also necessary for the heat-shock element (HSE)-mediated gene expression, nitrogen starvation GLN3-dependent transcription, pressure-induced differential regulation of the two tryptophan permeases TAT1 and TAT2 and sorting efficiency into multivesicular bodies. Also acts on RBP1. Plays a role in tolerance to o-dinitrobenzene. Involved in actin cytoskeleton organization and dynamics. Ubiquitinates the LAS17-binding proteins LSB1 and PIN3/LSB2 without directing them for degradation and affects LAS17 levels in a SLA1-dependent and LSB1/2-independent manner.12 Publications

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.26

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei777Glycyl thioester intermediate1

<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 functionTransferase
Biological processUbl conjugation pathway

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		YEAST:G3O-30288-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.2.B9, 984

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-983168, Antigen processing: Ubiquitination & Proteasome degradation

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00143

Protein family/group databases

Transport Classification Database

More...TCDBi		3.A.31.1.1, the endosomal sorting complexes required for transport iii (escrt-iii) family
8.A.30.1.4, the nedd4-family interacting protein-2 (nedd4) family

<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:
E3 ubiquitin-protein ligase RSP5 (EC:2.3.2.26)
Alternative name(s):
HECT-type E3 ubiquitin transferase RSP5
Reverses SPT-phenotype protein 5
<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:RSP5
Synonyms:MDP1, NPI1
Ordered Locus Names:YER125W
ORF Names:SYGP-ORF41
<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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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
  • UP000002311 <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> Componenti: Chromosome V

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YER125W

Saccharomyces Genome Database

More...SGDi		S000000927, RSP5

<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 Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi516Y → A: Has subtle defects on both initial ubiquitination and chain elongation of substrate proteins. 1
Mutagenesisi521Y → A: Has defects on both initial ubiquitination and chain elongation of substrate proteins. 1
Mutagenesisi537I → D: Has defects on both initial ubiquitination and chain elongation of substrate proteins. 1
Mutagenesisi618F → D: Has defects on both initial ubiquitination and chain elongation of substrate proteins. 1
Mutagenesisi733L → S in RSP5-1; impairs ubiquitin-thioester formation and catalysis of substrate ubiquitination. 1 Publication1
Mutagenesisi777C → A: Loss of ubiquitination. 1 Publication1

<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_00001203351 – 809E3 ubiquitin-protein ligase RSP5Add BLAST809

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-linki258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

The ubiquitination appears to be the result of an intramolecular transfer of ubiquitin.

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P39940

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

More...PaxDbi		P39940

PRoteomics IDEntifications database

More...PRIDEi		P39940

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P39940

<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

Component of the RSP5-BUL1/2 ubiquitin ligase complex composed of at least RSP5 and BUL1 or BUL2.

Forms also a ternary complex with RUP1 and UBP2.

Interacts (via WW domains) with LSB1, PIN3/LSB2 and RCR1 (via PY motifs).

Interacts with HSE1, LAS17, ROG3, ROD1 and RVS167.

9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P39940
With#Exp.IntAct
ACK1 [Q07622]3EBI-16219,EBI-38674
ADE12 [P80210]2EBI-16219,EBI-14267
ALY1 [P36117]4EBI-16219,EBI-26358
ALY2 [P47029]5EBI-16219,EBI-25974
ART10 [P18634]5EBI-16219,EBI-27197
ART5 [P53244]4EBI-16219,EBI-23201
BNA5 [Q05979]2EBI-16219,EBI-10016
BUL1 [P48524]4EBI-16219,EBI-3881
CDC14 [Q00684]2EBI-16219,EBI-4192
CSR2 [Q12734]2EBI-16219,EBI-32379
CTA1 [P15202]2EBI-16219,EBI-4061
CUE5 [Q08412]3EBI-16219,EBI-37580
DIA1 [P54005]3EBI-16219,EBI-27668
DUS1 [P53759]2EBI-16219,EBI-27885
ECM21 [P38167]2EBI-16219,EBI-21359
ENO2 [P00925]2EBI-16219,EBI-6475
FMP46 [P36141]2EBI-16219,EBI-26445
GPH1 [P06738]2EBI-16219,EBI-13389
HEM12 [P32347]2EBI-16219,EBI-5711
IMA1 [P53051]2EBI-16219,EBI-10464
IPP1 [P00817]2EBI-16219,EBI-9338
LDB19 [Q12502]3EBI-16219,EBI-2113927
LSB1 [P53281]2EBI-16219,EBI-23329
LYS1 [P38998]3EBI-16219,EBI-10264
LYS4 [P49367]2EBI-16219,EBI-10276
MCR1 [P36060]2EBI-16219,EBI-10565
MLS1 [P30952]3EBI-16219,EBI-10428
NPL3 [Q01560]2EBI-16219,EBI-12114
NPT1 [P39683]2EBI-16219,EBI-12218
PCK1 [P10963]2EBI-16219,EBI-13770
PFK2 [P16862]3EBI-16219,EBI-9435
PMU1 [P36069]2EBI-16219,EBI-26862
PTP1 [P25044]2EBI-16219,EBI-14183
PYC1 [P11154]2EBI-16219,EBI-14358
RCR1 [P38212]3EBI-16219,EBI-21381
RCR2 [Q03446]2EBI-16219,EBI-18180
RGM1 [Q00453]2EBI-16219,EBI-15073
ROD1 [Q02805]3EBI-16219,EBI-15679
ROG3 [P43602]3EBI-16219,EBI-22976
RPB8 [P20436]3EBI-16219,EBI-15794
SNA3 [P14359]2EBI-16219,EBI-26122
SNA4 [Q07549]2EBI-16219,EBI-22078
STM1 [P39015]3EBI-16219,EBI-11238
THI13 [Q07748]2EBI-16219,EBI-36080
THI21 [Q08975]3EBI-16219,EBI-30327
THI5 [P43534]2EBI-16219,EBI-19221
TKL1 [P23254]2EBI-16219,EBI-19291
TRE1 [Q08919]3EBI-16219,EBI-31915
TY1A-PL [Q12162]2EBI-16219,EBI-36658
TY2B-DR1 [Q12472]2EBI-16219,EBI-35737
UBC6 [P33296]2EBI-16219,EBI-19745
YBR056W [P38081]3EBI-16219,EBI-21453
YCL021W [P25561]3EBI-16219,EBI-21696
YHR131C [P38835]3EBI-16219,EBI-24724
YIP5 [P53108]2EBI-16219,EBI-24051
YJL218W [P40892]2EBI-16219,EBI-26263
YJR096W [P47137]3EBI-16219,EBI-25572
YKR047W [P36140]2EBI-16219,EBI-26441

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		36869, 1254 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2921, RSP5-BUL1 ubiquitin ligase complex
CPX-2923, RSP5-BUL2 ubiquitin ligase complex

Database of interacting proteins

More...DIPi		DIP-2238N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P39940

Protein interaction database and analysis system

More...IntActi		P39940, 189 interactors

Molecular INTeraction database

More...MINTi		P39940

STRING: functional protein association networks

More...STRINGi		4932.YER125W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P39940, protein

<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

1809
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		P39940

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P39940

<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 – 105C2PROSITE-ProRule annotationAdd BLAST105
Domaini229 – 262WW 1PROSITE-ProRule annotationAdd BLAST34
Domaini331 – 364WW 2PROSITE-ProRule annotationAdd BLAST34
Domaini387 – 420WW 3PROSITE-ProRule annotationAdd BLAST34
Domaini705 – 809HECTPROSITE-ProRule annotationAdd BLAST105

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 biasi315 – 322Poly-Ala8

<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

Belongs to the RSP5/NEDD4 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0940, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_002173_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P39940

KEGG Orthology (KO)

More...KOi		K10591

Identification of Orthologs from Complete Genome Data

More...OMAi		TYWEKPT

Family and domain databases

Conserved Domains Database

More...CDDi		cd00078, HECTc, 1 hit
cd00201, WW, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.150, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000008, C2_dom
IPR035892, C2_domain_sf
IPR024928, E3_ub_ligase_SMURF1
IPR000569, HECT_dom
IPR035983, Hect_E3_ubiquitin_ligase
IPR001202, WW_dom
IPR036020, WW_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00168, C2, 1 hit
PF00632, HECT, 1 hit
PF00397, WW, 3 hits

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001569, E3_ub_ligase_SMURF1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00239, C2, 1 hit
SM00119, HECTc, 1 hit
SM00456, WW, 3 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51045, SSF51045, 3 hits
SSF56204, SSF56204, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50004, C2, 1 hit
PS50237, HECT, 1 hit
PS01159, WW_DOMAIN_1, 3 hits
PS50020, WW_DOMAIN_2, 3 hits

<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.

P39940-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPSSISVKLV AAESLYKRDV FRSPDPFAVL TIDGYQTKST SAAKKTLNPY 
        60         70         80         90        100
WNETFKFDDI NENSILTIQV FDQKKFKKKD QGFLGVVNVR VGDVLGHLDE 
       110        120        130        140        150
DTATSSGRPR EETITRDLKK SNDGMAVSGR LIVVLSKLPS SSPHSQAPSG 
       160        170        180        190        200
HTASSSTNTS STTRTNGHST SSTRNHSTSH PSRGTAQAVE STLQSGTTAA 
       210        220        230        240        250
TNTATTSHRS TNSTSSATRQ YSSFEDQYGR LPPGWERRTD NFGRTYYVDH 
       260        270        280        290        300
NTRTTTWKRP TLDQTEAERG NQLNANTELE RRQHRGRTLP GGSSDNSSVT 
       310        320        330        340        350
VQVGGGSNIP PVNGAAAAAF AATGGTTSGL GELPSGWEQR FTPEGRAYFV 
       360        370        380        390        400
DHNTRTTTWV DPRRQQYIRT YGPTNTTIQQ QPVSQLGPLP SGWEMRLTNT 
       410        420        430        440        450
ARVYFVDHNT KTTTWDDPRL PSSLDQNVPQ YKRDFRRKVI YFRSQPALRI 
       460        470        480        490        500
LPGQCHIKVR RKNIFEDAYQ EIMRQTPEDL KKRLMIKFDG EEGLDYGGVS 
       510        520        530        540        550
REFFFLLSHE MFNPFYCLFE YSAYDNYTIQ INPNSGINPE HLNYFKFIGR 
       560        570        580        590        600
VVGLGVFHRR FLDAFFVGAL YKMMLRKKVV LQDMEGVDAE VYNSLNWMLE 
       610        620        630        640        650
NSIDGVLDLT FSADDERFGE VVTVDLKPDG RNIEVTDGNK KEYVELYTQW 
       660        670        680        690        700
RIVDRVQEQF KAFMDGFNEL IPEDLVTVFD ERELELLIGG IAEIDIEDWK 
       710        720        730        740        750
KHTDYRGYQE SDEVIQWFWK CVSEWDNEQR ARLLQFTTGT SRIPVNGFKD 
       760        770        780        790        800
LQGSDGPRRF TIEKAGEVQQ LPKSHTCFNR VDLPQYVDYD SMKQKLTLAV 

EETIGFGQE
Length:809
Mass (Da):91,816
Last modified:February 1, 1995 - v1
<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:i6F1836384479E70F
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
U18916 Genomic DNA Translation: AAC03223.1
BK006939 Genomic DNA Translation: DAA07785.1

Protein sequence database of the Protein Information Resource

More...PIRi		S43217

NCBI Reference Sequences

More...RefSeqi		NP_011051.3, NM_001179015.3

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YER125W_mRNA; YER125W; YER125W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		856862

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YER125W

<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
U18916 Genomic DNA Translation: AAC03223.1
BK006939 Genomic DNA Translation: DAA07785.1
PIRiS43217
RefSeqiNP_011051.3, NM_001179015.3

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
3OLMX-ray2.50A384-809[»]
4LCDX-ray3.10A/B383-809[»]
5HPLX-ray2.31A/B430-809[»]
SMRiP39940
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi36869, 1254 interactors
ComplexPortaliCPX-2921, RSP5-BUL1 ubiquitin ligase complex
CPX-2923, RSP5-BUL2 ubiquitin ligase complex
DIPiDIP-2238N
ELMiP39940
IntActiP39940, 189 interactors
MINTiP39940
STRINGi4932.YER125W

Protein family/group databases

TCDBi3.A.31.1.1, the endosomal sorting complexes required for transport iii (escrt-iii) family
8.A.30.1.4, the nedd4-family interacting protein-2 (nedd4) family

PTM databases

iPTMnetiP39940

Proteomic databases

MaxQBiP39940
PaxDbiP39940
PRIDEiP39940

Genome annotation databases

EnsemblFungiiYER125W_mRNA; YER125W; YER125W
GeneIDi856862
KEGGisce:YER125W

Organism-specific databases

EuPathDBiFungiDB:YER125W
SGDiS000000927, RSP5

Phylogenomic databases

eggNOGiKOG0940, Eukaryota
HOGENOMiCLU_002173_0_0_1
InParanoidiP39940
KOiK10591
OMAiTYWEKPT

Enzyme and pathway databases

UniPathwayiUPA00143
BioCyciYEAST:G3O-30288-MONOMER
BRENDAi2.3.2.B9, 984
ReactomeiR-SCE-983168, Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

EvolutionaryTraceiP39940

Protein Ontology

More...PROi		PR:P39940
RNActiP39940, protein

Family and domain databases

CDDicd00078, HECTc, 1 hit
cd00201, WW, 3 hits
Gene3Di2.60.40.150, 1 hit
InterProiView protein in InterPro
IPR000008, C2_dom
IPR035892, C2_domain_sf
IPR024928, E3_ub_ligase_SMURF1
IPR000569, HECT_dom
IPR035983, Hect_E3_ubiquitin_ligase
IPR001202, WW_dom
IPR036020, WW_dom_sf
PfamiView protein in Pfam
PF00168, C2, 1 hit
PF00632, HECT, 1 hit
PF00397, WW, 3 hits
PIRSFiPIRSF001569, E3_ub_ligase_SMURF1, 1 hit
SMARTiView protein in SMART
SM00239, C2, 1 hit
SM00119, HECTc, 1 hit
SM00456, WW, 3 hits
SUPFAMiSSF51045, SSF51045, 3 hits
SSF56204, SSF56204, 1 hit
PROSITEiView protein in PROSITE
PS50004, C2, 1 hit
PS50237, HECT, 1 hit
PS01159, WW_DOMAIN_1, 3 hits
PS50020, WW_DOMAIN_2, 3 hits

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 nameiRSP5_YEAST
<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: P39940
Secondary accession number(s): D3DM31
<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: February 1, 1995
Last sequence update: February 1, 1995
Last modified: August 12, 2020
This is version 207 of the entry and version 1 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 programFungal 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, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names
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