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Entry version 202 (13 Nov 2019)
Sequence version 1 (01 Feb 1995)
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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_section">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_section">'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_section">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

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 functionTransferase
Biological processUbl conjugation pathway

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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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_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:
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_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: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_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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<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 identifieri559292 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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
  • UP000002311 <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 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_and_biotech_section">'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.<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_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-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_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

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_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

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_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Q076223EBI-16219,EBI-38674
P802102EBI-16219,EBI-14267
P361174EBI-16219,EBI-26358
P470295EBI-16219,EBI-25974
P186345EBI-16219,EBI-27197
P532444EBI-16219,EBI-23201
Q059792EBI-16219,EBI-10016
P485244EBI-16219,EBI-3881
Q006842EBI-16219,EBI-4192
Q127342EBI-16219,EBI-32379
P152022EBI-16219,EBI-4061
Q084123EBI-16219,EBI-37580
P540053EBI-16219,EBI-27668
P537592EBI-16219,EBI-27885
P381672EBI-16219,EBI-21359
P009252EBI-16219,EBI-6475
P361412EBI-16219,EBI-26445
P067382EBI-16219,EBI-13389
P323472EBI-16219,EBI-5711
P530512EBI-16219,EBI-10464
P008172EBI-16219,EBI-9338
Q125023EBI-16219,EBI-2113927
P532812EBI-16219,EBI-23329
P389983EBI-16219,EBI-10264
P493672EBI-16219,EBI-10276
P360602EBI-16219,EBI-10565
P309523EBI-16219,EBI-10428
Q015602EBI-16219,EBI-12114
P396832EBI-16219,EBI-12218
P109632EBI-16219,EBI-13770
P168623EBI-16219,EBI-9435
P360692EBI-16219,EBI-26862
P250442EBI-16219,EBI-14183
P111542EBI-16219,EBI-14358
P382123EBI-16219,EBI-21381
Q034462EBI-16219,EBI-18180
Q004532EBI-16219,EBI-15073
Q028053EBI-16219,EBI-15679
P436023EBI-16219,EBI-22976
P204363EBI-16219,EBI-15794
P143592EBI-16219,EBI-26122
Q075492EBI-16219,EBI-22078
P390153EBI-16219,EBI-11238
Q077482EBI-16219,EBI-36080
Q089753EBI-16219,EBI-30327
P435342EBI-16219,EBI-19221
P232542EBI-16219,EBI-19291
Q089193EBI-16219,EBI-31915
Q121622EBI-16219,EBI-36658
Q124722EBI-16219,EBI-35737
P332962EBI-16219,EBI-19745
P380813EBI-16219,EBI-21453
P255613EBI-16219,EBI-21696
P388353EBI-16219,EBI-24724
P531082EBI-16219,EBI-24051
P408922EBI-16219,EBI-26263
P471373EBI-16219,EBI-25572
P361402EBI-16219,EBI-26441

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
36869, 1250 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

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DIPi
DIP-2238N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P39940

Protein interaction database and analysis system

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IntActi
P39940, 189 interactors

Molecular INTeraction database

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MINTi
P39940

STRING: functional protein association networks

More...
STRINGi
4932.YER125W

<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

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SMRi
P39940

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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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_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 – 88C2PROSITE-ProRule annotationAdd BLAST88
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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000208451

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P39940

KEGG Orthology (KO)

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KOi
K10591

Identification of Orthologs from Complete Genome Data

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OMAi
TYWEKPT

Family and domain databases

Conserved Domains Database

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CDDi
cd00078 HECTc, 1 hit
cd00201 WW, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

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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

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

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51045 SSF51045, 3 hits
SSF56204 SSF56204, 1 hit

PROSITE; a protein domain and family database

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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_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.

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

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EMBLi

GenBank nucleotide sequence database

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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

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PIRi
S43217

NCBI Reference Sequences

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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

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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

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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, 1250 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

HOGENOMiHOG000208451
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

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PROi
PR:P39940

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

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ProtoNeti
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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 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_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: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 13, 2019
This is version 202 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, Complete proteome, Reference proteome

Documents

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