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Entry version 199 (16 Oct 2019)
Sequence version 2 (01 Oct 1996)
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Protein

Ubiquitin carboxyl-terminal hydrolase 5

Gene

USP5

Organism
Homo sapiens (Human)
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

Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition.1 Publication

Miscellaneous

The UBP-type zinc finger domain crystallizes as a dimer linked by a disulfide bond between the Cys-195 residues of both molecules, but there is no evidence that the full-length USP5 exists as a dimer.

<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

  • Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). EC:3.4.19.12

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi199Zinc1
Metal bindingi202Zinc1
<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 sitei209Substrate1
Metal bindingi219Zinc1
Metal bindingi232Zinc1
Binding sitei259Substrate1
Binding sitei261Substrate; via carbonyl oxygen1
Binding sitei264Substrate1
<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 sitei335Nucleophile1
Active sitei818Proton acceptorPROSITE-ProRule annotation1

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 fingeri197 – 269UBP-typePROSITE-ProRule annotationAdd BLAST73

<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 functionHydrolase, Protease, Thiol protease
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.19.12 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-5689880 Ub-specific processing proteases
R-HSA-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes

Protein family/group databases

MEROPS protease database

More...
MEROPSi
C19.001

<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 carboxyl-terminal hydrolase 5 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 5
Isopeptidase T
Ubiquitin thioesterase 5
Ubiquitin-specific-processing protease 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:USP5
Synonyms:ISOT
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 12

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:12628 USP5

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
601447 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P45974

<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

<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>Mutagenesisi199C → A: Decreased rate of activity and decreased zinc binding. 1 Publication1
Mutagenesisi202C → A: Decreased rate of activity. 1 Publication1
Mutagenesisi219C → A: Decreased rate of activity. 1 Publication1
Mutagenesisi221 – 223RRY → KWF: Loss of polyubiquitin binding and subsequent activation. 1 Publication3
Mutagenesisi221R → A: Loss of polyubiquitin hydrolysis. Loss of ubiquitin binding; when associated with A-335. 1 Publication1
Mutagenesisi232H → A: Decreased rate of activity. 1 Publication1
Mutagenesisi261Y → F: Loss of polyubiquitin binding. 1 Publication1
Mutagenesisi335C → A: Loss of activity. Loss of ubiquitin binding; when associated with A-221. Lower affinity for triubiquitin and tetraubiquitin, but no effect on affinity for diubiquitin; when associated with E-666. Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with E-734. 1 Publication1
Mutagenesisi435D → A: Loss of polyubiquitin binding and hydrolysis. 1 Publication1
Mutagenesisi666M → E: Lower affinity for triubiquitin and tetraubiquitin, but no effect on affinity for diubiquitin; when associated with A-335. No effect on activity; when associated with E-734. 1 Publication1
Mutagenesisi734M → E: Lower affinity for diubiquitin, triubiquitin and tetraubiquitin; when associated with A-335. No effect on activity; when associated with E-666. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
8078

Open Targets

More...
OpenTargetsi
ENSG00000111667

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA37253

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P45974

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL6158

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2431

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
USP5

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1717869

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00000806232 – 858Ubiquitin carboxyl-terminal hydrolase 5Add BLAST857

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei2N-acetylalanineCombined sources1
Modified residuei156PhosphoserineCombined sources1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi195 ↔ 8161 Publication
Modified residuei292PhosphothreonineCombined sources1
Modified residuei623PhosphothreonineBy similarity1
Modified residuei779PhosphoserineCombined sources1
Modified residuei783PhosphoserineCombined sources1
Modified residuei785PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
CPTAC-603
CPTAC-604

Encyclopedia of Proteome Dynamics

More...
EPDi
P45974

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P45974

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P45974

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P45974

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

More...
PaxDbi
P45974

PeptideAtlas

More...
PeptideAtlasi
P45974

PRoteomics IDEntifications database

More...
PRIDEi
P45974

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
55692 [P45974-1]
55693 [P45974-2]

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
IPI00375145

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P45974

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

More...
PhosphoSitePlusi
P45974

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P45974

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P45974

<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
ENSG00000111667 Expressed in 217 organ(s), highest expression level in frontal cortex

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P45974 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P45974 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA006756

<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

Interacts with TRIML1.

By similarity

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
113751, 92 interactors

Database of interacting proteins

More...
DIPi
DIP-34459N

Protein interaction database and analysis system

More...
IntActi
P45974, 15 interactors

Molecular INTeraction database

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MINTi
P45974

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000229268

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P45974

<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

1858
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
P45974

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
P45974

<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>Domaini326 – 856USPAdd BLAST531
Domaini654 – 695UBA 1PROSITE-ProRule annotationAdd BLAST42
Domaini722 – 762UBA 2PROSITE-ProRule annotationAdd BLAST41

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni221 – 224Substrate binding4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The UBP-type zinc finger domain interacts selectively with an unmodified C-terminus of the proximal ubiquitin. Both UBA domains are involved in polyubiquitin recognition.

<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 peptidase C19 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri197 – 269UBP-typePROSITE-ProRule annotationAdd BLAST73

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0944 Eukaryota
COG5207 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156036

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000162311

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P45974

KEGG Orthology (KO)

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KOi
K11836

Identification of Orthologs from Complete Genome Data

More...
OMAi
ECGNLGC

Database of Orthologous Groups

More...
OrthoDBi
556111at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P45974

TreeFam database of animal gene trees

More...
TreeFami
TF300576

Family and domain databases

Conserved Domains Database

More...
CDDi
cd14383 UBA1_UBP5, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.40.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR038765 Papain-like_cys_pep_sf
IPR001394 Peptidase_C19_UCH
IPR015940 UBA
IPR009060 UBA-like_sf
IPR016652 Ubiquitinyl_hydrolase
IPR041432 UBP13_Znf-UBP_var
IPR041812 UBP5_UBA1
IPR018200 USP_CS
IPR028889 USP_dom
IPR013083 Znf_RING/FYVE/PHD
IPR001607 Znf_UBP

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00627 UBA, 2 hits
PF00443 UCH, 1 hit
PF02148 zf-UBP, 1 hit
PF17807 zf-UBP_var, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF016308 UBP, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00165 UBA, 2 hits
SM00290 ZnF_UBP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46934 SSF46934, 1 hit
SSF54001 SSF54001, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50030 UBA, 2 hits
PS00972 USP_1, 1 hit
PS00973 USP_2, 1 hit
PS50235 USP_3, 1 hit
PS50271 ZF_UBP, 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>Sequences (2+)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform Long (identifier: P45974-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAELSEEALL SVLPTIRVPK AGDRVHKDEC AFSFDTPESE GGLYICMNTF
60 70 80 90 100
LGFGKQYVER HFNKTGQRVY LHLRRTRRPK EEDPATGTGD PPRKKPTRLA
110 120 130 140 150
IGVEGGFDLS EEKFELDEDV KIVILPDYLE IARDGLGGLP DIVRDRVTSA
160 170 180 190 200
VEALLSADSA SRKQEVQAWD GEVRQVSKHA FSLKQLDNPA RIPPCGWKCS
210 220 230 240 250
KCDMRENLWL NLTDGSILCG RRYFDGSGGN NHAVEHYRET GYPLAVKLGT
260 270 280 290 300
ITPDGADVYS YDEDDMVLDP SLAEHLSHFG IDMLKMQKTD KTMTELEIDM
310 320 330 340 350
NQRIGEWELI QESGVPLKPL FGPGYTGIRN LGNSCYLNSV VQVLFSIPDF
360 370 380 390 400
QRKYVDKLEK IFQNAPTDPT QDFSTQVAKL GHGLLSGEYS KPVPESGDGE
410 420 430 440 450
RVPEQKEVQD GIAPRMFKAL IGKGHPEFST NRQQDAQEFF LHLINMVERN
460 470 480 490 500
CRSSENPNEV FRFLVEEKIK CLATEKVKYT QRVDYIMQLP VPMDAALNKE
510 520 530 540 550
ELLEYEEKKR QAEEEKMALP ELVRAQVPFS SCLEAYGAPE QVDDFWSTAL
560 570 580 590 600
QAKSVAVKTT RFASFPDYLV IQIKKFTFGL DWVPKKLDVS IEMPEELDIS
610 620 630 640 650
QLRGTGLQPG EEELPDIAPP LVTPDEPKGS LGFYGNEDED SFCSPHFSSP
660 670 680 690 700
TSPMLDESVI IQLVEMGFPM DACRKAVYYT GNSGAEAAMN WVMSHMDDPD
710 720 730 740 750
FANPLILPGS SGPGSTSAAA DPPPEDCVTT IVSMGFSRDQ ALKALRATNN
760 770 780 790 800
SLERAVDWIF SHIDDLDAEA AMDISEGRSA ADSISESVPV GPKVRDGPGK
810 820 830 840 850
YQLFAFISHM GTSTMCGHYV CHIKKEGRWV IYNDQKVCAS EKPPKDLGYI

YFYQRVAS
Length:858
Mass (Da):95,786
Last modified:October 1, 1996 - 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:iE99CB7CDFA682C65
GO
Isoform Short (identifier: P45974-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     629-652: GSLGFYGNEDEDSFCSPHFSSPTS → A

Show »
Length:835
Mass (Da):93,308
Checksum:i227CB29B11C7DAEA
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5H571F5H571_HUMAN
Ubiquitin carboxyl-terminal hydrola...
USP5
137Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti3 – 4EL → DV in CAA62690 (PubMed:7498549).Curated2
Sequence conflicti45I → V in CAA62690 (PubMed:7498549).Curated1
Sequence conflicti468K → R in AAA78934 (Ref. 4) Curated1
Sequence conflicti681G → D in AAA78934 (Ref. 4) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005259629 – 652GSLGF…SSPTS → A in isoform Short. 1 PublicationAdd BLAST24

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

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DDBJi
Links Updated
X91349 mRNA Translation: CAA62690.1
U47927 mRNA Translation: AAC50465.1
U47924 Genomic DNA Translation: AAB51314.1
U47924 Genomic DNA Translation: AAB51315.1
U35116 mRNA Translation: AAA78934.1
CH471116 Genomic DNA Translation: EAW88724.1
CH471116 Genomic DNA Translation: EAW88725.1
CH471116 Genomic DNA Translation: EAW88726.1
CH471116 Genomic DNA Translation: EAW88727.1
BC004889 mRNA Translation: AAH04889.1
BC005139 mRNA Translation: AAH05139.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS31733.1 [P45974-2]
CCDS41743.1 [P45974-1]

Protein sequence database of the Protein Information Resource

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PIRi
S68227

NCBI Reference Sequences

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RefSeqi
NP_001092006.1, NM_001098536.1 [P45974-1]
NP_003472.2, NM_003481.2 [P45974-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000229268; ENSP00000229268; ENSG00000111667 [P45974-1]
ENST00000389231; ENSP00000373883; ENSG00000111667 [P45974-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
8078

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:8078

UCSC genome browser

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UCSCi
uc001qrh.5 human [P45974-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
X91349 mRNA Translation: CAA62690.1
U47927 mRNA Translation: AAC50465.1
U47924 Genomic DNA Translation: AAB51314.1
U47924 Genomic DNA Translation: AAB51315.1
U35116 mRNA Translation: AAA78934.1
CH471116 Genomic DNA Translation: EAW88724.1
CH471116 Genomic DNA Translation: EAW88725.1
CH471116 Genomic DNA Translation: EAW88726.1
CH471116 Genomic DNA Translation: EAW88727.1
BC004889 mRNA Translation: AAH04889.1
BC005139 mRNA Translation: AAH05139.1
CCDSiCCDS31733.1 [P45974-2]
CCDS41743.1 [P45974-1]
PIRiS68227
RefSeqiNP_001092006.1, NM_001098536.1 [P45974-1]
NP_003472.2, NM_003481.2 [P45974-2]

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

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DAGNMR-A655-715[»]
2DAKNMR-A723-772[»]
2G43X-ray2.09A/B163-291[»]
2G45X-ray1.99A/D163-291[»]
3IHPX-ray2.80A/B1-858[»]
6DXHX-ray2.00A171-290[»]
6DXTX-ray1.95A/B171-290[»]
6NFTX-ray1.65A/B171-290[»]
SMRiP45974
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi113751, 92 interactors
DIPiDIP-34459N
IntActiP45974, 15 interactors
MINTiP45974
STRINGi9606.ENSP00000229268

Chemistry databases

BindingDBiP45974
ChEMBLiCHEMBL6158
GuidetoPHARMACOLOGYi2431

Protein family/group databases

MEROPSiC19.001

PTM databases

iPTMnetiP45974
PhosphoSitePlusiP45974
SwissPalmiP45974

Polymorphism and mutation databases

BioMutaiUSP5
DMDMi1717869

2D gel databases

REPRODUCTION-2DPAGEiIPI00375145

Proteomic databases

CPTACiCPTAC-603
CPTAC-604
EPDiP45974
jPOSTiP45974
MassIVEiP45974
MaxQBiP45974
PaxDbiP45974
PeptideAtlasiP45974
PRIDEiP45974
ProteomicsDBi55692 [P45974-1]
55693 [P45974-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
8078

Genome annotation databases

EnsembliENST00000229268; ENSP00000229268; ENSG00000111667 [P45974-1]
ENST00000389231; ENSP00000373883; ENSG00000111667 [P45974-2]
GeneIDi8078
KEGGihsa:8078
UCSCiuc001qrh.5 human [P45974-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8078
DisGeNETi8078

GeneCards: human genes, protein and diseases

More...
GeneCardsi
USP5
HGNCiHGNC:12628 USP5
HPAiHPA006756
MIMi601447 gene
neXtProtiNX_P45974
OpenTargetsiENSG00000111667
PharmGKBiPA37253

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0944 Eukaryota
COG5207 LUCA
GeneTreeiENSGT00940000156036
HOGENOMiHOG000162311
InParanoidiP45974
KOiK11836
OMAiECGNLGC
OrthoDBi556111at2759
PhylomeDBiP45974
TreeFamiTF300576

Enzyme and pathway databases

BRENDAi3.4.19.12 2681
ReactomeiR-HSA-5689880 Ub-specific processing proteases
R-HSA-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes

Miscellaneous databases

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

More...
ChiTaRSi
USP5 human
EvolutionaryTraceiP45974

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
USP5

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
8078
PharosiP45974
PMAP-CutDBiP45974

Protein Ontology

More...
PROi
PR:P45974

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000111667 Expressed in 217 organ(s), highest expression level in frontal cortex
ExpressionAtlasiP45974 baseline and differential
GenevisibleiP45974 HS

Family and domain databases

CDDicd14383 UBA1_UBP5, 1 hit
Gene3Di3.30.40.10, 3 hits
InterProiView protein in InterPro
IPR038765 Papain-like_cys_pep_sf
IPR001394 Peptidase_C19_UCH
IPR015940 UBA
IPR009060 UBA-like_sf
IPR016652 Ubiquitinyl_hydrolase
IPR041432 UBP13_Znf-UBP_var
IPR041812 UBP5_UBA1
IPR018200 USP_CS
IPR028889 USP_dom
IPR013083 Znf_RING/FYVE/PHD
IPR001607 Znf_UBP
PfamiView protein in Pfam
PF00627 UBA, 2 hits
PF00443 UCH, 1 hit
PF02148 zf-UBP, 1 hit
PF17807 zf-UBP_var, 1 hit
PIRSFiPIRSF016308 UBP, 1 hit
SMARTiView protein in SMART
SM00165 UBA, 2 hits
SM00290 ZnF_UBP, 1 hit
SUPFAMiSSF46934 SSF46934, 1 hit
SSF54001 SSF54001, 1 hit
PROSITEiView protein in PROSITE
PS50030 UBA, 2 hits
PS00972 USP_1, 1 hit
PS00973 USP_2, 1 hit
PS50235 USP_3, 1 hit
PS50271 ZF_UBP, 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 nameiUBP5_HUMAN
<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: P45974
Secondary accession number(s): D3DUS7, D3DUS8, Q96J22
<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, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2019
This is version 199 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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, Direct protein sequencing, 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. Peptidase families
    Classification of peptidase families and list of entries
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
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