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Q9HFS7

- UBP4_KLULA

UniProt

Q9HFS7 - UBP4_KLULA

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Protein
Ubiquitin carboxyl-terminal hydrolase 4
Gene
DOA4, UBP4, KLLA0E10275g
Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Ubiquitin thioesterase that acts at the late endosome/prevacuolar compartment to recover ubiquitin from ubiquitinated membrane proteins en route to the vacuole. Removes also ubiquitin from soluble proteins targeted to proteasomes. Is essential to maintain a normal level of free ubiquitin. Required for promoting coordination of DNA replication and avoids DNA overreplication By similarity.

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).

Enzyme regulationi

RFU1 is an inhibitor of deubiquitination activity By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei441 – 4411Nucleophile By similarity
Active sitei752 – 7521Proton acceptor By similarity

GO - Molecular functioni

  1. cysteine-type peptidase activity Source: UniProtKB-KW
  2. ubiquitinyl hydrolase activity Source: InterPro

GO - Biological processi

  1. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin carboxyl-terminal hydrolase 4 (EC:3.4.19.12)
Alternative name(s):
Deubiquitinating enzyme 4
Ubiquitin thioesterase 4
Ubiquitin-specific-processing protease 4
Gene namesi
Name:DOA4
Synonyms:UBP4
Ordered Locus Names:KLLA0E10275g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598: Chromosome E

Subcellular locationi

GO - Cellular componenti

  1. late endosome membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 796796Ubiquitin carboxyl-terminal hydrolase 4
PRO_0000376820Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9HFS7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini170 – 294125Rhodanese
Add
BLAST
Domaini432 – 794363USP
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase C19 family.
Contains 1 rhodanese domain.
Contains 1 USP domain.

Phylogenomic databases

eggNOGiCOG5533.
HOGENOMiHOG000248489.
KOiK11839.
OMAiEDLNQCG.
OrthoDBiEOG7R2BSX.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR001763. Rhodanese-like_dom.
IPR028889. UCH/PAN2.
[Graphical view]
PfamiPF00581. Rhodanese. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view]
SMARTiSM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HFS7-1 [UniParc]FASTAAdd to Basket

« Hide

MLEHNSKLFC KSLSQLSAVA SKVVAEDVEG EHFKQLLAKC IDTLSIYKSE    50
LRKLSCASKD TPPSQIYQLN ETLYVYYKIV SQIASQVIPG LAEFQQIKMN 100
SKKDSKDKEL LEIYSRLVSA LANDKQIGEV KRFIKNHSEE AAHDGTQHSY 150
ENGEFVSISQ LHSLIRHDND SSGILLVDIR PRMDFNDGHI KHNNVICIEP 200
ISFKESYTDS DILRKSLITA SDREVDLFKN RDKFRLIVLY TDTDEHTKYY 250
WQQLEVLQDI LCNRSFDKPL HHTKVIVLQN GVNAWKEKYP MELKKIMESA 300
ISDIRTKPVE HNFHPMALSN NNNIEKANSP SHSQTTSFTH YPDAPFLTNG 350
ASIKTAGLVP NQLLPSTSNL TKALQQNDEG NSEPYKLQPN GIKNHRQESN 400
NHANGTNCIV SSNGNNSVAK SGHPSINLDF AIGLVNLGNS CYLNCIIQCL 450
LGCHELSYIF LTNSYRKHVN VNSRLGSKGL LANYFSQLVQ KMYQQGKLQA 500
YNNTNMESTA VHPTQFKLAC GSINSLFKGK QQQDCQEFCQ FLLDGLHEDL 550
NQCGTNPPLK ELSPEAEKMR ETMPMRIASA IEWERYLTTD FSVIVDLFQG 600
QYASQLRCKI CAHTSTTYQA FSVLSVPVPR ARSCTIYDCF KEFTKLETLE 650
KDELWYCPYC KQRQPSTKQI IITRLPNNLI IHLKRFDNMM NKNNVFVNYP 700
NELDLTGFWI DDYNGEMPKD NGVSLPLRGQ KPPFNYRLFA VASHSGTLYG 750
GHYTSFVDKG RVGWCSFDDV SWRKIRRKDE YITPNAYVLF YRRVNM 796
Length:796
Mass (Da):90,929
Last modified:March 1, 2001 - v1
Checksum:i09A9F905579C14B2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF303215 Genomic DNA. Translation: AAG17929.1.
CR382125 Genomic DNA. Translation: CAG99500.1.
RefSeqiXP_454413.1. XM_454413.1.

Genome annotation databases

GeneIDi2894137.
KEGGikla:KLLA0E10275g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF303215 Genomic DNA. Translation: AAG17929.1 .
CR382125 Genomic DNA. Translation: CAG99500.1 .
RefSeqi XP_454413.1. XM_454413.1.

3D structure databases

ProteinModelPortali Q9HFS7.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2894137.
KEGGi kla:KLLA0E10275g.

Phylogenomic databases

eggNOGi COG5533.
HOGENOMi HOG000248489.
KOi K11839.
OMAi EDLNQCG.
OrthoDBi EOG7R2BSX.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR001763. Rhodanese-like_dom.
IPR028889. UCH/PAN2.
[Graphical view ]
Pfami PF00581. Rhodanese. 1 hit.
PF00443. UCH. 1 hit.
[Graphical view ]
SMARTi SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52821. SSF52821. 1 hit.
PROSITEi PS50206. RHODANESE_3. 1 hit.
PS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae."
    Amerik A.Y., Li S.J., Hochstrasser M.
    Biol. Chem. 381:981-992(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Genome evolution in yeasts."
    Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
    , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
    Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Entry informationi

Entry nameiUBP4_KLULA
AccessioniPrimary (citable) accession number: Q9HFS7
Secondary accession number(s): Q6CNS6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: March 1, 2001
Last modified: September 3, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3