Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O96612 (UBPB_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin hydrolase B

EC=3.4.19.12
Gene names
Name:ubpB
ORF Names:DDB_G0275021
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for proper prespore cell patterning. Plays a role in stabilizing mkkA by preventing it from being targeted for degradation. ubcB and ubpB differentially control ubiquitination/deubiquitination and degradation of mkkA in a cell-type-specific and temporally regulated manner. Ref.1

Catalytic activity

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).

Subunit structure

Interacts with mkkA (via F-box/WD40 domains). Ref.1

Developmental stage

Found at low levels in vegetative cells and at higher levels during aggregation and mound formation (4 and 8 hours of development). Ref.1

Disruption phenotype

Null cells differentiate into prestalk cells preferentially. They develop precociously and exhibit abnormal cell-type patterning with an increase in the prestalk domain and reduction in the prespore domain in the slug, and spore domain in a fruiting body. Null cells do not form the normal spherical sori seen in mature wild-type fruiting bodies. Instead, the sori remain elongated, similar to those seen in wild-type fruiting bodies that are not fully mature. The upper and lower cups of the fruiting body, which are derived from prestalk cells and anterior-like cells, are enlarged. The spore-containing region is reduced. Null cells form fruiting bodies at approximately 17 hours and exhibit precocious expression of the spore marker. The expression levels of the prespore/spore markers are lower in null cells compared to wild-type cells, whereas expression of the prestalk/stalk marker is elevated slightly. The loss of gene function, might lead to increased mkkA ubiquitination and a more rapid turnover of mkkA. This should result in a reduced level of mkkA activity, producing the above mentioned mkkA null cell type phenotype. Ref.1

Sequence similarities

Belongs to the peptidase C19 family.

Contains 1 USP domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Ubiquitin hydrolase B
PRO_0000389021

Regions

Domain19 – 450432USP
Compositional bias88 – 914Poly-Thr
Compositional bias92 – 954Poly-Ser
Compositional bias136 – 1449Poly-Gln

Sites

Active site3991Nucleophile By similarity
Active site4081Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
O96612 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: DADCD2CD07AFBFD7

FASTA45151,134
        10         20         30         40         50         60 
MKNIEEMPSK SQLVAHRSRG LINTSNTCFM NVILQSLTGC QLFLRVIKNL SDLEDLGKYP 

        70         80         90        100        110        120 
TLHSFNQFYT EYFSNPTSNI LNNNSNSTTT TSSSSTTATT TSTSNNNKSQ TPTSPIQQHH 

       130        140        150        160        170        180 
QSQTNGLSNQ PSVATQSQQQ QQPQPPINPK HFNDLVKSFN SKVSPVPQTT VSPHSMVQVS 

       190        200        210        220        230        240 
KKKLKLQLYN NSLPQTICQQ DAQEFLVFLL DLIHEEFLTL IKDIDIPKED DKSTPTSTSI 

       250        260        270        280        290        300 
VDDNWEVVGK KGKTAIITNS QQELPKTPIS QIFSGVLRSS FNRTGSKESI TVEPFYCLHL 

       310        320        330        340        350        360 
DIRPEEINSL EDALKFFMKP EIIEGYTCST KKIEISASKS WSFESLPRIL IVHFKRFAFE 

       370        380        390        400        410        420 
SDTSKKLDKL IRFPTQLSLS TASNHQTQKK YSLFSVVSHH GRGLSQGHYT CDIYQPQQAQ 

       430        440        450 
WIRYDDSTFT EVKEQDVLNR EAYLLLYQLV N 

« Hide

References

« Hide 'large scale' references
[1]"A novel, putative MEK kinase controls developmental timing and spatial patterning in Dictyostelium and is regulated by ubiquitin-mediated protein degradation."
Chung C.Y., Reddy T.B.K., Zhou K., Firtel R.A.
Genes Dev. 12:3564-3578(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH MKKA, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
Strain: AX3.
[2]"Sequence and analysis of chromosome 2 of Dictyostelium discoideum."
Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A.
Nature 418:79-85(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[3]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF093690 mRNA. Translation: AAC97115.1.
AAFI02000013 Genomic DNA. Translation: EAL69791.1. Different termination.

3D structure databases

ProteinModelPortalO96612.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0191402.

Protein family/group databases

MEROPSC19.A68.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0191402; DDB0191402; DDB_G0275021.
KEGGddi:DDB_G0275021.

Organism-specific databases

dictyBaseDDB_G0275021. ubpB.

Phylogenomic databases

eggNOGCOG5560.
InParanoidO96612.
KOK11841.
OMAINTSNTC.
PhylomeDBO96612.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
[Graphical view]
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameUBPB_DICDI
AccessionPrimary (citable) accession number: O96612
Secondary accession number(s): Q554A4, Q869X4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase