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Protein

Deubiquitination-protection protein dph1

Gene

dph1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Protects ubiquitin chains against dissambly by deubiquitinating enzymes thereby promoting protein degradation.1 Publication

GO - Molecular functioni

  • polyubiquitin binding Source: PomBase

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Deubiquitination-protection protein dph1
Gene namesi
Name:dph1
ORF Names:SPAC26A3.16
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC26A3.16.
PomBaseiSPAC26A3.16. dph1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Deubiquitination-protection protein dph1PRO_0000114901Add
BLAST

Proteomic databases

MaxQBiQ10169.

Interactioni

GO - Molecular functioni

  • polyubiquitin binding Source: PomBase

Protein-protein interaction databases

BioGridi279120. 28 interactions.
MINTiMINT-216436.

Structurei

3D structure databases

ProteinModelPortaliQ10169.
SMRiQ10169. Positions 310-352.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7878Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Domaini309 – 35345UBAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 UBA domain.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000216678.
KOiK04523.
OMAiPDGGMNA.
PhylomeDBiQ10169.

Family and domain databases

InterProiIPR006636. STI1_HS-bd.
IPR015940. UBA.
IPR009060. UBA-like.
IPR015496. Ubiquilin.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR10677. PTHR10677. 1 hit.
PfamiPF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 2 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q10169-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTNISLTIKA ANDQKYAVTV DSESSVLALK EAIAPVADIE KERQRLIYAG
60 70 80 90 100
RVLKDEESLK TYKIQDGHSI HLVKTLGQNP AAAATNVSDR TQQVPTNIQA
110 120 130 140 150
GQGANNPLAN LTSARYAGFN IPMPSASMFG PNPENPVPPS TEELANMLSN
160 170 180 190 200
PMVQSSINEM FSNPQMLDMI INSSPHLRNA PPYVRQMMQS PEFRRAMTDP
210 220 230 240 250
DTMRQMAQLH QQMGAAGIDP MSLMGGGLGG AGLGGLGGAG LGGFGGANNA
260 270 280 290 300
TAGIAGAAPV DQTAAANTIQ NLLNNLGGAG FGAGLGDAGL GAGLGGAASP
310 320 330 340 350
PAPAQDTRPP EERYAEQLSQ LNEMGFVDFE RNVQALRRSG GNVQGAIESL

LSDL
Length:354
Mass (Da):36,819
Last modified:October 1, 1996 - v1
Checksum:i1A99B2D97E73A831
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93239.1.
PIRiT38404.
RefSeqiNP_594159.1. NM_001019583.2.

Genome annotation databases

EnsemblFungiiSPAC26A3.16.1; SPAC26A3.16.1:pep; SPAC26A3.16.
GeneIDi2542667.
KEGGispo:SPAC26A3.16.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAA93239.1.
PIRiT38404.
RefSeqiNP_594159.1. NM_001019583.2.

3D structure databases

ProteinModelPortaliQ10169.
SMRiQ10169. Positions 310-352.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279120. 28 interactions.
MINTiMINT-216436.

Proteomic databases

MaxQBiQ10169.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC26A3.16.1; SPAC26A3.16.1:pep; SPAC26A3.16.
GeneIDi2542667.
KEGGispo:SPAC26A3.16.

Organism-specific databases

EuPathDBiFungiDB:SPAC26A3.16.
PomBaseiSPAC26A3.16. dph1.

Phylogenomic databases

HOGENOMiHOG000216678.
KOiK04523.
OMAiPDGGMNA.
PhylomeDBiQ10169.

Miscellaneous databases

NextBioi20803715.
PROiQ10169.

Family and domain databases

InterProiIPR006636. STI1_HS-bd.
IPR015940. UBA.
IPR009060. UBA-like.
IPR015496. Ubiquilin.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR10677. PTHR10677. 1 hit.
PfamiPF00627. UBA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00727. STI1. 2 hits.
SM00165. UBA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50030. UBA. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "Ubiquitin binding proteins protect ubiquitin conjugates from disassembly."
    Hartmann-Petersen R., Hendil K.B., Gordon C.
    FEBS Lett. 535:77-81(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiDSK2_SCHPO
AccessioniPrimary (citable) accession number: Q10169
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 118 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, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.