ID   DSK2_SCHPO              Reviewed;         354 AA.
AC   Q10169;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Deubiquitination-protection protein dph1;
GN   Name=dph1; ORFNames=SPAC26A3.16;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION.
RX   PubMed=12560082; DOI=10.1016/s0014-5793(02)03874-7;
RA   Hartmann-Petersen R., Hendil K.B., Gordon C.;
RT   "Ubiquitin binding proteins protect ubiquitin conjugates from
RT   disassembly.";
RL   FEBS Lett. 535:77-81(2003).
CC   -!- FUNCTION: Protects ubiquitin chains against dissambly by
CC       deubiquitinating enzymes thereby promoting protein degradation.
CC       {ECO:0000269|PubMed:12560082}.
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DR   EMBL; CU329670; CAA93239.1; -; Genomic_DNA.
DR   PIR; T38404; T38404.
DR   RefSeq; NP_594159.1; NM_001019583.2.
DR   AlphaFoldDB; Q10169; -.
DR   SMR; Q10169; -.
DR   BioGRID; 279120; 29.
DR   IntAct; Q10169; 3.
DR   MINT; Q10169; -.
DR   STRING; 4896.SPAC26A3.16.1; -.
DR   iPTMnet; Q10169; -.
DR   MaxQB; Q10169; -.
DR   PaxDb; Q10169; -.
DR   PRIDE; Q10169; -.
DR   EnsemblFungi; SPAC26A3.16.1; SPAC26A3.16.1:pep; SPAC26A3.16.
DR   GeneID; 2542667; -.
DR   KEGG; spo:SPAC26A3.16; -.
DR   PomBase; SPAC26A3.16; dph1.
DR   VEuPathDB; FungiDB:SPAC26A3.16; -.
DR   eggNOG; KOG0010; Eukaryota.
DR   HOGENOM; CLU_024293_0_1_1; -.
DR   OMA; GMDMFGP; -.
DR   PhylomeDB; Q10169; -.
DR   Reactome; R-SPO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR   PRO; PR:Q10169; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:PomBase.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:PomBase.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   InterPro; IPR006636; STI1_HS-bd.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   Pfam; PF00627; UBA; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00727; STI1; 2.
DR   SMART; SM00165; UBA; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   4: Predicted;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..354
FT                   /note="Deubiquitination-protection protein dph1"
FT                   /id="PRO_0000114901"
FT   DOMAIN          1..78
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          309..353
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
SQ   SEQUENCE   354 AA;  36819 MW;  1A99B2D97E73A831 CRC64;
     MTNISLTIKA ANDQKYAVTV DSESSVLALK EAIAPVADIE KERQRLIYAG RVLKDEESLK
     TYKIQDGHSI HLVKTLGQNP AAAATNVSDR TQQVPTNIQA GQGANNPLAN LTSARYAGFN
     IPMPSASMFG PNPENPVPPS TEELANMLSN PMVQSSINEM FSNPQMLDMI INSSPHLRNA
     PPYVRQMMQS PEFRRAMTDP DTMRQMAQLH QQMGAAGIDP MSLMGGGLGG AGLGGLGGAG
     LGGFGGANNA TAGIAGAAPV DQTAAANTIQ NLLNNLGGAG FGAGLGDAGL GAGLGGAASP
     PAPAQDTRPP EERYAEQLSQ LNEMGFVDFE RNVQALRRSG GNVQGAIESL LSDL