UBX2_SCHPO
ID UBX2_SCHPO Reviewed; 427 AA.
AC O14048;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=UBX domain-containing protein 2;
GN Name=ubx2; ORFNames=SPAC2C4.15c;
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 INTERACTION WITH CDC48.
RX PubMed=15120077; DOI=10.1016/j.cub.2004.04.029;
RA Hartmann-Petersen R., Wallace M., Hofmann K., Koch G., Johnsen A.H.,
RA Hendil K.B., Gordon C.;
RT "The Ubx2 and Ubx3 cofactors direct Cdc48 activity to proteolytic and
RT nonproteolytic ubiquitin-dependent processes.";
RL Curr. Biol. 14:824-828(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in CDC48-dependent protein degradation through the
CC ubiquitin/proteasome pathway. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with cdc48. {ECO:0000269|PubMed:15120077}.
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DR EMBL; CU329670; CAB16375.1; -; Genomic_DNA.
DR PIR; T38526; T38526.
DR RefSeq; NP_594518.1; NM_001019947.2.
DR AlphaFoldDB; O14048; -.
DR SMR; O14048; -.
DR BioGRID; 278032; 38.
DR IntAct; O14048; 3.
DR STRING; 4896.SPAC2C4.15c.1; -.
DR iPTMnet; O14048; -.
DR MaxQB; O14048; -.
DR PaxDb; O14048; -.
DR PRIDE; O14048; -.
DR EnsemblFungi; SPAC2C4.15c.1; SPAC2C4.15c.1:pep; SPAC2C4.15c.
DR GeneID; 2541532; -.
DR KEGG; spo:SPAC2C4.15c; -.
DR PomBase; SPAC2C4.15c; ubx2.
DR VEuPathDB; FungiDB:SPAC2C4.15c; -.
DR eggNOG; KOG1364; Eukaryota.
DR HOGENOM; CLU_021255_2_1_1; -.
DR InParanoid; O14048; -.
DR OMA; ICAFPRK; -.
DR PhylomeDB; O14048; -.
DR Reactome; R-SPO-8951664; Neddylation.
DR Reactome; R-SPO-9755511; KEAP1-NFE2L2 pathway.
DR PRO; PR:O14048; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0043130; F:ubiquitin binding; IPI:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:PomBase.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR017346; UBX_7/2.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00789; UBX; 1.
DR PIRSF; PIRSF037991; UCP037991_UBX7/2; 1.
DR SMART; SM00594; UAS; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..427
FT /note="UBX domain-containing protein 2"
FT /id="PRO_0000211005"
FT DOMAIN 349..425
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 115..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 427 AA; 47235 MW; 65F4A5F0940AB287 CRC64;
MDGDEASLVA NFCAITNSTP EKAQEYLSVA DGDLSTAITL FFESGGVTDV QSSYIEAPSQ
TEPVEEIRAP IAPTREVLVD PLADMSAGTS IMGNNFGFGG FPRMNRRQRR RMGIFDQSPS
QIPFPSSNTE DSSEESDSSS RASRLAKLFR PPYDIISNLS LDEARIEASS QKRWILVNLQ
TSTSFECQVL NRDLWKDESV KEVIRAHFLF LQLLDDEEPG MEFKRFYPVR STPHIAILDP
RTGERVKEWS KSFTPADFVI ALNDFLEGCT LDETSGRKNP LGAKSQKPVE AMSEDEQMHK
AIAASLGNGN STTESQGESS SQQAESHGVA DDTVHKIDSA ECDAEEPSPG PNVTRIQIRM
PNGARFIRRF SLTDPVSKVY AYVKGVAEGA DKQPFSLTFQ RKSLWTSLDS TIKEAGIQNT
ALQFEFQ
