UBX4_SCHPO
ID UBX4_SCHPO Reviewed; 425 AA.
AC Q9P7L2; Q9UU66;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=UBX domain-containing protein 4;
GN Name=ubx4; ORFNames=SPBC21C3.11;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 172-302, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, 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 -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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DR EMBL; CU329671; CAB76047.1; -; Genomic_DNA.
DR EMBL; AB027785; BAA87089.1; -; Genomic_DNA.
DR PIR; T50355; T50355.
DR RefSeq; NP_596591.1; NM_001022511.2.
DR AlphaFoldDB; Q9P7L2; -.
DR SMR; Q9P7L2; -.
DR BioGRID; 277102; 3.
DR STRING; 4896.SPBC21C3.11.1; -.
DR iPTMnet; Q9P7L2; -.
DR MaxQB; Q9P7L2; -.
DR PaxDb; Q9P7L2; -.
DR PRIDE; Q9P7L2; -.
DR EnsemblFungi; SPBC21C3.11.1; SPBC21C3.11.1:pep; SPBC21C3.11.
DR GeneID; 2540575; -.
DR KEGG; spo:SPBC21C3.11; -.
DR PomBase; SPBC21C3.11; ubx4.
DR VEuPathDB; FungiDB:SPBC21C3.11; -.
DR HOGENOM; CLU_576406_0_0_1; -.
DR InParanoid; Q9P7L2; -.
DR OMA; ACKGFQK; -.
DR PRO; PR:Q9P7L2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0012506; C:vesicle membrane; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:PomBase.
DR InterPro; IPR021569; TUG-UBL1.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF11470; TUG-UBL1; 1.
DR Pfam; PF00789; UBX; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..425
FT /note="UBX domain-containing protein 4"
FT /id="PRO_0000210996"
FT DOMAIN 341..390
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 224..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 425 AA; 46697 MW; DDAE8E1DC013DCAC CRC64;
MATIYACRGF HRVPVKLSPS STLQEVILSS YKQLGFSDWH NLELLHGDKK VDTSLLLRLS
GIINGAKLIV KESATNQSGK SSSSISPQSK KIKVALQLPG AARIIDEASS ETSIKQLLER
HSLLTKVSHV LINGRNFKSE EFDNPLLLYG IREGSILIRL FPIKAQQSIV SEQAPVSQTF
NGDVKEKKNA DLMDIESENK KDDIVESFPK YPVDAHKLLE PLPTPIPSLP STPSSYQNLP
SQSLTGESLP TVSNQEKDEG VIEKVAVNNT PSVSSKSPFP KKKSFSSMLA QVKKEKAENN
GSDGYDLQPT KSQLELYQSI LRKRANQVSS TSLTKSSSPK PLPSSAIVKF DFGNGKSIVH
EFSKDDNIET LRAFVASHLS PEESTSFQLT FSNYEALPTT GLIVEHIGRA VVRVHTISDP
VYAQR
