HUB1_SCHPO
ID HUB1_SCHPO Reviewed; 73 AA.
AC O94650;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ubiquitin-like modifier hub1;
GN Name=hub1; Synonyms=ubl4; ORFNames=SPBC31E1.03;
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, AND SUBCELLULAR LOCATION.
RX PubMed=15569151; DOI=10.1111/j.1365-2443.2004.00807.x;
RA Yashiroda H., Tanaka K.;
RT "Hub1 is an essential ubiquitin-like protein without functioning as a
RT typical modifier in fission yeast.";
RL Genes Cells 9:1189-1197(2004).
RN [3]
RP FUNCTION, INTERACTION WITH SNU66, AND MUTANT HUB1-4.
RX PubMed=15620657; DOI=10.1016/j.cub.2004.11.058;
RA Wilkinson C.R.M., Dittmar G.A.G., Ohi M.D., Uetz P., Jones N., Finley D.;
RT "Ubiquitin-like protein Hub1 is required for pre-mRNA splicing and
RT localization of an essential splicing factor in fission yeast.";
RL Curr. Biol. 14:2283-2288(2004).
RN [4]
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).
CC -!- FUNCTION: Forms a conjugate with snu66 and facilitates its localization
CC to the nucleus. Involved in morphogenesis. Required for efficient
CC splicing of pre-mRNA. {ECO:0000269|PubMed:15569151,
CC ECO:0000269|PubMed:15620657}.
CC -!- SUBUNIT: Interacts with snu66. {ECO:0000269|PubMed:15620657}.
CC -!- INTERACTION:
CC O94650; O94538: snu66; NbExp=2; IntAct=EBI-607734, EBI-607744;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329671; CAB39137.1; -; Genomic_DNA.
DR PIR; T40200; T40200.
DR RefSeq; NP_595099.1; NM_001021006.2.
DR AlphaFoldDB; O94650; -.
DR SMR; O94650; -.
DR BioGRID; 276917; 19.
DR IntAct; O94650; 1.
DR STRING; 4896.SPBC31E1.03.1; -.
DR MaxQB; O94650; -.
DR PaxDb; O94650; -.
DR EnsemblFungi; SPBC31E1.03.1; SPBC31E1.03.1:pep; SPBC31E1.03.
DR GeneID; 2540389; -.
DR KEGG; spo:SPBC31E1.03; -.
DR PomBase; SPBC31E1.03; hub1.
DR VEuPathDB; FungiDB:SPBC31E1.03; -.
DR eggNOG; KOG3493; Eukaryota.
DR HOGENOM; CLU_156193_2_0_1; -.
DR InParanoid; O94650; -.
DR OMA; HIKLEDY; -.
DR PhylomeDB; O94650; -.
DR PRO; PR:O94650; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IGI:PomBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0036211; P:protein modification process; IBA:GO_Central.
DR InterPro; IPR039732; Hub1/Ubl5.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR13042; PTHR13042; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..73
FT /note="Ubiquitin-like modifier hub1"
FT /id="PRO_0000114878"
FT DOMAIN 1..73
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT MUTAGEN 70
FT /note="M->K: In hub1-4; induces arrest of cell division in
FT G2; cells binucleate and septated."
SQ SEQUENCE 73 AA; 8435 MW; 894BED56B01FE365 CRC64;
MIEVLCNDRL GKKVRVKCMP DDTVGDFKKL VAAQTGTDPR RIVLKKWHSV FKDNITLADY
EIHDGMSLEM YYS