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LUB1_SCHPO
ID   LUB1_SCHPO              Reviewed;         718 AA.
AC   O94289;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   25-MAY-2022, entry version 137.
DE   RecName: Full=Ubiquitin homeostasis protein lub1;
GN   Name=lub1; ORFNames=SPBC887.04c;
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   REVISION OF GENE MODEL.
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
RN   [3]
RP   FUNCTION, INTERACTION WITH CDC48, AND SUBCELLULAR LOCATION.
RX   PubMed=14993272; DOI=10.1128/mcb.24.6.2324-2331.2004;
RA   Ogiso Y., Sugiura R., Kamo T., Yanagiya S., Lu Y., Okazaki K., Shuntoh H.,
RA   Kuno T.;
RT   "Lub1 participates in ubiquitin homeostasis and stress response via
RT   maintenance of cellular ubiquitin contents in fission yeast.";
RL   Mol. Cell. Biol. 24:2324-2331(2004).
CC   -!- FUNCTION: Acts as a negative regulator of vacuole-dependent ubiquitin
CC       degradation. {ECO:0000269|PubMed:14993272}.
CC   -!- SUBUNIT: Interacts with cdc48. {ECO:0000269|PubMed:14993272}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14993272}. Cytoplasm
CC       {ECO:0000269|PubMed:14993272}.
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DR   EMBL; CU329671; CAA21889.2; -; Genomic_DNA.
DR   PIR; T40729; T40729.
DR   RefSeq; NP_596478.2; NM_001022398.2.
DR   AlphaFoldDB; O94289; -.
DR   SMR; O94289; -.
DR   BioGRID; 277722; 175.
DR   STRING; 4896.SPBC887.04c.1; -.
DR   iPTMnet; O94289; -.
DR   MaxQB; O94289; -.
DR   PaxDb; O94289; -.
DR   EnsemblFungi; SPBC887.04c.1; SPBC887.04c.1:pep; SPBC887.04c.
DR   GeneID; 2541208; -.
DR   KEGG; spo:SPBC887.04c; -.
DR   PomBase; SPBC887.04c; lub1.
DR   VEuPathDB; FungiDB:SPBC887.04c; -.
DR   eggNOG; KOG0301; Eukaryota.
DR   HOGENOM; CLU_011791_2_0_1; -.
DR   InParanoid; O94289; -.
DR   OMA; HNVCALD; -.
DR   Reactome; R-SPO-8951664; Neddylation.
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:O94289; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0043130; F:ubiquitin binding; ISO:PomBase.
DR   GO; GO:0006281; P:DNA repair; ISS:PomBase.
DR   GO; GO:0016574; P:histone ubiquitination; NAS:PomBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR   GO; GO:0010992; P:ubiquitin recycling; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 3.10.20.870; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR015155; PFU.
DR   InterPro; IPR038122; PFU_sf.
DR   InterPro; IPR013535; PUL_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF09070; PFU; 1.
DR   Pfam; PF08324; PUL; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS51394; PFU; 1.
DR   PROSITE; PS51396; PUL; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Reference proteome; Repeat; Ubl conjugation pathway;
KW   WD repeat.
FT   CHAIN           1..718
FT                   /note="Ubiquitin homeostasis protein lub1"
FT                   /id="PRO_0000051070"
FT   REPEAT          12..50
FT                   /note="WD 1"
FT   REPEAT          54..98
FT                   /note="WD 2"
FT   REPEAT          101..139
FT                   /note="WD 3"
FT   REPEAT          140..178
FT                   /note="WD 4"
FT   REPEAT          180..217
FT                   /note="WD 5"
FT   REPEAT          218..257
FT                   /note="WD 6"
FT   REPEAT          259..296
FT                   /note="WD 7"
FT   DOMAIN          353..448
FT                   /note="PFU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00727"
FT   DOMAIN          462..717
FT                   /note="PUL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00729"
SQ   SEQUENCE   718 AA;  79222 MW;  DC74201E79CDB6C2 CRC64;
     MTSYELSREL GGHKQDVRGV CSISNELIGS ASRDGTYSVW EQINGEWTPH FYENHEGFVN
     CVCYVPAIDK NSRGYIFSGG QDKCGILQEV GTNSPSYYLF GHESNICSAS ALNSETIITG
     SWDSTARVWA LGQCKYVLKG HQSSVWAVLA LGEDIFITGS ADKLIKIWNG EKLVKSILAH
     NDCVRSLCQI PGGFASCSND GVIKLWTSDG EFLYELHGHT SFVYSLTYIH NQQLIASCGE
     DRTIRIWKGK ECLQCITLPT TSVWSVSSLP NGDLVCGSSD GFVRIFTVDK VRVAPTEVLK
     NFEERVSQFA ISSQEVGDIK KGSLPGLEIL SKPGKADGDV VMVRVNNDVE AYQWSQKENE
     WKKIGQVVDA VGNNRKQLFE GKEYDYVFDV DVADGQAPLK LPYNATENPY QAANRFLELN
     QLPLSYTDEV VKFIEKNTQG HSLESKKEPN LESQSSNKIK TTIFPVSQLL FSNANVPAMC
     QRLRSLNNTK SNPLPAKSID SLERALSSKK ITDTEKNELL ETCLSILDSW SLAERFPALD
     ALRLLAINSS SDLAPIFLEV FSRVVKSVPS SGNFESINVM LALRGLSNVV PNITDAEGVS
     KLMDCLTSTV PQASSAKDFK IAFATLAMNL SILLIQLNLE NTGIELLSIL FSFLDDPSPD
     NEAFYRALMA LGTLCTVPDI ALAASQIYHA QSIVHGIAER FSQEMRFVDA EKQILSLF
 
 
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