ID PUB1_SCHPO STANDARD; PRT; 767 AA. AC Q92462; O14454; DT 01-NOV-1997 (Rel. 35, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 01-OCT-2004 (Rel. 45, Last annotation update) DE E3 ubiquitin--protein ligase pub1 (EC 6.3.2.-). GN Name=pub1; ORFNames=SPAC11G7.02; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96205868; PubMed=8635463; RA Nefsky B., Beach D.; RT "Pub1 acts as an E6-AP-like protein ubiquitiin ligase in the RT degradation of cdc25."; RL EMBO J. 15:1301-1312(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=J227; RX MEDLINE=97340937; PubMed=9197411; RA Saleki R., Jia Z., Karagiannis J., Young P.G.; RT "Tolerance of low pH in Schizosaccharomyces pombe requires a RT functioning pub1 ubiquitin ligase."; RL Mol. Gen. Genet. 254:520-528(1997). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M., Lyne R., Stewart A., RA Sgouros J., Peat N., Hayles J., Baker S., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K., Murphy L., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fritzc C., Holzer E., Moestl D., Hilbert H., RA Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., RA Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [4] RP SUBCELLULAR LOCATION. RX PubMed=11956316; RA Tamai K.K., Shimoda C.; RT "The novel HECT-type ubiquitin-protein ligase Pub2p shares partially RT overlapping function with Pub1p in Schizosaccharomyces pombe."; RL J. Cell Sci. 115:1847-1857(2002). CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from CC an E2 ubiquitin-conjugating enzyme in the form of a thioester and CC then directly transfers the ubiquitin to targeted substrates. CC Regulates ubiquitination of cdc25. CC -!- PATHWAY: Ubiquitin conjugation; third step. CC -!- SUBCELLULAR LOCATION: Membrane-associated, and cytoplasmic. CC -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin- CC thiolester formation. CC -!- SIMILARITY: Contains 1 C2 domain. CC -!- SIMILARITY: Contains 1 HECT-type E3 ubiquitin-protein ligase CC domain. CC -!- SIMILARITY: Contains 3 WW domains. 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; Y07592; CAA68867.1; -. DR EMBL; U66716; AAB07514.1; -. DR EMBL; Z99161; CAB16207.1; -. DR EMBL; U62795; AAB63350.1; -. DR PIR; S66562; S66562. DR PIR; T37545; T37545. DR HSSP; Q62940; 1I5H. DR GeneDB_SPombe; SPAC11G7.02; -. DR InterPro; IPR000008; C2. DR InterPro; IPR008973; C2_CaLB. DR InterPro; IPR000569; HECT. DR InterPro; IPR002349; WW. DR InterPro; IPR001202; WW_Rsp5_WWP. DR Pfam; PF00168; C2; 1. DR Pfam; PF00632; HECT; 1. DR Pfam; PF00397; WW; 3. DR PRINTS; PR00403; WWDOMAIN. DR SMART; SM00239; C2; 1. DR SMART; SM00119; HECTc; 1. DR SMART; SM00456; WW; 3. DR PROSITE; PS00499; C2_DOMAIN_1; 1. DR PROSITE; PS50004; C2_DOMAIN_2; 1. DR PROSITE; PS50237; HECT; 1. DR PROSITE; PS01159; WW_DOMAIN_1; 3. DR PROSITE; PS50020; WW_DOMAIN_2; 3. KW Ligase; Repeat; Ubl conjugation; Ubl conjugation pathway. FT DOMAIN 17 32 C2 domain. FT DOMAIN 211 236 WW 1. FT DOMAIN 242 247 Poly-Ala. FT DOMAIN 294 319 WW 2. FT DOMAIN 351 376 WW 3. FT DOMAIN 463 767 HECT. FT BINDING 735 735 Ubiquitin (By similarity). FT CONFLICT 163 163 Q -> K (in Ref. 1). FT CONFLICT 609 609 Missing (in Ref. 1). FT CONFLICT 661 661 T -> K (in Ref. 1). SQ SEQUENCE 767 AA; 87267 MW; F1455A155EB9ACF7 CRC64; MSNSAQSRRI RVTIVAADGL YKRDVFRFPD PFAVLTVDGE QTHTTTAIKK TLNPYWNETF EVNVTDNSTI AIQVFDQKKF KKKGQGFLGV INLRVGDVLD LAIGGDEMLT RDLKKSNENT VVHGKIIINL STTAQSTLQV PSSAASGART QRTSITNDPQ SSQSSSVSRN PASSRAGSPT RDNAPAASPA SSEPRTFSSF EDQYGRLPPG WERRTDNLGR TYYVDHNTRS TTWIRPNLSS VAGAAAAELH SSASSANVTE GVQPSSSNAA RRTEASVLTS NATTAGSGEL PPGWEQRYTP EGRPYFVDHN TRTTTWVDPR RQQYIRSYGG PNNATIQQQP VSQLGPLPSG WEMRLTNTAR VYFVDHNTKT TTWDDPRLPS SLDQNVPQYK RDFRRKLIYF LSQPALHPLP GQCHIKVRRN HIFEDSYAEI MRQSATDLKK RLMIKFDGED GLDYGGLSRE YFFLLSHEMF NPFYCLFEYS SVDNYTLQIN PHSGINPEHL NYFKFIGRVI GLAIFHRRFV DAFFVVSFYK MILQKKVTLQ DMESMDAEYY RSLVWILDND ITGVLDLTFS VEDNCFGEVV TIDLKPNGRN IEVTEENKRE YVDLVTVWRI QKRIEEQFNA FHEGFSELIP QELINVFDER ELELLIGGIS EIDMEDWKKH TDYRSYSEND QIIKWFWELM DEWSNEKKSR LLQFTTGTSR IPVNGFKDLQ GSDGPRKFTI EKAGEPNKLP KAHTCFNRLD LPPYTSKKDL DHKLSIAVEE TIGFGQE //