CUL1_SCHPO
ID CUL1_SCHPO Reviewed; 767 AA.
AC O13790; Q9USB3; Q9UUL3;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Cullin-1;
DE Short=Cul-1;
DE AltName: Full=Cell division control 53 homolog;
GN Name=cul1; Synonyms=pcu1; ORFNames=SPAC17G6.12;
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 [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9990507; DOI=10.1046/j.1365-2443.1998.00225.x;
RA Kominami K., Ochotorena I., Toda T.;
RT "Two F-box/WD-repeat proteins Pop1 and Pop2 form hetero- and homo-complexes
RT together with cullin-1 in fission yeast SCF (Skip-cullin-1-F-box) ubiquitin
RT ligase.";
RL Genes Cells 3:721-735(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 197-359.
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 [4]
RP NEDDYLATION AT LYS-713, AND MUTAGENESIS OF LYS-713.
RX PubMed=10880460; DOI=10.1093/emboj/19.13.3475;
RA Osaka F., Saeki M., Katayama S., Aida N., Toh-e A., Kominami K., Toda T.,
RA Suzuki T., Chiba T., Tanaka K., Kato S.;
RT "Covalent modifier NEDD8 is essential for SCF ubiquitin-ligase in fission
RT yeast.";
RL EMBO J. 19:3475-3484(2000).
RN [5]
RP INTERACTION WITH POF3.
RX PubMed=11809834; DOI=10.1091/mbc.01-07-0333;
RA Katayama S., Kitamura K., Lehmann A., Nikaido O., Toda T.;
RT "Fission yeast F-box protein Pof3 is required for genome integrity and
RT telomere function.";
RL Mol. Biol. Cell 13:211-224(2002).
RN [6]
RP INTERACTION WITH SKP1.
RX PubMed=15147268; DOI=10.1111/j.1356-9597.2004.00730.x;
RA Lehmann A., Katayama S., Harrison C., Dhut S., Kitamura K., McDonald N.,
RA Toda T.;
RT "Molecular interactions of fission yeast Skp1 and its role in the DNA
RT damage checkpoint.";
RL Genes Cells 9:367-382(2004).
RN [7]
RP INTERACTION WITH POF14.
RX PubMed=17016471; DOI=10.1038/sj.emboj.7601329;
RA Tafforeau L., Le Blastier S., Bamps S., Dewez M., Vandenhaute J.,
RA Hermand D.;
RT "Repression of ergosterol level during oxidative stress by fission yeast F-
RT box protein Pof14 independently of SCF.";
RL EMBO J. 25:4547-4556(2006).
RN [8]
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: Core component of multiple cullin-RING-based SCF (SKP1-CUL1-
CC F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the
CC ubiquitination of target proteins. The functional specificity of the
CC SCF complex depends on the F-box protein as substrate recognition
CC component. SCF(pop1-pop2) is required for the maintenance of ploidy and
CC directs ubiquitination of cig2. {ECO:0000269|PubMed:9990507}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of multiple SCF (SKP1-CUL1-F-box) E3 ubiquitin-
CC protein ligase complexes formed of cul1, skp1, pip1 and a variable F-
CC box domain-containing protein as substrate-specific subunit (By
CC similarity). Binds to the pop1 homodimer, the pop2 homodimer and the
CC pop1/pop2 heterodimer forming the SCF(pop1-pop2) complex. Interacts
CC with pof3, pof14 and skp1. {ECO:0000250, ECO:0000269|PubMed:11809834,
CC ECO:0000269|PubMed:15147268, ECO:0000269|PubMed:17016471,
CC ECO:0000269|PubMed:9990507}.
CC -!- INTERACTION:
CC O13790; O74991: pof3; NbExp=2; IntAct=EBI-1154807, EBI-1153554;
CC O13790; O14170: pop2; NbExp=3; IntAct=EBI-1154807, EBI-1185414;
CC O13790; Q9Y709: skp1; NbExp=2; IntAct=EBI-1154807, EBI-1172248;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- PTM: Neddylated; enhancing the ubiquitin-ligase activity.
CC {ECO:0000250|UniProtKB:P47050}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; AB016896; BAA32428.2; -; Genomic_DNA.
DR EMBL; CU329670; CAB16223.1; -; Genomic_DNA.
DR EMBL; AB027897; BAA87201.1; -; Genomic_DNA.
DR PIR; T37844; T37844.
DR PIR; T43398; T43398.
DR RefSeq; NP_594259.1; NM_001019682.2.
DR AlphaFoldDB; O13790; -.
DR SMR; O13790; -.
DR BioGRID; 278857; 31.
DR IntAct; O13790; 7.
DR MINT; O13790; -.
DR STRING; 4896.SPAC17G6.12.1; -.
DR MaxQB; O13790; -.
DR PaxDb; O13790; -.
DR PRIDE; O13790; -.
DR EnsemblFungi; SPAC17G6.12.1; SPAC17G6.12.1:pep; SPAC17G6.12.
DR GeneID; 2542393; -.
DR KEGG; spo:SPAC17G6.12; -.
DR PomBase; SPAC17G6.12; cul1.
DR VEuPathDB; FungiDB:SPAC17G6.12; -.
DR eggNOG; KOG2166; Eukaryota.
DR HOGENOM; CLU_004747_6_1_1; -.
DR InParanoid; O13790; -.
DR OMA; GVYTAVH; -.
DR PhylomeDB; O13790; -.
DR Reactome; R-SPO-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR Reactome; R-SPO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-SPO-8951664; Neddylation.
DR Reactome; R-SPO-917937; Iron uptake and transport.
DR Reactome; R-SPO-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:O13790; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043224; C:nuclear SCF ubiquitin ligase complex; IDA:PomBase.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:PomBase.
DR GO; GO:0000822; F:inositol hexakisphosphate binding; EXP:PomBase.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:PomBase.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; PTHR11932; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Isopeptide bond; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..767
FT /note="Cullin-1"
FT /id="PRO_0000119808"
FT CROSSLNK 713
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000269|PubMed:10880460"
FT MUTAGEN 713
FT /note="K->R: Loss of neddylation; results in impaired cell
FT proliferation and marked stabilization of the cyclin-
FT dependent kinase inhibitor rum1."
FT /evidence="ECO:0000269|PubMed:10880460"
FT CONFLICT 23
FT /note="Missing (in Ref. 1; BAA32428)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="T -> TR (in Ref. 1; BAA32428)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="T -> A (in Ref. 1; BAA32428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 767 AA; 89426 MW; 458CA31B5D97FAA9 CRC64;
MTTLNTNDKD LPIVKKYDSL NGTWDFLKTG VSQIFERLDE GMTITKYMEL YTAIHNYCAD
ASKTITVDNF NDQTANVLGE ALYNNLVLYL EEYLARLRKE CISQTNHEEQ LAAYAKYWTR
FTTSARFINH LFGYLNRYWV KLKNRFTETL VYDIYTLCLV SWHHHVFSHI RDSLLQNLLY
MFTKKRLYEP TDMKYVEVCV DSITSLSFDK TDMTKPNLSS YKTFFETNFI ENTKNFYAKE
SSEYLASHSI TDYLKKAEIR LAEEEELVRL YLHESTLKPL LEATEDVLIA QHEEVLHNDF
ARMLDQNCSE DIIRMYRLMS RTPNGLQPLR QTFEEFVKRS GFAAVAKIVP QVGGEADVDP
KEYMEMLLST YKASKELVNT AFHGDTDFTK SLDTAFRELV NRNVVCQRSS SRSPELLAKY
ADSILRKSNK NVDIDDVEDC LSSIIIIFRY VEDKDVFQNF YTKLLAKRLV NGTSNSQDAE
SSMLSKLKEV CGFEYTSKLQ RMFQDISLSQ EITEAFWQLP QSRAGNIDFS ALVLGTSFWP
LSPNNVNFHL PEELVPLYEG FQNYYYSCHN GRKLSWLFHL SKGEIKARIN PQTNVTYVFQ
VSTYQMGVLL LYNHRDSYTY EELAKITGLS TDFLTGILNI FLKAKVLLLG DNDKLGDPNS
TYKINENFRM KKIRVQLNLP IRSEQKQESL ETHKTIEEDR KLLLQSAIVR IMKARRTLKH
VVLVKETIDQ IKSRFTPKVS DIKQCIDMLI EKEYLERQGR DEYIYLA
