SKP1_SCHPO
ID SKP1_SCHPO Reviewed; 161 AA.
AC Q9Y709;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Suppressor of kinetochore protein 1;
DE AltName: Full=P19/Skp1 homolog;
GN Name=skp1 {ECO:0000312|EMBL:CAB52607.1};
GN Synonyms=psh1 {ECO:0000312|EMBL:CAB52607.1},
GN sph1 {ECO:0000312|EMBL:CAB52607.1}; ORFNames=SPBC409.05;
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] {ECO:0000312|EMBL:BAA77790.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=10398680; DOI=10.1101/gad.13.13.1664;
RA Goshima G., Saitoh S., Yanagida M.;
RT "Proper metaphase spindle length is determined by centromere proteins Mis12
RT and Mis6 required for faithful chromosome segregation.";
RL Genes Dev. 13:1664-1677(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAB62325.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=11163211; DOI=10.1016/s1097-2765(00)00135-0;
RA Yamano H., Kitamura K., Kominami K., Lehmann A., Hunt T., Toda T.;
RT "The spike of S phase cyclin Cig2 expression at the G1-S border in fission
RT yeast requires both APC and SCF ubiquitin ligases.";
RL Mol. Cell 6:1377-1387(2000).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAD37024.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH POF6, AND
RP MUTAGENESIS OF ILE-139.
RX PubMed=12511573; DOI=10.1074/jbc.m211358200;
RA Hermand D., Bamps S., Tafforeau L., Vandenhaute J., Makela T.P.;
RT "Skp1 and the F-box protein Pof6 are essential for cell separation in
RT fission yeast.";
RL J. Biol. Chem. 278:9671-9677(2003).
RN [4] {ECO:0000312|EMBL:CAB52607.1}
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 [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PCU1; PIP1; POP1 AND
RP POP2.
RX PubMed=12167173; DOI=10.1186/1471-2091-3-22;
RA Seibert V., Prohl C., Schoultz I., Rhee E., Lopez R., Abderazzaq K.,
RA Zhou C., Wolf D.A.;
RT "Combinatorial diversity of fission yeast SCF ubiquitin ligases by
RT homo- and heterooligomeric assemblies of the F-box proteins Pop1p and
RT Pop2p.";
RL BMC Biochem. 3:22-22(2002).
RN [6] {ECO:0000305}
RP INTERACTION WITH MCS2 AND TFB3, AND MUTAGENESIS OF ILE-139.
RX PubMed=15555586; DOI=10.1016/j.bbrc.2004.10.190;
RA Bamps S., Westerling T., Pihlak A., Tafforeau L., Vandenhaute J.,
RA Maekelae T.P., Hermand D.;
RT "Mcs2 and a novel CAK subunit Pmh1 associate with Skp1 in fission yeast.";
RL Biochem. Biophys. Res. Commun. 325:1424-1432(2004).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=15147872; DOI=10.1016/j.febslet.2004.04.022;
RA Lehmann A., Toda T.;
RT "Fission yeast Skp1 is required for spindle morphology and nuclear membrane
RT segregation at anaphase.";
RL FEBS Lett. 566:77-82(2004).
RN [8] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CUL1; FBH1; POF1; POF2; POF3; POF4; POF5; POF6;
RP POF7; POF8; POF9; POF10; POF11; POF12; POF13; POP1 AND POP2, AND
RP MUTAGENESIS OF VAL-102; ILE-110 AND LEU-113.
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 [9] {ECO:0000305}
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 [10] {ECO:0000305}
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 [11]
RP IDENTIFICATION IN THE RAVE COMPLEX.
RX PubMed=18441123; DOI=10.1128/ec.00037-08;
RA Dawson K., Toone W.M., Jones N., Wilkinson C.R.;
RT "Loss of regulators of vacuolar ATPase function and ceramide synthesis
RT results in multidrug sensitivity in Schizosaccharomyces pombe.";
RL Eukaryot. Cell 7:926-937(2008).
RN [12]
RP INTERACTION WITH SIP1 AND SKP1.
RX PubMed=19243310; DOI=10.1042/bj20081659;
RA Jourdain I., Spielewoy N., Thompson J., Dhut S., Yates J.R., Toda T.;
RT "Identification of a conserved F-box protein 6 interactor essential for
RT endocytosis and cytokinesis in fission yeast.";
RL Biochem. J. 420:169-177(2009).
CC -!- FUNCTION: Required for cig2 degradation in the G2 and M phases of the
CC cell cycle. Together with pof6, essential for septum processing and
CC cell separation. Involved in mitotic progression, essential for the
CC execution of anaphase B; required for coordinated structural
CC alterations of mitotic spindles and segregation of nuclear membrane
CC structures at anaphase. Involved in the DNA damage checkpoint pathway
CC and maintenance of genome integrity. Component of the RAVE complex
CC which is required for stable assembly of the vacuolar ATPase complex V-
CC ATPase. {ECO:0000269|PubMed:11163211, ECO:0000269|PubMed:12167173,
CC ECO:0000269|PubMed:12511573, ECO:0000269|PubMed:15147268,
CC ECO:0000269|PubMed:15147872}.
CC -!- SUBUNIT: Essential component of the E3 ubiquitin ligase Skp1-Cullin-1-
CC F-box (SCF) complex. Interacts with cul1, fbh1, mcs2, pip1, pof1, pof2,
CC pof3, pof4, pof5, pof6, pof7, pof8, pof9, pof10, pof11, pof12, pof13,
CC pof14, pop1, pop2 and tfb3. Forms a complex with pof6 and sip1.
CC Component of the RAVE complex composed of rav1, rav2 and skp1.
CC {ECO:0000269|PubMed:12167173, ECO:0000269|PubMed:12511573,
CC ECO:0000269|PubMed:15147268, ECO:0000269|PubMed:15555586,
CC ECO:0000269|PubMed:17016471, ECO:0000269|PubMed:18441123,
CC ECO:0000269|PubMed:19243310}.
CC -!- INTERACTION:
CC Q9Y709; O13790: cul1; NbExp=2; IntAct=EBI-1172248, EBI-1154807;
CC Q9Y709; P36613: mcs2; NbExp=3; IntAct=EBI-1172248, EBI-1168694;
CC Q9Y709; O13959: pip1; NbExp=6; IntAct=EBI-1172248, EBI-1112060;
CC Q9Y709; O94684: pmh1; NbExp=3; IntAct=EBI-1172248, EBI-1168961;
CC Q9Y709; P87053: pof1; NbExp=2; IntAct=EBI-1172248, EBI-1185435;
CC Q9Y709; Q9P7W4: pof10; NbExp=5; IntAct=EBI-1172248, EBI-908406;
CC Q9Y709; Q10223: pof14; NbExp=5; IntAct=EBI-1172248, EBI-1793014;
CC Q9Y709; O74991: pof3; NbExp=3; IntAct=EBI-1172248, EBI-1153554;
CC Q9Y709; O14235: pof5; NbExp=2; IntAct=EBI-1172248, EBI-1185512;
CC Q9Y709; O74854: pof6; NbExp=4; IntAct=EBI-1172248, EBI-1185526;
CC Q9Y709; O74531: pof7; NbExp=2; IntAct=EBI-1172248, EBI-1185549;
CC Q9Y709; P87060: pop1; NbExp=2; IntAct=EBI-1172248, EBI-1185389;
CC Q9Y709; O14170: pop2; NbExp=3; IntAct=EBI-1172248, EBI-1185414;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12167173,
CC ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:12167173,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the SKP1 family. {ECO:0000255}.
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DR EMBL; AB027472; BAA77790.1; -; Genomic_DNA.
DR EMBL; AB067633; BAB62325.1; -; Genomic_DNA.
DR EMBL; AF071066; AAD37024.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB52607.1; -; Genomic_DNA.
DR PIR; T45459; T45459.
DR RefSeq; NP_595455.1; NM_001021365.2.
DR AlphaFoldDB; Q9Y709; -.
DR SMR; Q9Y709; -.
DR BioGRID; 277433; 54.
DR IntAct; Q9Y709; 37.
DR MINT; Q9Y709; -.
DR STRING; 4896.SPBC409.05.1; -.
DR iPTMnet; Q9Y709; -.
DR MaxQB; Q9Y709; -.
DR PaxDb; Q9Y709; -.
DR PRIDE; Q9Y709; -.
DR EnsemblFungi; SPBC409.05.1; SPBC409.05.1:pep; SPBC409.05.
DR GeneID; 2540917; -.
DR KEGG; spo:SPBC409.05; -.
DR PomBase; SPBC409.05; skp1.
DR VEuPathDB; FungiDB:SPBC409.05; -.
DR eggNOG; KOG1724; Eukaryota.
DR HOGENOM; CLU_059252_4_0_1; -.
DR InParanoid; Q9Y709; -.
DR OMA; PLKSADM; -.
DR PhylomeDB; Q9Y709; -.
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-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q9Y709; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; 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:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0043291; C:RAVE complex; IPI:PomBase.
DR GO; GO:0017117; C:single-stranded DNA-dependent ATP-dependent DNA helicase complex; IDA:PomBase.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IMP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0101026; P:mitotic nuclear membrane biogenesis; IMP:PomBase.
DR GO; GO:0045841; P:negative regulation of mitotic metaphase/anaphase transition; IMP:UniProtKB.
DR GO; GO:0006998; P:nuclear envelope organization; IMP:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0060542; P:regulation of strand invasion; IDA:PomBase.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IMP:PomBase.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:PomBase.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR016897; SKP1.
DR InterPro; IPR001232; SKP1-like.
DR InterPro; IPR036296; SKP1-like_dim_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR016072; Skp1_comp_dimer.
DR InterPro; IPR016073; Skp1_comp_POZ.
DR PANTHER; PTHR11165; PTHR11165; 1.
DR Pfam; PF01466; Skp1; 1.
DR Pfam; PF03931; Skp1_POZ; 1.
DR PIRSF; PIRSF028729; E3_ubiquit_lig_SCF_Skp; 1.
DR SMART; SM00512; Skp1; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF81382; SSF81382; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; DNA damage; Mitosis; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..161
FT /note="Suppressor of kinetochore protein 1"
FT /id="PRO_0000271429"
FT REGION 102..161
FT /note="Interaction with the F-box domain of F-box proteins"
FT /evidence="ECO:0000250"
FT MUTAGEN 102
FT /note="V->A: Causes G2 delay."
FT /evidence="ECO:0000269|PubMed:15147268"
FT MUTAGEN 110
FT /note="I->T: Prevents binding to pof1, pof3 and pof10.
FT Causes G2 delay."
FT /evidence="ECO:0000269|PubMed:15147268"
FT MUTAGEN 113
FT /note="L->F: Causes G2 delay."
FT /evidence="ECO:0000269|PubMed:15147268"
FT MUTAGEN 139
FT /note="I->N: Causes early cell cycle arrest. Prevents
FT binding to mcs2."
FT /evidence="ECO:0000269|PubMed:12511573,
FT ECO:0000269|PubMed:15555586"
SQ SEQUENCE 161 AA; 18772 MW; 07EA1E97A3556E78 CRC64;
MSKIKLISSD NEEFVVDQLI AERSMLIKNM LEDVGEINVP IPLPNVSSNV LRKVLEWCEH
HKNDLYSGTE EESDIRLKKS TDIDEWDRKF MAVDQEMLFE IVLASNYLDI KPLLDTGCKT
VANMIRGKSP EDIRKTFNIP NDFTPEEEEQ IRKENEWAED R
