SKP2_YEAST
ID SKP2_YEAST Reviewed; 763 AA.
AC P42843; D6W0N4; Q6B2L9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=F-box protein SKP2;
GN Name=SKP2; OrderedLocusNames=YNL311C; ORFNames=N0376;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1676;
RX PubMed=7502583; DOI=10.1002/yea.320111109;
RA Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C.;
RT "Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV
RT identifies six known genes, a new member of the hexose transporter family
RT and ten new open reading frames.";
RL Yeast 11:1077-1085(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP INTERACTION WITH SKP1, AND RECONSTITUTION OF THE SCF(SKP2) COMPLEX.
RX PubMed=14747994; DOI=10.1002/prot.10620;
RA Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.;
RT "Functional interaction of 13 yeast SCF complexes with a set of yeast E2
RT enzymes in vitro.";
RL Proteins 54:455-467(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SKP1.
RX PubMed=16432255; DOI=10.1074/mcp.m500368-mcp200;
RA Tagwerker C., Flick K., Cui M., Guerrero C., Dou Y., Auer B., Baldi P.,
RA Huang L., Kaiser P.;
RT "A tandem affinity tag for two-step purification under fully denaturing
RT conditions: application in ubiquitin profiling and protein complex
RT identification combined with in vivocross-linking.";
RL Mol. Cell. Proteomics 5:737-748(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-594, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP DISRUPTION PHENOTYPE, AND FUNCTION OF THE SCF(SKP2) COMPLEX.
RX PubMed=20936605; DOI=10.1002/yea.1823;
RA Yoshida S., Imoto J., Minato T., Oouchi R., Kamada Y., Tomita M., Soga T.,
RA Yoshimoto H.;
RT "A novel mechanism regulates H(2) S and SO(2) production in Saccharomyces
RT cerevisiae.";
RL Yeast 28:109-121(2011).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Probably recognizes and binds to phosphorylated target
CC proteins (By similarity). Regulates protein levels of sulfur metabolism
CC enzymes. The SCF(SKP2) complex may regulate some transcription factors
CC or regulators of cysteine and methionine biosynthesis. {ECO:0000250,
CC ECO:0000269|PubMed:20936605}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with SKP1. Component of the probable SCF(SKP2)
CC complex containing CDC53, SKP1, RBX1 and SKP2. May interact with
CC ribosomes. {ECO:0000269|PubMed:14747994, ECO:0000269|PubMed:16432255}.
CC -!- INTERACTION:
CC P42843; P52286: SKP1; NbExp=5; IntAct=EBI-28370, EBI-4090;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DISRUPTION PHENOTYPE: Stabilizes the adenosylphosphosulfate kinase
CC MET14 which leads to accumulation H(2)S and SO(2).
CC {ECO:0000269|PubMed:20936605}.
CC -!- MISCELLANEOUS: Present with 432 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z46259; CAA86384.1; -; Genomic_DNA.
DR EMBL; Z71587; CAA96240.1; -; Genomic_DNA.
DR EMBL; AY692711; AAT92730.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10250.1; -; Genomic_DNA.
DR PIR; S51300; S51300.
DR RefSeq; NP_014088.1; NM_001183149.1.
DR AlphaFoldDB; P42843; -.
DR BioGRID; 35528; 97.
DR DIP; DIP-1971N; -.
DR IntAct; P42843; 28.
DR MINT; P42843; -.
DR STRING; 4932.YNL311C; -.
DR iPTMnet; P42843; -.
DR MaxQB; P42843; -.
DR PaxDb; P42843; -.
DR PRIDE; P42843; -.
DR EnsemblFungi; YNL311C_mRNA; YNL311C; YNL311C.
DR GeneID; 855405; -.
DR KEGG; sce:YNL311C; -.
DR SGD; S000005255; SKP2.
DR VEuPathDB; FungiDB:YNL311C; -.
DR eggNOG; ENOG502QTPK; Eukaryota.
DR HOGENOM; CLU_409412_0_0_1; -.
DR InParanoid; P42843; -.
DR OMA; IPLWYSV; -.
DR BioCyc; YEAST:G3O-33298-MON; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:P42843; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P42843; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISA:SGD.
DR GO; GO:0030163; P:protein catabolic process; IMP:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0031335; P:regulation of sulfur amino acid metabolic process; IMP:SGD.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..763
FT /note="F-box protein SKP2"
FT /id="PRO_0000203366"
FT DOMAIN 54..100
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT MOD_RES 594
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 16
FT /note="V -> A (in Ref. 4; AAT92730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 763 AA; 88942 MW; 81102168449051BC CRC64;
MKRLQLFGRS KYFSLVSSAA KEEEEEEEGC ADAKSLLHST SHDIKSRSLR FNDKSSLMCL
PTKVLLLILR TLDFNTLVTL CQVNSRFYNL ITNEFLFQNV ILDSKLSLLK FNALIHSEFH
TSNIVTHSGD CSTQSRSQNA RFLVRSIEFK NPQSQDSLLK YSKFYNKSGQ DSIIAGSYKL
DSYDKDVKKL NNIRLNDETP IITSERIKLL DKLESNYFHY TYIELMLDII DYLPNLTRVI
LSDVEPNFKI PLWYSVFNDG SRDFFKKIIK GQQSITNEDL RTFQLSKKFV KEYESKYYSL
PRLKILEIKA NNKRQRTFNR QRHHQKLVLR PSLFCCFGII NELKLENVTI DTESLDTPME
FLPLFLKNED NELYSLQSPI TALTLDSCDV VPGNGILRLF HSYFKMVKHL SLLKINSKFD
LLLCSCFPSL SNLTIDCNSK CFTNEQVVGE SYYFQQRSLD TEDDFDDCNS MTETLFEAPS
DSKIITPPPT SSVVLSLNLN YISRTTGNDV SNNPSPDNNK KPAMLTAAQL QNFQRQRIPE
FHSFYHYYRL LWERLPSKNI SINVINIPFT NVYPLSPLSF WEHLARTITS VDETDEDVGD
ENDQETLIGY ENNSIRDNIP NANAVPNLST VMSPESDIHH TYYWNNSVRR CLRDSLIKLK
NRTIEYRDLD VEEFLQNVTL ENFFNDFQDP ENFKDIPNIN LWCFLRNLSK FKAVKIRMLR
HFSLCTPRTR YDWELLLKPV LRVNVPIEVR DKDGFVLYSY GQK
