YEAST:SKP1

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	SKP1 (synonyms: CBF3D)
Protein Name(s)	Suppressor of kinetochore protein 1 Centromere DNA-binding protein complex CBF3 subunit D E3 ubiquitin ligase complex SCF subunit SKP1
External Links
UniProt	P52286
EMBL	U43179 U61764 U32517 AY557730 BK006938
PIR	S59793
RefSeq	NP_010615.3
PDB	1NEX 3MKS 3V7D
PDBsum	1NEX 3MKS 3V7D
ProteinModelPortal	P52286
SMR	P52286
BioGrid	32385
DIP	DIP-1236N
IntAct	P52286
MINT	MINT-384072
STRING	4932.YDR328C
MaxQB	P52286
PaxDb	P52286
PeptideAtlas	P52286
PRIDE	P52286
EnsemblFungi	[example_ID YDR328C]
GeneID	851928
KEGG	sce:YDR328C
SGD	S000002736
eggNOG	COG5201
GeneTree	ENSGT00390000012652
HOGENOM	HOG000172184
InParanoid	P52286
KO	K03094
OMA	LENEWCE
OrthoDB	EOG7N37RH
BioCyc	YEAST:G3O-29884-MONOMER
Reactome	REACT_230653
UniPathway	UPA00143
EvolutionaryTrace	P52286
NextBio	969983
PRO	PR:P52286
Proteomes	UP000002311
Genevestigator	P52286
GO	GO:0031518 GO:0000777 GO:0005737 GO:0000776 GO:0005634 GO:0043291 GO:0019005 GO:0003688 GO:0010458 GO:0000082 GO:0000086 GO:0051382 GO:0006461 GO:0045116 GO:0042787 GO:0007096 GO:0043254 GO:0031146 GO:0000921 GO:0007035
InterPro	IPR011333 IPR016897 IPR001232 IPR016072 IPR016073
Pfam	PF01466 PF03931
PIRSF	PIRSF028729
SMART	SM00512
SUPFAM	SSF54695 SSF81382

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:2000766	negative regulation of cytoplasmic translation	PMID:26310304^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P45818)	Seeded From UniProt	complete
involved_in	GO:0051382	kinetochore assembly	PMID:12084919^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051382	kinetochore assembly	PMID:12084919^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045116	protein neddylation	PMID:9531531^[3]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000005924	P		Seeded From UniProt	complete
involved_in	GO:0045116	protein neddylation	PMID:9531531^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0043291	RAVE complex	PMID:11283612^[4]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000002610 SGD:S000003794	C		Seeded From UniProt	complete
part_of	GO:0043291	RAVE complex	PMID:11844802^[5]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000003794	C		Seeded From UniProt	complete
involved_in	GO:0043254	regulation of protein complex assembly	PMID:11283612^[4]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000002610 SGD:S000003794	P		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:9346239^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:9346238^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0031518	CBF3 complex	PMID:8670864^[8]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000004700	C		Seeded From UniProt	complete
part_of	GO:0031518	CBF3 complex	PMID:8706132^[9]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000004700	C		Seeded From UniProt	complete
part_of	GO:0031518	CBF3 complex	PMID:8706132^[9]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031518	CBF3 complex	PMID:8670864^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031518	CBF3 complex	PMID:19882662^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0031146	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process	PMID:9346238^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031146	SCF-dependent proteasomal ubiquitin-dependent protein catabolic process	PMID:9346239^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:9346239^[6]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000001885	C		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:9346238^[7]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000001885 SGD:S000002290	C		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:9346238^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0019005	SCF ubiquitin ligase complex	PMID:9346239^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0010458	exit from mitosis	PMID:17205042^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007096	regulation of exit from mitosis	PMID:17205042^[11]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000003814	P		Seeded From UniProt	complete
involved_in	GO:0007096	regulation of exit from mitosis	PMID:17205042^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007035	vacuolar acidification	PMID:11283612^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000002610 SGD:S000003794	P		Seeded From UniProt	complete
involved_in	GO:0007035	vacuolar acidification	PMID:11283612^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034622	cellular protein-containing complex assembly	PMID:15090617^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	has_output:(GO:0031518)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:11080155^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:11080155^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
contributes_to	GO:0004842	ubiquitin-protein transferase activity	PMID:9346239^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
contributes_to	GO:0061630	ubiquitin protein ligase activity	PMID:9346238^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003688	DNA replication origin binding	PMID:16421250^[14]	ECO:0000353	physical interaction evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0000921	septin ring assembly	PMID:16330709^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000086	G2/M transition of mitotic cell cycle	PMID:8706132^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000086	G2/M transition of mitotic cell cycle	PMID:8706131^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000082	G1/S transition of mitotic cell cycle	PMID:8706132^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000082	G1/S transition of mitotic cell cycle	PMID:8706131^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006511	ubiquitin-dependent protein catabolic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001232 InterPro:IPR016072 InterPro:IPR016073 InterPro:IPR016897 InterPro:IPR036296	P		Seeded From UniProt	complete
part_of	GO:0000776	kinetochore	PMID:12769845^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0000775	chromosome, centromeric region	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0137	C		Seeded From UniProt	complete
part_of	GO:0000776	kinetochore	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0995	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F		Seeded From UniProt	complete
part_of	GO:0005694	chromosome	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0158	C		Seeded From UniProt	complete
part_of	GO:0000777	condensed chromosome kinetochore	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0149	C		Seeded From UniProt	complete
involved_in	GO:0016567	protein ubiquitination	GO_REF:0000041	ECO:0000322	imported manually asserted information used in automatic assertion	UniPathway:UPA00143	P		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Jeon, S et al. (2015) Identification of Psk2, Skp1, and Tub4 as trans-acting factors for uORF-containing ROK1 mRNA in Saccharomyces cerevisiae. J. Microbiol. 53 616-22 PubMed GONUTS page
↑ ^2.0 ^2.1 Stemmann, O et al. (2002) Hsp90 enables Ctf13p/Skp1p to nucleate the budding yeast kinetochore. Proc. Natl. Acad. Sci. U.S.A. 99 8585-90 PubMed GONUTS page
↑ ^3.0 ^3.1 Lammer, D et al. (1998) Modification of yeast Cdc53p by the ubiquitin-related protein rub1p affects function of the SCFCdc4 complex. Genes Dev. 12 914-26 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 Seol, JH et al. (2001) Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly. Nat. Cell Biol. 3 384-91 PubMed GONUTS page
↑ Smardon, AM et al. (2002) The RAVE complex is essential for stable assembly of the yeast V-ATPase. J. Biol. Chem. 277 13831-9 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 Feldman, RM et al. (1997) A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91 221-30 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 Skowyra, D et al. (1997) F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91 209-19 PubMed GONUTS page
↑ ^8.0 ^8.1 Stemmann, O & Lechner, J (1996) The Saccharomyces cerevisiae kinetochore contains a cyclin-CDK complexing homologue, as identified by in vitro reconstitution. EMBO J. 15 3611-20 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 Connelly, C & Hieter, P (1996) Budding yeast SKP1 encodes an evolutionarily conserved kinetochore protein required for cell cycle progression. Cell 86 275-85 PubMed GONUTS page
↑ Kato, M et al. (2010) Remodeling of the SCF complex-mediated ubiquitination system by compositional alteration of incorporated F-box proteins. Proteomics 10 115-23 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Kim, N et al. (2006) A new function of Skp1 in the mitotic exit of budding yeast Saccharomyces cerevisiae. J. Microbiol. 44 641-8 PubMed GONUTS page
↑ Rodrigo-Brenni, MC et al. (2004) Sgt1p and Skp1p modulate the assembly and turnover of CBF3 complexes required for proper kinetochore function. Mol. Biol. Cell 15 3366-78 PubMed GONUTS page
↑ ^13.0 ^13.1 Blondel, M et al. (2000) Nuclear-specific degradation of Far1 is controlled by the localization of the F-box protein Cdc4. EMBO J. 19 6085-97 PubMed GONUTS page
↑ Koepp, DM et al. (2006) The F-box protein Dia2 regulates DNA replication. Mol. Biol. Cell 17 1540-8 PubMed GONUTS page
↑ Gillis, AN et al. (2005) A novel role for the CBF3 kinetochore-scaffold complex in regulating septin dynamics and cytokinesis. J. Cell Biol. 171 773-84 PubMed GONUTS page
↑ ^16.0 ^16.1 Bai, C et al. (1996) SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86 263-74 PubMed GONUTS page
↑ Kitagawa, K et al. (2003) Requirement of Skp1-Bub1 interaction for kinetochore-mediated activation of the spindle checkpoint. Mol. Cell 11 1201-13 PubMed GONUTS page

[PMID:26310304-1] Jeon, S et al. (2015) Identification of Psk2, Skp1, and Tub4 as trans-acting factors for uORF-containing ROK1 mRNA in Saccharomyces cerevisiae. J. Microbiol. 53 616-22 PubMed GONUTS page

[PMID:12084919-2] 2.0 ^2.1 Stemmann, O et al. (2002) Hsp90 enables Ctf13p/Skp1p to nucleate the budding yeast kinetochore. Proc. Natl. Acad. Sci. U.S.A. 99 8585-90 PubMed GONUTS page

[PMID:9531531-3] 3.0 ^3.1 Lammer, D et al. (1998) Modification of yeast Cdc53p by the ubiquitin-related protein rub1p affects function of the SCFCdc4 complex. Genes Dev. 12 914-26 PubMed GONUTS page

[PMID:11283612-4] 4.0 ^4.1 ^4.2 ^4.3 Seol, JH et al. (2001) Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly. Nat. Cell Biol. 3 384-91 PubMed GONUTS page

[PMID:11844802-5] Smardon, AM et al. (2002) The RAVE complex is essential for stable assembly of the yeast V-ATPase. J. Biol. Chem. 277 13831-9 PubMed GONUTS page

[PMID:9346239-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 Feldman, RM et al. (1997) A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91 221-30 PubMed GONUTS page

[PMID:9346238-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 Skowyra, D et al. (1997) F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91 209-19 PubMed GONUTS page

[PMID:8670864-8] 8.0 ^8.1 Stemmann, O & Lechner, J (1996) The Saccharomyces cerevisiae kinetochore contains a cyclin-CDK complexing homologue, as identified by in vitro reconstitution. EMBO J. 15 3611-20 PubMed GONUTS page

[PMID:8706132-9] 9.0 ^9.1 ^9.2 ^9.3 Connelly, C & Hieter, P (1996) Budding yeast SKP1 encodes an evolutionarily conserved kinetochore protein required for cell cycle progression. Cell 86 275-85 PubMed GONUTS page

[PMID:19882662-10] Kato, M et al. (2010) Remodeling of the SCF complex-mediated ubiquitination system by compositional alteration of incorporated F-box proteins. Proteomics 10 115-23 PubMed GONUTS page

[PMID:17205042-11] 11.0 ^11.1 ^11.2 Kim, N et al. (2006) A new function of Skp1 in the mitotic exit of budding yeast Saccharomyces cerevisiae. J. Microbiol. 44 641-8 PubMed GONUTS page

[PMID:15090617-12] Rodrigo-Brenni, MC et al. (2004) Sgt1p and Skp1p modulate the assembly and turnover of CBF3 complexes required for proper kinetochore function. Mol. Biol. Cell 15 3366-78 PubMed GONUTS page

[PMID:11080155-13] 13.0 ^13.1 Blondel, M et al. (2000) Nuclear-specific degradation of Far1 is controlled by the localization of the F-box protein Cdc4. EMBO J. 19 6085-97 PubMed GONUTS page

[PMID:16421250-14] Koepp, DM et al. (2006) The F-box protein Dia2 regulates DNA replication. Mol. Biol. Cell 17 1540-8 PubMed GONUTS page

[PMID:16330709-15] Gillis, AN et al. (2005) A novel role for the CBF3 kinetochore-scaffold complex in regulating septin dynamics and cytokinesis. J. Cell Biol. 171 773-84 PubMed GONUTS page

[PMID:8706131-16] 16.0 ^16.1 Bai, C et al. (1996) SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell 86 263-74 PubMed GONUTS page

[PMID:12769845-17] Kitagawa, K et al. (2003) Requirement of Skp1-Bub1 interaction for kinetochore-mediated activation of the spindle checkpoint. Mol. Cell 11 1201-13 PubMed GONUTS page

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YEAST:SKP1

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