Reviewed, UniProtKB/Swiss-Prot P52286 (SKP1_YEAST)

Names and origin

Protein names

Recommended name:
    Suppressor of kinetochore protein 1
Alternative name(s):
    Centromere DNA-binding protein complex CBF3 subunit D
    E3 ubiquitin ligase complex SCF subunit SKP1

Gene names

Name:	SKP1
Synonyms:	CBF3D
Ordered Locus Names:	YDR328C
ORF Names:	D9798.14

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	194 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins like phosphorylated SIC1. Participates in the attachment of chromosomes to the spindle. Acts as a regulatory component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters. The association of CBF3C with CBF3D and SGT1 is required for CBF3C activation and CBF3 assembly. SKP1/CBF3D could retrieve cyclins or cyclin-CDK-like proteins into the kinetochore thus providing cell cycle-regulated kinetochore activity. Involved in the regulation of methionine biosynthesis genes. Facilitates association of CDC53 with CDC4.
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Component of the E3 ubiquitin ligase complexes SCF with HRT1, some cullins like CDC53, and some F-box proteins like MET30 and CDC4. Interacts with CDC53 and MET30 to form the E3 ubiquitin ligase complex SCF(Met30) which also contains MET4. Forms complex SCF(Cdc4) together with CDC4 and CDC53. Component of the CBF3 complex, which is formed of CBF3A/CBF2, CBF3B/CEP3, CBF3C/CTF13 and CBF3D. Component of the RAVE complex composed of RAV1, RAV2 and SKP1/CBF3D. Interacts with RCY1, CBF3D and SGT1.
Subcellular location	Cytoplasm. Nucleus. Kinetochore.
Sequence similarities	Belongs to the SKP1 family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Chromosomal protein Cytoplasm Kinetochore Nucleus
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	G1/S transition of mitotic cell cycle Ref.1 Ref.2 Inferred from mutant phenotype. Source: SGD G2/M transition of mitotic cell cycle Ref.1 Ref.2 Inferred from mutant phenotype. Source: SGD SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Ref.6 Ref.7 Inferred from direct assay. Source: SGD cytokinesis Inferred from mutant phenotype. Source: SGD kinetochore assembly Inferred from direct assay. Source: SGD protein neddylation Inferred from genetic interaction. Source: SGD protein ubiquitination during ubiquitin-dependent protein catabolic process Ref.6 Ref.7 Inferred from direct assay. Source: SGD regulation of exit from mitosis Inferred from mutant phenotype. Source: SGD regulation of protein complex assembly Ref.11 Inferred from physical interaction. Source: SGD septin ring assembly Inferred from mutant phenotype. Source: SGD vacuolar acidification Ref.11 Inferred from genetic interaction. Source: SGD
Cellular component	CBF3 complex Ref.1 Ref.5 Inferred from direct assay. Source: SGD RAVE complex Ref.11 Inferred from physical interaction. Source: SGD SCF ubiquitin ligase complex Ref.6 Ref.7 Inferred from direct assay. Source: SGD condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA replication origin binding Inferred from physical interaction. Source: SGD protein binding Ref.2 Ref.9 Ref.11 Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P38352	1	EBI-4090,EBI-21172
	Q03899	1	EBI-4090,EBI-36201
	Q06479	1	EBI-4090,EBI-35627
CCNF	P41002	1	EBI-4090,EBI-1207574	From a different organism.
CDC4	P07834	3	EBI-4090,EBI-4434
CDC53	Q12018	4	EBI-4090,EBI-4321
COS111	P38308	1	EBI-4090,EBI-20947
CTF13	P35203	1	EBI-4090,EBI-4085
EFT1	P32324	1	EBI-4090,EBI-6333
GRR1	P24814	2	EBI-4090,EBI-7898
MET30	P39014	5	EBI-4090,EBI-11507
pof3	O74991	1	EBI-4090,EBI-1153554	From a different organism.
RAV1	P47104	1	EBI-4090,EBI-25471

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 194

193

Suppressor of kinetochore protein 1

PRO_0000187257

Regions

Compositional bias

66 – 74

9

Asp/Glu-rich (highly acidic)

Amino acid modifications

Modified residue

4

1

Phosphoserine

Modified residue

177

1

Phosphothreonine

Experimental info

Sequence conflict

48

1

E → D in AAC49492. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

194

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Beta strand

15 – 19

5

Helix

20 – 23

4

Helix

27 – 31

5

Beta strand

76 – 78

3

Helix

84 – 96

13

Turn

97 – 99

3

Helix

118 – 123

6

Helix

128 – 141

14

Helix

144 – 158

15

Helix

163 – 170

8

Helix

178 – 182

5

Sequences

	Sequence		Length	Mass (Da)
	P52286-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 746DDE6470A69432	FASTA	194	22,330
	10 20 30 40 50 60 MVTSNVVLVS GEGERFTVDK KIAERSLLLK NYLNDMHDSN LQNNSDSESD SDSETNHKSK 70 80 90 100 110 120 DNNNGDDDDE DDDEIVMPVP NVRSSVLQKV IEWAEHHRDS NFPDEDDDDS RKSAPVDSWD 130 140 150 160 170 180 REFLKVDQEM LYEIILAANY LNIKPLLDAG CKVVAEMIRG RSPEEIRRTF NIVNDFTPEE 190 EAAIRRENEW AEDR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Budding yeast SKP1 encodes an evolutionarily conserved kinetochore protein required for cell cycle progression." Connelly C., Hieter P. Cell 86:275-285(1996) [PubMed: 8706132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: ATCC 204508 / S288c.
[2]	"SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box." Bai C., Sen P., Hofmann K., Ma L., Goebl M., Harper J.W., Elledge S.J. Cell 86:263-274(1996) [PubMed: 8706131] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CDC4. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"The Saccharomyces cerevisiae kinetochore contains a cyclin-CDK complexing homologue, as identified by in vitro reconstitution." Stemmann O., Lechner J. EMBO J. 15:3611-3620(1996) [PubMed: 8670864] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-24, CHARACTERIZATION.
[6]	"F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex." Skowyra D., Craig K.L., Tyers M., Elledge S.J., Harper J.W. Cell 91:209-219(1997) [PubMed: 9346238] [Abstract] Cited for: FUNCTION, SUBUNIT.
[7]	"A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p." Feldman R.M., Correll C.C., Kaplan K.B., Deshaies R.J. Cell 91:221-230(1997) [PubMed: 9346239] [Abstract] Cited for: FUNCTION, SUBUNIT.
[8]	"Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein complexes that regulate cell division and methionine biosynthesis in yeast." Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L., Tyers M. Genes Dev. 12:692-705(1998) [PubMed: 9499404] [Abstract] Cited for: FUNCTION, INTERACTION WITH MET30 AND CDC53.
[9]	"Feedback-regulated degradation of the transcriptional activator Met4 is triggered by the SCF(Met30) complex." Rouillon A., Barbey R., Patton E.E., Tyers M., Thomas D. EMBO J. 19:282-294(2000) [PubMed: 10637232] [Abstract] Cited for: SUBUNIT.
[10]	"Skp1p and the F-box protein Rcy1p form a non-SCF complex involved in recycling of the SNARE Snc1p in yeast." Galan J.M., Wiederkehr A., Seol J.H., Haguenauer-Tsapis R., Deshaies R.J., Riezman H., Peter M. Mol. Cell. Biol. 21:3105-3117(2001) [PubMed: 11287615] [Abstract] Cited for: INTERACTION WITH RCY1.
[11]	"Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly." Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J. Nat. Cell Biol. 3:384-391(2001) [PubMed: 11283612] [Abstract] Cited for: IDENTIFICATION IN THE RAVE COMPLEX WITH RAV1 AND RAV2.
[12]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 AND THR-177, MASS SPECTROMETRY.
[13]	"Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase." Orlicky S., Tang X., Willems A., Tyers M., Sicheri F. Cell 112:243-256(2003) [PubMed: 12553912] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 7-166.
[14]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[15]	"The amino-terminal portion of the F-box protein Met30p mediates its nuclear import and assimilation into an SCF complex." Brunson L.E., Dixon C., Kozubowski L., Mathias N. J. Biol. Chem. 279:6674-6682(2004) [PubMed: 14660673] [Abstract] Cited for: INTERACTION WITH MET30.
[16]	"Sgt1p and Skp1p modulate the assembly and turnover of CBF3 complexes required for proper kinetochore function." Rodrigo-Brenni M.C., Thomas S., Bouck D.C., Kaplan K.B. Mol. Biol. Cell 15:3366-3378(2004) [PubMed: 15090617] [Abstract] Cited for: ASSEMBLY OF THE CBF3 COMPLEX, INTERACTION WITH CBF3C AND SGT1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U43179 Genomic DNA. Translation: AAB17500.1.
U61764 mRNA. Translation: AAC49492.1.
U32517 Genomic DNA. Translation: AAB64763.1.
AY557730 Genomic DNA. Translation: AAS56056.1.

PIR

S59793.

RefSeq

NP_010615.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NEX	X-ray	2.70	A/C	1-194	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:1236N.

IntAct

P52286.

Proteomic databases

PeptideAtlas

P52286.

Genome annotation databases

Ensembl

YDR328C. Saccharomyces cerevisiae. [Contig view]

GeneID

851928.

GenomeReviews

Gene locus YDR328C in contig Z71256_GR.

KEGG

sce:YDR328C.

NMPDR

fig|4932.3.peg.1381.

Organism-specific databases

CYGD

YDR328c.

SGD

S000002736. SKP1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P52286.

Gene expression databases

GermOnline

YDR328C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR011333. BTB/POZ_fold.
IPR016897. E3_ubiquit_lig_SCF_Skp.
IPR001232. Skp1_comp.
IPR016072. Skp1_comp_dimer.
IPR016073. Skp1_comp_POZ.
[Graphical view]

Gene3D

G3DSA:3.30.710.10. BTB/POZ_fold. 1 hit.

PANTHER

PTHR11165. Skp1. 1 hit.

Pfam

PF01466. Skp1. 1 hit.
PF03931. Skp1_POZ. 1 hit.
[Graphical view]

PIRSF

PIRSF028729. E3_ubiquit_lig_SCF_Skp. 1 hit.

SMART

SM00512. Skp1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P52286.

NextBio

969983.

Entry information

Entry name

SKP1_YEAST

Accession

Primary (citable) accession number: P52286
Secondary accession number(s): Q07186

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 85 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)