RPT1/YKL145W Protein Information

Standard Name	Rpt1p 1
Systematic Name	Ykl145wp
Alias	Cim5p 2 , Yta3p 3
ORF Classification	Verified
Description	One of six ATPases of the 19S regulatory particle of the 26S proteasome involved in the degradation of ubiquitinated substrates; required for optimal CDC20 transcription; interacts with Rpn12p and Ubr1p; mutant has aneuploidy tolerance (4, 5, 6, 7, 8)
Name Description	Regulatory Particle Triple-A protein, or Regulatory Particle Triphosphatase 1

Experimental Data
Molecules/cell	105 9

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	467
Molecular Weight (Da)	51,982
Isoelectric Point (pI)	5.17

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Rpt1p (InterPro)
Physical Interactions	There are 305 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI00000531A9 \| P33299 MIPS: YKL145W NCBI: 313882 \| 377656530 \| 377656532 \| 383875665 \| 383875667 \| 403071968 \| 410510 \| 464862 \| 486249 \| 6322704 \| NP_012777.1 GenBank/EMBL/DDBJ: DAA09017.1 \| X73571 \| Z22817 \| Z28145

Amino Acid Sequence (or in FASTA format)
1 MPPKEDWEKY KAPLEDDDKK PDDDKIVPLT EGDIQVLKSY GAAPYAAKLK 51 QTENDLKDIE ARIKEKAGVK ESDTGLAPSH LWDIMGDRQR LGEEHPLQVA 101 RCTKIIKGNG ESDETTTDNN NSGNSNSNSN QQSTDADEDD EDAKYVINLK 151 QIAKFVVGLG ERVSPTDIEE GMRVGVDRSK YNIELPLPPR IDPSVTMMTV 201 EEKPDVTYSD VGGCKDQIEK LREVVELPLL SPERFATLGI DPPKGILLYG 251 PPGTGKTLCA RAVANRTDAT FIRVIGSELV QKYVGEGARM VRELFEMART 301 KKACIIFFDE IDAVGGARFD DGAGGDNEVQ RTMLELITQL DGFDPRGNIK 351 VMFATNRPNT LDPALLRPGR IDRKVEFSLP DLEGRANIFR IHSKSMSVER 401 GIRWELISRL CPNSTGAELR SVCTEAGMFA IRARRKVATE KDFLKAVDKV 451 ISGYKKFSST SRYMQYN*

Amino Acid Sequence (or in FASTA format)

       1  MPPKEDWEKY KAPLEDDDKK PDDDKIVPLT EGDIQVLKSY GAAPYAAKLK
      51  QTENDLKDIE ARIKEKAGVK ESDTGLAPSH LWDIMGDRQR LGEEHPLQVA
     101  RCTKIIKGNG ESDETTTDNN NSGNSNSNSN QQSTDADEDD EDAKYVINLK
     151  QIAKFVVGLG ERVSPTDIEE GMRVGVDRSK YNIELPLPPR IDPSVTMMTV
     201  EEKPDVTYSD VGGCKDQIEK LREVVELPLL SPERFATLGI DPPKGILLYG
     251  PPGTGKTLCA RAVANRTDAT FIRVIGSELV QKYVGEGARM VRELFEMART
     301  KKACIIFFDE IDAVGGARFD DGAGGDNEVQ RTMLELITQL DGFDPRGNIK
     351  VMFATNRPNT LDPALLRPGR IDRKVEFSLP DLEGRANIFR IHSKSMSVER
     401  GIRWELISRL CPNSTGAELR SVCTEAGMFA IRARRKVATE KDFLKAVDKV
     451  ISGYKKFSST SRYMQYN*

external links for Rpt1p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	YPL+
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YeastGFP
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastRC Public Image Repository
Candida (CGD)	CYC2008 (complexes)	Pfam domains
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA
	YeastRC Two-Hybrid (Seattle)

References cited on this page View Complete Literature Guide for Rpt1p

1)	Finley D, et al. (1998) Unified nomenclature for subunits of the Saccharomyces cerevisiae proteasome regulatory particle. Trends Biochem Sci 23(7):244-5
2)	Ghislain M, et al. (1993) S. cerevisiae 26S protease mutants arrest cell division in G2/metaphase. Nature 366(6453):358-62
3)	Schnall R, et al. (1994) Identification of a set of yeast genes coding for a novel family of putative ATPases with high similarity to constituents of the 26S protease complex. Yeast 10(9):1141-55
4)	Takeuchi J and Toh-e A (1999) Genetic evidence for interaction between components of the yeast 26S proteasome: combination of a mutation in RPN12 (a lid component gene) with mutations in RPT1 (an ATPase gene) causes synthetic lethality. Mol Gen Genet 262(1):145-53
5)	Glickman MH, et al. (1998) The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol 18(6):3149-62
6)	Rubin DM, et al. (1998) Active site mutants in the six regulatory particle ATPases reveal multiple roles for ATP in the proteasome. EMBO J 17(17):4909-19
7)	Morris MC, et al. (2003) Cks1-dependent proteasome recruitment and activation of CDC20 transcription in budding yeast. Nature 423(6943):1009-13
8)	Torres EM, et al. (2010) Identification of aneuploidy-tolerating mutations. Cell 143(1):71-83
9)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41