CLB1/YGR108W Protein Information

Standard Name	Clb1p 1
Systematic Name	Ygr108wp
Alias	Scb1p 2
ORF Classification	Verified
Description	B-type cyclin involved in cell cycle progression; activates Cdc28p to promote the transition from G2 to M phase; accumulates during G2 and M, then targeted via a destruction box motif for ubiquitin-mediated degradation by the proteasome; CLB1 has a paralog, CLB2, that arose from the whole genome duplication (1, 2, 3, 4, 5)
Name Description	CycLin B 1

Experimental Data
Molecules/cell	300 6

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	471
Molecular Weight (Da)	54,870
Isoelectric Point (pI)	5.77

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 Clb1p (InterPro)
Physical Interactions	There are 17 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000012757A \| P24868 MIPS: YGR108W NCBI: 116159 \| 1323169 \| 171235 \| 172539 \| 6321545 \| NP_011622.1 GenBank/EMBL/DDBJ: DAA08200.1 \| M62389 \| M65069 \| Z72893

Amino Acid Sequence (or in FASTA format)
1 MSRSLLVENS RTINSNEEKG VNESQYILQK RNVPRTILGN VTNNANILQE 51 ISMNRKIGMK NFSKLNNFFP LKDDVSRADD FTSSFNDSRQ GVKQEVLNNK 101 ENIPEYGYSE QEKQQCSNDD SFHTNSTALS CNRLIYSENK SISTQMEWQK 151 KIMREDSKKK RPISTLVEQD DQKKFKLHEL TTEEEVLEEY EWDDLDEEDC 201 DDPLMVSEEV NDIFDYLHHL EIITLPNKAN LYKHKNIKQN RDILVNWIIK 251 IHNKFGLLPE TLYLAINIMD RFLCEEVVQL NRLQLVGTSC LFIASKYEEI 301 YSPSIKHFAY ETDGACSVED IKEGERFILE KLDFQISFAN PMNFLRRISK 351 ADDYDIQSRT LAKFLMEISI VDFKFIGILP SLCASAAMFL SRKMLGKGTW 401 DGNLIHYSGG YTKAKLYPVC QLLMDYLVGS TIHDEFLKKY QSRRFLKASI 451 ISIEWALKVR KNGYDIMTLH E*

Amino Acid Sequence (or in FASTA format)

       1  MSRSLLVENS RTINSNEEKG VNESQYILQK RNVPRTILGN VTNNANILQE
      51  ISMNRKIGMK NFSKLNNFFP LKDDVSRADD FTSSFNDSRQ GVKQEVLNNK
     101  ENIPEYGYSE QEKQQCSNDD SFHTNSTALS CNRLIYSENK SISTQMEWQK
     151  KIMREDSKKK RPISTLVEQD DQKKFKLHEL TTEEEVLEEY EWDDLDEEDC
     201  DDPLMVSEEV NDIFDYLHHL EIITLPNKAN LYKHKNIKQN RDILVNWIIK
     251  IHNKFGLLPE TLYLAINIMD RFLCEEVVQL NRLQLVGTSC LFIASKYEEI
     301  YSPSIKHFAY ETDGACSVED IKEGERFILE KLDFQISFAN PMNFLRRISK
     351  ADDYDIQSRT LAKFLMEISI VDFKFIGILP SLCASAAMFL SRKMLGKGTW
     401  DGNLIHYSGG YTKAKLYPVC QLLMDYLVGS TIHDEFLKKY QSRRFLKASI
     451  ISIEWALKVR KNGYDIMTLH E*

external links for Clb1p

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

References cited on this page View Complete Literature Guide for Clb1p

1)	Surana U, et al. (1991) The role of CDC28 and cyclins during mitosis in the budding yeast S. cerevisiae. Cell 65(1):145-61
2)	Ghiara JB, et al. (1991) A cyclin B homolog in S. cerevisiae: chronic activation of the Cdc28 protein kinase by cyclin prevents exit from mitosis. Cell 65(1):163-74
3)	Fitch I, et al. (1992) Characterization of four B-type cyclin genes of the budding yeast Saccharomyces cerevisiae. Mol Biol Cell 3(7):805-18
4)	Mendenhall MD and Hodge AE (1998) Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae. Microbiol Mol Biol Rev 62(4):1191-243
5)	Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61
6)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41