CLB2/YPR119W Protein Information

Standard Name	Clb2p 1
Systematic Name	Ypr119wp
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; CLB2 has a paralog, CLB1, that arose from the whole genome duplication (1, 2, 3, 4, 5)
Name Description	CycLin B 1

Experimental Data
Molecules/cell	339 6

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	491
Molecular Weight (Da)	56,246
Isoelectric Point (pI)	6.71

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 Clb2p (InterPro)
Physical Interactions	There are 121 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000012757E \| P24869 MIPS: YPR119W NCBI: 1066473 \| 116164 \| 171237 \| 5500 \| 6325376 \| NP_015444.1 GenBank/EMBL/DDBJ: DAA11534.1 \| M65070 \| U40828 \| X62319

Amino Acid Sequence (or in FASTA format)
1 MSNPIENTEN SQNTSSSRFL RNVQRLALNN VTNTTFQKSN ANNPALTNFK 51 STLNSVKKEG SRIPQFTRES VSRSTAAQEE KRTLKENGIQ LPKNNLLDDK 101 ENQDPSSQQF GALTSIKEGR AELPANISLQ ESSSAKEIIQ HDPLKGVGSS 151 TEVVHNSVEN EKLHPARSQL QVRNTESETD SGKKRPISTI VEQELPKKFK 201 VCDENGKEEY EWEDLDAEDV NDPFMVSEYV NDIFEYLHQL EVITLPKKED 251 LYQHRNIHQN RDILVNWLVK IHNKFGLLPE TLYLAINIMD RFLGKELVQL 301 DKLQLVGTSC LFIASKYEEV YSPSIKHFAS ETDGACTEDE IKEGEKFILK 351 TLKFNLNYPN PMNFLRRISK ADDYDIQSRT LAKFLLEISL VDFRFIGILP 401 SLCAAAAMFM SRKMLGKGKW DGNLIHYSGG YTKEELAPVC HMIMDYLVSP 451 IVHDEFHRKY QSRRFMKASI ISVQWALKVR KNGYDIMTLH E*

Amino Acid Sequence (or in FASTA format)

       1  MSNPIENTEN SQNTSSSRFL RNVQRLALNN VTNTTFQKSN ANNPALTNFK
      51  STLNSVKKEG SRIPQFTRES VSRSTAAQEE KRTLKENGIQ LPKNNLLDDK
     101  ENQDPSSQQF GALTSIKEGR AELPANISLQ ESSSAKEIIQ HDPLKGVGSS
     151  TEVVHNSVEN EKLHPARSQL QVRNTESETD SGKKRPISTI VEQELPKKFK
     201  VCDENGKEEY EWEDLDAEDV NDPFMVSEYV NDIFEYLHQL EVITLPKKED
     251  LYQHRNIHQN RDILVNWLVK IHNKFGLLPE TLYLAINIMD RFLGKELVQL
     301  DKLQLVGTSC LFIASKYEEV YSPSIKHFAS ETDGACTEDE IKEGEKFILK
     351  TLKFNLNYPN PMNFLRRISK ADDYDIQSRT LAKFLLEISL VDFRFIGILP
     401  SLCAAAAMFM SRKMLGKGKW DGNLIHYSGG YTKEELAPVC HMIMDYLVSP
     451  IVHDEFHRKY QSRRFMKASI ISVQWALKVR KNGYDIMTLH E*

external links for Clb2p

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

References cited on this page View Complete Literature Guide for Clb2p

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