YKL151C Protein Information

Systematic Name	Ykl151cp
ORF Classification	Verified
Description	NADHX dehydratase; converts (S)-NADHX to NADH in an ATP-dependent manner; homologous to Carkd in mammals, and the C-terminal domain of YjeF in E.coli; enzyme is widespread in eukaryotes, prokaryotes and archaea; YKL151C promoter contains STREs (stress response elements) and expression is induced by heat shock or methyl methanesulfonate; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm; protein abundance increases in response to DNA replication stress (1, 2, 3, 4, 5)

Experimental Data
Molecules/cell	3870 6

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	337
Molecular Weight (Da)	37,357
Isoelectric Point (pI)	7.48

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 Ykl151cp (InterPro)
Physical Interactions	There are 10 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI000013B738 \| P36059 MIPS: YKL151C NCBI: 407496 \| 45269721 \| 486262 \| 549726 \| 6322698 \| NP_012771.1 \| NM_001179717.1 GenBank/EMBL/DDBJ: DAA09012.1 \| AY557915 \| Z26877 \| Z28151
External Classifications	EC: 4.2.1.93 [ATP-dependent NAD(P)H-hydrate dehydratase]

Amino Acid Sequence (or in FASTA format)
1 MLAELSHREL IKLAQKRCIP PLLPKFHKGQ SGGRVCIIGG CEDYTGAPYF 51 SANATALMGC DLTHVICEYN AGTVIKSYTP NLMVHPYLRM SNTKLDVDMD 101 EQRKKINSLL DRIHVVVIGP GLGRDPLMLK SIKDIIRYIL EKHEGKIPLV 151 IDADGLFLVT QDSEVKEMLK SYPKGRVILT PNVVEFKRLC DAIGKKGDSH 201 SEMGSLIAQE LNCIVVEKGQ SDKIFSPDSE KDMLTNSEEG SNKRVGGQGD 251 TLTGAISCML AFSRAMYDFK ICEQEEKGES SNDKPLKNWV DYAMLSCYAG 301 CTITRECSRL GFKAKGRAMQ TTDLNDRVGE VFAKLFG*

Amino Acid Sequence (or in FASTA format)

       1  MLAELSHREL IKLAQKRCIP PLLPKFHKGQ SGGRVCIIGG CEDYTGAPYF
      51  SANATALMGC DLTHVICEYN AGTVIKSYTP NLMVHPYLRM SNTKLDVDMD
     101  EQRKKINSLL DRIHVVVIGP GLGRDPLMLK SIKDIIRYIL EKHEGKIPLV
     151  IDADGLFLVT QDSEVKEMLK SYPKGRVILT PNVVEFKRLC DAIGKKGDSH
     201  SEMGSLIAQE LNCIVVEKGQ SDKIFSPDSE KDMLTNSEEG SNKRVGGQGD
     251  TLTGAISCML AFSRAMYDFK ICEQEEKGES SNDKPLKNWV DYAMLSCYAG
     301  CTITRECSRL GFKAKGRAMQ TTDLNDRVGE VFAKLFG*

external links for Ykl151cp

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	GeneMANIA
YOGY

References cited on this page View Complete Literature Guide for Ykl151cp

1)	Treger JM, et al. (1998) Transcriptional factor mutations reveal regulatory complexities of heat shock and newly identified stress genes in Saccharomyces cerevisiae. J Biol Chem 273(41):26875-9
2)	Huh WK, et al. (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
3)	Sakaki K, et al. (2003) Response of genes associated with mitochondrial function to mild heat stress in yeast Saccharomyces cerevisiae. J Biochem 134(3):373-84
4)	Marbaix AY, et al. (2011) Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair. J Biol Chem 286(48):41246-52
5)	Tkach JM, et al. (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
6)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41