HCH1/YNL281W Protein Information Help

Standard Name Hch1p 1
Systematic Name Ynl281wp
ORF Classification Verified
Description Heat shock protein regulator; binds to Hsp90p and may stimulate ATPase activity; originally identified as a high-copy number suppressor of a HSP90 loss-of-function mutation; GFP-fusion protein localizes to the cytoplasm and nucleus; protein abundance increases in response to DNA replication stress (1, 2, 3, 4, 5)
Name Description High-Copy Hsp90 suppressor 1
Experimental Data
Molecules/cell 8530 6
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 153
Molecular Weight (Da) 17,246
Isoelectric Point (pI) 4.4

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Hch1p (InterPro)
Physical Interactions There are 24 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI000013BA6E | P53834
MIPS: YNL281W
NCBI: 1302353 | 1730645 | 6324048 | NP_014118.1
GenBank/EMBL/DDBJ: DAA10279.1 | Z71557
Amino Acid Sequence (or in FASTA format)
 
       1  MVVLNPNNWH WVDKNTLPWS KDYLNGKLTS LSTVSSDGKS KIELTQVSSI
      51  TGDSNVSQRK GKPICYFDLQ LSMNVKVTNL DTNKDDEDDD GILADGKLEI
     101  PEFMHDESDI PILSQGFDAF DGLVRSEFVP KVVETLLKYQ DDLIKEHSKD
     151  IQV*

external links for Hch1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Candida (CGD) BioPIXIE MIPS YeastGFP
YGOB CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
YOGY Complexome


DIP


GeneMANIA

References cited on this page View Complete Literature Guide for Hch1p
1) Nathan DF, et al.  (1999) Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation. Proc Natl Acad Sci U S A 96(4):1409-14
2) Panaretou B, et al.  (2002) Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol Cell 10(6):1307-18
3) Lotz GP, et al.  (2003) Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone. J Biol Chem 278(19):17228-35
4) Huh WK, et al.  (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
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