Basic Information

NameHit family protein 1 (EC 3.-.-.-) (Adenosine 5'-monophosphoramidase)
Uniprot IDQ04344
Systematic gene nameYDL125C
Standard gene nameHNT1
Gene namesHNT1 HIT1 YDL125C
Description from SGDYDL125C HNT1 SGDID:S000002283, Chr IV from 239398-239019,239606-239510, Genome Release 64-3-1, reverse complement, Verified ORF, "Adenosine 5'-monophosphoramidase; interacts physically and genetically with Kin28p, a CDK and TFIIK subunit, and genetically with CAK1; member of histidine triad (HIT) superfamily of nucleotide-binding proteins; protein abundance increases in response to DNA replication stress; human homolog HINT1 can complement yeast hnt1 mutant"
Protein length158
Downloadsequence (fasta, from Uniprot), modifications (csv format)
Database linksUniprot, SGD, TheCellVision.org, FungiDB

Sequence

MEPLISAPYL TTTKMSAPAT LDAACIFCKI IKSEIPSFKL IETKYSYAFL
DIQPTAEGHA LIIPKYHGAK LHDIPDEFLT DAMPIAKRLA KAMKLDTYNV
LQNNGKIAHQ EVDHVHFHLI PKRDEKSGLI VGWPAQETDF DKLGKLHKEL
LAKLEGSD

Legend

  • X K-acetylation
  • X SUMOylation
  • X Ubiquitination
  • X Phoshorylation

Structure

Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.


Use imported representation

Loading structure from server... It may take a while.

If you believe something went wrong, please make sure PDB ID is correct.
Please also make sure that WebGL is enabled in your browser.

References

[32, K-acetyl]Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications)
[39, SUMO]Bhagwat, N.R., Owens, S.N., Ito, M., Boinapalli, J.V,, Poa, P., Ditzel, A., Kopparapu, S., Mahalawat, M., Davies, O.R., Collins, S.R., Johnson, J.R., Krogan, N.J., Hunter, N. (2021). SUMO is a pervasive regulator of meiosis. Elife 10:e57720. (Publication) (All modifications)
[44, Ubi]Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[70, Ubi]Swaney, D.L.,  Beltrao, P.,  Starita, L.,  Guo, A.,  Rush, J.,  Fields, S.,  Krogan, N.J.,  Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications)
[97, Phos]Lanz MC, Yugandhar K, Gupta S, Sanford EJ, Faça VM, Vega S, Joiner AMN, Fromme JC, Yu H, Smolka MB (2021). In-depth and 3-dimensional exploration of the budding yeast phosphoproteome. EMBO Reports, e51121. (Publication) (All modifications)
[127, Phos]Zhou, X., Li, W., Liu, Y., Amon, A. (2021. Cross-compartment signal propagation in the mitotic exit network. Elife 10:e63645. (Publication) (All modifications)
[148, K-acetyl]Henriksen, P., Wagner, S. A., Weinert, B. T., et al. (2012). Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Molecular & Cellular Proteomics, 11(11), 1510-1522. (Publication) (All modifications)