| UniProt ID | HIR2_YEAST | |
|---|---|---|
| UniProt AC | P32480 | |
| Protein Name | Protein HIR2 | |
| Gene Name | HIR2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 875 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component of the HIR complex, which cooperates with ASF1 to promote replication-independent chromatin assembly. The HIR complex is also required for the periodic repression of three of the four histone gene loci during the cell cycle as well as for autogenous regulation of the HTA1-HTB1 locus by H2A and H2B. DNA-binding by the HIR complex may repress transcription by inhibiting nucleosome remodeling by the SWI/SNF complex. The HIR complex may also be required for transcriptional silencing of centromeric, telomeric and mating-type loci in the absence of CAF-1.. | |
| Protein Sequence | MRLLKYPLDIHNEQVNALAALGPYIILAGSGGHVMAWRQQQLVDTAFDRVMIKDLKPEVSFQVDQDTTGDIFFITGDLETLYIGSEHRLWGYSGWLCRDTNNINSVEKMNSKLLFECKSPSTITDVKYDINLGILFVLLSNENKILLFRHKTFDKLSEITIDKASKPITGIIDPTGQTFTVMTSDRSILVYQINKTGTHKLINKLTQHVQMYPLHYRISMSPQADILPVINSVKGVPNNATSCTALLDRNNNYKVTKTLVTPSSNGCRVLVYSPAFYEKPNLKKGTSTRYNLIATSGSTDGTILVWNTKRMKPLFNALQVSSTAINDMSWSQDGFTLFAISNDATLYTFAFQEKDLGVALPQTEIKSLQEVNKKLPKLEEPLAEQIPKSFPENIKLEESASAAPIPNDIGRSAVGKKPTKKKTANNQTNGIKTIQSTSMEFNTPSYTVPRDLKRKPKEATPSNIAPGSKKQKKELQPIDFLDTGLLLPNTSFSRIRLATPKIRSTFKYSPINNPNLILDVKNGSGNEQRPTIVKLTSKVLDQDQVLFQDFIPKLITICTAGDTFWSFCSEDGSIYIYSDSGRKLMAPLVLGVSISFLEACGTYLLCLTSIGELYCWNIEQKKLAFPTNTIYPLLNPSLRYSDDILTRAENITLCSITKKGVPLVTLSNGDGYLFDKNMETWLLVSDGWWAYGSQYWDTTNTTGLSSSKANTDSFNGSESNINEIVSDIKNDNQSIINFLECKTNDELNRKGRIKNLQRFARTILMKEGFENMEEIVTLSHLENKILISIRLEEPEEFSKLMMVYCIRLSELGYMDRLNDVFQWLYDDLPISGTGSAFADKDFKRNLLKKILIACGDIRQVQRVTTRYAKEMNIIS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 100 | Phosphorylation | SGWLCRDTNNINSVE CCEEECCCCCCCCHH | 15.71 | 28889911 | |
| 206 | Phosphorylation | HKLINKLTQHVQMYP HHHHHHHHHHCHHCC | 20.45 | 21126336 | |
| 388 | Acetylation | PLAEQIPKSFPENIK HHHHHCCCCCCCCCC | 67.37 | 24489116 | |
| 389 | Phosphorylation | LAEQIPKSFPENIKL HHHHCCCCCCCCCCC | 40.45 | 22369663 | |
| 399 | Phosphorylation | ENIKLEESASAAPIP CCCCCCHHCCCCCCC | 20.39 | 22369663 | |
| 401 | Phosphorylation | IKLEESASAAPIPND CCCCHHCCCCCCCCC | 33.95 | 22369663 | |
| 428 | Phosphorylation | KKTANNQTNGIKTIQ CCCCCCCCCCEEEEE | 37.22 | 28889911 | |
| 436 | Phosphorylation | NGIKTIQSTSMEFNT CCEEEEEECCCCCCC | 20.71 | 28889911 | |
| 438 | Phosphorylation | IKTIQSTSMEFNTPS EEEEEECCCCCCCCC | 22.89 | 27214570 | |
| 443 | Phosphorylation | STSMEFNTPSYTVPR ECCCCCCCCCCCCCC | 20.94 | 27214570 | |
| 460 | Phosphorylation | KRKPKEATPSNIAPG CCCCCCCCCCCCCCC | 28.48 | 22369663 | |
| 462 | Phosphorylation | KPKEATPSNIAPGSK CCCCCCCCCCCCCCH | 36.19 | 22369663 | |
| 711 | Phosphorylation | LSSSKANTDSFNGSE CCCCCCCCCCCCCCH | 37.57 | 30377154 | |
| 713 | Phosphorylation | SSKANTDSFNGSESN CCCCCCCCCCCCHHC | 20.69 | 28889911 | |
| 717 | Phosphorylation | NTDSFNGSESNINEI CCCCCCCCHHCHHHH | 38.67 | 27017623 | |
| 719 | Phosphorylation | DSFNGSESNINEIVS CCCCCCHHCHHHHHH | 44.71 | 30377154 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of HIR2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HIR2_YEAST !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of HIR2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438 AND SER-713, ANDMASS SPECTROMETRY. | |
