UniProt ID | CRZ1_YEAST | |
---|---|---|
UniProt AC | P53968 | |
Protein Name | Transcriptional regulator CRZ1 | |
Gene Name | CRZ1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 678 | |
Subcellular Localization | Nucleus . Cytoplasm . | |
Protein Description | Involved in the regulation of calcium ion homeostasis. Binds to the calcineurin-dependent response element. Transcriptionally regulates PMC1, PMR1, PMR2A and FKS2.. | |
Protein Sequence | MSFSNGNMASYMTSSNGEEQSINNKNDIDDNSAYRRNNFRNSSNSGSHTFQLSDLDLDVDMRMDSANSSEKISKNLSSGIPDSFDSNVNSLLSPSSGSYSADLNYQSLYKPDLPQQQLQQQQLQQQQQQQQQQQQQQQKQTPTLKVEQSDTFQWDDILTPADNQHRPSLTNQFLSPRSNYDGTTRSSGIDSNYSDTESNYHTPYLYPQDLVSSPAMSHLTANNDDFDDLLSVASMNSNYLLPVNSHGYKHISNLDELDDLLSLTYSDNNLLSASNNSDFNNSNNGIINTADTQNSTIAINKSKVGTNQKMLLTIPTSSTPSPSTHAAPVTPIISIQEFNEGHFPVKNEDDGTLQLKVRDNESYSATNNNNLLRPDDNDYNNEALSDIDRSFEDIINGRKLKLKKSRRRSSQTSNNSFTSRRSSRSRSISPDEKAKSISANREKLLEMADLLPSSENDNNRERYDNDSKTSYNTINSSNFNEDNNNNNLLTSKPKIESGIVNIKNELDDTSKDLGILLDIDSLGQFEQKVGFKNDDNHENNDNGTFSVKKNDNLEKLDSVTNNRKNPANFACDVCGKKFTRPYNLKSHLRTHTNERPFICSICGKAFARQHDRKRHEDLHTGKKRYVCGGKLKDGKPWGCGKKFARSDALGRHFKTESGRRCITPLYEEARQEKSGQES | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
32 | Phosphorylation | KNDIDDNSAYRRNNF CCCCCCCHHHHHHCC | 33.40 | 28889911 | |
42 | Phosphorylation | RRNNFRNSSNSGSHT HHHCCCCCCCCCCCE | 27.00 | 22369663 | |
43 | Phosphorylation | RNNFRNSSNSGSHTF HHCCCCCCCCCCCEE | 38.27 | 28132839 | |
45 | Phosphorylation | NFRNSSNSGSHTFQL CCCCCCCCCCCEEEC | 43.55 | 22369663 | |
47 | Phosphorylation | RNSSNSGSHTFQLSD CCCCCCCCCEEECCC | 21.12 | 22369663 | |
49 | Phosphorylation | SSNSGSHTFQLSDLD CCCCCCCEEECCCCC | 18.12 | 28132839 | |
53 | Phosphorylation | GSHTFQLSDLDLDVD CCCEEECCCCCCCEE | 25.91 | 22369663 | |
65 | Phosphorylation | DVDMRMDSANSSEKI CEEEECCCCCCHHHH | 21.73 | 30377154 | |
68 | Phosphorylation | MRMDSANSSEKISKN EECCCCCCHHHHHHH | 39.32 | 23749301 | |
69 | Phosphorylation | RMDSANSSEKISKNL ECCCCCCHHHHHHHH | 42.59 | 25752575 | |
71 | Ubiquitination | DSANSSEKISKNLSS CCCCCHHHHHHHHHC | 54.98 | 23749301 | |
141 | Phosphorylation | QQQQQKQTPTLKVEQ HHHHHHHCCCCCEEC | 25.85 | 24909858 | |
159 | Phosphorylation | FQWDDILTPADNQHR CCCCCCCCCCCCCCC | 19.43 | 28889911 | |
168 | Phosphorylation | ADNQHRPSLTNQFLS CCCCCCCCHHCCCCC | 48.02 | 19779198 | |
170 | Phosphorylation | NQHRPSLTNQFLSPR CCCCCCHHCCCCCCC | 31.17 | 28889911 | |
175 | Phosphorylation | SLTNQFLSPRSNYDG CHHCCCCCCCCCCCC | 21.40 | 28889911 | |
178 | Phosphorylation | NQFLSPRSNYDGTTR CCCCCCCCCCCCCCC | 43.03 | 23749301 | |
245 | Phosphorylation | NYLLPVNSHGYKHIS CCEEEECCCCCCCCC | 20.65 | 28889911 | |
316 | Phosphorylation | KMLLTIPTSSTPSPS CEEEEEECCCCCCCC | 31.30 | 21440633 | |
318 | Phosphorylation | LLTIPTSSTPSPSTH EEEEECCCCCCCCCC | 46.98 | 21440633 | |
319 | Phosphorylation | LTIPTSSTPSPSTHA EEEECCCCCCCCCCC | 27.79 | 21440633 | |
321 | Phosphorylation | IPTSSTPSPSTHAAP EECCCCCCCCCCCCC | 31.41 | 21440633 | |
330 | Phosphorylation | STHAAPVTPIISIQE CCCCCCCCCEEEEEE | 14.01 | 21440633 | |
362 | Phosphorylation | LKVRDNESYSATNNN EEECCCCCCCCCCCC | 30.55 | 28889911 | |
379 | Phosphorylation | LRPDDNDYNNEALSD CCCCCCCCCCHHHHH | 26.58 | 22369663 | |
385 | Phosphorylation | DYNNEALSDIDRSFE CCCCHHHHHHCHHHH | 39.30 | 22369663 | |
390 | Phosphorylation | ALSDIDRSFEDIING HHHHHCHHHHHHHCC | 29.28 | 25704821 | |
409 | Phosphorylation | LKKSRRRSSQTSNNS CCHHHCCCCCCCCCC | 25.61 | 22369663 | |
410 | Phosphorylation | KKSRRRSSQTSNNSF CHHHCCCCCCCCCCC | 35.35 | 22369663 | |
412 | Phosphorylation | SRRRSSQTSNNSFTS HHCCCCCCCCCCCCC | 35.06 | 22369663 | |
413 | Phosphorylation | RRRSSQTSNNSFTSR HCCCCCCCCCCCCCC | 26.78 | 22369663 | |
416 | Phosphorylation | SSQTSNNSFTSRRSS CCCCCCCCCCCCCCC | 33.87 | 22369663 | |
418 | Phosphorylation | QTSNNSFTSRRSSRS CCCCCCCCCCCCCCC | 22.57 | 22369663 | |
419 | Phosphorylation | TSNNSFTSRRSSRSR CCCCCCCCCCCCCCC | 24.56 | 22369663 | |
423 | Phosphorylation | SFTSRRSSRSRSISP CCCCCCCCCCCCCCH | 32.25 | 17287358 | |
425 | Phosphorylation | TSRRSSRSRSISPDE CCCCCCCCCCCCHHH | 32.12 | 17287358 | |
427 | Phosphorylation | RRSSRSRSISPDEKA CCCCCCCCCCHHHHH | 28.76 | 21082442 | |
429 | Phosphorylation | SSRSRSISPDEKAKS CCCCCCCCHHHHHHH | 27.78 | 21082442 | |
436 | Phosphorylation | SPDEKAKSISANREK CHHHHHHHHCCCHHH | 27.00 | 24930733 | |
453 | Phosphorylation | EMADLLPSSENDNNR HHHHHCCCCCCCCCC | 50.70 | 22369663 | |
454 | Phosphorylation | MADLLPSSENDNNRE HHHHCCCCCCCCCCC | 38.18 | 22369663 | |
473 | Phosphorylation | DSKTSYNTINSSNFN CCCCCCCCCCCCCCC | 17.19 | 23749301 | |
476 | Phosphorylation | TSYNTINSSNFNEDN CCCCCCCCCCCCCCC | 23.86 | 28889911 | |
490 | Phosphorylation | NNNNNLLTSKPKIES CCCCCCCCCCCCEEC | 37.56 | 30377154 | |
497 | Phosphorylation | TSKPKIESGIVNIKN CCCCCEECCCEEEEC | 36.97 | 22369663 | |
548 | Acetylation | DNGTFSVKKNDNLEK CCCCEEEECCCCHHH | 44.66 | 25381059 | |
555 | Acetylation | KKNDNLEKLDSVTNN ECCCCHHHHHHHCCC | 61.84 | 24489116 | |
558 | Phosphorylation | DNLEKLDSVTNNRKN CCHHHHHHHCCCCCC | 41.08 | 30377154 | |
663 | Phosphorylation | ESGRRCITPLYEEAR CCCCEEECHHHHHHH | 15.74 | 27214570 |
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 CRZ1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CRZ1_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 CRZ1_YEAST !! |
Kegg Drug | ||||||
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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-68; SER-69; SER-245;SER-321; SER-413; SER-427; SER-429 AND SER-453, AND MASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410 AND THR-412, ANDMASS SPECTROMETRY. |