UniProt ID | ARP4_YEAST | |
---|---|---|
UniProt AC | P80428 | |
Protein Name | Actin-related protein 4 | |
Gene Name | ARP4 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 489 | |
Subcellular Localization | Nucleus . | |
Protein Description | Chromatin interaction component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair. ARP4 recognizes H2AS128ph (gamma-H2A) and is required for NuA4 complex integrity. Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the INO80 complex which remodels chromatin by shifting nucleosomes. Its ability to induce transcription of some phosphate-responsive genes is modulated by inositol polyphosphates. The INO80 complex is involved in DNA repair by associating to gamma-H2A as a response to DNA damage.. | |
Protein Sequence | MSNAALQVYGGDEVSAVVIDPGSYTTNIGYSGSDFPQSILPSVYGKYTADEGNKKIFSEQSIGIPRKDYELKPIIENGLVIDWDTAQEQWQWALQNELYLNSNSGIPALLTEPVWNSTENRKKSLEVLLEGMQFEACYLAPTSTCVSFAAGRPNCLVVDIGHDTCSVSPIVDGMTLSKSTRRNFIAGKFINHLIKKALEPKEIIPLFAIKQRKPEFIKKTFDYEVDKSLYDYANNRGFFQECKETLCHICPTKTLEETKTELSSTAKRSIESPWNEEIVFDNETRYGFAEELFLPKEDDIPANWPRSNSGVVKTWRNDYVPLKRTKPSGVNKSDKKVTPTEEKEQEAVSKSTSPAANSADTPNETGKRPLEEEKPPKENNELIGLADLVYSSIMSSDVDLRATLAHNVVLTGGTSSIPGLSDRLMTELNKILPSLKFRILTTGHTIERQYQSWLGGSILTSLGTFHQLWVGKKEYEEVGVERLLNDRFR | |
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 |
---|---|---|---|---|---|
210 | Ubiquitination | IIPLFAIKQRKPEFI HEEEEEECCCCHHHH | 40.39 | 24961812 | |
227 | Acetylation | TFDYEVDKSLYDYAN HCCCCCCHHHHHHHC | 47.76 | 24489116 | |
309 | Phosphorylation | ANWPRSNSGVVKTWR CCCCCCCCCCCCCCC | 33.92 | 28889911 | |
323 | Acetylation | RNDYVPLKRTKPSGV CCCCCCCCCCCCCCC | 52.53 | 22865919 | |
338 | Phosphorylation | NKSDKKVTPTEEKEQ CCCCCCCCCCHHHHH | 33.11 | 21082442 | |
340 | Phosphorylation | SDKKVTPTEEKEQEA CCCCCCCCHHHHHHH | 47.62 | 17330950 | |
349 | Phosphorylation | EKEQEAVSKSTSPAA HHHHHHHHHCCCCCC | 28.12 | 21082442 | |
350 | Acetylation | KEQEAVSKSTSPAAN HHHHHHHHCCCCCCC | 51.67 | 23572591 | |
351 | Phosphorylation | EQEAVSKSTSPAANS HHHHHHHCCCCCCCC | 26.98 | 25521595 | |
352 | Phosphorylation | QEAVSKSTSPAANSA HHHHHHCCCCCCCCC | 42.33 | 25521595 | |
353 | Phosphorylation | EAVSKSTSPAANSAD HHHHHCCCCCCCCCC | 21.45 | 25521595 | |
358 | Phosphorylation | STSPAANSADTPNET CCCCCCCCCCCCCCC | 23.85 | 22890988 | |
361 | Phosphorylation | PAANSADTPNETGKR CCCCCCCCCCCCCCC | 27.94 | 22890988 | |
365 | Phosphorylation | SADTPNETGKRPLEE CCCCCCCCCCCCCCC | 55.43 | 22890988 | |
390 | Phosphorylation | IGLADLVYSSIMSSD HHHHHHHHHHHHCCC | 12.19 | 27017623 | |
391 | Phosphorylation | GLADLVYSSIMSSDV HHHHHHHHHHHCCCC | 13.10 | 27017623 | |
392 | Phosphorylation | LADLVYSSIMSSDVD HHHHHHHHHHCCCCC | 12.48 | 27017623 | |
396 | Phosphorylation | VYSSIMSSDVDLRAT HHHHHHCCCCCHHHH | 25.03 | 27017623 | |
436 | Acetylation | NKILPSLKFRILTTG HHHHHHCCEEEEECC | 36.61 | 24489116 | |
450 | Phosphorylation | GHTIERQYQSWLGGS CCHHHHHHHHHHCHH | 15.67 | 27017623 | |
452 | Phosphorylation | TIERQYQSWLGGSIL HHHHHHHHHHCHHHH | 21.23 | 27017623 | |
457 | Phosphorylation | YQSWLGGSILTSLGT HHHHHCHHHHHHHHH | 16.78 | 27017623 | |
460 | Phosphorylation | WLGGSILTSLGTFHQ HHCHHHHHHHHHHEE | 21.89 | 27017623 | |
461 | Phosphorylation | LGGSILTSLGTFHQL HCHHHHHHHHHHEEE | 22.74 | 27017623 | |
464 | Phosphorylation | SILTSLGTFHQLWVG HHHHHHHHHEEECCC | 24.20 | 27017623 |
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 ARP4_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ARP4_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 ARP4_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 THR-338; SER-349 ANDSER-353, AND MASS SPECTROMETRY. |