| UniProt ID | FIMB_YEAST | |
|---|---|---|
| UniProt AC | P32599 | |
| Protein Name | Fimbrin | |
| Gene Name | SAC6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 642 | |
| Subcellular Localization | ||
| Protein Description | Binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity.. | |
| Protein Sequence | MNIVKLQRKFPILTQEDLFSTIEKFRAIDLDDKGWVEKQQALEAVSKDGDATYDEARETLKHVGVDASGRVELDDYVGLVAKLRESKTGAAPQTTFNVAPNSTPIVSTAATGLQHKGKGTQAKIIVAGSQTGTTHTINEEERREFTKHINSVLAGDQDIGDLLPFPTDTFQLFDECRDGLVLSKLINDSVPDTIDTRVLNWPKKGKELNNFQASENANIVINSAKAIGCVVVNVHSEDIIEGREHLILGLIWQIIRRGLLSKIDIKLHPELYRLLEDDETLEQFLRLPPEQILLRWFNYHLKQANWNRRVTNFSKDVSDGENYTILLNQLDPALCSKAPLQTTDLMERAEQVLQNAEKLDCRKYLTPSSLVAGNPKLNLAFVAHLFNTHPGLEPIQEEEKPEIEEFDAEGEREARVFTLWLNSLDVDPPVISLFDDLKDGLILLQAYEKVMPGAVDFKHVNKRPASGAEISRFKALENTNYAVDLGRAKGFSLVGIEGSDIVDGNKLLTLGLVWQLMRRNISITMKTLSSSGRDMSDSQILKWAQDQVTKGGKNSTIRSFKDQALSNAHFLLDVLNGIAPGYVDYDLVTPGNTEEERYANARLAISIARKLGALIWLVPEDINEVRARLIITFIASLMTLNK | |
| 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 |
|---|---|---|---|---|---|
| 5 | Succinylation | ---MNIVKLQRKFPI ---CCCHHCCCCCCC | 34.80 | 23954790 | |
| 5 | Acetylation | ---MNIVKLQRKFPI ---CCCHHCCCCCCC | 34.80 | 24489116 | |
| 5 | Ubiquitination | ---MNIVKLQRKFPI ---CCCHHCCCCCCC | 34.80 | 24961812 | |
| 9 | Ubiquitination | NIVKLQRKFPILTQE CCHHCCCCCCCCCHH | 42.40 | 17644757 | |
| 14 | Phosphorylation | QRKFPILTQEDLFST CCCCCCCCHHHHHHH | 30.54 | 22369663 | |
| 20 | Phosphorylation | LTQEDLFSTIEKFRA CCHHHHHHHHHHHHC | 35.45 | 21551504 | |
| 24 | Ubiquitination | DLFSTIEKFRAIDLD HHHHHHHHHHCCCCC | 35.98 | 17644757 | |
| 33 | Acetylation | RAIDLDDKGWVEKQQ HCCCCCCCCHHHHHH | 55.10 | 24489116 | |
| 38 | Ubiquitination | DDKGWVEKQQALEAV CCCCHHHHHHHHHHH | 37.78 | 24961812 | |
| 38 | Acetylation | DDKGWVEKQQALEAV CCCCHHHHHHHHHHH | 37.78 | 24489116 | |
| 47 | Ubiquitination | QALEAVSKDGDATYD HHHHHHCCCCCCCHH | 60.16 | 23749301 | |
| 47 | Succinylation | QALEAVSKDGDATYD HHHHHHCCCCCCCHH | 60.16 | 23954790 | |
| 47 | Acetylation | QALEAVSKDGDATYD HHHHHHCCCCCCCHH | 60.16 | 24489116 | |
| 61 | Acetylation | DEARETLKHVGVDAS HHHHHHHHHCCCCCC | 43.60 | 24489116 | |
| 87 | Ubiquitination | VAKLRESKTGAAPQT HHHHHHCCCCCCCCE | 46.34 | 17644757 | |
| 88 | Phosphorylation | AKLRESKTGAAPQTT HHHHHCCCCCCCCEE | 41.13 | 21440633 | |
| 102 | Phosphorylation | TFNVAPNSTPIVSTA EEECCCCCCCEEEEC | 34.20 | 21440633 | |
| 103 | Phosphorylation | FNVAPNSTPIVSTAA EECCCCCCCEEEECC | 24.55 | 25752575 | |
| 107 | Phosphorylation | PNSTPIVSTAATGLQ CCCCCEEEECCCCCC | 17.04 | 30377154 | |
| 108 | Phosphorylation | NSTPIVSTAATGLQH CCCCEEEECCCCCCC | 14.93 | 27017623 | |
| 111 | Phosphorylation | PIVSTAATGLQHKGK CEEEECCCCCCCCCC | 35.64 | 20377248 | |
| 116 | Ubiquitination | AATGLQHKGKGTQAK CCCCCCCCCCCCEEE | 49.73 | 17644757 | |
| 123 | Ubiquitination | KGKGTQAKIIVAGSQ CCCCCEEEEEEECCC | 24.13 | 17644757 | |
| 129 | Phosphorylation | AKIIVAGSQTGTTHT EEEEEECCCCCCCCC | 18.16 | 25752575 | |
| 131 | Phosphorylation | IIVAGSQTGTTHTIN EEEECCCCCCCCCCC | 37.89 | 21440633 | |
| 133 | Phosphorylation | VAGSQTGTTHTINEE EECCCCCCCCCCCHH | 20.84 | 24961812 | |
| 134 | Phosphorylation | AGSQTGTTHTINEEE ECCCCCCCCCCCHHH | 20.54 | 24961812 | |
| 136 | Phosphorylation | SQTGTTHTINEEERR CCCCCCCCCCHHHHH | 24.33 | 24961812 | |
| 146 | Phosphorylation | EEERREFTKHINSVL HHHHHHHHHHHHHHH | 19.57 | 24961812 | |
| 184 | Ubiquitination | RDGLVLSKLINDSVP CCCHHHHHHHCCCCC | 49.58 | 23749301 | |
| 184 | Acetylation | RDGLVLSKLINDSVP CCCHHHHHHHCCCCC | 49.58 | 24489116 | |
| 189 | Phosphorylation | LSKLINDSVPDTIDT HHHHHCCCCCCCCCH | 30.94 | 29688323 | |
| 193 | Phosphorylation | INDSVPDTIDTRVLN HCCCCCCCCCHHHHC | 18.06 | 29688323 | |
| 196 | Phosphorylation | SVPDTIDTRVLNWPK CCCCCCCHHHHCCCC | 20.87 | 29688323 | |
| 266 | Acetylation | LLSKIDIKLHPELYR CHHHHCCEECHHHHH | 36.67 | 24489116 | |
| 302 | Acetylation | RWFNYHLKQANWNRR HHHHHHHHHCCCCHH | 33.77 | 24489116 | |
| 315 | Ubiquitination | RRVTNFSKDVSDGEN HHCCCCCCCCCCCCC | 58.99 | 17644757 | |
| 337 | Ubiquitination | LDPALCSKAPLQTTD CCHHHHCCCCCCCHH | 53.69 | 17644757 | |
| 358 | Acetylation | QVLQNAEKLDCRKYL HHHHHHHHCCCHHHC | 47.41 | 24489116 | |
| 363 | Acetylation | AEKLDCRKYLTPSSL HHHCCCHHHCCHHHH | 51.44 | 25381059 | |
| 363 | Ubiquitination | AEKLDCRKYLTPSSL HHHCCCHHHCCHHHH | 51.44 | 23749301 | |
| 366 | Phosphorylation | LDCRKYLTPSSLVAG CCCHHHCCHHHHHCC | 20.31 | 27214570 | |
| 376 | Ubiquitination | SLVAGNPKLNLAFVA HHHCCCCCCCHHHHH | 54.74 | 17644757 | |
| 458 | Acetylation | MPGAVDFKHVNKRPA CCCCCCCCCCCCCCC | 42.03 | 24489116 | |
| 466 | Phosphorylation | HVNKRPASGAEISRF CCCCCCCCCCCCHHH | 41.02 | 19823750 | |
| 471 | Phosphorylation | PASGAEISRFKALEN CCCCCCCHHHHHHCC | 24.14 | 30377154 | |
| 474 | Ubiquitination | GAEISRFKALENTNY CCCCHHHHHHCCCCE | 51.45 | 23749301 | |
| 474 | Acetylation | GAEISRFKALENTNY CCCCHHHHHHCCCCE | 51.45 | 24489116 | |
| 522 | Phosphorylation | QLMRRNISITMKTLS HHHHCCCCEEEEECC | 18.63 | 25521595 | |
| 524 | Phosphorylation | MRRNISITMKTLSSS HHCCCCEEEEECCCC | 13.06 | 25521595 | |
| 531 | Phosphorylation | TMKTLSSSGRDMSDS EEEECCCCCCCCCHH | 34.18 | 21440633 | |
| 536 | Phosphorylation | SSSGRDMSDSQILKW CCCCCCCCHHHHHHH | 38.10 | 22369663 | |
| 538 | Phosphorylation | SGRDMSDSQILKWAQ CCCCCCHHHHHHHHH | 16.29 | 22369663 | |
| 542 | Acetylation | MSDSQILKWAQDQVT CCHHHHHHHHHHHHH | 41.95 | 24489116 |
| 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 FIMB_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FIMB_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 FIMB_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-129, AND MASSSPECTROMETRY. | |
| "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-466, AND MASSSPECTROMETRY. | |
