P18961
Gene name |
YPK2 (YKR2, YMR104C, YM9718.03C) |
Protein name |
Serine/threonine-protein kinase YPK2/YKR2 |
Names |
|
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YMR104C |
EC number |
2.7.11.1: Protein-serine/threonine kinases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for P18961
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P18961-F1 | Predicted | AlphaFoldDB |
12 variants for P18961
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s13-475324 | 43 | H>Q | No | SGRP | |
| s13-475251 | 68 | P>S | No | SGRP | |
| s13-475159 | 98 | R>S | No | SGRP | |
| s13-475125 | 110 | P>S | No | SGRP | |
| s13-474894 | 187 | A>S | No | SGRP | |
| s13-474719 | 245 | R>P | No | SGRP | |
| s13-474680 | 258 | L>P | No | SGRP | |
| s13-474623 | 277 | K>R | No | SGRP | |
| s13-474467 | 329 | V>A | No | SGRP | |
| s13-474440 | 338 | P>H | No | SGRP | |
| s13-474398 | 352 | K>R | No | SGRP | |
| s13-473598 | 619 | I>L | No | SGRP |
No associated diseases with P18961
5 regional properties for P18961
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Protein kinase domain | 344 - 599 | IPR000719 |
| domain | AGC-kinase, C-terminal | 600 - 670 | IPR000961 |
| active_site | Serine/threonine-protein kinase, active site | 463 - 475 | IPR008271 |
| binding_site | Protein kinase, ATP binding site | 350 - 373 | IPR017441 |
| domain | Protein kinase, C-terminal | 620 - 660 | IPR017892 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.11.1 | Protein-serine/threonine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
| protein serine/threonine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| cell wall organization | A process that results in the assembly, arrangement of constituent parts, or disassembly of the cell wall, the rigid or semi-rigid envelope lying outside the cell membrane of plant, fungal and most prokaryotic cells, maintaining their shape and protecting them from osmotic lysis. |
| eisosome assembly | The aggregation, arrangement and bonding together of a set of components to form an eisosome, a cell part that is composed of the eisosome membrane and eisosome filaments. The eisosome membrane, also called the MCC domain, is a furrow-like plasma membrane sub-domain with associated integral transmembrane proteins. The eisosome filaments form a scaffolding lattice on the cytoplasmic face of the membrane. |
| peptidyl-serine phosphorylation | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. |
| regulation of cell shape | Any process that modulates the surface configuration of a cell. |
| regulation of fungal-type cell wall organization | Any process that modulates the rate, frequency or extent of the formation, arrangement of constituent parts, or disassembly of the fungal-type cell wall. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MHSWRISKFK | LGRSKEDDGS | SEDENEKSWG | NGLFHFHHGE | KHHDGSPKNH | NHEHEHHIRK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| INTNETLPSS | LSSPKLRNDA | SFKNPSGIGN | DNSKASERKA | SQSSTETQGP | SSESGLMTVK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VYSGKDFTLP | FPITSNSTIL | QKLLSSGILT | SSSNDASEVA | AIMRQLPRYK | RVDQDSAGEG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LIDRAFATKF | IPSSILLPGS | TNSSPLLYFT | IEFDNSITTI | SPDMGTMEQP | VFNKISTFDV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TRKLRFLKID | VFARIPSLLL | PSKNWQQEIG | EQDEVLKEIL | KKINTNQDIH | LDSFHLPLNL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KIDSAAQIRL | YNHHWISLER | GYGKLNITVD | YKPSKNKPLS | IDDFDLLKVI | GKGSFGKVMQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VRKKDTQKIY | ALKALRKAYI | VSKCEVTHTL | AERTVLARVD | CPFIVPLKFS | FQSPEKLYLV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LAFINGGELF | YHLQHEGRFS | LARSRFYIAE | LLCALDSLHK | LDVIYRDLKP | ENILLDYQGH |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IALCDFGLCK | LNMKDNDKTD | TFCGTPEYLA | PEILLGQGYT | KTVDWWTLGI | LLYEMMTGLP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PYYDENVPVM | YKKILQQPLL | FPDGFDPAAK | DLLIGLLSRD | PSRRLGVNGT | DEIRNHPFFK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DISWKKLLLK | GYIPPYKPIV | KSEIDTANFD | QEFTKEKPID | SVVDEYLSAS | IQKQFGGWTY |
| 670 | |||||
| IGDEQLGDSP | SQGRSIS |