Q54RB7

PR
Gene name
shkA (shk1, DDB_G0283267)
Protein name
Dual specificity protein kinase shkA
Names
SH2 domain-containing protein 1, SH2 domain-containing protein A
Species
Dictyostelium discoideum (Slime mold)
KEGG Pathway
ddi:DDB_G0283267
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)

1-74 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

184-192 (Activation loop from InterPro)

Target domain

45-304 (Protein kinase domain)

Relief mechanism

Assay

206-210 (Activation loop from InterPro)

Target domain

45-304 (Protein kinase domain)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for Q54RB7

Entry ID Method Resolution Chain Position Source
AF-Q54RB7-F1 Predicted AlphaFoldDB

No variants for Q54RB7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q54RB7

No associated diseases with Q54RB7

6 regional properties for Q54RB7

Type Name Position InterPro Accession
domain Protein kinase domain 45 - 304 IPR000719
domain SH2 domain 422 - 503 IPR000980
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 46 - 300 IPR001245
active_site Serine/threonine-protein kinase, active site 163 - 175 IPR008271
binding_site Protein kinase, ATP binding site 51 - 72 IPR017441
domain ShkA/ShkC, SH2 domain 413 - 525 IPR035844

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • Membrane
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cell cortex The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.

4 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.
protein tyrosine kinase activity Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate.

4 GO annotations of biological process

Name Definition
actin cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
chemotaxis The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis).
negative regulation of signal transduction Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction.
phagocytosis A vesicle-mediated transport process that results in the engulfment of external particulate material by phagocytes and their delivery to the lysosome. The particles are initially contained within phagocytic vacuoles (phagosomes), which then fuse with primary lysosomes to effect digestion of the particles.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MATQQQQQQQ QQQQQQIKAR KDIQIQQAQS ASDILGPPEI SETEITTESI LGDGSFGTVY
70 80 90 100 110 120
KGRCRLKDVA VKVMLKQVDQ KTLTDFRKEV AIMSKIFHPN IVLFLGACTS TPGKLMICTE
130 140 150 160 170 180
LMKGNLESLL LDPMVKLPLI TRMRMAKDAA LGVLWLHSSN PVFIHRDLKT SNLLVDANLT
190 200 210 220 230 240
VKVCDFGLSQ IKQRGENLKD GQDGAKGTPL WMAPEVLQGR LFNEKADVYS FGLVLWQIFT
250 260 270 280 290 300
RQELFPEFDN FFKFVAAICE KQLRPSIPDD CPKSLKELIQ KCWDPNPEVR PSFEGIVSEL
310 320 330 340 350 360
EEIIIDCCIP DEYGAILWKN HFKHENEANW KDFINVFSNF VGLTNANTPS MSDLLQFSPN
370 380 390 400 410 420
LNGSTIELNF KCLKSIIVSS PKGPHEEEVV LMEQFGKVLA WFGNLKEDGS QILDKIRQLM
430 440 450 460 470 480
ECAWFHGDIS TSESENRLRQ KPEGTFLVRF STSEYGAYTI SKVSKNGGIS HQRIHRPQGK
490 500 510 520
FQVNNSKYLS VKELITGEAQ ALGINTPCLG SRFLSLIYKA QLSGYIN