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

334-355 (Activation loop from InterPro)

Target domain

191-453 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

1 structures for P26818

Entry ID Method Resolution Chain Position Source
AF-P26818-F1 Predicted AlphaFoldDB

101 variants for P26818

Variant ID(s) Position Change Description Diseaes Association Provenance
rs435087802 59 F>C No EVA
rs458951028 125 S>* No EVA
rs454008968 150 I>L No EVA
rs472332874 151 E>D No EVA
rs439448173 152 E>A No EVA
rs476290544 158 R>P No EVA
rs443373509 162 F>L No EVA
rs461709741 167 E>D No EVA
rs480292150 168 S>T No EVA
rs479309657 215 K>N No EVA
rs468709169 216 M>I No EVA
rs435788475 217 Y>H No EVA
rs447661082 231 Q>L No EVA
rs442790003 263 T>N No EVA
rs461063156 320 P>H No EVA
rs444189994 328 H>N No EVA
rs469953630 328 H>Q No EVA
rs442306352 332 R>S No EVA
rs481022364 332 R>T No EVA
rs460821709 348 H>R No EVA
rs479390756 351 V>L No EVA
rs799206177 367 A>T No EVA
rs451916363 378 G>S No EVA
rs443774002 379 C>W No EVA
rs455953676 380 M>K No EVA
rs482805847 389 S>I No EVA
rs450103557 393 Q>H No EVA
rs469246522 396 T>P No EVA
rs481412120 398 D>Y No EVA
rs466774498 399 K>N No EVA
rs433624865 404 R>P No EVA
rs452245335 405 M>L No EVA
rs464283165 405 M>T No EVA
rs449836089 418 S>P No EVA
rs453035323 448 K>T No EVA
rs438494603 456 I>L No EVA
rs463331676 462 Y>S No EVA
rs435747196 466 Y>* No EVA
rs454181721 471 I>L No EVA
rs439697429 472 P>A No EVA
rs443629327 473 P>L No EVA
rs476618708 473 P>T No EVA
rs462840335 474 R>* No EVA
rs460346799 475 G>A No EVA
rs448245929 475 G>W No EVA
rs445746478 483 F>S No EVA
rs445746478 483 F>Y No EVA
rs464253896 484 D>E No EVA
rs468657580 487 S>* No EVA
rs449643909 487 S>T No EVA
rs454143828 489 D>G No EVA
rs435859589 489 D>Y No EVA
rs472627381 490 E>A No EVA
rs472627381 490 E>G No EVA
rs433398441 491 E>G No EVA
rs451762479 492 D>Y No EVA
rs476770259 493 T>N No EVA
rs443607847 494 K>Q No EVA
rs462147233 496 I>V No EVA
rs434577885 505 L>P No EVA
rs452916026 509 F>S No EVA
rs471547241 517 W>R No EVA
rs438380135 524 T>K No EVA
rs476063670 546 Q>H No EVA
rs436083018 553 Y>S No EVA
rs466604398 580 Y>H No EVA
rs433601193 590 W>R No EVA
rs475658558 596 S>* No EVA
rs451403715 629 Q>H No EVA
rs472577235 629 Q>K No EVA
rs432929109 629 Q>L No EVA
rs443303273 630 F>C No EVA
rs476077549 630 F>I No EVA
rs476077549 630 F>V No EVA
rs461706379 631 V>G No EVA
rs459016403 636 S>R No EVA
rs450844494 639 E>G No EVA
rs463437889 641 V>L No EVA
rs448951661 643 W>G No EVA
rs467613838 643 W>L No EVA
rs434607486 645 K>E No EVA
rs465107347 646 E>D No EVA
rs446522362 646 E>G No EVA
rs456933080 648 T>K No EVA
rs436708736 649 E>K No EVA
rs455169121 650 T>R No EVA
rs473610413 651 F>L No EVA
rs440632301 654 A>D No EVA
rs470909851 658 L>R No EVA
rs462800255 659 R>P No EVA
rs462800255 659 R>Q No EVA
rs461241903 661 A>G No EVA
rs449148154 661 A>P No EVA
rs479652106 663 K>Q No EVA
rs446654250 664 F>V No EVA
rs465017680 666 N>K No EVA
rs450487929 670 S>A No EVA
rs468946398 673 V>A No EVA
rs455215394 684 N>D No EVA
rs473748634 686 N>Y No EVA
rs452597691 688 L>R No EVA

No associated diseases with P26818

6 regional properties for P26818

Type Name Position InterPro Accession
domain Protein kinase domain 191 - 453 IPR000719
domain AGC-kinase, C-terminal 454 - 533 IPR000961
domain Pleckstrin homology domain 558 - 654 IPR001849
active_site Serine/threonine-protein kinase, active site 313 - 325 IPR008271
domain RGS domain 54 - 175 IPR016137
binding_site Protein kinase, ATP binding site 197 - 220 IPR017441

Functions

Description
EC Number 2.7.11.15 Protein-serine/threonine kinases
Subcellular Localization
  • Postsynapse
  • Presynapse
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
anchoring junction A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix.
cell projection A prolongation or process extending from a cell, e.g. a flagellum or axon.
postsynapse The part of a synapse that is part of the post-synaptic cell.
presynapse The part of a synapse that is part of the presynaptic cell.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
beta-adrenergic receptor kinase activity Catalysis of the reaction: ATP + beta-adrenergic receptor = ADP + phospho-beta-adrenergic receptor.
G protein-coupled receptor binding Binding to a G protein-coupled receptor.
G protein-coupled receptor kinase activity Catalysis of the reaction: ATP + G protein-coupled receptor = ADP + G protein-coupled receptor phosphate.
protein kinase activity Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP.

5 GO annotations of biological process

Name Definition
desensitization of G protein-coupled receptor signaling pathway The process that stops, prevents, or reduces the frequency, rate or extent of G protein-coupled receptor signaling pathway after prolonged stimulation with an agonist of the pathway.
G protein-coupled receptor signaling pathway The series of molecular signals initiated by a ligand binding to its receptor, in which the activated receptor promotes the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, and ends with regulation of a downstream cellular process. The pathway can start from the plasma membrane, Golgi or nuclear membrane.
protein phosphorylation The process of introducing a phosphate group on to a protein.
receptor internalization A receptor-mediated endocytosis process that results in the movement of receptors from the plasma membrane to the inside of the cell. The process begins when cell surface receptors are monoubiquitinated following ligand-induced activation. Receptors are subsequently taken up into endocytic vesicles from where they are either targeted to the lysosome or vacuole for degradation or recycled back to the plasma membrane.
regulation of signal transduction Any process that modulates the frequency, rate or extent of signal transduction.

20 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P21146 GRK2 Beta-adrenergic receptor kinase 1 Bos taurus (Bovine) PR
P43249 GRK5 G protein-coupled receptor kinase 5 Bos taurus (Bovine) SS
P32865 Gprk1 G protein-coupled receptor kinase 1 Drosophila melanogaster (Fruit fly) PR
P25098 GRK2 Beta-adrenergic receptor kinase 1 Homo sapiens (Human) PR
Q15835 GRK1 Rhodopsin kinase GRK1 Homo sapiens (Human) PR
P34947 GRK5 G protein-coupled receptor kinase 5 Homo sapiens (Human) EV
P32298 GRK4 G protein-coupled receptor kinase 4 Homo sapiens (Human) SS
P43250 GRK6 G protein-coupled receptor kinase 6 Homo sapiens (Human) EV
P35626 GRK3 Beta-adrenergic receptor kinase 2 Homo sapiens (Human) PR
O70293 Grk6 G protein-coupled receptor kinase 6 Mus musculus (Mouse) SS
Q8VEB1 Grk5 G protein-coupled receptor kinase 5 Mus musculus (Mouse) SS
Q99MK8 Grk2 Beta-adrenergic receptor kinase 1 Mus musculus (Mouse) PR
Q9WVL4 Grk1 Rhodopsin kinase GRK1 Mus musculus (Mouse) PR
Q3UYH7 Adrbk2 Beta-adrenergic receptor kinase 2 Mus musculus (Mouse) PR
Q62833 Grk5 G protein-coupled receptor kinase 5 Rattus norvegicus (Rat) SS
P26817 Grk2 Beta-adrenergic receptor kinase 1 Rattus norvegicus (Rat) PR
P97711 Grk6 G protein-coupled receptor kinase 6 Rattus norvegicus (Rat) SS
P26819 Grk3 Beta-adrenergic receptor kinase 2 Rattus norvegicus (Rat) PR
Q09639 grk-2 G protein-coupled receptor kinase 2 Caenorhabditis elegans PR
O48963 PHOT1 Phototropin-1 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MADLEAVLAD VSYLMAMEKS KATPAARASK KIVLPEPSIR SVMQKYLEER HEITFDKIFN
70 80 90 100 110 120
QRIGFLLFKD FCLNEINEAV PQVKFYEEIK EYEKLENEED RLCRSRQIYD TYIMKELLSC
130 140 150 160 170 180
SHPFSKQAVE HVQSHLSKKQ VTSTLFQPYI EEICESLRGS IFQKFMESDK FTRFCQWKNV
190 200 210 220 230 240
ELNIHLTMND FSVHRIIGRG GFGEVYGCRK ADTGKMYAMK CLDKKRIKMK QGETLALNER
250 260 270 280 290 300
IMLSLVSTGD CPFIVCMTYA FHTPDKLCFI LDLMNGGDLH YHLSQHGVFS EKEMRFYATE
310 320 330 340 350 360
IILGLEHMHN RFVVYRDLKP ANILLDEHGH VRISDLGLAC DFSKKKPHAS VGTHGYMAPE
370 380 390 400 410 420
VLQKGTAYDS SADWFSLGCM LFKLLRGHSP FRQHKTKDKH EIDRMTLTMN VELPDVFSPE
430 440 450 460 470 480
LKSLLEGLLQ RDVSKRLGCH GGSAQELKTH DFFRGIDWQH VYLQKYPPPL IPPRGEVNAA
490 500 510 520 530 540
DAFDIGSFDE EDTKGIKLLD CDQELYKNFP LVISERWQQE VAETVYEAVN ADTDKIEARK
550 560 570 580 590 600
RAKNKQLGHE EDYALGRDCI VHGYMLKLGN PFLTQWQRRY FYLFPNRLEW RGEGESRQSL
610 620 630 640 650 660
LTMEQIVSVE ETQIKDKKCI LLRIKGGKQF VLQCESDPEF VQWKKELTET FMEAQRLLRR
670 680
APKFLNKSRS AVVELSKPPL CHRNSNGL