A0A3P8RM62 · A0A3P8RM62_AMPPE

Function

function

Protein kinase which is a key regulator of actin cytoskeleton and cell polarity.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Activity regulation

Activated by RHOA binding. Inhibited by Y-27632.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site105ATP (UniProtKB | ChEBI)
Active site198Proton acceptor

GO annotations

AspectTerm
Cellular Componentbleb
Cellular Componentcentriole
Cellular ComponentGolgi membrane
Cellular Componentlamellipodium
Cellular Componentplasma membrane
Cellular Componentruffle
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionprotein serine kinase activity
Molecular Functionprotein serine/threonine kinase activity
Molecular Functionsmall GTPase binding
Biological Processactin cytoskeleton organization
Biological Processepicardial cell to mesenchymal cell transition
Biological Processnegative regulation of adherens junction organization
Biological Processpositive regulation of stress fiber assembly
Biological ProcessRho protein signal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Rho-associated protein kinase
  • EC number

Organism names

Accessions

  • Primary accession
    A0A3P8RM62

Proteomes

Subcellular Location

Cell membrane
Cell projection, bleb
Cell projection, lamellipodium
Cell projection, ruffle
Golgi apparatus membrane
; Peripheral membrane protein
Membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Homodimer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, coiled coil, compositional bias.

TypeIDPosition(s)Description
Domain76-338Protein kinase
Domain341-409AGC-kinase C-terminal
Region407-429Disordered
Domain476-560REM-1
Region568-598Disordered
Coiled coil752-898
Coiled coil931-993
Domain956-1022RhoBD
Coiled coil1028-1115
Domain1128-1327PH
Domain1238-1293Phorbol-ester/DAG-type
Region1321-1364Disordered
Compositional bias1331-1364Polar residues

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,364
  • Mass (Da)
    158,462
  • Last updated
    2019-02-13 v1
  • Checksum
    663C897E2637FB85
MSAGESMEARFEKIDAMLKDPKSEINTDCLLDGLDALVYDLDFPALRKNKSIDNFLNRYKETISKIRDLRMKAEDYEVVKVIGRGAFGEVQLVRHKATSKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSSWVVQLFFAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWARFYTAEVVLALDGIHSMGFIHRDVKPDNMLLDKAGHLKLADFGTCMKMNKDGMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNALTFPDDSDISNDAKNLICAFLTDREVRLGRNGVDEIKRHPFFKNDQWTWENIRETAAPVVPELSSDIDTSNFDDIEEDRGEEETFPIPKAFVGNQLPFVGFTYYSNQHPLRSSTATKTSDKRSSSTKEDKSHLENLQKRIYQLEEQLHSEMQLKDELEQKCRTSNTKIEKIMKELDEEANLRKSAEASVSLLEKDKIMLQHRFTEYQRKADQEAEKRRNLENEVSTLKEQLEDMKKISQNSQASNDKIAQLQSQLEEANDLLRAESDTAARLRKSHTEVAKSMSQLESLNRDLQERSRAADGEKAQLEKELLLLQSTLDSERRNYSQGSEEIRELQARMAGLQEDNKNLKLSLSKVETERKQAQERSNNLEKEKNNLEIDLNYKLKTLQQRLEQEHTEHRVTRAQLTDKYESIEEAKSAAMTAVQQKMSEENGARMRAESRVVEVEKQCSMLEFDLKQSVQKMEQLMKQKERLEDEVKILRIQVEQESSKRGLTQNELKSRMQEVDRLRCSEKQLKQEINTALESKRSLEFQLAQLTKQYRGNEGQMRELQDQLEAEQYFSTLYKTQVKELKEEIEERNRQVQEAHKRMQDLNSERDSLSAQLDLTVTKAESEQLARALQEEQYFELSQENKKAVTRHKQEIGEKESTITRLEESNKTLTKDVENLSKEKTELNEKLRTQEEEYAAQKEEIANTIKANYEKVLNTERTLKTQAVNKLAEIMNRKDMKLDQKKKGSTADLRKKEKENRKLQLELNQEKEKFNHMAIKYQKELSEMQAQLSEECTYRNELQMQLDSKESDIEQLREKLNDLQQRMDNSSVTSLQTDETDSNIAESRLEGWLSIPNRANIKRYGWKKQYVVVSSKKILFYNDEQDKEQSNPSMVLDIDKLFHVRPVTQGDVYRAETEEIPRIFQILYANEGECRKEAEMETVPQGDKTNCLPHKGHEFIPTLYHFPSNCEACAKPLWHVFKPPPALECRRCHVKCHKDHLDKKEDVIPPCKVNYDVTSARDMLLLALTQDEQKKWIGHLGKKIPKTPPSTFSRASPRSMSTRSGPNQSFRKNPKSNTGKLS

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A3P8RLE1A0A3P8RLE1_AMPPE1217

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1331-1364Polar residues

Keywords

Genome annotation databases

Similar Proteins

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