Q7TT49

SS
Gene name
Cdc42bpb
Protein name
Serine/threonine-protein kinase MRCK beta
Names
EC 2.7.11.1 , CDC42-binding protein kinase beta , DMPK-like beta , Myotonic dystrophy kinase-related CDC42-binding kinase beta , MRCK beta , Myotonic dystrophy protein kinase-like beta
Species
Rattus norvegicus (Rat)
KEGG Pathway
rno:113960
EC number
2.7.11.1: Protein-serine/threonine kinases
Protein Class

Descriptions

CDC42BPA(MRCK) is a Cdc42-binding serine/threonine kinase which is an important downstream effector of CDC42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. A region containing the two distal CC domains (CC2 and CC3; residues 658-930) interacts intramolecularly with the kinase domain and negatively regulates its activity.

Autoinhibitory domains (AIDs)

656-927 (Coiled-coil domains) SS

Target domain

76-342 (Protein kinase domain)

Relief mechanism

Ligand binding

Assay

Accessory elements

217-241 (Activation loop from InterPro)

Target domain

3-411 (Protein kinase domain)

Relief mechanism

Assay

References

Autoinhibited structure

Activated structure

1 structures for Q7TT49

Entry ID Method Resolution Chain Position Source
AF-Q7TT49-F1 Predicted AlphaFoldDB

2 variants for Q7TT49

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3320983995 386 G>S No EVA
rs3320866879 1633 L>P No EVA

No associated diseases with Q7TT49

5 regional properties for Q7TT49

Type Name Position InterPro Accession
domain Bromo adjacent homology (BAH) domain 45 - 187 IPR001025
domain AAA+ ATPase domain 590 - 741 IPR003593
domain ATPase, AAA-type, core 594 - 736 IPR003959
domain Cdc6, C-terminal 830 - 917 IPR015163
domain AAA lid domain 764 - 800 IPR041083

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • Cytoplasm
  • Cell membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cell junction
  • Cell projection, lamellipodium
  • Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction
  • This concentration is PH-domain dependent (By similarity)
  • Detected at the leading edge of migrating and wounded cells; this localization requires the presence of catalytically active CDC42 (PubMed:21240187)
  • Localizes in the lamellipodium in a FAM89B/LRAP25-dependent manner (By similarity)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

7 GO annotations of cellular component

Name Definition
actomyosin Any complex of actin, myosin, and accessory proteins.
cell leading edge The area of a motile cell closest to the direction of movement.
cell-cell junction A cell junction that forms a connection between two or more cells of an organism; excludes direct cytoplasmic intercellular bridges, such as ring canals in insects.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
lamellipodium A thin sheetlike process extended by the leading edge of a migrating cell or extending cell process; contains a dense meshwork of actin filaments.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

7 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
magnesium ion binding Binding to a magnesium (Mg) ion.
protein kinase activity Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction
protein serine kinase activity Catalysis of the reactions
protein serine/threonine kinase activity Catalysis of the reactions
protein-containing complex binding Binding to a macromolecular complex.
small GTPase binding Binding to a small monomeric GTPase.

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.
actomyosin structure 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 containing both actin and myosin or paramyosin. The myosin may be organized into filaments.
cell migration The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues.
protein phosphorylation The process of introducing a phosphate group on to a protein.

15 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q28021 ROCK2 Rho-associated protein kinase 2 Bos taurus (Bovine) SS
Q9W1B0 gek Serine/threonine-protein kinase Genghis Khan Drosophila melanogaster (Fruit fly) SS
Q5VT25 CDC42BPA Serine/threonine-protein kinase MRCK alpha Homo sapiens (Human) EV
O75116 ROCK2 Rho-associated protein kinase 2 Homo sapiens (Human) SS
Q13464 ROCK1 Rho-associated protein kinase 1 Homo sapiens (Human) SS
Q9Y5S2 CDC42BPB Serine/threonine-protein kinase MRCK beta Homo sapiens (Human) SS
P70336 Rock2 Rho-associated protein kinase 2 Mus musculus (Mouse) SS
Q3UU96 Cdc42bpa Serine/threonine-protein kinase MRCK alpha Mus musculus (Mouse) SS
P70335 Rock1 Rho-associated protein kinase 1 Mus musculus (Mouse) SS
Q80UW5 Cdc42bpg Serine/threonine-protein kinase MRCK gamma Mus musculus (Mouse) PR
Q7TT50 Cdc42bpb Serine/threonine-protein kinase MRCK beta Mus musculus (Mouse) SS
M3TYT0 ROCK2 Rho-associated protein kinase 2 Sus scrofa (Pig) SS
O54874 Cdc42bpa Serine/threonine-protein kinase MRCK alpha Rattus norvegicus (Rat) SS
Q62868 Rock2 Rho-associated protein kinase 2 Rattus norvegicus (Rat) EV
Q63644 Rock1 Rho-associated protein kinase 1 Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MSAKVRLKKL EQLLLDGPWR NESSLSVETL LDVLVCLYTE CSHSALRRDK YVAEFLEWAK
70 80 90 100 110 120
PFTQLVKDMQ LHREDFEIIK VIGRGAFGEV AVVKMKNTER IYAMKILNKW EMLKRAETAC
130 140 150 160 170 180
FREERDVLVN GDCQWITALH YAFQDENYLY LVMDYYVGGD LLTLLSKFED KLPEDMARFY
190 200 210 220 230 240
IGEMVLAIDS IHQLHYVHRD IKPDNVLLDV NGHIRLADFG SCLKMNDDGT VQSSVAVGTP
250 260 270 280 290 300
DYISPEILQA MEDGMGKYGP ECDWWSLGVC MYEMLYGETP FYAESLVETY GKIMNHEERF
310 320 330 340 350 360
QFPSHVTDVS EEAKDLIQRL ICSRERRLGQ NGIEDFKKHA FFEGLNWENI RNLEAPYIPD
370 380 390 400 410 420
VSSPSDTSNF DVDDDVLRNI EILPPGSHTG FSGLHLPFIG FTFTTESCFS DRGSLKSMIQ
430 440 450 460 470 480
SNTLTKDEDV QRDLENSLQI EAYERRIRRL EQEKLELSRK LQESTQTVQS LHGSTRALGN
490 500 510 520 530 540
SNRDKEIKRL NEELERMKSK MADSNRLERQ LEDTVTLRQE HEDSTQRLKG LEKQYRLARQ
550 560 570 580 590 600
EKEELHKQLV EASERLKSQT KELKDAHQQR KRALQEFSEL NERMAELRSQ KQKVSRQLRD
610 620 630 640 650 660
KEEEMEVAMQ KIDSMRQDIR KSEKSRKELE ARLEDAVAEA SKERKLREHS ESFSKQMERE
670 680 690 700 710 720
LETLKVKQGG RGPGATLEHQ QEISKIRSEL EKKVLFYEEE LVRREASHVL EVKNVKKEVH
730 740 750 760 770 780
ESESHQLALQ KEVLMLKDKL EKSKRERHSE MEEAIGAMKD KYERERAMLF DENKKLTAEN
790 800 810 820 830 840
EKLCSFVDKL TAQNRQLEDE LQDLASKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS
850 860 870 880 890 900
KMTEELETLR SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVHEELRKV
910 920 930 940 950 960
KDTSLAFESK LKESEAKNRE LLEEMQSLKK RMEEKFRADT GLKLPDFQDP IFEYFNTAPL
970 980 990 1000 1010 1020
AHDLTFRTSS ASDQETQASK LDLSPSVSVA TSTEQQEDAA RSQQRPSTVP LPNTQALAMA
1030 1040 1050 1060 1070 1080
GPKPKAHQFS IKSFPSPTQC SHCTSLMVGL IRQGYACEVC AFSCHVSCKD SAPQVCPIPP
1090 1100 1110 1120 1130 1140
EQSKRPLGVD VQRGIGTAYK GYVKVPKPTG VKKGWQRAYA VVCDCKLFLY DLPEGKSTQP
1150 1160 1170 1180 1190 1200
GVIASQVLDL RDDEFAVSSV LASDVIHATR RDIPCIFRVT ASLLGSPSKT SSLLILTENE
1210 1220 1230 1240 1250 1260
NEKRKWVGIL EGLQAILHKN RLRSQVVHVA QEAYDSSLPL IKTVLAAAIV DGDRIAVGLE
1270 1280 1290 1300 1310 1320
EGLYVIELTR DVIVRAADCK KVYQIELAPK EKLILLLCGR NHHVHLYPWT SFDGAEASNF
1330 1340 1350 1360 1370 1380
DIKLPETKGC QLIATGTLRK SSSTCLFVAV KRLVLCYEIQ RTKPFHRKFN EIVAPGHVQW
1390 1400 1410 1420 1430 1440
MAMFKDRLCV GYPSGFSLLS IQGDGQPLDL VNPADPSLAF LSQQSFDALC AVELKSEEYL
1450 1460 1470 1480 1490 1500
LCFSHMGLYV DPQGRRSRTQ ELMWPAAPVA CSCSSSHVTV YSEYGVDVFD VRTMEWVQTI
1510 1520 1530 1540 1550 1560
GLRRIRPLNS DGSLNLLGCE PPRLIYFKNK FSGTVLNVPD TSDNSKKQML RTRSKRRFVF
1570 1580 1590 1600 1610 1620
KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG DGMQVLMDLP LSAAPTAQEE
1630 1640 1650 1660 1670 1680
KQGPAPTGLP RQLPSRNKPY VSWPSSGGSE PGVPVPLRSM SDPDQDFDKE PDSDSTKHST
1690 1700 1710
PSNSSNPSGP PSPNSPHRSQ LPLEGLDQPA CDA