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)

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

Autoinhibited structure

Activated structure

1 structures for Q7TT50

Entry ID Method Resolution Chain Position Source
AF-Q7TT50-F1 Predicted AlphaFoldDB

77 variants for Q7TT50

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3403065453 45 A>V No EVA
rs3389228781 63 T>I No EVA
rs3389221817 69 M>I No EVA
rs3389221836 85 G>E No EVA
rs3389277262 109 K>N No EVA
rs3389263715 168 F>I No EVA
rs3389221894 170 D>E No EVA
rs3389263915 170 D>N No EVA
rs3412748218 175 D>Y No EVA
rs3389257967 178 R>S No EVA
rs3413157024 204 D>V No EVA
rs3389277263 258 Y>N No EVA
rs3389277289 259 G>R No EVA
rs3404050720 311 E>G No EVA
rs3403015290 312 E>* No EVA
rs3389257895 316 L>R No EVA
rs3389257968 339 H>R No EVA
rs3389259182 349 N>D No EVA
rs3403740404 350 I>L No EVA
rs3403803902 351 R>P No EVA
rs3389228844 376 M>K No EVA
rs3410930421 448 R>P No EVA
rs3389246156 461 L>Q No EVA
rs230873833 492 E>D No EVA
rs3389263713 505 N>Y No EVA
rs13481651 585 S>A No EVA
rs3403065423 665 K>E No EVA
rs3389277221 668 Q>K No EVA
rs3389193117 669 G>V No EVA
rs3389270117 673 P>L No EVA
rs214560430 676 A>S No EVA
rs3389263745 714 N>I No EVA
rs3389263759 748 H>Q No EVA
rs3389221820 781 E>* No EVA
rs3389261087 873 M>K No EVA
rs3389234566 882 A>D No EVA
rs38926352 893 V>I No EVA
rs3389261617 946 D>N No EVA
rs29149337 991 T>P No EVA
rs3389270145 995 Q>* No EVA
rs3549714903 1001 R>P No EVA
rs3403065404 1019 M>L No EVA
rs3389228811 1040 C>R No EVA
rs3389270136 1041 S>G No EVA
rs3389259204 1042 H>R No EVA
rs3389259194 1074 Q>* No EVA
rs3389263687 1120 A>T No EVA
rs29145242 1171 R>Q No EVA
rs3389259137 1203 K>R No EVA
rs3389220243 1243 A>P No EVA
rs3389246175 1252 G>E No EVA
rs3389257890 1309 W>* No EVA
rs3389228854 1309 W>R No EVA
rs3389263721 1320 F>I No EVA
rs3389246217 1342 S>L No EVA
rs3389263717 1353 L>V No EVA
rs3389277214 1355 L>H No EVA
rs3389220224 1364 P>H No EVA
rs3389270066 1373 V>M No EVA
rs3389257958 1381 M>I No EVA
rs3389277280 1423 Q>R No EVA
rs3389259168 1426 F>Y No EVA
rs3389228816 1437 E>* No EVA
rs3389246186 1445 H>L No EVA
rs3389260041 1456 R>G No EVA
rs3389270104 1461 E>D No EVA
rs3411600490 1469 V>I No EVA
rs3389220200 1491 V>M No EVA
rs3549837711 1523 R>H No EVA
rs242035398 1535 I>V No EVA
rs3389220193 1548 Q>R No EVA
rs3389246160 1574 M>I No EVA
rs3389257950 1594 V>L No EVA
rs3412914295 1595 A>T No EVA
rs3403803921 1597 M>STCMPSPGPM* No EVA
rs3389257910 1600 G>W No EVA
rs3389220232 1601 D>N No EVA

No associated diseases with Q7TT50

8 regional properties for Q7TT50

Type Name Position InterPro Accession
domain Protein kinase domain 251 - 504 IPR000719
domain SH2 domain 130 - 229 IPR000980
domain Serine-threonine/tyrosine-protein kinase, catalytic domain 252 - 500 IPR001245
domain SH3 domain 65 - 126 IPR001452
active_site Tyrosine-protein kinase, active site 366 - 378 IPR008266
binding_site Protein kinase, ATP binding site 257 - 279 IPR017441
domain Tyrosine-protein kinase, catalytic domain 251 - 500 IPR020635
domain Tyrosine-protein kinase Fgr, SH2 domain 128 - 228 IPR035693

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
  • Detected at the leading edge of migrating and wounded cells; this localization requires the presence of catalytically active CDC42
  • Localizes in the lamellipodium in a FAM89B/LRAP25-dependent manner
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.

6 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 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
Q80UW5 Cdc42bpg Serine/threonine-protein kinase MRCK gamma Mus musculus (Mouse) PR
Q3UU96 Cdc42bpa Serine/threonine-protein kinase MRCK alpha Mus musculus (Mouse) SS
P70335 Rock1 Rho-associated protein kinase 1 Mus musculus (Mouse) SS
P70336 Rock2 Rho-associated protein kinase 2 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
Q7TT49 Cdc42bpb Serine/threonine-protein kinase MRCK beta Rattus norvegicus (Rat) SS
10 20 30 40 50 60
MSAKVRLKKL EQLLLDGPWR NDSALSVETL 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 DVDDDMLRNI EILPPGSHTG FSGLHLPFIG FTFTTESCFS DRGSLKSMTQ
430 440 450 460 470 480
SNTLTKDEDV QRDLENSLQI EAYERRIRRL EQEKLELSRK LQESTQTVQS LHGSTRALGN
490 500 510 520 530 540
SNRDKEIKRL NEELERMKSK MADSNRLERQ LEDTVTLRQE HEDSTHRLKG LEKQYRLARQ
550 560 570 580 590 600
EKEELHKQLV EASERLKSQT KELKDAHQQR KRALQEFSEL NERMSELRSL KQKVSRQLRD
610 620 630 640 650 660
KEEEMEVAMQ KIDSMRQDLR KSEKSRKELE ARLEDAAAEA SKERKLREHS ESFCKQMERE
670 680 690 700 710 720
LEALKVKQGG RGPGAASEHQ QEISKIRSEL EKKVLFYEEE LVRREASHVL EVKNVKKEVH
730 740 750 760 770 780
DSESHQLALQ KEVLMLKDKL EKSKRERHSE MEEAIGTVKD 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 QLVQEELRKV
910 920 930 940 950 960
KDSSLAFESK LKESEAKNRE LLEEMQSLRK RMEEKFRADT GLKLPDFQDS IFEYFNTAPL
970 980 990 1000 1010 1020
AHDLTFRTSS ASDQETQASK MDLSPSVSVA TSTEQQEDMA RPQQRPSPVP LPSTQALAMA
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
GVVASQVLDL RDEEFAVSSV LASDVIHATR RDIPCIFRVT ASLLGSPSKT SSLLILTENE
1210 1220 1230 1240 1250 1260
NEKRKWVGIL EGLQAILHKN RLKSQVVHVA QEAYDSSLPL IKAVLAAAIV DGDRIAVGLE
1270 1280 1290 1300 1310 1320
EGLYVIELTR DVIVRAADCK KVYQIELAPK EKIAILLCGR NHHVHLYPWS SFDGAEASNF
1330 1340 1350 1360 1370 1380
DIKLPETKGC QLIATGTLRK SSSTCLFVAV KRLILCYEIQ RTKPFHRKFS ELVAPGHVQW
1390 1400 1410 1420 1430 1440
MAVFKDRLCV GYPSGFSLLS IQGDGPPLDL VNPTDPSLAF LSQQSFDALC AVELKSEEYL
1450 1460 1470 1480 1490 1500
LCFSHMGLYV DPQGRRSRMQ ELMWPAAPVA CSCSPTHVTV YSEYGVDVFD VRTMEWVQTI
1510 1520 1530 1540 1550 1560
GLRRIRPLNS DGSLNLLGCE PPRLIYFKNK FSGTILNVPD TSDNSKKQML RTRSKRRFVF
1570 1580 1590 1600 1610 1620
KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG DGMQVLMDLP LSAAPTVQEE
1630 1640 1650 1660 1670 1680
KQGPTPAGLP RQPPSRSKPY VSWPSSGGSE PGVPVPLRSM SDPDQDFDKE PDSDSTKHST
1690 1700 1710
PSNSSNPSGP PSPNSPHRSQ LPMEGLDQPS CDA