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

212-236 (Activation loop from InterPro)

Target domain

71-337 (Protein kinase domain)

Relief mechanism

Assay

Autoinhibited structure

Activated structure

1 structures for Q80UW5

Entry ID Method Resolution Chain Position Source
AF-Q80UW5-F1 Predicted AlphaFoldDB

69 variants for Q80UW5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389521968 9 E>D No EVA
rs3408821410 22 L>I No EVA
rs3389525275 39 A>P No EVA
rs3389517054 54 A>T No EVA
rs3389525310 62 K>R No EVA
rs3389521521 70 D>E No EVA
rs3389521954 138 F>I No EVA
rs3412967854 158 T>A No EVA
rs3389469241 173 Q>H No EVA
rs3389533523 189 L>M No EVA
rs3389521149 218 L>M No EVA
rs3389533524 219 R>C No EVA
rs3408859107 234 T>A No EVA
rs3409010429 240 P>L No EVA
rs3389531202 252 H>Q No EVA
rs3389536715 286 G>C No EVA
rs3389521168 293 D>N No EVA
rs3389513375 312 I>F No EVA
rs3389469287 339 G>W No EVA
rs3389521527 381 S>P No EVA
rs3407907516 400 S>C No EVA
rs3409010441 408 S>T No EVA
rs3389521178 412 M>K No EVA
rs3389525319 415 P>L No EVA
rs3409010420 418 T>A No EVA
rs3389533451 468 K>E No EVA
rs3409298438 519 R>L No EVA
rs3408821408 522 E>* No EVA
rs3408225934 522 E>D No EVA
rs3408859124 522 E>V No EVA
rs3408859056 527 L>R No EVA
rs3389514294 560 G>D No EVA
rs3389526715 561 Q>K No EVA
rs3408532981 563 T>A No EVA
rs3389514264 567 Q>H No EVA
rs3389488059 591 E>D No EVA
rs3389533450 596 G>* No EVA
rs3389526759 648 Q>L No EVA
rs3409298450 669 R>Q No EVA
rs3389526714 767 E>K No EVA
rs3389429698 816 S>C No EVA
rs3389522491 817 F>L No EVA
rs3408931845 842 E>V No EVA
rs3389488078 850 S>N No EVA
rs3389514252 856 V>L No EVA
rs3389488037 927 P>L No EVA
rs3389531164 934 R>L No EVA
rs3389478210 935 T>I No EVA
rs3389526752 948 A>V No EVA
rs3389513430 970 A>T No EVA
rs3389536780 981 D>E No EVA
rs3389522522 999 D>N No EVA
rs3389522472 1027 F>Y No EVA
rs3409100101 1065 R>Q No EVA
rs3389429667 1140 A>V No EVA
rs3389514919 1178 C>G No EVA
rs3389521244 1194 L>F No EVA
rs3389478128 1207 L>Q No EVA
rs3389501194 1211 P>S No EVA
rs3389488020 1287 S>G No EVA
rs3389522482 1296 A>V No EVA
rs3389536722 1311 E>A No EVA
rs3389429704 1343 R>* No EVA
rs3389521188 1371 K>E No EVA
rs3389533509 1377 L>I No EVA
rs3389533512 1415 D>G No EVA
rs3408859037 1420 Q>H No EVA
rs3389521908 1477 Q>L No EVA
rs3389521924 1540 S>T No EVA

No associated diseases with Q80UW5

10 regional properties for Q80UW5

Type Name Position InterPro Accession
domain CRIB domain 1436 - 1472 IPR000095
domain Protein kinase domain 71 - 337 IPR000719
domain AGC-kinase, C-terminal 338 - 408 IPR000961
domain Citron homology (CNH) domain 1091 - 1371 IPR001180
domain Pleckstrin homology domain 946 - 1067 IPR001849
domain Protein kinase C-like, phorbol ester/diacylglycerol-binding domain 877 - 926 IPR002219
active_site Serine/threonine-protein kinase, active site 191 - 203 IPR008271
domain Myotonic dystrophy protein kinase, coiled coil 743 - 797 IPR014930
binding_site Protein kinase, ATP binding site 77 - 100 IPR017441
domain Protein kinase, C-terminal 357 - 398 IPR017892

Functions

Description
EC Number 2.7.11.1 Protein-serine/threonine kinases
Subcellular Localization
  • Cytoplasm
  • Concentrates at the leading edge of cells
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cell leading edge The area of a motile cell closest to the direction of movement.
centriolar satellite A small (70-100 nm) cytoplasmic granule that contains a number of centrosomal proteins; centriolar satellites traffic toward microtubule minus ends and are enriched near the centrosome.
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.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

4 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: 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.

5 GO annotations of biological process

Name Definition
actin cytoskeleton reorganization A process that is carried out at the cellular level which results in dynamic structural changes to the arrangement of constituent parts 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.
localization Any process in which a cell, a substance, or a cellular entity, such as a protein complex or organelle, is transported, tethered to or otherwise maintained in a specific location. In the case of substances, localization may also be achieved via selective degradation.
peptidyl-threonine phosphorylation The phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine.
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
O75116 ROCK2 Rho-associated protein kinase 2 Homo sapiens (Human) SS
Q13464 ROCK1 Rho-associated protein kinase 1 Homo sapiens (Human) SS
Q5VT25 CDC42BPA Serine/threonine-protein kinase MRCK alpha Homo sapiens (Human) EV
Q9Y5S2 CDC42BPB Serine/threonine-protein kinase MRCK beta Homo sapiens (Human) SS
Q7TT50 Cdc42bpb Serine/threonine-protein kinase MRCK beta 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
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
MEQRLRALEQ LVRGEAGGSP GLDGLLDLLL GVHQELSSAP LRRERNVAQF LSWASPFVTK
70 80 90 100 110 120
VKELRLQRDD FEILKVIGRG AFGEVAVVRQ RGSGQIFAMK MLHKWEMLKR AETACFREER
130 140 150 160 170 180
DVLVKGDSRW VTALHYAFQD EEYLYLVMDY YAGGDLLTLL SRFEDRLPPE LAQFYLAEMV
190 200 210 220 230 240
LAIHSLHQLG YVHRDVKPDN ILLDMNGHIR LADFGSCLRL NNNGMVDSSV AVGTPDYISP
250 260 270 280 290 300
EILQAMEEGK GHYGPQCDWW SLGVCAYELL FGETPFYAES LVETYGKIMN HEDHLQFPAD
310 320 330 340 350 360
VTDVPASAQD LIRQLLCRQE ERLGRGGLDD FRKHPFFEGV DWERLATSTA PYIPELRGPM
370 380 390 400 410 420
DTSNFDVDDD TLNRPETLPP SSHGAFSGHH LPFVGFTYTS GSPFDVQSSE LMAAPEGTPH
430 440 450 460 470 480
CVEQVKVELS HKCQEPLHGP LQPQELVRLQ KEVQVLQEKL AETLRDSKAS LSQTDGLHAR
490 500 510 520 530 540
SPAPNIQLQQ EKDRLQQELT EAQAALRVQD AELCQAQNRQ EEFLQRLWEA QEREAAAASQ
550 560 570 580 590 600
IQALNSQLEE AWVVRRELEG QVTTLSQEVT RLQGQCKQES SQAKTVHAAP ETNGIGSPEG
610 620 630 640 650 660
QSQEAQLRKE VAALREQLEH ACSQGISVGK EEVLCRLQEE NQRLSREQER LAGELELELQ
670 680 690 700 710 720
SKQRLEGERR ETESNWEAQI ADILSWVNDE KVSRGYLQAL ATKMAEELES LRNVGTQTLP
730 740 750 760 770 780
TRPLDHQWKA RRLQKMEASA RLELQSALEA EIRAKQSLQE QLTQVQEAQR QAERRLQEAE
790 800 810 820 830 840
KQSQALQQEV AELREELQAR GPGDARPSTS LIPLLSFWNT EKDSAKDPGN SGEGPRSGAE
850 860 870 880 890 900
AELRPEGRRS LRMGSVFPRV PAATTTPAEG PPAKPGSHTL RPRSFPSPTK CLRCTSLMLG
910 920 930 940 950 960
LGRQGLGCDT CGYFCHSACA SQAPPCPVPP ELLRTALGVH PETGTGTAYE GFLSVPRPSG
970 980 990 1000 1010 1020
VRRGWQRVYA ALSDSRLLLF DAPDPRGSLA SGVLLQALDL RDPQFSATPV LAPDVIHAQS
1030 1040 1050 1060 1070 1080
KDLPRIFRVT ASQLTVPPTT CTVLLLAENE GERERWLQVL GELQRLLLDA RPRPRPVYTL
1090 1100 1110 1120 1130 1140
KEAYDNGLPL LPHALCAAVI DQERLALGTE EGLFVIHLHS NDIFQVGDCR RVQRLAVSSA
1150 1160 1170 1180 1190 1200
AGLLAVLCGR GPSVRLFALD ELESAEVAGA KIPESRGCQA LVAGRILQAR TPVLCVAVKR
1210 1220 1230 1240 1250 1260
QVLCYQLGPG PGPWQRRIRE LQAPAPVQSL GLLGDRLCVG AAGTFALYPL LNEAAPLALG
1270 1280 1290 1300 1310 1320
TGLVAEELPA SRGGLGEALG AVELSLSELL LLFATAGVYV DSAGRKSRSH ELLWPAAPTG
1330 1340 1350 1360 1370 1380
WGYTAPYLTV FSENALDVFD VRRAEWVQTV PLKKVRPLNP EGSLFLYGTE KVRLTYLRNP
1390 1400 1410 1420 1430 1440
LAEKDEFDIP DLTDNSRRQL FRTKSKRRFF FRVSDELRQQ QRREMLKDPF VRSKFISPPT
1450 1460 1470 1480 1490 1500
NFNHLVHVGP TEGRPNTRDG TRAQEQKSRG ARSSGPQRPH SFSEAFRRPV STGSDGLPGE
1510 1520 1530 1540 1550
TDPLVKRKPW TSLSSESVSC PQGSLSPAAS LIQVSERPRS LPPDPESESS P