Q8CIQ7

PR
Gene name
Dock3 (Moca)
Protein name
Dedicator of cytokinesis protein 3
Names
Modifier of cell adhesion, Presenilin-binding protein, PBP
Species
Mus musculus (Mouse)
KEGG Pathway
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1619-1694 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q8CIQ7

Entry ID Method Resolution Chain Position Source
AF-Q8CIQ7-F1 Predicted AlphaFoldDB

No variants for Q8CIQ7

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q8CIQ7

No associated diseases with Q8CIQ7

10 regional properties for Q8CIQ7

Type Name Position InterPro Accession
domain SH3 domain 6 - 67 IPR001452
domain Dedicator of cytokinesis protein 3, DHR2 domain 1232 - 1623 IPR026800
domain C2 DOCK-type domain 417 - 606 IPR027007
domain DOCKER domain 1225 - 1632 IPR027357
domain Dedicator of cytokinesis, N-terminal domain 70 - 412 IPR032376
domain Dedicator of cytokinesis 3, SH3 domain 10 - 65 IPR035767
domain Dedicator of cytokinesis B, C2 domain 420 - 608 IPR037811
domain DOCKER, Lobe A 1219 - 1343 IPR046769
domain DOCKER, Lobe B 1401 - 1483 IPR046770
domain DOCKER, Lobe C 1526 - 1624 IPR046773

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

3 GO annotations of molecular function

Name Definition
guanyl-nucleotide exchange factor activity Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions.
SH3 domain binding Binding to a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins.
small GTPase binding Binding to a small monomeric GTPase.

1 GO annotations of biological process

Name Definition
small GTPase mediated signal transduction The series of molecular signals in which a small monomeric GTPase relays a signal.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q92608 DOCK2 Dedicator of cytokinesis protein 2 Homo sapiens (Human) PR
Q9H7D0 DOCK5 Dedicator of cytokinesis protein 5 Homo sapiens (Human) PR
Q14185 DOCK1 Dedicator of cytokinesis protein 1 Homo sapiens (Human) PR
Q8BUR4 Dock1 Dedicator of cytokinesis protein 1 Mus musculus (Mouse) PR
Q8C3J5 Dock2 Dedicator of cytokinesis protein 2 Mus musculus (Mouse) PR
10 20 30 40 50 60
MWTPTEEEKY GVVICSFRGS VPQGLVLEIG ETVQILEKCE GWYRGVSTKK PNVKGLFPAN
70 80 90 100 110 120
YIHLKKAIVS NRGQYETVVP LEDSIVTEVT TTLQEWASLW KQLYVKHKVD LFYKLRHVMN
130 140 150 160 170 180
ELIDLRRQLL SGHLTQDQVR EVKRHITVRL DWGNEHLGLD LVPRKDFEVV DSDQISVSDL
190 200 210 220 230 240
YKMHLSSRQS VQQSTSQVDT MRPRHGETCR MPVPYHFFFS LKSFTYNTIG EDSDVFFSLY
250 260 270 280 290 300
DMREGKQISE RFLVRLNKNG GPRNPEKIER MCALFTDLSS KDMKRDLYIV AHVIRIGRML
310 320 330 340 350 360
LNDSKKGPAH LHYRRPYGCA VLSILDVLQS LTELKEEKDF VLKVYTCNNE SEWTQIHENI
370 380 390 400 410 420
IRKSSTKYSA PSASHGLIIS LQLFRGDMEQ IRRENPMIFN RGLAITRKLG FPDVIMPGDI
430 440 450 460 470 480
RNDLYLTLEK GDFERGGKSV QKNIEVTMYV LYADGEILKD CISLGSGEPN RSSYHSFVLY
490 500 510 520 530 540
HSNSPRWGEI IKLPIPIDRF RGSHLRFEFR HCSTKDKGEK KLFGFAFSPL MRDDGTTLSD
550 560 570 580 590 600
DIHELYVYKC DENSTFNNHA LYLGLPCCKE DYNGCPNIPS SLIFQRSKES FFISTQLSST
610 620 630 640 650 660
KLTQNVDLLA LLKWKAFPDR IMDILGRLRH VSGEEIVKFL QDILDTLFVI LDDNTEKYGL
670 680 690 700 710 720
LVFQSLVFII NLLRDIKYFH FRPVMDTYIQ KHFAGALAYK ELIRCLKWYM DCSAELIRQD
730 740 750 760 770 780
HIQEAMRALE YLFKFIVQSR ILYSRATCGM EEEQFRSSIQ ELFQSIRFVL SLDSRNSETL
790 800 810 820 830 840
LFTQAALLNS FPTIFDELLQ MFTVQEVAEF VRGTLGSMPS TVHIGQSMDV VKLQSIARTV
850 860 870 880 890 900
DSRLFSFSES RRILLPVVLH HIHLHLRQQK ELLICSGILG SIFSIVKTSS LEADVMEEVE
910 920 930 940 950 960
MMVESLLDVL LQTLLTIMSK SHAQEAVRGH CPVTAEITGE YVSCLLSLLR QMCDTHFQHL
970 980 990 1000 1010 1020
LDNFQSKDEL KEFLLKIFCV FRNLMKMSVF PRDWMVMRLL TSNIIVTTVQ YLSSALHKNF
1030 1040 1050 1060 1070 1080
TETDFDFKVW NSYFSLAVLF INQPSLQLEI ITSAKRKKIL DKYGDMRVMM AYELFSMWQN
1090 1100 1110 1120 1130 1140
LGEHKIHFIP GMIGPFLGVT LVPQPEVRNI MIPIFHDMMD WEQRKNGNFK QVEAELIDKL
1150 1160 1170 1180 1190 1200
DSMVSEGKGD ESYRELFGLL TQLFGPYPSL LEKVEQETWR ETGISFVTSV TRLMERLLDY
1210 1220 1230 1240 1250 1260
RDCMKGEETE NKKVGCTVNL MNFYKSEINK EEMYIRYIHK LCDMHLQAEN YTEAAFTLLL
1270 1280 1290 1300 1310 1320
YCELLQWEDR PLREFLHYPS QTEWQRKEGL CRKIIHYFNK GKSWEFGIPL CRELACQYES
1330 1340 1350 1360 1370 1380
LYDYQSLSWI RKMEASYYDN IIEQQRLEPE FFRVGFYGRK FPFFLRNKEY VCRGHDYERL
1390 1400 1410 1420 1430 1440
EAFQQRMLSE FPQAVAMQHP NHPDDAILQC DAQYLQIYAV TPIPDYVDVL QMDRVPDRVK
1450 1460 1470 1480 1490 1500
SFYRVNNVRK FRYDRPFHKG PKDKDNEFKS LWIERTTLTL THSLPGISRW FEVERRELVE
1510 1520 1530 1540 1550 1560
VSPLENAIQV VENKNQELRA LISQYQHKQV HGNINLLSMC LNGVIDAAVN GGIARYQEAF
1570 1580 1590 1600 1610 1620
FDKDYITKHP GDAEKISQLK ELMQEQVHVL GVGLAVHEKF VHPEMRPLHK KLIDQFQMMR
1630 1640 1650 1660 1670 1680
ASLYHEFPGL DKLSPACSGT STPRGNVLAS HSPMSPENIK MTHRHSPMNL MGTGRHSSSS
1690 1700 1710 1720 1730 1740
LSSHASSEAG NMMMMGDNSM GEAPEDLYHH MQLAYHNPRY QGSVTNVSVL SSSQASPSSS
1750 1760 1770 1780 1790 1800
SLSSTHSAPS QMITSAPSST RGSPSLPDKY RHAREMMLLL PTHRDRPSSA MYPAAILENG
1810 1820 1830 1840 1850 1860
QPPNFQRALF QQVVGACKPC SDPNLSMAEK GHYSLHFDAF HHPLGDTPPA LPARTLRKSP
1870 1880 1890 1900 1910 1920
LHPIPASPTS PQSGLDGSNS TLSGSASSGV SSLSESNFGH SSEAPPRTDT MDSMPSQAWN
1930 1940 1950 1960 1970 1980
GDEGLEPPYL PVHYSLSESA VLDAIKSQPC RSHSAPGCVL PQDPMDPPAL PPKPYHPRLP
1990 2000 2010 2020
ALEHDEGMLL REEAERPRGL HRKASLPPGS VKEEQARLAW EHGRGEQ