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

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q06440

Entry ID Method Resolution Chain Position Source
AF-Q06440-F1 Predicted AlphaFoldDB

16 variants for Q06440

Variant ID(s) Position Change Description Diseaes Association Provenance
s12-991056 95 H>Y No SGRP
s12-991113 114 N>D No SGRP
s12-991131 120 H>Y No SGRP
s12-991365 198 A>T No SGRP
s12-991953 394 G>S No SGRP
s12-991999 409 P>Q No SGRP
s12-992241 490 V>I No SGRP
s12-992304 511 A>T No SGRP
s12-992329 519 V>A No SGRP
s12-992328 519 V>I No SGRP
s12-992332 520 T>S No SGRP
s12-992445 558 E>K No SGRP
s12-992538 589 A>T No SGRP
s12-992569 599 R>K No SGRP
s12-992598 609 K>Q No SGRP
s12-992659 629 T>M No SGRP

No associated diseases with Q06440

1 regional properties for Q06440

Type Name Position InterPro Accession
domain Glycosyltransferase 2-like 242 - 441 IPR001173

Functions

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

1 GO annotations of cellular component

Name Definition
actin cortical patch An endocytic patch that consists of an actin-containing structure found at the plasma membrane in cells; formed of networks of branched actin filaments that lie just beneath the plasma membrane and assemble, move, and disassemble rapidly. An example of this is the actin cortical patch found in Saccharomyces cerevisiae.

4 GO annotations of molecular function

Name Definition
actin filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
Arp2/3 complex binding Binding to an Arp2/3 complex, a protein complex that contains two actin-related proteins, Arp2 and Arp3, and five novel proteins (ARPC1-5).
microtubule binding Binding to a microtubule, a filament composed of tubulin monomers.
protein-macromolecule adaptor activity The binding activity of a protein that brings together two or more macromolecules in contact, permitting those molecules to function in a coordinated way. The adaptor can bring together two proteins, or a protein and another macromolecule such as a lipid or a nucleic acid.

5 GO annotations of biological process

Name Definition
actin cortical patch localization Any process in which actin cortical patches are transported to, or maintained in, a specific location. An actin cortical patch is a discrete actin-containing structure found just beneath the plasma membrane in fungal cells.
actin filament 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. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
microtubule-based process Any cellular process that depends upon or alters the microtubule cytoskeleton, that part of the cytoskeleton comprising microtubules and their associated proteins.
negative regulation of Arp2/3 complex-mediated actin nucleation Any process that stops, prevents, or reduces the frequency, rate or extent of actin nucleation mediated by the Arp2/3 complex and interacting proteins.
positive regulation of Arp2/3 complex-mediated actin nucleation Any process that activates or increases the frequency, rate or extent of Arp2/3 complex-mediated actin nucleation.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9ULV4 CORO1C Coronin-1C Homo sapiens (Human) PR
Q9UQ03 CORO2B Coronin-2B Homo sapiens (Human) PR
Q6QEF8 CORO6 Coronin-6 Homo sapiens (Human) PR
Q9WUM3 Coro1b Coronin-1B Mus musculus (Mouse) PR
Q9WUM4 Coro1c Coronin-1C Mus musculus (Mouse) PR
Q920M5 Coro6 Coronin-6 Mus musculus (Mouse) PR
10 20 30 40 50 60
MSGKFVRASK YRHVFGQAAK KELQYEKLKV TNNAWDSNLL KTNGKFIAVN WNASGGGAFA
70 80 90 100 110 120
VIPIEEVGKA PDQVPLFRGH TAQVLDTDFD PFNDHRIASG SDDSKIGIWD IPENYKFHDH
130 140 150 160 170 180
VDEDGEPIDI KPVKFLTGHA RKVGHVLYHP VAENVLASSS GDYTVKLWNV ETGKDMITLK
190 200 210 220 230 240
HPDMVTSMSF SYDGNYLATV ARDKKLRVWN IREEKIVSEG PAHTGAKNQR VVWLGNSDRL
250 260 270 280 290 300
ATTGFSKLSD RQIGIWDAFN IEKGDLGGFY TVDQSSGILM PFYDEGNKIL YLVGKGDGNI
310 320 330 340 350 360
RYYEFQNDEL FELSEFQSTE AQRGFAVAPK RMVNVKENEV LKGFKTVVDQ RIEPVSFFVP
370 380 390 400 410 420
RRSEEFQEDI YPDAPSNKPA LTAEEWFSGK SVEGPILVSM RSIYDGSAPS FHEAKRPQQP
430 440 450 460 470 480
TTQETALEEK KEQPKVEKPI SESEKEVKQE APKSPSPLKS ASSSSTINHV LKEDNSINKL
490 500 510 520 530 540
LKKSSDIDQV NNAEDPSRDT SGWEEADDEP APIKIETPVT PTETKKDRTP KVEPSKELKP
550 560 570 580 590 600
EPVSIATDRK QEQSLPQEEK SSEKTKSPEQ EKSATPPSSI TAAKTAITAS SKEEPSAART
610 620 630 640 650
SPKSLGLKKS VEKLSTLVLQ LEDVVDKLTK ANLDKDERLL KLEQKIGELS K