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 Q920M5

Entry ID Method Resolution Chain Position Source
AF-Q920M5-F1 Predicted AlphaFoldDB

27 variants for Q920M5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389180407 81 T>S No EVA
rs3389176913 92 H>Y No EVA
rs3389192056 110 Q>H No EVA
rs3389145611 141 P>L No EVA
rs3389189311 171 D>A No EVA
rs3389177804 225 A>S No EVA
rs3389177817 258 V>M No EVA
rs3389181745 260 L>Q No EVA
rs3389145609 261 Q>R No EVA
rs3402553945 281 V>L No EVA
rs3389117950 289 S>C No EVA
rs3389177802 304 H>D No EVA
rs3402232775 311 S>L No EVA
rs3389189327 314 P>S No EVA
rs3389189307 337 Y>F No EVA
rs3389169315 362 L>R No EVA
rs3389145659 367 P>A No EVA
rs3389185717 373 L>Q No EVA
rs3389182989 419 P>S No EVA
rs3389195049 421 R>C No EVA
rs3389192026 423 Q>H No EVA
rs3389194999 436 E>G No EVA
rs3389156083 439 L>M No EVA
rs231898673 441 E>D No EVA
rs215623923 447 D>E No EVA
rs3389185693 469 G>V No EVA
rs1133561570 471 D>G No EVA

No associated diseases with Q920M5

4 regional properties for Q920M5

Type Name Position InterPro Accession
domain Cryptochrome/DNA photolyase, FAD-binding domain 287 - 485 IPR005101
domain DNA photolyase, N-terminal 5 - 160 IPR006050
conserved_site Cryptochrome/DNA photolyase class 1, conserved site, C-terminal 336 - 348 IPR018394-1
conserved_site Cryptochrome/DNA photolyase class 1, conserved site, C-terminal 356 - 375 IPR018394-2

Functions

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

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

1 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.

2 GO annotations of biological process

Name Definition
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.
cell migration The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. Cell migration is a central process in the development and maintenance of multicellular organisms.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q06440 CRN1 Coronin-like protein Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q9ULV4 CORO1C Coronin-1C Homo sapiens (Human) PR
Q9UQ03 CORO2B Coronin-2B Homo sapiens (Human) PR
Q6QEF8 CORO6 Coronin-6 Homo sapiens (Human) PR
Q9D2V7 Coro7 Coronin-7 Mus musculus (Mouse) PR
Q9WUM3 Coro1b Coronin-1B Mus musculus (Mouse) PR
Q9WUM4 Coro1c Coronin-1C Mus musculus (Mouse) PR
10 20 30 40 50 60
MSRRVVRQSK FRHVFGQAAK ADQAYEDIRV SKVTWDSAFC AVNPKFLAII VEAGGGGAFI
70 80 90 100 110 120
VLPLAKTGRV DKNYPLVTGH TGPVLDIDWC PHNDNVIASA SDDTTVMVWQ IPDYTPVRNI
130 140 150 160 170 180
TEPVITLEGH SKRVGILSWH PTARNVLLSA GGDNVIIIWN VGTGEVLLSL DDIHPDVIHS
190 200 210 220 230 240
VCWNSNGSLL ATTCKDKTLR IIDPRKSQVV AERARPHEGA RPLRAVFTAD GKLLSTGFSR
250 260 270 280 290 300
MSERQLALWD PNNFEEPVAL QEMDTSNGVL LPFYDPDSSI VYLCGKGDSS IRYFEITEEP
310 320 330 340 350 360
PFVHYLNTFS SKEPQRGMGF MPKRGLDVSK CEIARFYKLH ERKCEPIIMT VPRKSDLFQD
370 380 390 400 410 420
DLYPDTPGPE PALEADEWLS GQDAEPVLIS LKEGYVPPKH RELRVTKRNI LDVRPPASPR
430 440 450 460 470
RSQSASEAPL SQHTLETLLE EIKALRDRVQ AQEERITALE NMLCELVDGT D