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 Q9R099

Entry ID Method Resolution Chain Position Source
AF-Q9R099-F1 Predicted AlphaFoldDB

24 variants for Q9R099

Variant ID(s) Position Change Description Diseaes Association Provenance
rs230785214 44 Q>L No EVA
rs245033064 60 N>T No EVA
rs257872324 74 T>M No EVA
rs3388796662 143 D>G No EVA
rs3388783826 165 R>W No EVA
rs3388794803 218 L>R No EVA
rs240967829 219 S>A No EVA
rs3388783772 227 N>K No EVA
rs3388804393 248 D>N No EVA
rs3388804371 289 R>G No EVA
rs3388790610 305 D>Y No EVA
rs3388778834 309 K>* No EVA
rs3388797626 317 L>I No EVA
rs3388790663 369 E>G No EVA
rs254006661 382 F>L No EVA
rs3388799433 394 F>L No EVA
rs3388768329 396 N>T No EVA
rs3388796696 418 S>N No EVA
rs3388793275 428 T>I No EVA
rs3396211405 431 Q>H No EVA
rs3388778831 431 Q>L No EVA
rs3388778831 431 Q>P No EVA
rs3396301512 433 A>G No EVA
rs3396009482 436 S>G No EVA

No associated diseases with Q9R099

9 regional properties for Q9R099

Type Name Position InterPro Accession
repeat WD40 repeat 75 - 114 IPR001680-1
repeat WD40 repeat 173 - 214 IPR001680-2
repeat WD40 repeat 214 - 253 IPR001680-3
repeat WD40 repeat 264 - 303 IPR001680-4
repeat WD40 repeat 358 - 395 IPR001680-5
conserved_site WD40 repeat, conserved site 199 - 213 IPR019775
repeat G-protein beta WD-40 repeat 101 - 115 IPR020472-1
repeat G-protein beta WD-40 repeat 199 - 213 IPR020472-2
repeat G-protein beta WD-40 repeat 290 - 304 IPR020472-3

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
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).

3 GO annotations of molecular function

Name Definition
phosphoprotein binding Binding to a phosphorylated protein.
protein kinase binding Binding to a protein kinase, any enzyme that catalyzes the transfer of a phosphate group, usually from ATP, to a protein substrate.
translation initiation factor binding Binding to a translation initiation factor, any polypeptide factor involved in the initiation of ribosome-mediated translation.

3 GO annotations of biological process

Name Definition
cellular response to glucose starvation Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of glucose.
cellular response to hypoxia Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating lowered oxygen tension. Hypoxia, defined as a decline in O2 levels below normoxic levels of 20.8 - 20.95%, results in metabolic adaptation at both the cellular and organismal level.
endoplasmic reticulum unfolded protein response The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9Y4P3 TBL2 Transducin beta-like protein 2 Homo sapiens (Human) PR
10 20 30 40 50 60
MELPQMPELM GLSLLVGLLA LVATAAVARG WLRAEEKPSQ PVCQKENEPK KSGSKKQKQN
70 80 90 100 110 120
QRVRKEKPQQ HSFTHPLLAA ALKSHSGNIS CMDFSSNGKY LATCADDRTV RIWSTKDFLQ
130 140 150 160 170 180
REHRSMRANV ELDHATLVRF SPDCRAFIVW LANGDTLRVF KMTKREDGGF TFTATPEDFP
190 200 210 220 230 240
KKHKAPIINI GIADTGKFIM TASSDTTVLI WNLKGQVLST INTNQMNNSH AVISPCSRFV
250 260 270 280 290 300
GSCGFTPDVK VWEVCFGKKG EFQEVLRAFE LKGHSASVHS FAFSNDSRRM ASVSKDGTWK
310 320 330 340 350 360
LWDTDVEYKK QQDPYLLRTG RFEEASTMPC RLALSPDTHV LALATGTNIH LFNTRRGEKE
370 380 390 400 410 420
EYFECVHGEC IADLTFDITG RFLASCGDRA VRLFHNTPGH RAVVEEMQSL LKRASSESTR
430 440
QRLQQQLTQA QEALKSLGAL KK