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 Q3ZBU9

Entry ID Method Resolution Chain Position Source
AF-Q3ZBU9-F1 Predicted AlphaFoldDB

62 variants for Q3ZBU9

Variant ID(s) Position Change Description Diseaes Association Provenance
rs453662329 8 I>L No EVA
rs433585524 23 V>G No EVA
rs446100537 52 S>N No EVA
rs477580646 52 S>R No EVA
rs460697518 53 F>I No EVA
rs135996099 61 R>K No EVA
rs441875976 153 E>Q No EVA
rs378297087 188 N>T No EVA
rs208513069 195 L>H No EVA
rs474481014 195 L>I No EVA
rs441387430 242 Q>K No EVA
rs472788395 250 M>R No EVA
rs453167751 273 A>G No EVA
rs473201344 273 A>T No EVA
rs454826749 274 L>P No EVA
rs443511564 275 D>A No EVA
rs463561256 275 D>N No EVA
rs471702828 276 R>G No EVA
rs452377231 276 R>H No EVA
rs471702828 276 R>S No EVA
rs473279908 277 A>P No EVA
rs453290281 277 A>V No EVA
rs436538581 278 E>G No EVA
rs433085013 280 A>P No EVA
rs433085013 280 A>S No EVA
rs437469080 282 R>P No EVA
rs444811445 285 K>M No EVA
rs444811445 285 K>R No EVA
rs479428122 287 K>E No EVA
rs465818579 287 K>R No EVA
rs448957342 288 E>Q No EVA
rs443433557 290 V>A No EVA
rs463545216 290 V>I No EVA
rs477875207 304 E>D No EVA
rs438715831 310 E>Q No EVA
rs473218499 310 E>V No EVA
rs442906653 311 T>P No EVA
rs474334275 311 T>S No EVA
rs457520768 312 S>Y No EVA
rs452027731 316 R>* No EVA
rs435117641 317 S>N No EVA
rs722065468 335 Q>H No EVA
rs1117906329 358 G>S No EVA
rs444356800 410 D>E No EVA
rs444262565 413 T>S No EVA
rs475598738 417 T>A No EVA
rs438837443 420 Y>C No EVA
rs436605836 427 R>S No EVA
rs453442500 427 R>T No EVA
rs474477413 430 S>N No EVA
rs475427086 436 N>S No EVA
rs437534026 461 E>A No EVA
rs479004349 464 E>A No EVA
rs466104630 468 K>R No EVA
rs449303193 470 V>G No EVA
rs463875937 473 K>* No EVA
rs444324299 474 R>Q No EVA
rs478391876 476 E>* No EVA
rs458392141 479 K>N No EVA
rs481906246 481 E>K No EVA
rs1114378429 492 D>N No EVA
rs441469213 493 G>R No EVA

No associated diseases with Q3ZBU9

1 regional properties for Q3ZBU9

Type Name Position InterPro Accession
domain UBX domain 312 - 395 IPR001012

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Peripheral membrane protein
  • Nucleus envelope
  • Both the N- and the C-terminus face the cytosol
  • Also found in the nucleus envelope contiguous to the ER
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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).
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
nuclear envelope The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space).

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

2 GO annotations of biological process

Name Definition
response to unfolded protein Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an unfolded protein stimulus.
ubiquitin-dependent ERAD pathway The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P38349 UBX7 UBX domain-containing protein 7 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q92575 UBXN4 UBX domain-containing protein 4 Homo sapiens (Human) PR
Q8VCH8 Ubxn4 UBX domain-containing protein 4 Mus musculus (Mouse) PR
Q5HZY0 Ubxn4 UBX domain-containing protein 4 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MLWFQGAIPA AIASAKRSGA VFVVFVAGDD EQSTQMAASW EDEKVTEASS NSFVAIKIDT
70 80 90 100 110 120
RSEACLQFSQ IYPVVCVPSS FFIGDSGIPL EVIAGSISAD ELVTRIHKVR QMHSLKGEAS
130 140 150 160 170 180
LANGSQSEGS VSTPSASFEH NNTSENCQSR NVELCETPST SDTKSDSATG GESSGQTTVS
190 200 210 220 230 240
QEPSGCSNQR PTEDLTVRVE RLTKKLEERR EEKRKEEEQR EIKKEIERRK TGKEMLDYKR
250 260 270 280 290 300
KQEEELTKRM LEERNREKAE DRAARERIKQ QIALDRAERA ARFAKTKEEV EAAKAAALLA
310 320 330 340 350 360
KQAEMEIKRE TSTKERSTVA RIQFRLPDGS SFTNQFPSDA PLEEARQFAA QTVGNTYGNF
370 380 390 400 410 420
SLATMFPRRE FTKEDYKKKL LDLELAPSAS VVLLPAGRPT TSMVHSSSGD FWTLLGTVLY
430 440 450 460 470 480
PFLAIWRLIS NFLFSNPPPA QTSVRAASLE TSNLASSSNS EKREPVRKRV LEKRGEDFKK
490 500
EGKIYRLRTQ DDGEDENNTW NGNSTQQM