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 P22010

Entry ID Method Resolution Chain Position Source
AF-P22010-F1 Predicted AlphaFoldDB

No variants for P22010

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P22010

No associated diseases with P22010

2 regional properties for P22010

Type Name Position InterPro Accession
domain Bromodomain 62 - 172 IPR001487
domain Putative transcription factor GTE, bromodomain 69 - 167 IPR037377

Functions

Description
EC Number 3.6.4.10 Acting on ATP; involved in cellular and subcellular movement
Subcellular Localization
  • Endoplasmic reticulum lumen
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

1 GO annotations of cellular component

Name Definition
luminal surveillance complex A multiprotein complex that recognizes ERAD-luminal misfolded substrates and brings them to the ubiquitination/extraction machinery. In yeast, this complex consists of Yos9p, Kar2p and Hrd3p proteins.

4 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient.
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
unfolded protein binding Binding to an unfolded protein.

6 GO annotations of biological process

Name Definition
fungal-type cell wall beta-glucan biosynthetic process The chemical reactions and pathways resulting in the formation of beta-glucans, compounds composed of glucose residues linked by beta-D-glucosidic bonds, found in the walls of fungal cells.
karyogamy involved in conjugation with cellular fusion During sexual reproduction, the creation of a single nucleus from multiple nuclei as a result of fusing the lipid bilayers that surround each nuclei. This occurs after cytogamy.
post-translational protein targeting to membrane, translocation The process in which a protein translocates through the ER membrane posttranslationally.
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.
SRP-dependent cotranslational protein targeting to membrane, translocation The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MFSARKSSVG WLVSSLAVFY VLLAVIMPIA LTGSQSSRVV ARAAEDHEDY GTVIGIDLGT
70 80 90 100 110 120
TYSCVAVMKN GKTEILANEQ GNRITPSYVS FTDDERLIGD AAKNQAASNP KNTIFDIKRL
130 140 150 160 170 180
IGLQYNDPTV QRDIKHLPYT VVNKGNKPYV EVTVKGEKKE FTPEEVSGMI LGKMKQIAED
190 200 210 220 230 240
YLGKKVTHAV VTVPAYFNDA QRQATKDAGA IAGLNILRIV NEPTAAAIAY GLDKTEDEHQ
250 260 270 280 290 300
IIVYDLGGGT FDVSLLSIEN GVFEVQATAG DTHLGGEDFD YKLVRHFAQL FQKKHDLDVT
310 320 330 340 350 360
KNDKAMAKLK REAEKAKRSL SSQTSTRIEI DSFFNGIDFS ETLTRAKFEE LNLALFKKTL
370 380 390 400 410 420
KPVEKVLKDS GLQKEDIDDI VLVGGSTRIP KVQQLLEKFF NGKKASKGIN PDEAVAYGAA
430 440 450 460 470 480
VQAGVLSGEE GVEDIVLLDV NALTLGIETT GGVMTPLIKR NTAIPTKKSQ IFSTAVDNQK
490 500 510 520 530 540
AVRIQVYEGE RAMVKDNNLL GNFELSDIRA APRGVPQIEV TFALDANGIL TVSATDKDTG
550 560 570 580 590 600
KSESITIAND KGRLSQDDID RMVEEAEKYA AEDAKFKAKS EARNTFENFV HYVKNSVNGE
610 620 630 640 650 660
LAEIMDEDDK ETVLDNVNES LEWLEDNSDV AEAEDFEEKM ASFKESVEPI LAKASASQGS
670
TSGEGFEDED DDDYFDDEL