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 Q96W30

Entry ID Method Resolution Chain Position Source
AF-Q96W30-F1 Predicted AlphaFoldDB

No variants for Q96W30

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q96W30

No associated diseases with Q96W30

3 regional properties for Q96W30

Type Name Position InterPro Accession
conserved_site Heat shock protein 70, conserved site 7 - 14 IPR018181-1
conserved_site Heat shock protein 70, conserved site 195 - 208 IPR018181-2
conserved_site Heat shock protein 70, conserved site 332 - 346 IPR018181-3

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
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

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.

2 GO annotations of biological process

Name Definition
protein quality control for misfolded or incompletely synthesized proteins The chemical reactions and pathways resulting in the breakdown of misfolded or attenuated proteins.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAPAIGIDLG TTYSCVGIFR DDRIEIIAND QGNRTTPSFV AFTDTERLIG DAAKNQVAMN
70 80 90 100 110 120
PSNTVFDAKR LIGRKFADPE VQSDMKHFPF KVIDKAGKPV ISVEFKGEEK QFTPEEISSM
130 140 150 160 170 180
VLTKMRETAE SYLGGTVNNA VVTVPAYFND SQRQATKDAG LIAGLNVLRI INEPTAAAIA
190 200 210 220 230 240
YGLDKKAEGE RNVLIFDLGG GTFDVSLLTI EEGIFEVKST AGDTHLGGED FDNRLVNHFV
250 260 270 280 290 300
NEFKRKHKKD LSSNARALRR LRTACERAKR TLSSAAQTSI EIDSLYEGID FYTSITRARF
310 320 330 340 350 360
EELCQDLFRS TMDPVERVLR DAKIDKSSVH EIVLVGGSTR IPRIQKLVSD FFNGKEPNKS
370 380 390 400 410 420
INPDEAVAYG AAVQAAILSG DTTSKSTNEI LLLDVAPLSV GIETAGGVMT PLIKRNTTIP
430 440 450 460 470 480
TKKSETFSTF ADNQPGVLIQ VFEGERARTK DNNLLGKFEL TGIPPAPRGV PQIEVTFDVD
490 500 510 520 530 540
ANGIMNVSAL EKGTGKTNKI VITNDKGRLS KEEIERMLAE AEKYKAEDEA EASRISAKNG
550 560 570 580 590 600
LESYAYSLRN TISDSKVDEK LDASDKEKLK TEIDKTVSWL DENQTATKEE FEAQQKELES
610 620 630 640 650
VANPIMMKFY GAGGEGGAPG AGFPGAGGPG GFPGAGAGGA HSGGDDGPTV EEVD