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 B8GNX1

Entry ID Method Resolution Chain Position Source
AF-B8GNX1-F1 Predicted AlphaFoldDB

No variants for B8GNX1

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B8GNX1

No associated diseases with B8GNX1

3 regional properties for B8GNX1

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 192 - 205 IPR018181-2
conserved_site Heat shock protein 70, conserved site 337 - 351 IPR018181-3

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

3 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
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.

No GO annotations of biological process

Name Definition
No GO annotations for biological process

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGKIIGIDLG TTNSCVAVME GDKAKVIENA EGARTTPSIV AFTEDGEVLV GQAAKRQAVT
70 80 90 100 110 120
NPKNTLFAVK RLIGRRFEEP EVQKDIKLVP YEIFKADNGD AWVRVRDKKM APPEISARVL
130 140 150 160 170 180
QKMKKTAEDY LGEPVTEAVI TVPAYFNDSQ RQATKDAGKI AGLEVKRIIN EPTAAALAYG
190 200 210 220 230 240
LDKKRGDSKV AVYDLGGGTF DVSIIEIAEV DGEHQFEVLA TNGDTFLGGE DFDMRLIDYL
250 260 270 280 290 300
VEEFKKEQGI DLKGDPLAMQ RLKESAEKAK IELSSSQQTD VNLPYITADA SGPKHMNIKV
310 320 330 340 350 360
TRAKLESLVE ELIKRTIEPC KVALKDAGLS VSDIDDVILV GGQTRMPKVQ DAVKNFFGKE
370 380 390 400 410 420
PRKDVNPDEA VAVGAAIQAG VLGGEVKDVL LLDVTPLSLG IETLGGVMTK LIEKNTTIPT
430 440 450 460 470 480
KATQVFSTAD DNQTAVTVHV LQGEREMASA NKSLGRFDLT DIPPAPRGVP QVEVMFDIDA
490 500 510 520 530 540
NGILNVSAKD KATGKQQSIV IKASSGLSDE EVERMVRDAE AHADEDKRFH ELVAARNQAD
550 560 570 580 590 600
NLVHATEKSL KELGDQVEAG EKQAIESALS ELREAMKGDN KDEIETRTQK LAEASGKLAE
610 620 630 640
RVYAKQSAEG GAGEGAGAEQ ASAQQDDVVD AEFEEVDDKK K