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 Q24798

Entry ID Method Resolution Chain Position Source
AF-Q24798-F1 Predicted AlphaFoldDB

No variants for Q24798

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q24798

No associated diseases with Q24798

2 regional properties for Q24798

Type Name Position InterPro Accession
repeat GTF2I-like repeat 98 - 192 IPR004212-1
repeat GTF2I-like repeat 323 - 417 IPR004212-2

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
endoplasmic reticulum lumen The volume enclosed by the membranes of the endoplasmic reticulum.

3 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.

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
MGLSTYVGIF LLCILTLSRC KSGKEEYGTV IGIDLGTTYS CVGVFKNGRV EIIANDQGNR
70 80 90 100 110 120
ITPSYVAFSG DGERLIGDAA KNQLTSNPKN TLFDAKRLIG RDYHDKDVQG DIKRYPFKVI
130 140 150 160 170 180
NKNNKPYMKV QVGSEEKGFA PEEVSAMVLS KMKEIAEAYL GTEVTHAVVT VPAYFNDAQR
190 200 210 220 230 240
QATKDAGAIA GLTVLRIINE PTAAAIAYGL EKKDTEKNIL VFDLGGGTFD VSLLTIDNGV
250 260 270 280 290 300
FEVVATSGDT HLGGEDFDQR LIDYFVKLYK KKEGKDITKD DRAVQKLRRE VEKAKRTLST
310 320 330 340 350 360
EHSTMIEIDN LFEGKDFSEP LTRARFEELN NDLFRSTLKP VMKVMEDSGL KKEDIDDIVL
370 380 390 400 410 420
VGGSTRIPKI QQLVKEFFNG KEPIRGINPD EAVAYGAAVQ AGVISGVEDT GDIVLLDVCP
430 440 450 460 470 480
LTMGIETVGG VMTKLIPRNT VIPTKKSQIF STAADNQPTV TIQVFEGERP MTKDNHFLGK
490 500 510 520 530 540
FDLTGIPPAP RGLPQIEVTF EIDVNGILRV SAEDKGTGKK SNIVINKETN RITPEEIERM
550 560 570 580 590 600
IQDAEKFSDQ DKQVKERVEV RNDLESLAYS IKNQVKDKEK MGGKLSDDEI KTIEDAADEA
610 620 630 640 650
IKWMENNPQA ETSDYKKQKA NLESVVQPIV SKLYEGAAPP PPTESTPKEE L