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 A7S2N8

Entry ID Method Resolution Chain Position Source
AF-A7S2N8-F1 Predicted AlphaFoldDB

No variants for A7S2N8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A7S2N8

No associated diseases with A7S2N8

No regional properties for A7S2N8

Type Name Position InterPro Accession
No domain, repeats, and functional sites for A7S2N8

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
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.

2 GO annotations of molecular function

Name Definition
UFM1 ligase activity Catalysis of the transfer of UFM1 to a substrate protein via the reaction X-UFM1 + S --> X + S-UFM1, where X is either an E2 or E3 enzyme, the X-UFM1 linkage is a thioester bond, and the S-UFM1 linkage is an isopeptide bond between the C-terminal amino acid of UFM1 and the epsilon-amino group of lysine residues in the substrate.
UFM1 transferase activity Catalysis of the transfer of UFM1 from one protein to another via the reaction X-UFM1 + Y --> Y-UFM1 + X, where both X-UFM1 and Y-UFM1 are covalent linkages.

3 GO annotations of biological process

Name Definition
protein K69-linked ufmylation A protein ufmylation process in which a polymer of the ubiquitin-like protein UFM1 is formed by linkages between lysine residues at position 69 of the UFM1 monomers, is added to a protein.
regulation of proteasomal ubiquitin-dependent protein catabolic process Any process that modulates the frequency, rate or extent of the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
response to endoplasmic reticulum stress Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in 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
MADWDEIKKL AADFHRVQLT STAHKLSERN CIEIVQKLIN TGLLEVIYTT DGKEYLTPQQ
70 80 90 100 110 120
LEREIKDELF VHGGRFFLLN LVDLQQIINV DLSHVDNKVS EILRHDKSLV LIQGDLIDKD
130 140 150 160 170 180
YLDRMAEEIN ETLQEAGQVF IAELSKTFSL PTDFMLEVVE SRLDIQIMGK LDQMDRNVLY
190 200 210 220 230 240
THAFIARQTA RMRGVLSAIT RPTQFSNIIS KYGFQEKLFY SVIGDLLSSK RIMGSTQGRQ
250 260 270 280 290 300
DKISFVPDVY TQAQNNWVDD FFKQNGYVEY DALTRLGITD GKQFLKRRYH GNEIFLPTCC
310 320 330 340 350 360
VGERVLDQAD AAIDDALSSG TWVDIMPHLP TPFTPDDAEQ LLQHCLKTPG RSTAHVYCSS
370 380 390 400 410 420
IVASDKFVEA CKAPFETRMH AKAKKDAAES PALFAELSKK DLASLKGGGG GADRREARKE
430 440 450 460 470 480
DRRKTASSGG KGGGSVGGRG GRETKTKKVK KKDFRNRNDE DDTNEADSRS NPDELQFMTT
490 500 510 520 530 540
EEIAEVLRKD RPDIDDDFLE ELAQEMHRPL TRAYQQVARA VLQSSGDKKR KSHAEIQEKV
550 560 570 580 590 600
NALWANAKLF DKSINLFPED VQVHLSRHLL RTVCTDITNL MVNMLAADHM LAVTDETTIT
610 620 630 640 650 660
PETRLKIIKK MPEEIKAPLT KLNSSLTAKE TEEFFAQFDL VAGQGLCELM IKKLDKKKER
670 680 690 700 710 720
QISIERRAAL QEQLRHEDEP AMTLHLAVSL LFQHFTSSLL HAPGRCVPQI VALLAEHVTP
730 740 750 760 770 780
EQHEILLRCQ SLVVKQLTRS GSDEVEEEAG DEHENEAGVE KSTAVLLEEG MREIKKMVLE
LKKDNSKNES