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 P54074

Entry ID Method Resolution Chain Position Source
AF-P54074-F1 Predicted AlphaFoldDB

11 variants for P54074

Variant ID(s) Position Change Description Diseaes Association Provenance
s13-505639 103 N>S No SGRP
s13-505689 120 V>I No SGRP
s13-505701 124 V>F No SGRP
s13-505941 204 F>L No SGRP
s13-506196 289 K>E No SGRP
s13-506331 334 A>T No SGRP
s13-506787 486 D>N No SGRP
s13-506979 550 K>E No SGRP
s13-507001 557 T>I No SGRP
s13-507088 586 F>Y No SGRP
s13-507204 625 K>Q No SGRP

No associated diseases with P54074

No regional properties for P54074

Type Name Position InterPro Accession
No domain, repeats, and functional sites for P54074

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Nucleus inner membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
Asi complex A nuclear ubiquitin ligase multiprotein complex located in the inner nuclear membrane (INM) that recognizes and ubiquitinates misfolded INM proteins and also some proteins involved in sterol biosynthesis, during ER-associated protein degradation (ERAD). In S. cerevisiae, this complex contains the ubiquitin ligases Asi1p and Asi3p.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.
nuclear inner membrane The inner, i.e. lumen-facing, lipid bilayer of the nuclear envelope.
nuclear periphery The portion of the nuclear lumen proximal to the inner nuclear membrane.

3 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
ubiquitin-protein transferase activity Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y --> Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages.

4 GO annotations of biological process

Name Definition
cellular response to amino acid stimulus 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 an amino acid stimulus. An amino acid is a carboxylic acids containing one or more amino groups.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
transcription factor catabolic process The chemical reactions and pathways resulting in the breakdown of a sequence-specific DNA-binding transcription factor by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNSSTSSENV FINSFSYLNQ TSQAVISGNS TFANVINFPY RLGLSFIGAV NLQYEQTVKS
70 80 90 100 110 120
EEIPPTLRSV FDTIGFFFSP YAIFCFVIAI VLNRFVVFYA VLNNGSRRTL PLWLSNVFHV
130 140 150 160 170 180
SAVVVLAMVS LGPLTLGKDF KILGDPAFAQ EKFLLNIFYA FAYSYCVETI FTIMRNSSPL
190 200 210 220 230 240
EGTDYSLFEL SIQFYTMTNN NTKFLDSPDY IIDCSMAILS RILIHLVEIF RLRNYRLLFS
250 260 270 280 290 300
TIMNLCHICY LGIRVKQGGW KSLPFSVKFR HFPKLFSVSI ICLSLLIFKL SCLIRWDPFG
310 320 330 340 350 360
KSRNSCELLQ FYPLSRNWKK YLNYTGEEDF SAMATKFALL LCSGTELMEK GIRREFPAIN
370 380 390 400 410 420
IPDNVNEKFF ISGYLNELSK PYKENTSISF PKKNSSILKQ RFFLMFPKSI IWIMKKLVGQ
430 440 450 460 470 480
VFFGFRDNKD EDIPDNDPSK MLKITKTNSL NNSAGHKEDI ELELLNTSDD EYSEDYEPSE
490 500 510 520 530 540
VESLGDSDEE NLEEDSLIFN ETRDALLDLF SSEDNEVHTD YNWIMSTSRI LQQKLLSDKT
550 560 570 580 590 600
LTRASILDTK LSEVDETFGT ESDFDLSCAV CKVNERNTVL WPCRCFAICE DCRISLGLRG
610 620
FSTCVCCRSK VHGYCKVHPV SDSK