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 Q9UTG2

Entry ID Method Resolution Chain Position Source
AF-Q9UTG2-F1 Predicted AlphaFoldDB

4 variants for Q9UTG2

Variant ID(s) Position Change Description Diseaes Association Provenance
I_2799569_T_C 171 K>E No Jeffares_SNPs
I_2799448_A_G 211 L>S No Jeffares_SNPs
I_2799440_T_G 214 N>H No Jeffares_SNPs
I_2799116_T_C 322 S>G No Jeffares_SNPs

No associated diseases with Q9UTG2

3 regional properties for Q9UTG2

Type Name Position InterPro Accession
domain C2 domain 1 - 112 IPR000008
domain HECT domain 317 - 671 IPR000569
domain WW domain 242 - 275 IPR001202

Functions

Description
EC Number 2.3.2.26 Aminoacyltransferases
Subcellular Localization
  • Membrane ; Peripheral membrane protein
  • Cytoplasm
  • Predominantly found at the cell surface of the polar regions
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
cell cortex of cell tip The region directly beneath the plasma membrane at the cell tip. The cell tip is the region at either end of the longest axis of a cylindrical or elongated cell.
cell division site The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

1 GO annotations of molecular function

Name Definition
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.

5 GO annotations of biological process

Name Definition
cytoplasm to vacuole transport by the NVT pathway A pathway targeting soluble cytosolic proteins to the vacuole lumen. It uses a selective autophagy receptor protein Nbr1, which is an ortholog of mammalian NBR1, and is remotely related to S. cerevisiae Cvt pathway receptor protein Atg19. Similar to the Cvt pathway, the cargos transported by this pathway are hydrolases, which presumably contribute to the hydrolytic activities in the vacuole lumen. Different from the Cvt pathway, this pathway does not require the macroautophagy machinery, but instead relies on the ESCRT machinery for cargo sequestration. This pathway is observed in the fission yeast S. pombe.
proteasome-mediated 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 ubiquitin, and mediated by the proteasome.
protein modification by small protein conjugation or removal A protein modification process in which one or more groups of a small protein, such as ubiquitin or a ubiquitin-like protein, are covalently attached to or removed from a target protein.
protein polyubiquitination Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MENIRFEVQL TILHVEGLWK NGLLRSLKPY LLISVDDDQF IKTNVASGTL RLSWGFTQKL
70 80 90 100 110 120
TVSPQSIILL QLFDEKQKNE TSDGFVGLGA AVVNSFLPFN NPKDDYKTRI TLRSPSGSYR
130 140 150 160 170 180
GSVVCLFKRS KFLPEELPAD KSQICTDIID DASGCAWETR IDEFGHVYYL KSPQLSVISA
190 200 210 220 230 240
ISHEKLENLT PKQLKEVFSQ FLFNNQSKSS LKINLEYKVI KHLLEHYPLA LSVRQQVAVE
250 260 270 280 290 300
KGPLPAGWEM RLSEDYHVYF VDHSTKTTTW SDPRDNVVAS DSVSENTDSI QQINDEYQRK
310 320 330 340 350 360
IAYMYDRPEM AVNDAQLQLK VSRATTFEDA YDIISKLSVS DMKKKLLIRF RNEDGLDYGG
370 380 390 400 410 420
VSREFFYILS HAIFNPGYSL FEYATDDNYG LQISPLSSVN PDFRSYFRFV GRVMGLAIYH
430 440 450 460 470 480
RRYLDVQFVL PFYKRILQKP LCLEDVKDVD EVYYESLKWI KNNDVDESLC LNFSVEENRF
490 500 510 520 530 540
GESVTVDLIP NGRNIAVNNQ NKMNYLKALT EHKLVTSTEE QFNALKGGLN ELIPDSVLQI
550 560 570 580 590 600
FNENELDTLL NGKRDIDVQD WKRFTDYRSY TETDDIVIWF WELLSEWSPE KKAKLLQFAT
610 620 630 640 650 660
GTSRLPLSGF KDMHGSDGPR KFTIEKVGHI SQLPKAHTCF NRLDIPPYNS KEELEQKLTI
670
AIQETAGFGT E