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 G3X9C2

Entry ID Method Resolution Chain Position Source
AF-G3X9C2-F1 Predicted AlphaFoldDB

21 variants for G3X9C2

Variant ID(s) Position Change Description Diseaes Association Provenance
rs248488400 9 T>A No EVA
rs3388873830 22 S>L No EVA
rs3388885634 30 Q>H No EVA
rs3388887638 37 S>Y No EVA
rs3388893022 78 P>L No EVA
rs3388867424 79 P>Q No EVA
rs246634168 113 P>H No EVA
rs246634168 113 P>R No EVA
rs3388867483 115 G>D No EVA
rs3388885678 191 L>M No EVA
rs3388890450 193 A>T No EVA
rs3388898918 196 R>H No EVA
rs3413155304 198 T>M No EVA
rs3388867434 222 S>P No EVA
rs222446508 236 Y>H No EVA
rs3388885636 238 Q>E No EVA
rs3388885686 249 G>E No EVA
rs3388896358 249 G>V No EVA
rs3388896760 250 L>V No EVA
rs3388873890 251 R>W No EVA
rs3388867479 253 T>A No EVA

No associated diseases with G3X9C2

1 regional properties for G3X9C2

Type Name Position InterPro Accession
domain F-box associated (FBA) domain 83 - 264 IPR007397

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
SCF ubiquitin ligase complex A ubiquitin ligase complex in which a cullin from the Cul1 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a Skp1 adaptor and an F-box protein. SCF complexes are involved in targeting proteins for degradation by the proteasome. The best characterized complexes are those from yeast and mammals (with core subunits named Cdc53/Cul1, Rbx1/Hrt1/Roc1).

No GO annotations of molecular function

Name Definition
No GO annotations for molecular function

5 GO annotations of biological process

Name Definition
glycoprotein catabolic process The chemical reactions and pathways resulting in the breakdown of a glycoprotein, a protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide.
positive regulation of cell population proliferation Any process that activates or increases the rate or extent of cell proliferation.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
SCF-dependent proteasomal 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, with ubiquitin-protein ligation catalyzed by an SCF (Skp1/Cul1/F-box protein) complex, and mediated by the proteasome.
ubiquitin-dependent ERAD pathway The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9UJU2 LEF1 Lymphoid enhancer-binding factor 1 Homo sapiens (Human) PR
Q6DIA9 Fbxo27 F-box only protein 27 Mus musculus (Mouse) PR
Q80UW2 Fbxo2 F-box only protein 2 Mus musculus (Mouse) PR
10 20 30 40 50 60
MEKTQDRDTL SGRMEAEGSL NSEELPPHPQ SPPPPPSPRS PTSPVTPELP QPNAPTEVEA
70 80 90 100 110 120
RQLLVEEWGP LSGKLELPPR ISWQLLFLER PLYRNLLSSP NPEGINIYQP APPTGPTRKP
130 140 150 160 170 180
LKELGNFRGW YITTQNLQGP LSWTVKEQCV NLLAKKLWEE LLDDEQPDIT IMDWFEDSRL
190 200 210 220 230 240
DQCVYELHVW LLAADRRTVI AQHHVAPRTN GRGPPGRWIQ VSHVFRQYGP GVRFVYFQHK
250 260
AKNRMEPGGL RRTRVTDSSV SVQLRE