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 Q29EY2

Entry ID Method Resolution Chain Position Source
AF-Q29EY2-F1 Predicted AlphaFoldDB

No variants for Q29EY2

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q29EY2

No associated diseases with Q29EY2

No regional properties for Q29EY2

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q29EY2

Functions

Description
EC Number
Subcellular Localization
  • Golgi apparatus membrane ; Multi-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
Golgi cis cisterna The Golgi cisterna closest to the endoplasmic reticulum; the first processing compartment through which proteins pass after export from the ER.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.
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.

1 GO annotations of molecular function

Name Definition
3'-phosphoadenosine 5'-phosphosulfate transmembrane transporter activity Enables the transfer of 3'-phosphoadenosine 5'-phosphosulfate, a naturally occurring mixed anhydride synthesized from adenosine 5'-phosphosulfate, from one side of a membrane to the other.

2 GO annotations of biological process

Name Definition
3'-phosphoadenosine 5'-phosphosulfate transport The directed movement of 3'-phosphoadenosine 5'-phosphosulfate, a naturally occurring mixed anhydride synthesized from adenosine 5'-phosphosulfate, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
heparan sulfate proteoglycan biosynthetic process The chemical reactions and pathways resulting in the formation of the heparan sulfate proteoglycan, a glycosaminoglycan with repeat unit consisting of alternating alpha-(1->4)-linked hexuronic acid and glucosamine residues; the former are a mixture of sulfated and nonsulfated D-glucuronic acid and L-iduronic acid; the L-iduronic acid is either sulfated or acetylated on its amino group as well as being sulfated on one of its hydroxyl groups; heparan sulfate chains are covalently linked to peptidyl-serine by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylosyl to serine residues.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGDGQAGSVI NINGSASGQQ APTSNSPTLT RKSSSSELPP ELRILCFDLT HYNQTTQFLL
70 80 90 100 110 120
SCAGVFILYI LYGYLQELIF TVEGFKPFGW FLTLVQFGYY IGFGLVERRL EAYRSGRRSL
130 140 150 160 170 180
WNVEPAPRCI PMKTYLVLAA LTLGTMGLSN SSLGYLNYPT QVIFKCCKLI PVLVGSILIQ
190 200 210 220 230 240
GKRYGPLDFA AASCMCIGLA WFTLADSQMT PNFNLLGVAM ISGALLCDAA IGNVQEKAMK
250 260 270 280 290 300
EHKAPSSEVV FYSYGLGFVY LFVIMLVTGN FFSGFAFCLE HPLQTFGYGF LFSLSGYLGI
310 320 330 340 350 360
QFVLALVRSS GAPIAATVTT ARKAVTIAFS FVLFSKPFTV QYLWSGLIVV LGIYLNVYSK
370 380 390
KNKLTFADIR SRFKQFGFRL ARSPSRKFLV EV