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 Q8BSL4

Entry ID Method Resolution Chain Position Source
AF-Q8BSL4-F1 Predicted AlphaFoldDB

11 variants for Q8BSL4

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389103875 5 Q>H No EVA
rs3389097421 15 V>L No EVA
rs3389094896 45 S>C No EVA
rs3400484535 134 K>M No EVA
rs3400953461 134 K>N No EVA
rs3401035813 134 K>Q No EVA
rs3389099486 178 L>P No EVA
rs3389090656 190 I>T No EVA
rs3389094861 193 Y>F No EVA
rs3389099474 216 D>N No EVA
rs3401161745 317 D>E No EVA

No associated diseases with Q8BSL4

1 regional properties for Q8BSL4

Type Name Position InterPro Accession
domain Sulfotransferase domain 91 - 335 IPR000863

Functions

Description
EC Number 2.8.2.23 Sulfotransferases
Subcellular Localization
  • Golgi apparatus membrane ; Single-pass type II membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
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
[heparan sulfate]-glucosamine 3-sulfotransferase 1 activity Catalysis of the reaction: 3'-phosphoadenylyl sulfate + -glucosamine 3-sulfate has a substrate consensus sequence of Glc(N2S>NAc)+/-6S GlcA GlcN2S*+/-6S GlcA>IdoA+/-2S Glc(N2S/NAc)+/-6S.

5 GO annotations of biological process

Name Definition
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.
heparan sulfate proteoglycan biosynthetic process, enzymatic modification The modification, often by sulfation, of sugars incorporated into heparan sulfate after polymerization.
negative regulation of coagulation Any process that stops, prevents, or reduces the frequency, rate or extent of coagulation.
protein sulfation The addition of a sulfate group as an ester to a protein amino acid.
regulation of viral entry into host cell Any process that modulates the frequency, rate or extent of the viral entry into the host cell.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q8IZT8 HS3ST5 Heparan sulfate glucosamine 3-O-sulfotransferase 5 Homo sapiens (Human) PR
O35310 Hs3st1 Heparan sulfate glucosamine 3-O-sulfotransferase 1 Mus musculus (Mouse) PR
Q9ESG5 Hs3st1 Heparan sulfate glucosamine 3-O-sulfotransferase 1 Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MLFKQQVWLR QKLLVLGSLA VGSLLYLVAR VGSLDRLQPI CPVESRFGGA HNQAELPLRA
70 80 90 100 110 120
LQFKRGLLHE FRKGNSSKEQ VHLHDLVQQL PKAIIIGVRK GGTRALLEML NLHPAVVKAS
130 140 150 160 170 180
QEIHFFDNDE NYAKGIEWYR KKMPFSYPQQ ITIEKSPAYF ITEEVPERIY KMNSSIKLLI
190 200 210 220 230 240
IVREPTTRAI SDYTQVLEGK ERKNKTYYKF EKLAIDPNTC EVNTKYKAVR TSIYTKHLER
250 260 270 280 290 300
WLKYFPIEQF HIVDGDRLIT EPLPELQLVE KFLNLPPRIS QYNLYFNATR GFYCLRFNII
310 320 330 340
FNKCLAGSKG RIHPEVDPSV ITKLRKFFHP FNQKFYQITG RTLNWP