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 P52844

Entry ID Method Resolution Chain Position Source
AF-P52844-F1 Predicted AlphaFoldDB

No variants for P52844

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P52844

No associated diseases with P52844

1 regional properties for P52844

Type Name Position InterPro Accession
domain Sulfotransferase domain 38 - 287 IPR000863

Functions

Description
EC Number 2.8.2.4 Sulfotransferases
Subcellular Localization
  • Cytoplasm, cytosol
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.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.

6 GO annotations of molecular function

Name Definition
aryl sulfotransferase activity Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + a phenol = adenosine 3',5'-bisphosphate + an aryl sulfate.
estrone sulfotransferase activity Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + estrone = adenosine 3',5'-bisphosphate + estrone 3-sulfate.
flavonol 3-sulfotransferase activity Catalysis of the reaction: 3'-phospho-5'-adenylyl sulfate + quercetin = adenosine 3',5'-diphosphate + H(+) + quercetin 3-sulfate.
steroid binding Binding to a steroid, any of a large group of substances that have in common a ring system based on 1,2-cyclopentanoperhydrophenanthrene.
steroid sulfotransferase activity Catalysis of the reaction: 3'-phosphoadenosine 5'-phosphosulfate + a phenolic steroid = adenosine 3',5'-bisphosphate + steroid O-sulfate.
sulfotransferase activity Catalysis of the transfer of a sulfate group from 3'-phosphoadenosine 5'-phosphosulfate to the hydroxyl group of an acceptor, producing the sulfated derivative and 3'-phosphoadenosine 5'-phosphate.

7 GO annotations of biological process

Name Definition
3'-phosphoadenosine 5'-phosphosulfate metabolic process The chemical reactions and pathways involving 3'-phosphoadenosine 5'-phosphosulfate, a naturally occurring mixed anhydride. It is an intermediate in the formation of a variety of sulfo compounds in biological systems.
estrogen catabolic process The chemical reactions and pathways resulting in the breakdown of estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
estrogen metabolic process The chemical reactions and pathways involving estrogens, C18 steroid hormones that can stimulate the development of female sexual characteristics. Also found in plants.
ethanol catabolic process The chemical reactions and pathways resulting in the breakdown of ethanol, CH3-CH2-OH, a colorless, water-miscible, flammable liquid produced by alcoholic fermentation.
female pregnancy The set of physiological processes that allow an embryo or foetus to develop within the body of a female animal. It covers the time from fertilization of a female ovum by a male spermatozoon until birth.
positive regulation of fat cell differentiation Any process that activates or increases the frequency, rate or extent of adipocyte differentiation.
sulfation The addition of a sulfate group to a molecule.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
METSMPEYYE VFGDFHGFLM DKRFTKYWED IETFLARPDD LLIVTYPKSG STWISEIVDM
70 80 90 100 110 120
IYKEGDVEKC KEDALFNRIP DLECRNEDLI NGIKQLKEKE SPRIVKTHLP AKLLPASFWE
130 140 150 160 170 180
KNCKIIYLCR NAKDVVVSYY YFFLIMKSYP NPKSFSEFVE KFMEGQVPYG SWYDHVKSWW
190 200 210 220 230 240
EKSKNSRVLF MFYEDMKEDI RREVVKLIEF LERDPSAELV DRIIQHTSFQ EMKNNPCTNY
250 260 270 280 290
SMLPETMIDL KVSPFMRKGI VGDWRNHFPE ALRERFEEHY QRHMKDCPVK FRAEL