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 P82343

Entry ID Method Resolution Chain Position Source
AF-P82343-F1 Predicted AlphaFoldDB

24 variants for P82343

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389520865 69 Y>N No EVA
rs3389557063 71 S>N No EVA
rs29037794 89 E>A No EVA
rs3389565038 96 R>P No EVA
rs3389576579 101 G>D No EVA
rs3389576505 107 V>M No EVA
rs3389574826 137 V>A No EVA
rs230068560 141 V>M No EVA
rs3389579787 144 Q>K No EVA
rs13464455 148 I>M No EVA
rs3389532844 153 Q>* No EVA
rs3411044176 187 S>R No EVA
rs3410567003 192 L>H No EVA
rs262190641 202 M>K No EVA
rs3389557808 244 Q>H No EVA
rs3389560655 265 D>E No EVA
rs3410791322 269 R>V No EVA
rs3408352691 275 K>TFPEGILEQKPASFQCVA* No EVA
rs3411044132 361 Y>H No EVA
rs3412729484 363 N>I No EVA
rs3410826470 363 N>Y No EVA
rs3389520895 390 C>R No EVA
rs3389564136 391 E>K No EVA
rs240952421 404 A>V No EVA

No associated diseases with P82343

4 regional properties for P82343

Type Name Position InterPro Accession
domain RIO kinase 66 - 289 IPR000687
domain RIO2 kinase winged helix domain, N-terminal 9 - 91 IPR015285
conserved_site RIO kinase, conserved site 224 - 235 IPR018935
domain Serine/threonine-protein kinase Rio2 94 - 276 IPR030484

Functions

Description
EC Number 5.1.3.8 Acting on carbohydrates and derivatives
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
enzyme inhibitor activity Binds to and stops, prevents or reduces the activity of an enzyme.
identical protein binding Binding to an identical protein or proteins.
N-acylglucosamine 2-epimerase activity Catalysis of the reaction: N-acyl-D-glucosamine = N-acyl-D-mannosamine.
peptidase inhibitor activity Binds to and stops, prevents or reduces the activity of a peptidase, any enzyme that catalyzes the hydrolysis peptide bonds.
purine nucleotide binding Binding to a purine nucleotide, a compound consisting of a purine nucleoside esterified with (ortho)phosphate.

6 GO annotations of biological process

Name Definition
carbohydrate metabolic process The chemical reactions and pathways involving carbohydrates, any of a group of organic compounds based of the general formula Cx(H2O)y.
N-acetylglucosamine metabolic process The chemical reactions and pathways involving N-acetylglucosamine. The D isomer is a common structural unit of glycoproteins in plants, bacteria and animals; it is often the terminal sugar of an oligosaccharide group of a glycoprotein.
N-acetylmannosamine metabolic process The chemical reactions and pathways involving N-acetylmannosamine, the acetylated derivative of mannosamine, 2-amino-2-deoxymannose.
N-acetylneuraminate catabolic process The chemical reactions and pathways resulting in the breakdown of N-acetylneuraminate, the anion of 5-(acetylamino)-3,5-dideoxy-D-glycero-D-galacto-non-3-ulosonic acid.
negative regulation of catalytic activity Any process that stops or reduces the activity of an enzyme.
negative regulation of endopeptidase activity Any process that decreases the frequency, rate or extent of endopeptidase activity, the endohydrolysis of peptide bonds within proteins.

1 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q2KIS1 RENBP N-acylglucosamine 2-epimerase Bos taurus (Bovine) PR
10 20 30 40 50 60
MEKERETLQV WKKRVEQELD RVIAFWMEHS HDQEHGGFFT CLGRDGKVYD HLKYVWLQGR
70 80 90 100 110 120
QVWMYCRLYR SFERFRRVEL LDAARAGGEF LLRYARVAPP GKKCAFVLTR DGRPVKVQRT
130 140 150 160 170 180
IFSECFYTMA MNELWKVTGE VRYQSEAIEM MDQIIHWVRE DPAGLGRPQL SGALATEPMA
190 200 210 220 230 240
VPMMLLSLVE QLGEEDEELT NMYAELGDWC VHRILQHVQR DGQVVLENVS EDGKELPGCL
250 260 270 280 290 300
GRHQNPGHTL EAGWFLLQYA LRKGDPKLRM HIIDKFLLLP FHSGWDPEHG GLFYFQDADG
310 320 330 340 350 360
LCPTQLEWNM KLWWPHSEAM IAFLMGYSDS GDPALLHLFY KVAEYTFRQF RDPEYGEWFG
370 380 390 400 410
YLNQEGKVAL TIKGGPFKGC FHVPRCLAMC EQILGALLQR LEPAPLDSSP AVSTHEGSK