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 P24521

Entry ID Method Resolution Chain Position Source
AF-P24521-F1 Predicted AlphaFoldDB

21 variants for P24521

Variant ID(s) Position Change Description Diseaes Association Provenance
s13-712384 24 T>P No SGRP
s13-712460 49 G>E No SGRP
s13-712538 75 S>T No SGRP
s13-712618 102 K>E No SGRP
s13-712632 106 D>E No SGRP
s13-712635 107 D>E No SGRP
s13-712646 111 R>T No SGRP
s13-712717 135 R>C No SGRP
s13-712888 192 A>S No SGRP
s13-713011 233 I>V No SGRP
s13-713023 237 T>S No SGRP
s13-713044 244 H>Y No SGRP
s13-713053 247 D>N No SGRP
s13-713062 250 D>N No SGRP
s13-713101 263 G>R No SGRP
s13-713467 385 Q>E No SGRP
s13-713536 408 T>A No SGRP
s13-713561 416 A>D No SGRP
s13-713572 420 N>D No SGRP
s13-713636 441 K>R No SGRP
s13-713659 449 L>F No SGRP

No associated diseases with P24521

3 regional properties for P24521

Type Name Position InterPro Accession
conserved_site GHMP kinase, ATP-binding, conserved site 150 - 160 IPR006203
domain GHMP kinase N-terminal domain 149 - 216 IPR006204
domain GHMP kinase, C-terminal domain 360 - 412 IPR013750

Functions

Description
EC Number 2.7.4.2 Phosphotransferases with a phosphate group as acceptor
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
phosphomevalonate kinase activity Catalysis of the reaction: (R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate + ADP + H(+).

4 GO annotations of biological process

Name Definition
ergosterol biosynthetic process The chemical reactions and pathways resulting in the formation of ergosterol, (22E)-ergosta-5,7,22-trien-3-beta-ol, a sterol found in ergot, yeast and moulds.
farnesyl diphosphate biosynthetic process, mevalonate pathway The pathway that converts acetate, in the form of acetyl-CoA, to farnesyl diphosphate (FPP) through a series of mevalonate intermediates. Farnesyl diphosphate is an important substrate for other essential pathways, such as biosynthesis of sterols.
isopentenyl diphosphate biosynthetic process, mevalonate pathway The chemical reactions and pathways resulting in the formation of isopentenyl diphosphate, via the intermediate mevalonate. This pathway converts acetate, in the form of acetyl-CoA, to isopentenyl diphosphate (IPP), the fundamental unit in isoprenoid biosynthesis, through a series of mevalonate intermediates.
organic acid phosphorylation The process of introducing one or more phosphate groups into an organic acid.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSELRAFSAP GKALLAGGYL VLDTKYEAFV VGLSARMHAV AHPYGSLQGS DKFEVRVKSK
70 80 90 100 110 120
QFKDGEWLYH ISPKSGFIPV SIGGSKNPFI EKVIANVFSY FKPNMDDYCN RNLFVIDIFS
130 140 150 160 170 180
DDAYHSQEDS VTEHRGNRRL SFHSHRIEEV PKTGLGSSAG LVTVLTTALA SFFVSDLENN
190 200 210 220 230 240
VDKYREVIHN LAQVAHCQAQ GKIGSGFDVA AAAYGSIRYR RFPPALISNL PDIGSATYGS
250 260 270 280 290 300
KLAHLVDEED WNITIKSNHL PSGLTLWMGD IKNGSETVKL VQKVKNWYDS HMPESLKIYT
310 320 330 340 350 360
ELDHANSRFM DGLSKLDRLH ETHDDYSDQI FESLERNDCT CQKYPEITEV RDAVATIRRS
370 380 390 400 410 420
FRKITKESGA DIEPPVQTSL LDDCQTLKGV LTCLIPGAGG YDAIAVITKQ DVDLRAQTAN
430 440 450
DKRFSKVQWL DVTQADWGVR KEKDPETYLD K