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

2 structures for Q99PI5

Entry ID Method Resolution Chain Position Source
7KIQ X-ray 252 A A/B/C/D/E/F/G/H/I/J 459-549 PDB
AF-Q99PI5-F1 Predicted AlphaFoldDB

57 variants for Q99PI5

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389478815 4 V>M No EVA
rs3389489609 14 T>A No EVA
rs3389479377 24 Q>H No EVA
rs3389470102 29 G>A No EVA
rs864263291 39 Q>L No EVA
rs3389481394 49 H>L No EVA
rs3389437613 69 I>N No EVA
rs3389478810 73 A>T No EVA
rs3389446864 79 K>R No EVA
rs3389478802 87 F>L No EVA
rs107726727 125 S>P No EVA
rs3389494225 154 K>R No EVA
rs3408011749 164 Q>* No EVA
rs3389446855 172 A>G No EVA
rs3389472894 179 D>Y No EVA
rs3407926542 205 K>N No EVA
rs864273097 245 S>F No EVA
rs3389470024 249 V>M No EVA
rs3389478826 265 T>M No EVA
rs3389472848 266 W>* No EVA
rs3389485021 278 R>K No EVA
rs3389472851 291 T>A No EVA
rs233411544 321 T>S No EVA
rs3389481431 354 I>V No EVA
rs220121637 375 K>R No EVA
rs3389446843 387 G>S No EVA
rs3389446819 416 Y>D No EVA
rs3407880668 439 Q>H No EVA
rs3389494292 451 S>N No EVA
rs3389470061 499 P>H No EVA
rs3408093559 507 L>SKI* No EVA
rs3389427969 508 V>L No EVA
rs3389457314 539 T>I No EVA
rs3389446831 555 W>* No EVA
rs3389494265 570 E>K No EVA
rs3389478411 591 P>R No EVA
rs263009407 592 T>S No EVA
rs3389479454 595 R>I No EVA
rs3389457373 630 A>T No EVA
rs3389472537 658 S>N No EVA
rs250094278 677 N>D No EVA
rs212288053 679 N>S No EVA
rs3389478828 701 L>F No EVA
rs3389489630 714 A>T No EVA
rs3389481464 732 A>T No EVA
rs3389494252 742 R>P No EVA
rs3389472598 743 G>D No EVA
rs3389470090 764 P>L No EVA
rs3389472538 772 H>Q No EVA
rs3389470071 789 N>I No EVA
rs108530074 799 R>K No EVA
rs3408277529 814 Y>* No EVA
rs3407945254 816 Y>S No EVA
rs3407945301 817 T>S No EVA
rs3408011736 820 G>E No EVA
rs3389446850 844 K>R No EVA
rs3389481472 882 D>Y No EVA

No associated diseases with Q99PI5

4 regional properties for Q99PI5

Type Name Position InterPro Accession
domain Lipin, N-terminal 1 - 107 IPR007651
domain Lipin/Ned1/Smp2 (LNS2) 634 - 859 IPR013209
domain LNS2/PITP 682 - 838 IPR031315
domain Lipin, middle domain 466 - 558 IPR031703

Functions

Description
EC Number 3.1.3.4 Phosphoric monoester hydrolases
Subcellular Localization
  • Nucleus
  • Cytoplasm, cytosol
  • Endoplasmic reticulum membrane
  • Translocates from cytosol to endoplasmic reticulum membrane with increasing levels of oleate
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
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.

2 GO annotations of molecular function

Name Definition
phosphatidate phosphatase activity Catalysis of the reaction: a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.
transcription coactivator activity A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator.

6 GO annotations of biological process

Name Definition
cellular lipid metabolic process The chemical reactions and pathways involving lipids, as carried out by individual cells.
cellular response to insulin stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms.
fatty acid catabolic process The chemical reactions and pathways resulting in the breakdown of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes.
lipid metabolic process The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids.
positive regulation of transcription by RNA polymerase II Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter.
triglyceride biosynthetic process The chemical reactions and pathways resulting in the formation of a triglyceride, any triester of glycerol.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9BQK8 LPIN3 Phosphatidate phosphatase LPIN3 Homo sapiens (Human) PR
Q14693 LPIN1 Phosphatidate phosphatase LPIN1 Homo sapiens (Human) PR
Q92539 LPIN2 Phosphatidate phosphatase LPIN2 Homo sapiens (Human) PR
Q91ZP3 Lpin1 Phosphatidate phosphatase LPIN1 Mus musculus (Mouse) PR
Q9FMN2 PAH2 Phosphatidate phosphatase PAH2 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MNYVGQLAGQ VLVTVKELYK GINQATLSGC IDVVVVRQQD GSYQCSPFHV RFGKLGVLRS
70 80 90 100 110 120
KEKVIDIEIN GSAVDLHMKL GDNGEAFFVE ETEEEYEKLP AYLATSPIPT EDQFFKHIET
130 140 150 160 170 180
PLVKSSGNER PAQSSDVSHT LESEAVFTQS SVKKKKRRRK KCKQDNRKEE QAASPVAEDV
190 200 210 220 230 240
GDVGVSSDDE KRAQAARGSS NASLKEEDYK EPSLFHSGDN YPLSDGDWSP LETTYPQAVC
250 260 270 280 290 300
PKSDSELEVK PSESLLRSEP HMEWTWGGFP ESTKVTKRER YDYHPRTATI TPSENTHFRV
310 320 330 340 350 360
IPSEDSLIRE VEKDATVEDT TCTIVKPKPR ALCKQLSDAA STELPESPLE APQISSLLDA
370 380 390 400 410 420
DPVPSPSAEA PSEPKPAAKD SPTKKKGVHK RSQHQGPDDI YLDDLKALEP EVAALYFPKS
430 440 450 460 470 480
DTDPGSRQWP ESDTFSGSQS PQSVGSAAAD SGTECLSDSA MDLPDVTLSL CGGLSENGEI
490 500 510 520 530 540
SKEKFMEHII TYHEFAENPG LIDNPNLVIR IYNRYYNWAL AAPMILSLQV FQKSLPKATV
550 560 570 580 590 600
ESWVKDKMPK KSGRWWFWRK KESMIKQLPE TKEGKSEVPP ANDLPSNAEE PTSARPAEND
610 620 630 640 650 660
TSSDEGSQEL EESIKVDPIT VETLSHCGTA SYKKSLRLSS DQIAKLKLHD GPNDVVFSIT
670 680 690 700 710 720
TQYQGTCRCA GTIYLWNWND KVIISDIDGT ITKSDALGQI LPQLGKDWTH QGIARLYHSI
730 740 750 760 770 780
NENGYKFLYC SARAIGMADM TRGYLHWVND KGTILPRGPL MLSPSSLFSA FHREVIEKKP
790 800 810 820 830 840
EKFKIECLND IKNLFAPSRQ PFYAAFGNRP NDVYAYTQVG VPDCRIFTVN PKGELIQERT
850 860 870 880 890
KGNKSSYHRL SELVEHVFPL LSKEQNSAFP CPEFSSFCYW RDPIPDLDLD DLA