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 Q6PA06

Entry ID Method Resolution Chain Position Source
AF-Q6PA06-F1 Predicted AlphaFoldDB

23 variants for Q6PA06

Variant ID(s) Position Change Description Diseaes Association Provenance
rs266076387 7 A>V No EVA
rs3389494753 55 M>T No EVA
rs3389494814 65 L>F No EVA
rs3408079917 121 K>M No EVA
rs3389481840 138 T>* No EVA
rs3389460183 142 G>V No EVA
rs3389489674 153 W>* No EVA
rs3389448526 156 V>M No EVA
rs3389489696 161 R>* No EVA
rs3389475526 176 G>A No EVA
rs3389494809 178 F>S No EVA
rs3389440022 253 S>P No EVA
rs3389482972 256 L>V No EVA
rs3389429967 283 H>Y No EVA
rs3389494810 318 E>V No EVA
rs3389472310 333 A>V No EVA
rs3389448523 355 Y>* No EVA
rs3389482973 407 P>L No EVA
rs222962485 424 V>A No EVA
rs3389494811 437 G>R No EVA
rs3389448453 461 K>E No EVA
rs3389494760 479 F>L No EVA
rs3410685691 481 V>I No EVA

No associated diseases with Q6PA06

3 regional properties for Q6PA06

Type Name Position InterPro Accession
domain Protein kinase domain 77 - 327 IPR000719
active_site Serine/threonine-protein kinase, active site 196 - 208 IPR008271
binding_site Protein kinase, ATP binding site 83 - 106 IPR017441

Functions

Description
EC Number
Subcellular Localization
  • Endoplasmic reticulum membrane ; Multi-pass membrane protein
  • Localizes at endoplasmic reticulum (ER) three-way tubular junctions
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum tubular network membrane The membrane of the endoplasmic reticulum tubular network.
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.

3 GO annotations of molecular function

Name Definition
GTP binding Binding to GTP, guanosine triphosphate.
GTPase activity Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate.
identical protein binding Binding to an identical protein or proteins.

4 GO annotations of biological process

Name Definition
endoplasmic reticulum organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum.
endoplasmic reticulum tubular network membrane organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the endoplasmic reticulum (ER) tubular network membrane.
Golgi organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the Golgi apparatus.
protein homooligomerization The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9VC57 atl Atlastin Drosophila melanogaster (Fruit fly) PR
Q6ZN66 GBP6 Guanylate-binding protein 6 Homo sapiens (Human) PR
Q8NHH9 ATL2 Atlastin-2 Homo sapiens (Human) PR
10 20 30 40 50 60
MAEGDEAARR QQPQQGLRRR RQTSDSSVGV NHVSSTTSLG EDYEDDDLVN SDEVMKKPCP
70 80 90 100 110 120
VQIVLAHEDD HNFELDEEAL EQILLQEHIR DLNIVVVSVA GAFRKGKSFL LDFMLRYMYN
130 140 150 160 170 180
KDSQSWIGGN NEPLTGFTWR GGCERETTGI QVWNEVFVID RPNGTKVAVL LMDTQGAFDS
190 200 210 220 230 240
QSTIKDCATV FALSTMTSSV QVYNLSQNIQ EDDLQHLQLF TEYGRLAMEE IYQKPFQTLM
250 260 270 280 290 300
FLIRDWSYPY EHSYGLEGGK QFLEKRLQVK QNQHEELQNV RKHIHNCFSN LGCFLLPHPG
310 320 330 340 350 360
LKVATNPSFD GRLKDIDEDF KRELRNLVPL LLAPENLVEK EISGSKVTCR DLVEYFKAYI
370 380 390 400 410 420
KIYQGEELPH PKSMLQATAE ANNLAAVAGA RDVYCKSMEQ VCGGDKPYIA PSDLERKHLD
430 440 450 460 470 480
LKEVALKQFR SVKKMGGDEF CRRYQDQLEA EIEETYANFI KHNDGKNIFY AARTPATLFA
490 500 510 520 530 540
VMFAMYIISG LTGFIGLNSI AVLCNLVMGL ALTSLCTWAY VKYSGEFREI GTMIDQIAET
550 560 570 580
LWEQVLKPLG DNLMEENIRQ SVTNSIKAGL TDQVSHHARL KTD