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

3 structures for Q9SKR2

Entry ID Method Resolution Chain Position Source
7AS6 X-ray 200 A A 253-397 PDB
7ATP X-ray 210 A A 253-397 PDB
AF-Q9SKR2-F1 Predicted AlphaFoldDB

22 variants for Q9SKR2

Variant ID(s) Position Change Description Diseaes Association Provenance
tmp_2_9014887_C_T 21 L>F No 1000Genomes
tmp_2_9015239_G_A 48 D>N No 1000Genomes
ENSVATH00240906 84 Y>F No 1000Genomes
ENSVATH14526711 125 P>L No 1000Genomes
tmp_2_9016696_G_T 246 V>F No 1000Genomes
tmp_2_9016867_A_C 274 K>Q No 1000Genomes
ENSVATH05545125 278 M>I No 1000Genomes
ENSVATH13307605 337 G>V No 1000Genomes
ENSVATH05545126 338 N>S No 1000Genomes
ENSVATH00240910 339 P>A No 1000Genomes
ENSVATH00240911 357 H>Q Plants were checked bi-weekly for presence of first buds and the average flowering time of 4 plants of the same accession were collected [16c and 16 hrs daylight] Plants were checked bi-weekly for presence of first buds and the average flowering time of 4 plants of the same accession were collected [22c and 16 hrs daylight] [EnsemblGenome] No 1000Genomes
ENSVATH13307606 357 H>Y No 1000Genomes
ENSVATH13307607 363 E>A No 1000Genomes
ENSVATH13307608 370 G>S No 1000Genomes
ENSVATH05545129 371 G>D No 1000Genomes
ENSVATH05545130 387 E>A No 1000Genomes
tmp_2_9017304_G_C 395 E>D No 1000Genomes
tmp_2_9017371_G_T 418 A>S No 1000Genomes
tmp_2_9017486_T_A 456 V>E No 1000Genomes
tmp_2_9017552_G_A 478 R>H No 1000Genomes
tmp_2_9017565_C_A 482 H>Q No 1000Genomes
tmp_2_9017581_A_T 488 T>S No 1000Genomes

No associated diseases with Q9SKR2

25 regional properties for Q9SKR2

Type Name Position InterPro Accession
domain F-box domain 1 - 50 IPR001810
repeat Parallel beta-helix repeat 198 - 217 IPR006626-1
repeat Parallel beta-helix repeat 238 - 260 IPR006626-2
repeat Parallel beta-helix repeat 427 - 448 IPR006626-3
repeat Parallel beta-helix repeat 449 - 470 IPR006626-4
repeat Parallel beta-helix repeat 471 - 493 IPR006626-5
repeat Parallel beta-helix repeat 494 - 516 IPR006626-6
repeat Parallel beta-helix repeat 517 - 539 IPR006626-7
repeat Parallel beta-helix repeat 540 - 562 IPR006626-8
repeat Parallel beta-helix repeat 563 - 585 IPR006626-9
repeat Parallel beta-helix repeat 586 - 608 IPR006626-10
repeat Parallel beta-helix repeat 609 - 631 IPR006626-11
repeat Parallel beta-helix repeat 632 - 654 IPR006626-12
repeat Parallel beta-helix repeat 655 - 677 IPR006626-13
repeat Parallel beta-helix repeat 719 - 741 IPR006626-14
repeat Parallel beta-helix repeat 742 - 764 IPR006626-15
repeat Parallel beta-helix repeat 766 - 788 IPR006626-16
repeat Parallel beta-helix repeat 789 - 811 IPR006626-17
repeat Parallel beta-helix repeat 834 - 856 IPR006626-18
domain Carbohydrate-binding/sugar hydrolysis domain 341 - 515 IPR006633-1
domain Carbohydrate-binding/sugar hydrolysis domain 540 - 676 IPR006633-2
domain Carbohydrate-binding/sugar hydrolysis domain 685 - 810 IPR006633-3
domain Periplasmic copper-binding protein NosD, beta helix domain 724 - 870 IPR007742
repeat Parallel beta-helix repeat-2 534 - 573 IPR022441
domain Right handed beta helix domain 425 - 572 IPR039448

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane; Single-pass membrane protein ; Cytoplasmic side
  • Endosome membrane; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 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).
endosome membrane The lipid bilayer surrounding an endosome.
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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

2 GO annotations of molecular function

Name Definition
lipid binding Binding to a lipid.
metal ion binding Binding to a metal ion.

2 GO annotations of biological process

Name Definition
endocytosis A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
lipid transport The directed movement of lipids into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. Lipids are compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9BSJ8 ESYT1 Extended synaptotagmin-1 Homo sapiens (Human) PR
Q3TZZ7 Esyt2 Extended synaptotagmin-2 Mus musculus (Mouse) PR
Q3U7R1 Esyt1 Extended synaptotagmin-1 Mus musculus (Mouse) PR
A0JJX5 SYT4 Synaptotagmin-4 Arabidopsis thaliana (Mouse-ear cress) PR
B6ETT4 SYT2 Synaptotagmin-2 Arabidopsis thaliana (Mouse-ear cress) PR
Q7XA06 SYT3 Synaptotagmin-3 Arabidopsis thaliana (Mouse-ear cress) PR
Q5M7N9 esyt3 Extended synaptotagmin-3 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
10 20 30 40 50 60
MGFFSTILGF CGFGVGISLG LVIGYVLFVY LLPNDVKDPE IRSIADQDPK AMLRMLPEIP
70 80 90 100 110 120
LWVKNPDFDR VDWINRFLEY MWPYLDKAIC KTAKNIAKPI IEEQIPKYKI DSVEFETLTL
130 140 150 160 170 180
GSLPPTFQGM KVYLTDEKEL IMEPCLKWAA NPNILVAIKA FGLKATVQVV DLQVFAQPRI
190 200 210 220 230 240
TLKPLVPSFP CFANIYVSLM EKPHVDFGLK LGGADLMSIP GLYRFVQEQI KDQVANMYLW
250 260 270 280 290 300
PKTLVVPILD PAKAFRRPVG IVHVKVVRAV GLRKKDLMGG ADPFVKIKLS EDKIPSKKTT
310 320 330 340 350 360
VKHKNLNPEW NEEFKFSVRD PQTQVLEFSV YDWEQVGNPE KMGMNVLALK EMVPDEHKAF
370 380 390 400 410 420
TLELRKTLDG GEDGQPPDKY RGKLEVELLY KPFTEEEMPK GFEETQAVQK APEGTPAAGG
430 440 450 460 470 480
MLVVIVHSAE DVEGKHHTNP YVRIYFKGEE RKTKHVKKNR DPRWNEEFTF MLEEPPVREK
490 500 510 520 530 540
LHVEVLSTSS RIGLLHPKET LGYVDIPVVD VVNNKRMNQK FHLIDSKNGK IQIELEWRTA
S