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 Q9ESK3

Entry ID Method Resolution Chain Position Source
AF-Q9ESK3-F1 Predicted AlphaFoldDB

40 variants for Q9ESK3

Variant ID(s) Position Change Description Diseaes Association Provenance
rs8276988 6 A>V No EVA
rs214830573 10 A>G No EVA
rs3388489836 50 C>Y No EVA
rs3388490654 84 K>N No EVA
rs3388488619 97 Q>H No EVA
rs3388489549 114 W>* No EVA
rs3388490764 134 R>* No EVA
rs3388489440 137 F>L No EVA
rs3388487830 201 S>N No EVA
rs3388488376 207 T>N No EVA
rs3388491112 212 L>V No EVA
rs3388489769 215 K>M No EVA
rs3388487835 220 I>F No EVA
rs3390297959 232 R>M No EVA
rs8277066 251 Q>R No EVA
rs3390249604 274 W>* No EVA
rs3388488641 299 G>E No EVA
rs3388488608 314 E>G No EVA
rs3388487824 334 R>G No EVA
rs3388487554 344 G>S No EVA
rs3388487855 347 V>E No EVA
rs3388491305 359 S>I No EVA
rs217054125 388 R>L No EVA
rs3388488167 395 A>T No EVA
rs3388489713 405 N>S No EVA
rs3388489502 462 A>V No EVA
rs3388491123 470 D>G No EVA
rs3388490822 474 Q>* No EVA
rs3388488073 480 F>Y No EVA
rs3388490723 504 P>H No EVA
rs3388490683 512 Q>* No EVA
rs3388488158 513 L>M No EVA
rs3388488440 529 F>Y No EVA
rs3388491227 534 C>S No EVA
rs3388490805 576 V>D No EVA
rs3388488810 582 N>I No EVA
rs30395437 585 A>E No EVA
rs8277025 601 R>C No EVA
rs864265735 627 D>V No EVA
rs3413086952 666 A>S No EVA

No associated diseases with Q9ESK3

8 regional properties for Q9ESK3

Type Name Position InterPro Accession
active_site Cysteine peptidase, cysteine active site 67 - 78 IPR000169
domain Peptidase C2, calpain, catalytic domain 2 - 329 IPR001300
domain Peptidase C2, calpain, large subunit, domain III 344 - 480 IPR022682-1
domain Peptidase C2, calpain, large subunit, domain III 514 - 636 IPR022682-2
domain Peptidase C2, calpain, domain III 338 - 488 IPR022683-1
domain Peptidase C2, calpain, domain III 507 - 645 IPR022683-2
domain Calpain subdomain III 337 - 490 IPR033883-1
domain Calpain subdomain III 506 - 647 IPR033883-2

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

12 GO annotations of cellular component

Name Definition
cell cortex The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoskeleton A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
intracellular membrane-bounded organelle Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane.
mitochondrial inner membrane The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae.
mitochondrial intermembrane space The region between the inner and outer lipid bilayers of the mitochondrial envelope.
mitochondrial matrix The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation.
mitochondrial outer membrane The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
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.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

3 GO annotations of molecular function

Name Definition
calcium-dependent cysteine-type endopeptidase activity Catalysis of the hydrolysis of nonterminal peptide bonds in a polypeptide chain by a mechanism using a cysteine residue at the enzyme active center, and requiring the presence of calcium.
cytoskeletal protein binding Binding to a protein component of a cytoskeleton (actin, microtubule, or intermediate filament cytoskeleton).
SNARE binding Binding to a SNARE (soluble N-ethylmaleimide-sensitive factor attached protein receptor) protein.

14 GO annotations of biological process

Name Definition
actin cytoskeleton reorganization A process that is carried out at the cellular level which results in dynamic structural changes to the arrangement of constituent parts of cytoskeletal structures comprising actin filaments and their associated proteins.
aging A developmental process that is a deterioration and loss of function over time. Aging includes loss of functions such as resistance to disease, homeostasis, and fertility, as well as wear and tear. Aging includes cellular senescence, but is more inclusive. May precede death and may succeed developmental maturation (GO:0021700).
autophagy of mitochondrion The autophagic process in which mitochondria are delivered to a type of vacuole and degraded in response to changing cellular conditions.
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.
mitochondrion organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a mitochondrion; includes mitochondrial morphogenesis and distribution, and replication of the mitochondrial genome as well as synthesis of new mitochondrial components.
positive regulation of apoptotic process Any process that activates or increases the frequency, rate or extent of cell death by apoptotic process.
positive regulation of glucose import Any process that activates or increases the frequency, rate or extent of the import of the hexose monosaccharide glucose into a cell or organelle.
positive regulation of insulin secretion Any process that activates or increases the frequency, rate or extent of the regulated release of insulin.
positive regulation of intracellular transport Any process that activates or increases the frequency, rate or extent of the directed movement of substances within cells.
positive regulation of type B pancreatic cell apoptotic process Any process that activates or increases the frequency, rate or extent of type B pancreatic cell apoptotic process.
protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
response to nutrient levels Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting the presence, absence, or concentration of nutrients.
type B pancreatic cell apoptotic process Any apoptotic process in a type B pancreatic cell, a cell located towards center of the islets of Langerhans that secretes insulin.

19 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q27970 CAPN1 Calpain-1 catalytic subunit Bos taurus (Bovine) PR
Q27971 CAPN2 Calpain-2 catalytic subunit Bos taurus (Bovine) PR
P00789 Calpain-1 catalytic subunit Gallus gallus (Chicken) PR
Q9VXH6 CalpC Calpain-C Drosophila melanogaster (Fruit fly) PR
O14815 CAPN9 Calpain-9 Homo sapiens (Human) PR
Q6MZZ7 CAPN13 Calpain-13 Homo sapiens (Human) PR
P07384 CAPN1 Calpain-1 catalytic subunit Homo sapiens (Human) PR
Q9HC96 CAPN10 Calpain-10 Homo sapiens (Human) PR
G3UZ78 Adgb Androglobin Mus musculus (Mouse) PR
O08529 Capn2 Calpain-2 catalytic subunit Mus musculus (Mouse) PR
O35350 Capn1 Calpain-1 catalytic subunit Mus musculus (Mouse) PR
Q3UW68 Capn13 Calpain-13 Mus musculus (Mouse) PR
Q9D805 Capn9 Calpain-9 Mus musculus (Mouse) PR
P35750 CAPN1 Calpain-1 catalytic subunit Sus scrofa (Pig) PR
P43367 CAPN2 Calpain-2 catalytic subunit Sus scrofa (Pig) PR
O35920 Capn9 Calpain-9 Rattus norvegicus (Rat) PR
P97571 Capn1 Calpain-1 catalytic subunit Rattus norvegicus (Rat) PR
Q5BK10 Capn13 Calpain-13 Rattus norvegicus (Rat) PR
Q07009 Capn2 Calpain-2 catalytic subunit Rattus norvegicus (Rat) PR
10 20 30 40 50 60
MRAVRAETPA RELFRDAAFP ASDSSLFYNL STPLAQFRED ITWRRPQEIC ATPQLFPDNP
70 80 90 100 110 120
WEGQVKQGLL GDCWFLCACA ALQKSQHLLD QVFPPGQPGW SDQKYQGFFT CRIWQFGHWE
130 140 150 160 170 180
EVTIDDRLPC LAGRLCFSRC QREDVFWLPL LEKAYAKVHG SYEHLWAGQV ADALVDLTGS
190 200 210 220 230 240
LAERWSLKDV TKASGQQDRP SGGEHRTCRQ LLHLKDRCLI SCSVLSPRAG ARELGEFHAF
250 260 270 280 290 300
IISDLQELRS QTGQGILLLR IHNPWGRRCW QGLWREGGEG WNQVEPAKES ELLAQLQEGE
310 320 330 340 350 360
FWVEEEEFLR EFDEVTIGYP VTEAGHLQSL HTERVLCHTR TLPGAWVTGQ SAGGCRNNSC
370 380 390 400 410 420
FPCNPKFWLR LLEPSEVCVA VLQRPRRRLV GQTRALAGAS PAPVNLPGKD YQAVGLHIWK
430 440 450 460 470 480
VEKRKISLPR VLSAPPVAGT ACHAYDREIH LRCELSPGYY LAVPSTFLKD VPGQFLLRVF
490 500 510 520 530 540
STGKISLSAV RLATKGASPG TALPAGEWET VQLQGCWRAG QTAGGSRNFA SYPCNPCLPF
550 560 570 580 590 600
SVPEGAGPRY IRITLQQHCR LSDSQLHPIG FHVFQVPADG ENQDACSLLL QEPLLSCVPH
610 620 630 640 650 660
RYAQEVSRLC LLSVGNYRIV PSTYLPDTEG TFTVTIATRI DRQSIHSQEM LGQLLQEVSF
MAVMKA