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

7 structures for Q1XH17

Entry ID Method Resolution Chain Position Source
7XV2 X-ray 275 A A 79-470 PDB
7XYY X-ray 710 A A/B 2-477 PDB
7XYZ X-ray 462 A A/B/C/D 7-470 PDB
7XZ0 X-ray 328 A A/B 79-470 PDB
7XZ1 X-ray 520 A A/B 7-470 PDB
7XZ2 X-ray 350 A A/B/C/D 7-470 PDB
AF-Q1XH17-F1 Predicted AlphaFoldDB

23 variants for Q1XH17

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3388946493 33 F>L No EVA
rs3398617584 42 A>E No EVA
rs3388950329 102 T>I No EVA
rs3388931453 108 C>* No EVA
rs33182050 126 Q>H No EVA
rs3388931483 146 R>C No EVA
rs229541754 150 T>S No EVA
rs3398544563 156 H>P No EVA
rs3388931529 162 E>* No EVA
rs3388908254 212 L>Q No EVA
rs3388946533 215 Y>* No EVA
rs3388923927 230 A>T No EVA
rs3388950566 298 A>E No EVA
rs3398130882 378 Q>PL* No EVA
rs33189379 385 L>V No EVA
rs3388946525 399 E>K No EVA
rs3388950572 410 P>Q No EVA
rs3388958121 418 S>C No EVA
rs3388955968 418 S>N No EVA
rs3388940387 431 N>K No EVA
rs3388954643 436 T>M No EVA
rs3398535066 475 E>D No EVA
rs220771768 477 A>S No EVA

No associated diseases with Q1XH17

10 regional properties for Q1XH17

Type Name Position InterPro Accession
domain B-box-type zinc finger 81 - 122 IPR000315
domain Zinc finger, RING-type 14 - 57 IPR001841
domain B30.2/SPRY domain 271 - 475 IPR001870
domain SPRY domain 342 - 473 IPR003877
domain Butyrophylin-like, SPRY domain 287 - 304 IPR003879-1
domain Butyrophylin-like, SPRY domain 327 - 351 IPR003879-2
domain Butyrophylin-like, SPRY domain 357 - 370 IPR003879-3
domain Butyrophylin-like, SPRY domain 404 - 428 IPR003879-4
domain SPRY-associated 288 - 341 IPR006574
conserved_site Zinc finger, RING-type, conserved site 29 - 38 IPR017907

Functions

Description
EC Number
Subcellular Localization
  • Cell membrane, sarcolemma
  • Cytoplasmic vesicle membrane
  • Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine
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.
cytoplasmic vesicle membrane The lipid bilayer surrounding a cytoplasmic vesicle.
sarcolemma The outer membrane of a muscle cell, consisting of the plasma membrane, a covering basement membrane (about 100 nm thick and sometimes common to more than one fiber), and the associated loose network of collagen fibers.

5 GO annotations of molecular function

Name Definition
identical protein binding Binding to an identical protein or proteins.
phosphatidylserine binding Binding to phosphatidylserine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of L-serine.
ubiquitin conjugating enzyme binding Binding to a ubiquitin conjugating enzyme, any of the E2 proteins.
ubiquitin protein ligase activity Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S -> X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond: an isopeptide bond between the C-terminal glycine of ubiquitin and the epsilon-amino group of lysine residues in the substrate or, in the linear extension of ubiquitin chains, a peptide bond the between the C-terminal glycine and N-terminal methionine of ubiquitin residues.
zinc ion binding Binding to a zinc ion (Zn).

11 GO annotations of biological process

Name Definition
exocytosis A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell.
muscle organ development The process whose specific outcome is the progression of the muscle over time, from its formation to the mature structure. The muscle is an organ consisting of a tissue made up of various elongated cells that are specialized to contract and thus to produce movement and mechanical work.
muscle system process A organ system process carried out at the level of a muscle. Muscle tissue is composed of contractile cells or fibers.
negative regulation of insulin receptor signaling pathway Any process that stops, prevents, or reduces the frequency, rate or extent of insulin receptor signaling.
negative regulation of insulin-like growth factor receptor signaling pathway Any process that stops, prevents, or reduces the frequency, rate or extent of insulin-like growth factor receptor signaling.
negative regulation of myotube differentiation Any process that decreases the frequency, rate or extent of myotube differentiation. Myotube differentiation is the process in which a relatively unspecialized cell acquires specialized features of a myotube cell. Myotubes are multinucleated cells that are formed when proliferating myoblasts exit the cell cycle, differentiate and fuse.
plasma membrane repair The resealing of a cell plasma membrane after cellular wounding due to, for instance, mechanical stress.
proteasome-mediated ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, and mediated by the proteasome.
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.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.
vesicle budding from membrane The evagination of a membrane, resulting in formation of a vesicle.

46 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q5E9G4 TRIM10 Tripartite motif-containing protein 10 Bos taurus (Bovine) PR
Q2T9Z0 TRIM17 E3 ubiquitin-protein ligase TRIM17 Bos taurus (Bovine) PR
E1BJS7 TRIM71 E3 ubiquitin-protein ligase TRIM71 Bos taurus (Bovine) PR
Q7YRV4 TRIM21 E3 ubiquitin-protein ligase TRIM21 Bos taurus (Bovine) PR
Q1PRL4 TRIM71 E3 ubiquitin-protein ligase TRIM71 Gallus gallus (Chicken) PR
Q7YR32 TRIM10 Tripartite motif-containing protein 10 Pan troglodytes (Chimpanzee) PR
O15553 MEFV Pyrin Homo sapiens (Human) SS
Q9BTV5 FSD1 Fibronectin type III and SPRY domain-containing protein 1 Homo sapiens (Human) PR
Q9H2S5 RNF39 RING finger protein 39 Homo sapiens (Human) PR
P19474 TRIM21 E3 ubiquitin-protein ligase TRIM21 Homo sapiens (Human) PR
Q9UJV3 MID2 Probable E3 ubiquitin-protein ligase MID2 Homo sapiens (Human) PR
P29590 PML Protein PML Homo sapiens (Human) PR
Q9C029 TRIM7 E3 ubiquitin-protein ligase TRIM7 Homo sapiens (Human) PR
Q9NQ86 TRIM36 E3 ubiquitin-protein ligase TRIM36 Homo sapiens (Human) PR
Q86UV6 TRIM74 Tripartite motif-containing protein 74 Homo sapiens (Human) PR
Q9UPQ4 TRIM35 E3 ubiquitin-protein ligase TRIM35 Homo sapiens (Human) PR
Q86UV7 TRIM73 Tripartite motif-containing protein 73 Homo sapiens (Human) PR
Q8N9V2 TRIML1 Probable E3 ubiquitin-protein ligase TRIML1 Homo sapiens (Human) PR
Q86XT4 TRIM50 E3 ubiquitin-protein ligase TRIM50 Homo sapiens (Human) PR
Q5EBN2 TRIM61 Putative tripartite motif-containing protein 61 Homo sapiens (Human) PR
Q9BZY9 TRIM31 E3 ubiquitin-protein ligase TRIM31 Homo sapiens (Human) PR
Q2Q1W2 TRIM71 E3 ubiquitin-protein ligase TRIM71 Homo sapiens (Human) PR
Q9BXM9 FSD1L FSD1-like protein Homo sapiens (Human) PR
Q6ZMU5 TRIM72 Tripartite motif-containing protein 72 Homo sapiens (Human) PR
Q8BZT2 Sh3rf2 E3 ubiquitin-protein ligase SH3RF2 Mus musculus (Mouse) PR
Q60953 Pml Protein PML Mus musculus (Mouse) PR
Q99PQ1 Trim12a Tripartite motif-containing protein 12A Mus musculus (Mouse) PR
Q61510 Trim25 E3 ubiquitin/ISG15 ligase TRIM25 Mus musculus (Mouse) PR
Q1PSW8 Trim71 E3 ubiquitin-protein ligase TRIM71 Mus musculus (Mouse) PR
P86449 Trim43c Tripartite motif-containing protein 43C Mus musculus (Mouse) PR
Q3TL54 Trim43a Tripartite motif-containing protein 43A Mus musculus (Mouse) PR
Q7TPM3 Trim17 E3 ubiquitin-protein ligase TRIM17 Mus musculus (Mouse) PR
Q810I2 Trim50 E3 ubiquitin-protein ligase TRIM50 Mus musculus (Mouse) PR
Q9JJ26 Mefv Pyrin Mus musculus (Mouse) SS
Q9WUH5 Trim10 Tripartite motif-containing protein 10 Mus musculus (Mouse) PR
O77666 TRIM26 Tripartite motif-containing protein 26 Sus scrofa (Pig) PR
O19085 TRIM10 Tripartite motif-containing protein 10 Sus scrofa (Pig) PR
Q865W2 TRIM50 E3 ubiquitin-protein ligase TRIM50 Sus scrofa (Pig) PR
Q920M2 Rnf39 RING finger protein 39 Rattus norvegicus (Rat) PR
Q9JJ25 Mefv Pyrin Rattus norvegicus (Rat) SS
Q810I1 Trim50 E3 ubiquitin-protein ligase TRIM50 Rattus norvegicus (Rat) PR
D3ZVM4 Trim71 E3 ubiquitin-protein ligase TRIM71 Rattus norvegicus (Rat) PR
A0JPQ4 Trim72 Tripartite motif-containing protein 72 Rattus norvegicus (Rat) PR
F6QEU4 trim71 E3 ubiquitin-protein ligase TRIM71 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
Q640S6 trim72 Tripartite motif-containing protein 72 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) PR
E7FAM5 trim71 E3 ubiquitin-protein ligase TRIM71 Danio rerio (Zebrafish) (Brachydanio rerio) PR
10 20 30 40 50 60
MSAAPGLLRQ ELSCPLCLQL FDAPVTAECG HSFCRACLIR VAGEPAADGT VACPCCQAPT
70 80 90 100 110 120
RPQALSTNLQ LSRLVEGLAQ VPQGHCEEHL DPLSIYCEQD RTLVCGVCAS LGSHRGHRLL
130 140 150 160 170 180
PAAEAQARLK TQLPQQKMQL QEACMRKEKT VAVLEHQLVE VEETVRQFRG AVGEQLGKMR
190 200 210 220 230 240
MFLAALESSL DREAERVRGD AGVALRRELS SLNSYLEQLR QMEKVLEEVA DKPQTEFLMK
250 260 270 280 290 300
FCLVTSRLQK ILSESPPPAR LDIQLPVISD DFKFQVWKKM FRALMPALEE LTFDPSSAHP
310 320 330 340 350 360
SLVVSSSGRR VECSDQKAPP AGEDTRQFDK AVAVVAQQLL SQGEHYWEVE VGDKPRWALG
370 380 390 400 410 420
VMAADASRRG RLHAVPSQGL WLLGLRDGKI LEAHVEAKEP RALRTPERPP ARIGLYLSFA
430 440 450 460 470
DGVLAFYDAS NPDVLTPIFS FHERLPGPVY PIFDVCWHDK GKNAQPLLLV GPEQEQA