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 Q8BZT2

Entry ID Method Resolution Chain Position Source
2CUC NMR - A 385-441 PDB
2DJQ NMR - A 128-182 PDB
AF-Q8BZT2-F1 Predicted AlphaFoldDB

49 variants for Q8BZT2

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389494563 2 D>E No EVA
rs3408101517 15 C>G No EVA
rs3407417914 16 F>L No EVA
rs3407417869 18 K>N No EVA
rs3389499259 18 K>R No EVA
rs247903170 21 V>A No EVA
rs3389447898 49 C>S No EVA
rs3389492520 51 E>D No EVA
rs3389447862 57 F>Y No EVA
rs3389466332 62 A>T No EVA
rs3389492506 86 G>A No EVA
rs224494940 120 V>I No EVA
rs3389514538 124 M>L No EVA
rs3408645502 125 D>E No EVA
rs3389500336 256 L>I No EVA
rs3389410564 257 L>P No EVA
rs3389503756 265 S>L No EVA
rs3389496388 267 T>I No EVA
rs3389494620 299 G>R No EVA
rs3408374916 351 S>C No EVA
rs3408557670 352 S>C No EVA
rs241026896 353 T>A No EVA
rs3408645468 353 T>R No EVA
rs3407418397 355 Q>L No EVA
rs3389514583 359 S>Y No EVA
rs3389457511 368 H>Q No EVA
rs259249556 372 M>L No EVA
rs3389514611 459 T>S No EVA
rs3389503806 461 C>S No EVA
rs3389494571 477 F>L No EVA
rs3389466329 479 E>D No EVA
rs244629030 483 R>Q No EVA
rs3389500310 496 A>T No EVA
rs3389496383 504 T>I No EVA
rs3389512224 518 V>M No EVA
rs3389492479 519 R>W No EVA
rs262772941 532 V>I No EVA
rs3408646869 539 F>S No EVA
rs3389466313 560 Y>N No EVA
rs3389512259 575 E>V No EVA
rs239931621 589 T>P No EVA
rs3389496385 604 N>D No EVA
rs3389496430 630 S>F No EVA
rs3389508532 632 L>F No EVA
rs3389499244 637 N>H No EVA
rs3389503750 641 G>D No EVA
rs3389514610 649 V>A No EVA
rs3389479139 666 P>A No EVA
rs3389501537 681 Q>H No EVA

No associated diseases with Q8BZT2

10 regional properties for Q8BZT2

Type Name Position InterPro Accession
repeat Armadillo 116 - 157 IPR000225-1
repeat Armadillo 159 - 203 IPR000225-2
repeat Armadillo 201 - 242 IPR000225-3
repeat Armadillo 245 - 284 IPR000225-4
repeat Armadillo 286 - 326 IPR000225-5
repeat Armadillo 328 - 368 IPR000225-6
repeat Armadillo 370 - 410 IPR000225-7
repeat Armadillo 413 - 453 IPR000225-8
domain Importin-alpha, importin-beta-binding domain 1 - 105 IPR002652
repeat Atypical Arm repeat 467 - 513 IPR032413

Functions

Description
EC Number 2.3.2.27 Aminoacyltransferases
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
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.

5 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
phosphatase binding Binding to a phosphatase.
protein phosphatase 1 binding Binding to a protein phosphatase 1.
protein phosphatase inhibitor activity Binds to and stops, prevents or reduces the activity of a protein phosphatase, an enzyme that hydrolyzes phosphate groups from phosphorylated 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.

8 GO annotations of biological process

Name Definition
negative regulation of apoptotic process Any process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process.
negative regulation of JNK cascade Any process that stops, prevents, or reduces the frequency, rate or extent of signal transduction mediated by the JNK cascade.
negative regulation of protein ubiquitination Any process that stops, prevents, or reduces the frequency, rate or extent of the addition of ubiquitin groups to a protein.
positive regulation of cell migration Any process that activates or increases the frequency, rate or extent of cell migration.
positive regulation of JNK cascade Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the JNK cascade.
positive regulation of proteasomal ubiquitin-dependent protein catabolic process Any process that activates or increases the frequency, rate or extent of 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 autoubiquitination The ubiquitination by a protein of one or more of its own amino acid residues, or residues on an identical protein. Ubiquitination occurs on the lysine residue by formation of an isopeptide crosslink.
protein ubiquitination The process in which one or more ubiquitin groups are added to a protein.

52 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
Q6ZMU5 TRIM72 Tripartite motif-containing protein 72 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
Q9WUH5 Trim10 Tripartite motif-containing protein 10 Mus musculus (Mouse) PR
Q7TPM3 Trim17 E3 ubiquitin-protein ligase TRIM17 Mus musculus (Mouse) PR
Q1XH17 Trim72 Tripartite motif-containing protein 72 Mus musculus (Mouse) PR
Q60953 Pml Protein PML Mus musculus (Mouse) PR
Q9JJ26 Mefv Pyrin Mus musculus (Mouse) SS
Q99PQ1 Trim12a Tripartite motif-containing protein 12A Mus musculus (Mouse) PR
Q61510 Trim25 E3 ubiquitin/ISG15 ligase TRIM25 Mus musculus (Mouse) PR
Q810I2 Trim50 E3 ubiquitin-protein ligase TRIM50 Mus musculus (Mouse) PR
Q1PSW8 Trim71 E3 ubiquitin-protein ligase TRIM71 Mus musculus (Mouse) PR
Q3TL54 Trim43a Tripartite motif-containing protein 43A Mus musculus (Mouse) PR
P86449 Trim43c Tripartite motif-containing protein 43C Mus musculus (Mouse) PR
Q9JK48 Sh3glb1 Endophilin-B1 Mus musculus (Mouse) PR
Q62420 Sh3gl2 Endophilin-A1 Mus musculus (Mouse) PR
Q62419 Sh3gl1 Endophilin-A2 Mus musculus (Mouse) PR
Q62421 Sh3gl3 Endophilin-A3 Mus musculus (Mouse) PR
Q9JLQ0 Cd2ap CD2-associated protein Mus musculus (Mouse) SS
Q8R550 Sh3kbp1 SH3 domain-containing kinase-binding protein 1 Mus musculus (Mouse) SS
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
A0JPQ4 Trim72 Tripartite motif-containing protein 72 Rattus norvegicus (Rat) PR
Q810I1 Trim50 E3 ubiquitin-protein ligase TRIM50 Rattus norvegicus (Rat) PR
D3ZVM4 Trim71 E3 ubiquitin-protein ligase TRIM71 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
MDDLTLLDLL ECPVCFEKLD VTAKVLPCQH TFCKPCLQRI FKAHKELRCP ECRTLVFCSI
70 80 90 100 110 120
EALPANLLLV RLLDGVRSGQ SSWKGGSFRR PRILTLQDNR KAKSSPRSLQ ASPFRLVPSV
130 140 150 160 170 180
RIHMDGVPRA KALCNYRGKN PGDLKFNKGD VILLRRQLDE NWYQGEINGV SGIFPASSVE
190 200 210 220 230 240
VIKQLPQPPP LCRALYNFDL RDKDKSENQD CLTFLKDDVI TVISRVDENW AEGKLGDKVG
250 260 270 280 290 300
IFPILFVEPN VSARHLLENK GHQLSRTRHL SLMSSPSRGK ATNTSSLRKS PGSRRKGSGQ
310 320 330 340 350 360
FSMTTALNTL NRTVHSPEGH QMVEISTPML ISSNSPSVLT QHGDKADFPT SSTGQVSSSQ
370 380 390 400 410 420
PAPASPGHST AMVSVPSSQQ HLSNNMFVAL HTYSAHRPEE LDLQKGEGIR VLGKYQDGWL
430 440 450 460 470 480
KGLSLLTGRT GIFPSDYVIP VFSSTARKTS SFPDSRSPTV CTTWALSTSS VSSQGSFAEG
490 500 510 520 530 540
DPRQSGPFKS VFVPTAVVNP SRSTPGPGSS GQGSLRKVRS SMRKNGSLQR PVQSGIPTFM
550 560 570 580 590 600
VGSLRCSPTM VIRPQRFQFY PPQGMTPSPT PIMVEMGSKS IYTGEPALTC INRGSKTRIH
610 620 630 640 650 660
SAGNSIIMEG KETPIKSEPP PKPPASAPPS ILVKPENSKN GTEKQVKTVR FQNYSPPPTK
670 680 690 700 710 720
HSASSPTSGK HDHPATLKGS QHEAVSSGGE MTILFAHRSG CHSGQQTDLR RKSAFGKTMP
730
LLSTASATQT LFPSK