F6V6I0

PR
Gene name
usp13
Protein name
Ubiquitin carboxyl-terminal hydrolase 13
Names
Deubiquitinating enzyme 13, Ubiquitin thioesterase 13, Ubiquitin-specific-processing protease 13
Species
Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
KEGG Pathway
EC number
3.4.19.12: Omega peptidases
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

50-122 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for F6V6I0

Entry ID Method Resolution Chain Position Source
AF-F6V6I0-F1 Predicted AlphaFoldDB

No variants for F6V6I0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for F6V6I0

No associated diseases with F6V6I0

3 regional properties for F6V6I0

Type Name Position InterPro Accession
domain Protein kinase domain 72 - 346 IPR000719
binding_site Protein kinase, ATP binding site 78 - 101 IPR017441
domain Serine/threonine-protein kinase OSR1/WNK, CCT domain 460 - 517 IPR024678

Functions

Description
EC Number 3.4.19.12 Omega peptidases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

4 GO annotations of molecular function

Name Definition
cysteine-type deubiquitinase activity An thiol-dependent isopeptidase activity that cleaves ubiquitin from a target protein to which it is conjugated.
cysteine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile.
ubiquitin binding Binding to ubiquitin, a protein that when covalently bound to other cellular proteins marks them for proteolytic degradation.
zinc ion binding Binding to a zinc ion (Zn).

7 GO annotations of biological process

Name Definition
autophagy The cellular catabolic process in which cells digest parts of their own cytoplasm; allows for both recycling of macromolecular constituents under conditions of cellular stress and remodeling the intracellular structure for cell differentiation.
cell population proliferation The multiplication or reproduction of cells, resulting in the expansion of a cell population.
protein K63-linked deubiquitination A protein deubiquitination process in which a K63-linked ubiquitin chain, i.e. a polymer of ubiquitin formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is removed from a protein.
protein stabilization Any process involved in maintaining the structure and integrity of a protein and preventing it from degradation or aggregation.
regulation of autophagy Any process that modulates the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm.
regulation of DNA-templated transcription Any process that modulates the frequency, rate or extent of cellular DNA-templated transcription.
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 a ubiquitin group, or multiple ubiquitin groups, to the protein.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P45974 USP5 Ubiquitin carboxyl-terminal hydrolase 5 Homo sapiens (Human) PR
Q92995 USP13 Ubiquitin carboxyl-terminal hydrolase 13 Homo sapiens (Human) PR
P56399 Usp5 Ubiquitin carboxyl-terminal hydrolase 5 Mus musculus (Mouse) PR
10 20 30 40 50 60
MAEDLGELLV PYMPTIRVPK SGDRVYKTEC AFSYDSPESD GGLYVCMSTF LGFGREHVER
70 80 90 100 110 120
HYRKTGQSVY MHLKRHIRLK ATGASGGAFP KRINGRLFLD LENNTEMNTE DYEYEDEAKL
130 140 150 160 170 180
VIFPDHFEIA LPNIEELPAL VTIACDAVLN SKSPYRKLDQ ESWEEELQVS KFANNLVQID
190 200 210 220 230 240
NGVKIPPSGW KCSKCDLQEN LWLNLTDGSI MCGRWFCSGS GGNGHALEHH KQMGYPLAVR
250 260 270 280 290 300
LGSITPDGAD VYSFDEEEAV IDPHLAKHLA HFGIDMLQMQ GSENGVLDNE VKPRVNEWEV
310 320 330 340 350 360
IQETGLKLKP MFGSGYTGIK NLGNSSYLTT VMQVIFSIPE FQRAYVGNLT RIFDYAPLDP
370 380 390 400 410 420
TQDFSTQMAK LGHGLLSGQF SKPPMKSELI EQVMKEEHKP QPKGINTRMF KALMSKGHTE
430 440 450 460 470 480
FSSNRQQDAE EFFLHFINLV ERNSIGAENP SDVFRFLVEE RTQCCQSRKV RYTERVDYIM
490 500 510 520 530 540
QLPVPMETAT NKEELIAYDL KRREAESAKR PPPELVRAKI PFSACLQAFT EPENVPDFWS
550 560 570 580 590 600
SALQAKSAGV KTSRFASFPE YLVVQIKKFT FGLDWVPKKL DVSIDMPDLL DINHLRATGL
610 620 630 640 650 660
KSGEEELPDI APPIIIPDDP NGRMAESLLS GSGSNVNSSF KGAQPLNLPF GKKEAKLLRY
670 680 690 700 710 720
MERMVEKFGF KFSVRLSVEI DFAEPLIIPG CGTVTSTSSH GQNALLNQPP EEIVALICSM
730 740 750 760 770 780
GFPRNHALQA LRATNNNLER ALDWMFSHPE SEEGADNVSG CVDTENNPNG IITDSEQEGP
790 800 810 820 830 840
RIKDGNGRYE LFGIISHAGT STMSGHYVCH IKKEGRWVIY NDHKVSASER PPKELGYIYF
YHRISC