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 P50101

Entry ID Method Resolution Chain Position Source
AF-P50101-F1 Predicted AlphaFoldDB

20 variants for P50101

Variant ID(s) Position Change Description Diseaes Association Provenance
s13-875433 150 L>M No SGRP
s13-876108 375 Y>H No SGRP
s13-876505 507 E>G No SGRP
s13-876529 515 G>D No SGRP
s13-876537 518 Q>E No SGRP
s13-876746 587 I>M No SGRP
s13-876944 653 M>I No SGRP
s13-877042 686 R>M No SGRP
s13-877101 706 A>T No SGRP
s13-877202 739 K>N No SGRP
s13-877395 804 I>L No SGRP
s13-877434 817 K>E No SGRP
s13-877527 848 I>V No SGRP
s13-877656 891 E>K No SGRP
s13-877743 920 V>M No SGRP
s13-877785 934 I>F No SGRP
s13-878151 1056 H>N No SGRP
s13-878183 1066 E>D No SGRP
s13-878218 1078 E>G No SGRP
s13-878482 1166 S>L No SGRP

No associated diseases with P50101

7 regional properties for P50101

Type Name Position InterPro Accession
domain Peptidase C19, ubiquitin carboxyl-terminal hydrolase 205 - 533 IPR001394
domain MATH/TRAF domain 39 - 179 IPR002083
conserved_site Ubiquitin specific protease, conserved site 206 - 221 IPR018200-1
conserved_site Ubiquitin specific protease, conserved site 449 - 466 IPR018200-2
domain Ubiquitin carboxyl-terminal hydrolase 7, ICP0-binding domain 649 - 936 IPR024729
domain Ubiquitin specific protease domain 205 - 536 IPR028889
domain Ubiquitin carboxyl-terminal hydrolase, C-terminal 966 - 1217 IPR029346

Functions

Description
EC Number 3.4.19.12 Omega peptidases
Subcellular Localization
  • Cytoplasm, cytosol
  • Peroxisome
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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).
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.
peroxisome A small organelle enclosed by a single membrane, and found in most eukaryotic cells. Contains peroxidases and other enzymes involved in a variety of metabolic processes including free radical detoxification, lipid catabolism and biosynthesis, and hydrogen peroxide metabolism.

2 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.

4 GO annotations of biological process

Name Definition
free ubiquitin chain depolymerization The process in which free ubiquitin chains, compounds composed of a large number of ubiquitin monomers, are broken down.
protein deubiquitination The removal of one or more ubiquitin groups from a protein.
regulation of protein stability Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
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.

2 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q93009 USP7 Ubiquitin carboxyl-terminal hydrolase 7 Homo sapiens (Human) PR
Q6A4J8 Usp7 Ubiquitin carboxyl-terminal hydrolase 7 Mus musculus (Mouse) PR
10 20 30 40 50 60
MSSEDELGSI GTVFPGSPID KSIGSILPQF DEEVETLLED SFTWNIPDWN ELTNPKYNSP
70 80 90 100 110 120
RFRIGDFEWD ILLFPQGNHN KGVAVYLEPH PEEKLDETTG EMVPVDPDWY CCAQFAIGIS
130 140 150 160 170 180
RPGNGDTINL INKSHHRFNA LDTDWGFANL IDLNNLKHPS KGRPLSFLNE GTLNITAYVR
190 200 210 220 230 240
ILKDPTGVLW HNFLNYDSKK VTGYVGFRNQ GATCYLNSLL QSYFFTKYFR KLVYEIPTEH
250 260 270 280 290 300
ESPNNSVPLA LQRAFYQLQV SDIPLDTLEL TRSFGWDTAE SFTQHDVQEL NRILMDRLEN
310 320 330 340 350 360
NMKGTPVEGK LNEIFVGKMK SYIKCINVDY ESARVEDFWD LQLNVKNFKN LQESFDNYIE
370 380 390 400 410 420
MELMNGENQY AAQDYGLQDA QKGVIFESFP PVLHLQLKRF EYDFNYDQMV KVNDKYEFPE
430 440 450 460 470 480
TIDLSPFVDK DVLKKTLDSE NKDKNPYVYN LHGVLVHSGD ISTGHYYTLI KPGVEDQWYR
490 500 510 520 530 540
FDDERVWRVT KKQVFQENFG CDRLPDEKVR TMTRGEYQNY IIQRHTSAYM LVYIRQEQEE
550 560 570 580 590 600
DLLRPVLESD VPKHVITRVR EEIKERETKE KEIREAHLYV TLRLHSIKEF IHYEGFDYFA
610 620 630 640 650 660
HDGFRLFAEE LNDSGLQQIN LKVLRTTKLS DIFASIKETM NIPQERDVKY WKMDYRRNST
670 680 690 700 710 720
LRLTQPINFE SVNITLQEAL KKEKKRTMQT QYGEEGVAST EEDDKALLET VSFLDLFIEE
730 740 750 760 770 780
PYLELQFLNK LKEASLISKA QLDDELISTI RTNLPELTKG GIEPVFATDN KSNLLFVKSY
790 800 810 820 830 840
DPHTQKLLGF GHFAVNQLQQ LSDISAIIED SISSNEKLTF YEEVQPGTIN EIYMKETIYD
850 860 870 880 890 900
ADIDTGDIVS FEVPGAVLPD TFPVYATIKD FYSYLRYRVK LKFSKFDGSS EEYGVSNEIP
910 920 930 940 950 960
ESFEFWISAY APYDDLARMV SKYAHVKPEY LKIIALYSNG RFVLKSTSLL NDYLLKDFNC
970 980 990 1000 1010 1020
DQIPPFAFEV LSVPLKELER LRPIKLYWLK NSYIHYQCFE FEVANDYTES QFLEKVQHKI
1030 1040 1050 1060 1070 1080
GFTDEEKENI LLWTNTNFQF QGLLSDQNTF KDVSKHSLLF GRILPEESKL FKELNRLENV
1090 1100 1110 1120 1130 1140
QTSSLEDFMD DENATDRPMD DEQDLGMAIE HSEDMKGRIV VVQQYFKDLE NRHGISFLFN
1150 1160 1170 1180 1190 1200
LIPDETFPKT KDRLHAKFGL GQKEFSKIKL SIGYSTEEGT VFRSLQGFSD EELDKVILYD
1210 1220
IMSNLDYIYM DHPDRLRSHS SYDRPMIIKN