USP13

Ubiquitin carboxyl-terminal hydrolase 13

863 amino acids

Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data.

Belongs to the peptidase C19 family.

97.278 kDa

MQRRGALFGMPGGSGSRKMAAGDIGELLVPHMPTIRVPRSGDRVYKNECAFSYDSPNSEGGLYVCMNTFLAFGREHVERHFRKTGQSVYMHLKRHVREKVRGASGGALPKRRNSKMFLDLDTDDDLNSDDYEYEDEAKLVIFPDHYEIALPNIEELPALVTIACDAVLSSKSPYRKQDPDTWENELPVSKYANNLTQLDNGVRIPPSGWKCARCDLRENLWLNLTDGSVLCGKWFFDSSGGNGHALEHYRDTGYPLAVKLGTITPDGADVYSFQEEEAVLDPHLAKHLAHFGIDMLHMHGTENGLQDNDIKPRVSEWEVIQETGTKLKPMYGPGYTGLKNLGNSCYLSSVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLSGQYSKPPVKSELIEQVMKEEHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERNRIGSENPSDVFRFLVEERIQCCQTRKVRYTERVDYLMQLPVAMEAATNKDELIAYELTRREAESNRRPLPELVRAKIPFSACLQAFSEPENVDDFWSSALQAKSAGVKTSRFASFPEYLVVQIKKFTFGLDWVPKKFDVSVDMPDLLDINHLRARGLQPGEEELPDISPPIVIPDDSKDRLMTQLIDPSDIDESSVMQLAEMGFPLEACRKAVYFTGNMGAEVAFNWIVVHMEEPDFAEPLTMPGYGGAASAGASVFGATGLDNQPPEETVAIITSMGFHRNQAIQALRATNSNLERALDWIFSHPEFEEDSDFVIEMENNANANIVSEAKPEGPRVKDGSGMYELFAFISHMGTSTMSGHYVCHIKKEGRWVIYNDHKVCASERPPKDLGYMYFYRRIPS

USP13

Ubiquitin carboxyl-terminal hydrolase 13

863 amino acids

Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data.

Belongs to the peptidase C19 family.

97.327 kDa

MQRRGALFGMPGGSGGRKMAAGDIGELLVPHMPTIRVPRSGDRVYKNECAFSYDSPNSEGGLYVCMNTFLAFGREHVERHFRKTGQSVYMHLKRHVREKVRGASGGALPKRRNSKIFLDLDTDDDLNSDDYEYEDEAKLVIFPDHYEIALPNIEELPALVTIACDAVLSSKSPYRKQDPDTWENELPVSKYANNLTQLDNGVRIPPSGWKCARCDLRENLWLNLTDGSVLCGKWFFDSSGGNGHALEHYRDMGYPLAVKLGTITPDGADVYSFQEEEPVLDPHLAKHLAHFGIDMLHMHGTENGLQDNDIKLRVSEWEVIQESGTKLKPMYGPGYTGLKNLGNSCYLSSVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLSGQYSKPPVKSELIEQVMKEEHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERNRIGSENPSDVFRFLVEERIQCCQTRKVRYTERVDYLMQLPVAMEAATNKDELIAYELTRREAEANRRPLPELVRAKIPFSACLQAFSEPENVDDFWSSALQAKSAGVKTSRFASFPEYLVVQIKKFTFGLDWVPKKFDVSIDMPDLLDINHLRARGLQPGEEELPDISPPIVIPDDSKDRLMNQLIDPSDIDESSVMQLAEMGFPLEACRKAVYFTGNMGAEVAFNWIIVHMEEPDFAEPLTMPGYGGAASAGASVFGASGLDNQPPEEIVAIITSMGFQRNQAIQALRATNNNLERALDWIFSHPEFEEDSDFVIEMENNANANIISEAKPEGPRVKDGSGTYELFAFISHMGTSTMSGHYICHIKKEGRWVIYNDHKVCASERPPKDLGYMYFYRRIPS

USP13

Ubiquitin carboxyl-terminal hydrolase 13

862 amino acids

Deubiquitinase that mediates deubiquitination of target proteins and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD).

Belongs to the peptidase C19 family.

96.649 kDa

MQRAALFGGGDAQMAAGDLGELLVPYMPTIRVPKSGDRVYKTECAFSYDSPDSEGGLYVCMNTFLGFGREHIERHYRKTGQCVYLHLKRHVIEKVPGASGGALPKRRNAKLFLDLEANGDLSSDDFEYEDEAKLVIFPDHYEISLPNIEELPALVTIASDALLSAKSPYRKQDPDSWEEELQASKHAKSLVQLDNGVRIPPSGWKCSKCDLRENLWLNLTDGSVLCGKWFFDGSGGNGHAMEHYKETGYPLAVKLGTITPDGADVYSFDEEEPVLDPHIAKHLAHFGIDMLQMQVAENGLRDNDIKPRVSEWEVIQEAGVKLKPMYGPGYTGMKNLGNSCYLNAVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPTQDFNTQMAKLGHGLLSGQYSKPPMKSELIEQVMKEEHKPQQNGISPQMFKAFISKDHTEFSSNRQQDAQEFFLHLINLVERNPVGSENPSDVFRFLVEERTQCCQSRKVRYTERVDYIMQLPVAMEAATNKDELIAYELKRREAEAARRAPPELVRAKIPFSACLQAFSEPTNVEDFWSSALQAKSAGVKTSRFASFPQYLVVQIKKFTFGLDWIPKKLDVSIDMPDFLDISHLRAMGLQPGEEELPDIAPPIIIPEDPKDRMMNNFVESLDIDESSVMQLAEMGFPLEACRKAVYYTGNLGAEVAFNWIIAHMEEPDFAEPLVVPVFGGAASSGVAGLGAVGLDNQPPEEMVSIIISMGFQRSLAIQALKATNNNLERALEWIFSHPELEEEDGEPALNVMDLENHTNANILAEARSEGPRIKDGPGRYELFGFISHMGTSTMSGHYVCHLKKEGRWVIYNDLRVCASERPPKDLGYIYFYHRIPS

usp13

Ubiquitin carboxyl-terminal hydrolase 13

860 amino acids

Deubiquitinase that mediates deubiquitination of target proteins and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD).

Belongs to the peptidase C19 family.

97.452 kDa

MATDLGELLVPYMPTIRVPRTGDRVFKSECAFSYDSPESEGGLYVCMNSFLGFGREHVERHYRKTGQSVYMHLKRHVKEKATGAAGGAIPRRRNGKVFLDLELNRDFNGDDYEYEDEAKLVIFPDHYEIPLPNIEELPALVTIACDAVLNAPSPYKKQESDSWEEEIQVSRHARSLRQLDNGVRIPPSGWKCAKCEMRENLWLNLTDGSVLCGKWFFDGSGGNGHALEHYRESNFPLAVKLNTITPDGADIYSFDEEEAVLDPHISEHLLHFGIDMLQMQRTENGHHTDNHVQPRISDWEVIQEAGLKLKPVYGSGYTGIKNLGNSCYLSTTMQVLFSIPEFQRAYAGNLQRIFDYSPLDPTQDFNTQMAKLGHGLLSGQYSKPPMKSELIEQVMKEEHKQQQQRGISPKMFKALVSKGHPEFSSNRQQDAHEFLLHLINLVERNNSGSENPSDVFRFIVEERTQCCQSQKVRYTQRVDYLMQLPVPLEAASNREELIAYEGKRKEAEENMRPLPEVVRARVPFTACLQAFTEPENVPDFWSSALQAKSAGVKTSRFATFPEYMIVQLKKFTFGVDWVPKKLDMSVDVPDFLDLNRLRATGLQAGEEELPDLTPPIVIPEDTRDSSTNNSLESPEIDESSVMQLAEMGFPLEACRKAVYYTGNMGAEMAFNWIIAHMEEPDFAEPLAVPTYMESDLPSPSLPTTSALDNQPPEESISILTSMGFPRHHTIQALKASNNNLERALDWIFTHPDCEDESEAMSDTADTEPNDNSFSNANAHTDSSLSPDQDLSSPRVRDGPGRYELFAFISHMGTSTMSGHYVCHIKKEGRWLIYNDHKVCLSERPPKDLGYMYFYRRLSSC

Usp13

Ubiquitin carboxyl-terminal hydrolase 13

858 amino acids

Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data.

Belongs to the peptidase C19 family.

96.723 kDa

MQRRGALFSVPGGGGKMAAGDLGELLVPHMPTIRVPRSGDRVYKNECAFSYDSPNSEGGLYVCMNTFLAFGREHVERHFRKTGQSVYMHLKRHMREKVRGASGGALPKRRNSKIFLDLDMDDDLNSDDYEYEDEAKLVIFPDHYEIALPNIEELPALVTIACDAVLSSKSPYRKQDPDTWENEVPVSKYANNLVQLDNGVRIPPSGWKCARCDLRENLWLNLTDGSVLCGKWFFDSSGGNGHALEHYRDMGYPLAVKLGTITPDGADVYSFQEEGPVSDPHLAKHLAHFGIDMLHTQGTENGLRDNDIKPRVSEWEVIQESGTKLKPMYGPGYTGLKNLGNSCYLSSVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLSGQYSKPPVKSELIEQVMKEEHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERNRIGSENPSDVFRFLVEERIQCCQTRKVRYTERVDYLMQLPVAMEAATNKDELITYELMRREAEANRRPLPELVRAKIPFSACLQAFAEPDNVDDFWSSALQAKSAGVKTSRFASFPEYLVVQIKKFTFGLDWVPRKFDVSIDMPDLLDISHLRARGLQPGEEELPDISPPIVIPDDSKDRLMNQLIDPSDIDESSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVHMEEPDFAEPLAIPGYGGAGASVFGATGLDNQPPEEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFSHPEFEEDSDFVIEMENNANANIVSEAKPEGPRVKDGSGMYELFAFISHMGTSTMSGHYVCHIKKEGRWVIYNDHKVCASERPPKDLGYMYFYRRIPS

usp13

Ubiquitin carboxyl-terminal hydrolase 13

846 amino acids

Deubiquitinase that mediates deubiquitination of target proteins and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD).

Belongs to the peptidase C19 family.

95.089 kDa

MAEDLGELLVPYMPTIRVPKSGDRVYKTECAFSYDSPESDGGLYVCMSTFLGFGREHVERHYRKTGQSVYMHLKRHIRLKATGASGGAFPKRINGRLFLDLENNTEMNTEDYEYEDEAKLVIFPDHFEIALPNIEELPALVTIACDAVLNSKSPYRKLDQESWEEELQVSKFANNLVQIDNGVKIPPSGWKCSKCDLQENLWLNLTDGSIMCGRWFCSGSGGNGHALEHHKQMGYPLAVRLGSITPDGADVYSFDEEEAVIDPHLAKHLAHFGIDMLQMQGSENGVLDNEVKPRVNEWEVIQETGLKLKPMFGSGYTGIKNLGNSSYLTTVMQVIFSIPEFQRAYVGNLTRIFDYAPLDPTQDFSTQMAKLGHGLLSGQFSKPPMKSELIEQVMKEEHKPQPKGINTRMFKALMSKGHTEFSSNRQQDAEEFFLHFINLVERNSIGAENPSDVFRFLVEERTQCCQSRKVRYTERVDYIMQLPVPMETATNKEELIAYDLKRREAESAKRPPPELVRAKIPFSACLQAFTEPENVPDFWSSALQAKSAGVKTSRFASFPEYLVVQIKKFTFGLDWVPKKLDVSIDMPDLLDINHLRATGLKSGEEELPDIAPPIIIPDDPNGRMAESLLSGSGSNVNSSFKGAQPLNLPFGKKEAKLLRYMERMVEKFGFKFSVRLSVEIDFAEPLIIPGCGTVTSTSSHGQNALLNQPPEEIVALICSMGFPRNHALQALRATNNNLERALDWMFSHPESEEGADNVSGCVDTENNPNGIITDSEQEGPRIKDGNGRYELFGIISHAGTSTMSGHYVCHIKKEGRWVIYNDHKVSASERPPKELGYIYFYHRISC