ZUP1

Zinc finger-containing ubiquitin peptidase 1

579 amino acids

Deubiquitinase with endodeubiquitinase activity that specifically interacts with and cleaves 'Lys-63'-linked long polyubiquitin chains. Shows only weak activity against 'Lys-11' and 'Lys-48'-linked chains. Plays an important role in genome stability pathways, functioning to prevent spontaneous DNA damage and also promote cellular survival in response to exogenous DNA damage. Modulates the ubiquitination status of replication protein A (RPA) complex proteins in response to replication stress.

Belongs to the peptidase C78 family. ZUFSP subfamily.

66.307 kDa

MLSCDICGETVSSEPDMKAHLLIVHMENEVICPFCKLSGVNYDEMCFHIETAHFEQNELERNFERINTVQYGISDNRKDSSLQCRADINSSVHSACASNQPKISAQSLPKDGTLKHKDFYSENLTESRKFLKSTEKQSDRTKIKESIYETMYSPPECPFCGKIEDNSQDMETHVKTKHADLLDTPLEDCNQLLYDCPMCGLVCTNYHILQEHVDLHLEESSFGQGVNRVQCSRDLELAQQLQQEEDRKRRSEESRQEMEEFQKLQRQYGLDNSGGYKQQQLRNMEIEVNRGRMHPSEFHRRKADMMESLAIGVDDGKTKTSGIMEALYRYYQNAATDVRRVWLSAGVDHFHSSFGDKGWGCGYRNFQMLLSSLLQNDAYDDSLKGMSVPCIPKIQSMIEDAWKEGFDPQGASQLNDKLQGTKAWIGACEIYTLLTSLRIKCRIVDFHKSTGPLGTHPRLFEWILSYYASEREGSPKVVCTSKPPIYLQHQGHSRTVVGIEEKKNRTLCLLVFDPGCPSREMQKLLKHDMEVSSLKQLRKFVGNLKHKQYQIVAVEGVLSSEEKIARRQASQVFTAEKIP

ZUP1

Zinc finger-containing ubiquitin peptidase 1

578 amino acids

Deubiquitinase with endodeubiquitinase activity that specifically interacts with and cleaves 'Lys-63'-linked long polyubiquitin chains. Shows only weak activity against 'Lys-11' and 'Lys-48'-linked chains (PubMed:29576528, PubMed:29563501, PubMed:29476094). Plays an important role in genome stability pathways, functioning to prevent spontaneous DNA damage and also promote cellular survival in response to exogenous DNA damage (PubMed:29576528, PubMed:29576527). Modulates the ubiquitination status of replication protein A (RPA) complex proteins in response to replication stress (PubMed:29563501).

Belongs to the peptidase C78 family. ZUFSP subfamily.

65.959 kDa

MLSCNICGETVTSEPDMKAHLIVHMESEIICPFCKLSGVNYDEMCFHIETAHFEQNTLERNFERINTVQYGTSDNKKDNTLQCGMEVNSSILSGCASNHPKNSAQNLTKDSTLKHEGFYSENLTESRKFLKSREKQSSLTEIKGSVYETTYSPPECPFCGKIEEHSEDMETHVKTKHANLLDIPLEDCDQPLYDCPMCGLICTNYHILQEHVDLHLEENSFQQGMDRVQCSGDLQLAHQLQQEEDRKRRSEESRQEIEEFQKLQRQYGLDNSGGYKQQQLRNMEIEVNRGRMPPSEFHRRKADMMESLALGFDDGKTKTSGIIEALHRYYQNAATDVRRVWLSSVVDHFHSSLGDKGWGCGYRNFQMLLSSLLQNDAYNDCLKGMLIPCIPKIQSMIEDAWKEGFDPQGASQLNNRLQGTKAWIGACEVYILLTSLRVKCHIVDFHKSTGPLGTHPRLFEWILNYYSSEGEGSPKVVCTSKPPIYLQHQGHSRTVIGIEEKKNRTLCLLILDPGCPSREMQKLLKQDIEASSLKQLRKSMGNLKHKQYQILAVEGALSLEEKLARRQASQVFTAEKIP

ZUP1

Zinc finger-containing ubiquitin peptidase 1

578 amino acids

Deubiquitinase with endodeubiquitinase activity that specifically interacts with and cleaves 'Lys-63'-linked long polyubiquitin chains. Shows only weak activity against 'Lys-11' and 'Lys-48'-linked chains. Plays an important role in genome stability pathways, functioning to prevent spontaneous DNA damage and also promote cellular survival in response to exogenous DNA damage. Modulates the ubiquitination status of replication protein A (RPA) complex proteins in response to replication stress.

Belongs to the peptidase C78 family. ZUFSP subfamily.

65.775 kDa

MLSCDICGETVTSEPDMKAHLIVHMENEIVCPFCKLSGVSYDEMCFHIETAHFEQNTLERNFERINTVQFGTSDNKKDNTLQCGMEVNSSILSGCASNHPKNSSQCLTKDSTLKHETFYSENLTESRKFLKSREKQSGLTEVKGSIYETTYGPPECPFCGKIEEHSEDMETHVKTTHANLLDISLEDCDQPLYDCPMCGLICTNYHILQEHVDLHLEENSFCQGMDRVQCSGDLQLAHQLQQEEDRKRRSEESRQEIEEFQKLQRQYGLDNSGGYKQQQLRNMEIEVNRGRMPPSEFHRRKADMMESLAIGIDDGKTKTSGIIEALHRYYQNAATDVRQVWLSSVVDHFHSSLGDKGWGCGYRNFQMLLSSLLQNDAYDDCLKGMSVPCIPKIQSMIEDAWKEGFDPQGASQLNNRLQGTKAWIGACEVYILLTSLRVKCHIVDFHKSTGPLGTHPRLFEWILNYYSSEGEGSPKVVCTSKPPIYLQHQGHSRTVIGIEEKKNRTLCLLIFDPGCPSREMQKLLKQDVEASSLKQLRKSMGNLKHKQYQIVAVEGALSPEEKVARRQDSQVFTAEKIP

Zup1

Zinc finger-containing ubiquitin peptidase 1

577 amino acids

Deubiquitinase with endodeubiquitinase activity that specifically interacts with and cleaves 'Lys-63'-linked long polyubiquitin chains. Shows only weak activity against 'Lys-11' and 'Lys-48'-linked chains. Plays an important role in genome stability pathways, functioning to prevent spontaneous DNA damage and also promote cellular survival in response to exogenous DNA damage. Modulates the ubiquitination status of replication protein A (RPA) complex proteins in response to replication stress.

Belongs to the peptidase C78 family. ZUFSP subfamily.

65.593 kDa

MLSCNICGETVNSEPDMKAHLIVHMENEIICPFCKLSGINYNEICFHIETVHFEQNAPEKNSEKLAAVQYGHSDRKNTNLQSTAEVTSGIHSACASSFPKESSESLPKDRTVKHEAFYTENITESRKYQKSREKKPGLSEAQGSIYETTYSPPECPFCGKIEGCSQDMEIHVKTKHASLLESPLKDCHQPLYDCPMCGLVCTNYHILQEHVDLHLEESSFQQGMDRVQCSSDRELAHRLQQEEDRKRKSEESRQEREEFQKLQRQYGLDNSGGYKQQQLRHMELEVNRGRMHPSEFHSRKADMLESIAIGIDDGKTKTSGIIEALHRYYQNTATDVRCVWLSTVVDHFHSSFGDKGWGCGYRNFQMLLSSLLQSDVYGDCLKGMAVPCIPKIQSMIEDAWNEGFDPQGASQLNNKLQGTKAWIGACEIYTLLTSLRVKCRIIDFHKSTGPLGTHPRLFEWILNYYSSETEGTPKIVCTSKPPIYLQHQGHSRTVVGIEEKKNRTLCLLVFDPGCPSREMQKLLKQDMEASSLRQLRKSVGNLKHKQYQIVAVEGVLSPEEKVARKQASQVFTAEKIP

Zup1

Zinc finger-containing ubiquitin peptidase 1

577 amino acids

Deubiquitinase with endodeubiquitinase activity that specifically interacts with and cleaves 'Lys-63'-linked long polyubiquitin chains. Shows only weak activity against 'Lys-11' and 'Lys-48'-linked chains. Plays an important role in genome stability pathways, functioning to prevent spontaneous DNA damage and also promote cellular survival in response to exogenous DNA damage. Modulates the ubiquitination status of replication protein A (RPA) complex proteins in response to replication stress.

Belongs to the peptidase C78 family. ZUFSP subfamily.

65.722 kDa

MLSCDICGETVTSEPDRKAHLIVHMENEIICPFCKLSGINYNEMCFHIETAHFEQTTPEKSFETLAAVQYENSDLGNTKLHSTVEVTSGIHSACASNFPKESSESLSKDRTLKQEAFYTESVAESRKYQKSREKQSGLSEAQGSIYETTYSPPECPFCGRIERYSQDMEIHVKTKHASLLESPLEDCHQPLYDCPMCGLVCTNYHILQEHVDLHLEESSFQQGMDRVQCSSDRELAHQLQQEEERKRKSEESRQEREEFQKLQRQYGLDNSGGYKQQQLRHMELEVTRGRMHPSEFHSRKADMLESIAVGIDDGKTKTSGIIEALHRYYQNIATDVRCVWLSTVVDHFHSSFGDKGWGCGYRNFQMLLSSLLQNEVYSDCLKGMSVPCIPKIQSMIEDAWNEGFDPQGASQLNNKLQGTKAWIGACEIYTLLTSLKVKCRIIDFHKSTGPSGTHPRLFEWILNYYSSETEGAPKVVCTSKPPVYLQHQGHSRTVVGIEERKNRTLCLLIFDPGCPSREMQKLLKQDMEAGSLRQLRKCVGNLKHKQYQIVAVEGILSPEERAARKQASQVFTAEKIP