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USP8

Gene
USP8
Protein
Ubiquitin carboxyl-terminal hydrolase 8
Organism
Homo sapiens
Length
1118 amino acids
Function
Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1. Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-medaited APP cleavage and amyloid-beta formation (PubMed:27302062).
Similarity
Belongs to the peptidase C19 family.
Mass
127.523 kDa
Sequence
MPAVASVPKELYLSSSLKDLNKKTEVKPEKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQDYFHSILGPGNIKKAVEEAERLSESLKLRYEEAEVRKKLEEKDRQEEAQRLQQKRQETGREDGGTLAKGSLENVLDSKDKTQKSNGEKNEKCETKEKGAITAKELYTMMTDKNISLIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLQIGTTLRSLKDALFKWESKTVLRNEPLVLEGGYENWLLCYPQYTTNAKVTPPPRRQNEEVSISLDFTYPSLEESIPSKPAAQTPPASIEVDENIELISGQNERMGPLNISTPVEPVAASKSDVSPIIQPVPSIKNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILRTGTFREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKAKPQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKADNRKRYKEENNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFYTSLGPRVTDVAT

Gene
Usp8
Protein
Ubiquitin carboxyl-terminal hydrolase 8
Organism
Mus musculus
Length
1080 amino acids
Function
Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1 (By similarity). Deubiquitinates BACE1 which inhibits BACE1 lysosomal degradation and modulates BACE-mediated APP cleavage and amyloid-beta formation (By similarity).
Similarity
Belongs to the peptidase C19 family.
Mass
122.611 kDa
Sequence
MPAVASVPKELYLSSSLKDLNKKTEVKPEKTSTKNYIHSAQKIFKTAEECRLDRDEERAYVLYMKYVAVYNLIKKRPDFKQQQDYYLSILGPANIKKAIEEAERLSESLKLRYEEAEVRKQLEEKDRREEEQLQQQKRQEMGREDSGAAAKRSVENLLDSKTKTQRINGEKSEGAAAAERGAITAKELYTMMMDKNTSLIIMDARKIQDYQHSCILDSLSVPEEAISPGVTASWIEANLSDDSKDTWKKRGSVDYVVLLDWFSSAKDLLLGTTLRSLKDALFKWESKTVLRHEPLVLEGGYENWLLCYPQFTTNAKVTPPPRSRAEEVSVSLDFTYPSLEEPVPSKLPTQMPPPPIETNEKALLVTDQDEKLRLSTQPALAGPGAAPRAEASPIIQPAPATKSVPQVDRTKKPSVKLPEDHRIKSENTDQSGRVLSDRSTKPVFPSPTTMLTDEEKARIHQETALLMEKNKQEKELWDKQQKEQKEKLRREEQERKAGKTQDADERDSTENQHKAKDGQEKKDSKQTKTEDRELSADGAQEATGTQRQSKSEHEASDAKVPVEGKRCPTSEAQKRPADVSPASVSGELNAGKAQREPLTRARSEEMGRIVPGLPLGWAKFLDPITGTFRYYHSPTNTVHMYPPEMAPSSAPPSTPPTHKVKPQVPAERDREPSKLKRSYSSPDITQALQEEEKRRPAVTPMVNRENKPPCYPKAEISRLSASQIRNLNPVFGGSGPALTGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKVTIGKINDQFAGSSQQDSQELLLFLMDGLHEDLNKADNRKRHKEENNEHLDDLQAAEHAWQKHKQLNESIIVALFQGQFKSTVQCLTCRRRSRTFEAFMYLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNSLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVRSSAAYILFYTSLGPRITDVAT