ID  Q28CN3;
PN  Ubiquitin carboxyl-terminal hydrolase 33;
GN  usp33;
OS  8364;
SL  Nucleus Position: SL-0198;
SL  Comments: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TEY7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q8TEY7}. Note=Associates with centrosomes predominantly in S and G2 phases but less in G1 phase (By similarity). {ECO:0000250|UniProtKB:Q8TEY7}.
DR  UNIPROT: Q28CN3;
DR  UNIPROT: B7ZU27;
DR  UNIPROT: F7EIJ9;
DR  Pfam: PF06337;
DR  Pfam: PF00443;
DR  Pfam: PF02148;
DR  PROSITE: PS51283;
DR  PROSITE: PS00972;
DR  PROSITE: PS00973;
DR  PROSITE: PS50235;
DR  PROSITE: PS50271;
DE  Function: Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of ccp110 in S and G2/M phase, leading to stabilize ccp110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of robo1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of robo1. Acts as a regulator of G- protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (arrb1 and arrb2) and beta-2 adrenergic receptor (adrb2). Deubiquitinates dio2, thereby regulating thyroid hormone regulation. Mediates deubiquitination of both 'Lys- 48'- and 'Lys-63'-linked polyubiquitin chains (By similarity). {ECO:0000250}.
DE  Reference Proteome: Yes;
GO  GO:0005813;
GO  GO:0005737;
GO  GO:0048471;
GO  GO:0004843;
GO  GO:0004197;
GO  GO:0008270;
GO  GO:0007411;
GO  GO:0016477;
GO  GO:0051298;
GO  GO:0006897;
GO  GO:0016579;
GO  GO:0071108;
GO  GO:0070536;
GO  GO:0008277;
GO  GO:0006511;
TP  Membrane Topology: Unknown; Source: UniProt - Sequence Analysis;
SQ  MSSLVCDCPHLESVGEVTKEELIKKSHGSCQDCRVRGPNLWACLENGCSYVGCGESHVDHSTLHSQDTKHCLTVNLTTLR
SQ  VWCYTCSKEVFLDRKLSTQPTSAKLQDSHTQESKMSSSLTLKIPAAVVSENLDIELEEEDELKTRGLTGLKNIGNTCYMN
SQ  AALQALSNCPPLTHYFLDCGGLARTDKKPALCKSYQKLMSDIWHKNRPGFVIPTNLFQGIKSVNPTFRGYSQQDAQEFLR
SQ  CLMDVLHEELKEQIVEVEEDAQTGIVEENLDEDKSQSDNDFHSCDSGSSSDHAESESRKLSEELTESTMLIHEDQKDVES
SQ  CKTWQKEKKFSNNLNQNHFLQDFEKNIQSTIEESECLKQETVKVQIQSKAADFTAEVNMNDLPTSQTPLLNEGATTHLSS
SQ  SPPKPGAVWTGHKKVPGLCPAKKRKQKKYHSVIADIFDGTIVSSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSS
SQ  HQSSLVKAGSCGEAYAPQGWIAFFLEYFKSWFWGPTVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGVKFCKVQKFPE
SQ  ILCIHLKRFRHELMFSTKIGTHVSFPLEGLDLQPFLAKDSPSQIVTYDLLSVICHHGTASSGHYIAYCRNNLNNLWYEFD
SQ  DQSVTEVSEATVQNAEAYVLFYRKASEEAQKERRRVSCLLNIMEPSLLQFYISRQWLNKFKTFAEPGPISNNDFLCIHGG
SQ  VPPRKASFIEDLVVMLPQNIWDYLYSRYGGGPAVNHLYVCYTCQTEMEKIEKRRKMELETFIRLNKAFQEEESPAVIYCI
SQ  SMQWFREWEGFVKSKDSDPPGPIDNTKIAAAKCGHITLRQGADSGQISEETWLFLQSIYGGGPEITLRQNVTLAESEGGH
SQ  AEEKIDVETRNI
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