Tag | Content |
---|---|
UniProt Accession | UBP7_HUMAN; Q93009; |
Entrez ID | 7874 |
GenBank Protein ID | NM_001321858.1; NM_003470.2; |
GenBank Nucleotide ID | NP_001308787.1; NP_003461.2; |
Protein Name | Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.4.19.12) (Deubiquitinating enzyme 7) (Herpesvirus-associated ubiquitin-specific protease) (Ubiquitin thioesterase 7) (Ubiquitin-specific-processing protease 7) |
Gene Name | USP7; HAUSP |
Organism | Homo sapiens |
NCBI Taxa ID | 9606 |
Functional Description | Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX (PubMed:11923872, PubMed:15053880, PubMed:16964248, PubMed:18716620, PubMed:25283148). Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation (PubMed:15053880, PubMed:16845383, PubMed:18566590, PubMed:20153724). Deubiquitinates p53/TP53, preventing degradation of p53/TP53, and enhances p53/TP53-dependent (view all) |
Sequence (Fasta) | MNHQQQQQQQ KAGEQQLSEP EDMEMEAGDT DDPPRITQNP VINGNVALSD GHNTAEEDME 60 DDTSWRSEAT FQFTVERFSR LSESVLSPPC FVRNLPWKIM VMPRFYPDRP HQKSVGFFLQ 120 CNAESDSTSW SCHAQAVLKI INYRDDEKSF SRRISHLFFH KENDWGFSNF MAWSEVTDPE 180 KGFIDDDKVT FEVFVQADAP HGVAWDSKKH TGYVGLKNQG ATCYMNSLLQ TLFFTNQLRK 240 AVYMMPTEGD DSSKSVPLAL QRVFYELQHS DKPVGTKKLT KSFGWETLDS FMQHDVQELC 300 RVLLDNVENK MKGTCVEGTI PKLFRGKMVS YIQCKEVDYR SDRREDYYDI QLSIKGKKNI 360 FESFVDYVAV EQLDGDNKYD AGEHGLQEAE KGVKFLTLPP VLHLQLMRFM YDPQTDQNIK 420 INDRFEFPEQ LPLDEFLQKT DPKDPANYIL HAVLVHSGDN HGGHYVVYLN PKGDGKWCKF 480 DDDVVSRCTK EEAIEHNYGG HDDDLSVRHC TNAYMLVYIR ESKLSEVLQA VTDHDIPQQL 540 VERLQEEKRI EAQKRKERQE AHLYMQVQIV AEDQFCGHQG NDMYDEEKVK YTVFKVLKNS 600 SLAEFVQSLS QTMGFPQDQI RLWPMQARSN GTKRPAMLDN EADGNKTMIE LSDNENPWTI 660 FLETVDPELA ASGATLPKFD KDHDVMLFLK MYDPKTRSLN YCGHIYTPIS CKIRDLLPVM 720 CDRAGFIQDT SLILYEEVKP NLTERIQDYD VSLDKALDEL MDGDIIVFQK DDPENDNSEL 780 PTAKEYFRDL YHRVDVIFCD KTIPNDPGFV VTLSNRMNYF QVAKTVAQRL NTDPMLLQFF 840 KSQGYRDGPG NPLRHNYEGT LRDLLQFFKP RQPKKLYYQQ LKMKITDFEN RRSFKCIWLN 900 SQFREEEITL YPDKHGCVRD LLEECKKAVE LGEKASGKLR LLEIVSYKII GVHQEDELLE 960 CLSPATSRTF RIEEIPLDQV DIDKENEMLV TVAHFHKEVF GTFGIPFLLR IHQGEHFREV 1020 MKRIQSLLDI QEKEFEKFKF AIVMMGRHQY INEDEYEVNL KDFEPQPGNM SHPRPWLGLD 1080 HFNKAPKRSR YTYLEKAIKI HN 1103 |
|
Database | Annotation |
---|---|
CTD (Curated) (count: 1) | MESH:D001749 ; Urinary Bladder Neoplasms |
GWASdb (count: 4) | rs201638486; Multiple complex diseases; Null
rs2126999; Multiple complex diseases; Null rs2437716; Multiple complex diseases; Null rs12929193; Multiple complex diseases; Null |
PTM | Modification Sites |
---|---|
Phosphorylation (count: 19) (view all) | 1050 VMMGRHQYINEDEYE dbPAF
1056 QYINEDEYEVNLKDF dbPAF 1091 KAPKRSRYTYLEKAI dbPAF 1092 APKRSRYTYLEKAIK dbPAF 1093 PKRSRYTYLEKAIKI dbPAF 143 AVLKIINYRDDEKSF dbPAF |
Acetylation (count: 26) (view all) | 1033 SLLDIQEKEFEKFKF PLMD
1037 IQEKEFEKFKFAIVM PLMD 1084 LGLDHFNKAPKRSRY PLMD 1096 SRYTYLEKAIKIHN* PLMD 254 TEGDDSSKSVPLALQ PLMD 272 YELQHSDKPVGTKKL PLMD |
Ubiquitination (count: 38) (view all) | 1033 SLLDIQEKEFEKFKF PLMD
1039 EKEFEKFKFAIVMMG PLMD 1096 SRYTYLEKAIKIHN* PLMD 148 INYRDDEKSFSRRIS PLMD 240 FFTNQLRKAVYMMPT PLMD 254 TEGDDSSKSVPLALQ PLMD |
Sumoylation (count: 2) | 869 RDLLQFFKPRQPKKL PLMD
882 KLYYQQLKMKITDFE PLMD |
Malonylation (count: 3) | 1084 LGLDHFNKAPKRSRY PLMD
272 YELQHSDKPVGTKKL PLMD 327 IPKLFRGKMVSYIQC PLMD |
Network | Interaction | ||
---|---|---|---|
A | B | Source | |