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Q93009

- UBP7_HUMAN

UniProt

Q93009 - UBP7_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 7

Gene

USP7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (04 Nov 2008)
      Previous versions | rss
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    Functioni

    Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. 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. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Exhibits a preference towards 'Lys-48'-linked Ubiquitin chains.13 Publications

    Catalytic activityi

    Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

    Enzyme regulationi

    Inhibited by N-ethyl-maleimide (NEM) and divalent cations. Tolerates high concentrations of NaCl but is inhibited at concentrations of 195 mM and higher.1 Publication

    pH dependencei

    Active from pH 7.0 to 9.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei223 – 2231Nucleophile
    Active sitei464 – 4641Proton acceptorCurated

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. p53 binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein C-terminus binding Source: UniProtKB
    5. transcription factor binding Source: UniProtKB
    6. ubiquitin protein ligase binding Source: UniProtKB
    7. ubiquitin-specific protease activity Source: UniProtKB
    8. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. maintenance of DNA methylation Source: UniProtKB
    2. multicellular organismal development Source: UniProtKB-KW
    3. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
    4. protein deubiquitination Source: UniProtKB
    5. regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    6. transcription-coupled nucleotide-excision repair Source: UniProtKB
    7. ubiquitin-dependent protein catabolic process Source: InterPro
    8. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    DNA damage, DNA repair, Host-virus interaction, Ubl conjugation pathway

    Enzyme and pathway databases

    SignaLinkiQ93009.

    Protein family/group databases

    MEROPSiC19.016.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 7 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 7
    Herpesvirus-associated ubiquitin-specific protease
    Ubiquitin thioesterase 7
    Ubiquitin-specific-processing protease 7
    Gene namesi
    Name:USP7
    Synonyms:HAUSP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:12630. USP7.

    Subcellular locationi

    Nucleus. Cytoplasm. NucleusPML body
    Note: Present in a minority of ND10 nuclear bodies. Association with ICP0/VMW110 at early times of infection leads to an increased proportion of USP7-containing ND10. Colocalizes with ATXN1 in the nucleus. Colocalized with DAXX in speckled structures. Colocalized with PML and PTEN in promyelocytic leukemia protein (PML) nuclear bodies.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi164 – 1641D → A: Decreased binding to p53/TP53 and MDM2. 1 Publication
    Mutagenesisi165 – 1651W → A: Loss of binding to p53/TP53 and MDM2. 1 Publication
    Mutagenesisi223 – 2231C → A: Complete loss of activity. Localized in the nucleus and does not inhibit FOXO4-dependent transcriptional activity. 7 Publications
    Mutagenesisi223 – 2231C → S: No effect on p53/TP53 and PTEN binding but is defective in deubiquitinating p53/TP53 and PTEN. 7 Publications
    Mutagenesisi456 – 4561H → A: Complete loss of activity. 1 Publication
    Mutagenesisi464 – 4641H → A: Complete loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA37255.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11021102Ubiquitin carboxyl-terminal hydrolase 7PRO_0000080626Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei18 – 181Phosphoserine4 Publications
    Modified residuei869 – 8691N6-acetyllysine; alternate1 Publication
    Cross-linki869 – 869Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate2 Publications
    Modified residuei963 – 9631Phosphoserine2 Publications
    Modified residuei1084 – 10841N6-acetyllysine1 Publication
    Modified residuei1096 – 10961N6-acetyllysine1 Publication

    Post-translational modificationi

    Isoform 1: Phosphorylated. Isoform 1 is phosphorylated at positions Ser-18 and Ser-963. Isoform 2: Not phosphorylated.4 Publications
    Isoform 1: Polyneddylated. Isoform 2: Not Polyneddylated.
    Isoform 1 and isoform 2: Not sumoylated.
    Isoform 1 and isoform 2: Polyubiquitinated by herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110; leading to its subsequent proteasomal degradation. Isoform 1: Ubiquitinated at Lys-869.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ93009.
    PaxDbiQ93009.
    PRIDEiQ93009.

    PTM databases

    PhosphoSiteiQ93009.

    Expressioni

    Tissue specificityi

    Widely expressed. Overexpressed in prostate cancer.1 Publication

    Gene expression databases

    ArrayExpressiQ93009.
    BgeeiQ93009.
    CleanExiHS_USP7.
    GenevestigatoriQ93009.

    Organism-specific databases

    HPAiCAB008108.
    HPA015641.

    Interactioni

    Subunit structurei

    Monomer. Homodimer. Part of a complex with DAXX, MDM2, RASSF1 and USP7. Part of a complex with DAXX, MDM2 and USP7. Interacts with MDM2; the interaction is independent of p53/TP53. Interacts with DAXX; the interaction is direct and independent of MDM2 and p53/TP53. Interacts with FOXO4; the interaction is enhanced in presence of hydrogen peroxide and occurs independently of p53/TP53. Interacts with p53/TP53; the interaction is enhanced in response to DNA damage; the interaction is impaired by TSPYL5. Interacts with PTEN; the interaction is direct. Interacts with UBXN6. Interacts with ATXN1 and the strength of interaction is influenced by the length of the poly-Gln region in ATXN1. A weaker interaction seen with mutants having longer poly-Gln regions. Interacts with KIAA1530/UVSSA. Isoform 1 and isoform 2 interact with herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110. Interacts with Epstein-Barr virus EBNA1. EBNA1 shows a 10-fold higher affinity than p53/TP53 and can compete with it for USP7 binding. Binding to ICP0/VMW110 may modulate the substrate specificity or activity of USP7 to stabilize viral proteins. Interacts with MEX3C and antagonizes its ability to degrade mRNA. Interacts with DNMT1 and UHRF1.22 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BMI1P352267EBI-302474,EBI-2341576
    CBX8Q9HC527EBI-302474,EBI-712912
    DAXXQ9UER713EBI-302474,EBI-77321
    EBNA1P032114EBI-302474,EBI-996522From a different organism.
    MALP211453EBI-302474,EBI-3932027
    MDM2Q0098718EBI-302474,EBI-389668
    MDM4O1515115EBI-302474,EBI-398437
    Mdm4O356184EBI-302474,EBI-2603376From a different organism.
    MEX3CQ5U5Q33EBI-302474,EBI-2864451
    MYD88Q998363EBI-302474,EBI-447677
    PCGF2P352275EBI-302474,EBI-2129767
    RB1P064008EBI-302474,EBI-491274
    RING1Q065874EBI-302474,EBI-752313
    RNF2Q994964EBI-302474,EBI-722416
    SMAD3P840222EBI-302474,EBI-347161
    TBCBQ994262EBI-302474,EBI-764356
    TP53P0463717EBI-302474,EBI-366083
    TSPYL5Q86VY44EBI-302474,EBI-3436472

    Protein-protein interaction databases

    BioGridi113622. 200 interactions.
    DIPiDIP-29053N.
    IntActiQ93009. 105 interactions.
    MINTiMINT-234628.
    STRINGi9606.ENSP00000343535.

    Structurei

    Secondary structure

    1
    1102
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi67 – 7711
    Helixi78 – 803
    Beta strandi90 – 923
    Beta strandi95 – 10410
    Beta strandi113 – 12210
    Beta strandi131 – 14010
    Helixi146 – 1483
    Beta strandi150 – 15910
    Helixi160 – 1623
    Beta strandi164 – 1729
    Helixi173 – 1764
    Turni179 – 1813
    Beta strandi182 – 1854
    Beta strandi188 – 19710
    Beta strandi201 – 2033
    Turni209 – 2113
    Turni221 – 2244
    Helixi225 – 2339
    Helixi236 – 2449
    Turni252 – 2543
    Helixi256 – 26914
    Helixi277 – 2837
    Turni288 – 2936
    Helixi296 – 31116
    Turni315 – 3184
    Helixi319 – 3246
    Beta strandi326 – 33813
    Beta strandi340 – 35213
    Helixi360 – 3678
    Beta strandi371 – 3733
    Helixi375 – 3773
    Helixi382 – 3843
    Beta strandi389 – 3979
    Beta strandi400 – 4067
    Beta strandi409 – 4124
    Turni413 – 4153
    Beta strandi417 – 4204
    Beta strandi429 – 4324
    Helixi434 – 4363
    Beta strandi437 – 4393
    Beta strandi442 – 4443
    Beta strandi447 – 45812
    Beta strandi460 – 4623
    Beta strandi464 – 4696
    Beta strandi473 – 4753
    Beta strandi477 – 4815
    Beta strandi484 – 4885
    Helixi490 – 4934
    Helixi495 – 4973
    Turni507 – 5104
    Beta strandi511 – 52010
    Helixi521 – 5233
    Helixi524 – 5274
    Helixi533 – 5353
    Helixi538 – 55114
    Helixi561 – 5633
    Beta strandi564 – 5718
    Helixi572 – 5754
    Beta strandi580 – 5834
    Turni586 – 5883
    Beta strandi592 – 5976
    Helixi602 – 61312
    Helixi617 – 6193
    Beta strandi620 – 6278
    Beta strandi633 – 6353
    Helixi640 – 6434
    Beta strandi645 – 6473
    Helixi648 – 6525
    Beta strandi656 – 6649
    Helixi667 – 6704
    Turni671 – 6733
    Turni681 – 6833
    Beta strandi684 – 69310
    Turni694 – 6974
    Beta strandi698 – 70811
    Helixi713 – 7153
    Helixi717 – 7248
    Beta strandi732 – 7398
    Beta strandi742 – 7454
    Beta strandi749 – 7524
    Helixi753 – 7564
    Beta strandi764 – 7707
    Helixi773 – 7775
    Beta strandi778 – 7803
    Helixi783 – 79210
    Beta strandi793 – 8008
    Beta strandi809 – 8146
    Helixi819 – 83012
    Helixi834 – 8363
    Beta strandi837 – 8404
    Helixi861 – 8644
    Beta strandi870 – 8723
    Beta strandi875 – 8806
    Helixi885 – 8895
    Beta strandi894 – 8996
    Beta strandi905 – 9106
    Helixi918 – 9269
    Beta strandi939 – 9457
    Beta strandi948 – 9536
    Helixi959 – 9613
    Beta strandi969 – 9746
    Helixi977 – 9793
    Turni984 – 9863
    Beta strandi987 – 99812
    Beta strandi1002 – 101211
    Helixi1017 – 102812
    Helixi1032 – 10354
    Beta strandi1039 – 10446
    Beta strandi1047 – 10504
    Turni1053 – 10553
    Helixi1060 – 10623
    Beta strandi1070 – 10723
    Beta strandi1076 – 10805

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NB8X-ray2.30A/B208-560[»]
    1NBFX-ray2.30A/B/E208-560[»]
    1YY6X-ray1.70A54-204[»]
    1YZEX-ray2.00A/B/C54-205[»]
    2F1WX-ray1.65A53-206[»]
    2F1XX-ray2.30A/B53-200[»]
    2F1YX-ray1.70A53-198[»]
    2F1ZX-ray3.20A/B43-560[»]
    2FOJX-ray1.60A54-205[»]
    2FOOX-ray2.20A54-205[»]
    2FOPX-ray2.10A54-205[»]
    2KVRNMR-A537-664[»]
    2XXNX-ray1.60A63-205[»]
    2YLMX-ray2.70A560-1084[»]
    3MQRX-ray1.80A54-205[»]
    3MQSX-ray2.40C54-205[»]
    4JJQX-ray1.95A54-205[»]
    4KG9X-ray1.70A54-205[»]
    4M5WX-ray2.24A207-560[»]
    4M5XX-ray2.19A/B207-560[»]
    4PYZX-ray2.84A/B537-793[»]
    ProteinModelPortaliQ93009.
    SMRiQ93009. Positions 63-554, 560-1083.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ93009.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini68 – 195128MATHPROSITE-ProRule annotationAdd
    BLAST
    Domaini214 – 521308USPAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 208208Interaction with TSPYL5Add
    BLAST
    Regioni53 – 208156Interaction with p53/TP53, MDM2 and EBNA1Add
    BLAST
    Regioni70 – 205136Necessary for nuclear localizationAdd
    BLAST
    Regioni622 – 801180Interaction with ICP0/VMW110Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 107Poly-Gln

    Domaini

    The C-terminus plays a role in its oligomerization.By similarity

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 1 MATH domain.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Phylogenomic databases

    eggNOGiCOG5077.
    HOGENOMiHOG000160240.
    HOVERGENiHBG018029.
    KOiK11838.
    OMAiAMSDGHN.
    OrthoDBiEOG75B84G.
    PhylomeDBiQ93009.
    TreeFamiTF105667.

    Family and domain databases

    InterProiIPR002083. MATH.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR008974. TRAF-like.
    IPR028889. UCH/PAN2.
    IPR024729. USP7_ICP0-binding_dom.
    IPR029346. USP_C.
    [Graphical view]
    PfamiPF00917. MATH. 1 hit.
    PF00443. UCH. 1 hit.
    PF14533. USP7_C2. 1 hit.
    PF12436. USP7_ICP0_bdg. 1 hit.
    [Graphical view]
    SMARTiSM00061. MATH. 1 hit.
    [Graphical view]
    SUPFAMiSSF49599. SSF49599. 1 hit.
    PROSITEiPS50144. MATH. 1 hit.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q93009-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MNHQQQQQQQ KAGEQQLSEP EDMEMEAGDT DDPPRITQNP VINGNVALSD     50
    GHNTAEEDME DDTSWRSEAT FQFTVERFSR LSESVLSPPC FVRNLPWKIM 100
    VMPRFYPDRP HQKSVGFFLQ CNAESDSTSW SCHAQAVLKI INYRDDEKSF 150
    SRRISHLFFH KENDWGFSNF MAWSEVTDPE KGFIDDDKVT FEVFVQADAP 200
    HGVAWDSKKH TGYVGLKNQG ATCYMNSLLQ TLFFTNQLRK AVYMMPTEGD 250
    DSSKSVPLAL QRVFYELQHS DKPVGTKKLT KSFGWETLDS FMQHDVQELC 300
    RVLLDNVENK MKGTCVEGTI PKLFRGKMVS YIQCKEVDYR SDRREDYYDI 350
    QLSIKGKKNI FESFVDYVAV EQLDGDNKYD AGEHGLQEAE KGVKFLTLPP 400
    VLHLQLMRFM YDPQTDQNIK INDRFEFPEQ LPLDEFLQKT DPKDPANYIL 450
    HAVLVHSGDN HGGHYVVYLN PKGDGKWCKF DDDVVSRCTK EEAIEHNYGG 500
    HDDDLSVRHC TNAYMLVYIR ESKLSEVLQA VTDHDIPQQL VERLQEEKRI 550
    EAQKRKERQE AHLYMQVQIV AEDQFCGHQG NDMYDEEKVK YTVFKVLKNS 600
    SLAEFVQSLS QTMGFPQDQI RLWPMQARSN GTKRPAMLDN EADGNKTMIE 650
    LSDNENPWTI FLETVDPELA ASGATLPKFD KDHDVMLFLK MYDPKTRSLN 700
    YCGHIYTPIS CKIRDLLPVM CDRAGFIQDT SLILYEEVKP NLTERIQDYD 750
    VSLDKALDEL MDGDIIVFQK DDPENDNSEL PTAKEYFRDL YHRVDVIFCD 800
    KTIPNDPGFV VTLSNRMNYF QVAKTVAQRL NTDPMLLQFF KSQGYRDGPG 850
    NPLRHNYEGT LRDLLQFFKP RQPKKLYYQQ LKMKITDFEN RRSFKCIWLN 900
    SQFREEEITL YPDKHGCVRD LLEECKKAVE LGEKASGKLR LLEIVSYKII 950
    GVHQEDELLE CLSPATSRTF RIEEIPLDQV DIDKENEMLV TVAHFHKEVF 1000
    GTFGIPFLLR IHQGEHFREV MKRIQSLLDI QEKEFEKFKF AIVMMGRHQY 1050
    INEDEYEVNL KDFEPQPGNM SHPRPWLGLD HFNKAPKRSR YTYLEKAIKI 1100
    HN 1102
    Length:1,102
    Mass (Da):128,302
    Last modified:November 4, 2008 - v2
    Checksum:iF1A5A5C421396E45
    GO
    Isoform 2 (identifier: Q93009-2)

    Also known as: USP7 beta

    Sequence is not available

    Note: No experimental confirmation available.

    Length:
    Mass (Da):
    Isoform 3 (identifier: Q93009-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-25: MNHQQQQQQQKAGEQQLSEPEDMEM → MAGNHRLGL

    Note: No experimental confirmation available.

    Show »
    Length:1,086
    Mass (Da):126,269
    Checksum:i0CC92229880D2E2B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti201 – 2011H → I AA sequence (PubMed:9034339)Curated
    Sequence conflicti205 – 2051W → P AA sequence (PubMed:9034339)Curated
    Sequence conflicti207 – 2071S → Q AA sequence (PubMed:9034339)Curated
    Sequence conflicti1045 – 10451M → T in CAA96580. (PubMed:9034339)Curated
    Sequence conflicti1066 – 10661Q → T AA sequence (PubMed:9034339)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2525MNHQQ…EDMEM → MAGNHRLGL in isoform 3. 1 PublicationVSP_054884Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z72499 mRNA. Translation: CAA96580.1.
    AK302771 mRNA. Translation: BAH13801.1.
    AC022167 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85194.1.
    CCDSiCCDS32385.1. [Q93009-1]
    CCDS66941.1. [Q93009-3]
    RefSeqiNP_003461.2. NM_003470.2. [Q93009-1]
    UniGeneiHs.386939.

    Genome annotation databases

    EnsembliENST00000344836; ENSP00000343535; ENSG00000187555. [Q93009-1]
    ENST00000381886; ENSP00000371310; ENSG00000187555. [Q93009-3]
    GeneIDi7874.
    KEGGihsa:7874.
    UCSCiuc002czl.2. human. [Q93009-1]

    Polymorphism databases

    DMDMi212276477.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z72499 mRNA. Translation: CAA96580.1 .
    AK302771 mRNA. Translation: BAH13801.1 .
    AC022167 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85194.1 .
    CCDSi CCDS32385.1. [Q93009-1 ]
    CCDS66941.1. [Q93009-3 ]
    RefSeqi NP_003461.2. NM_003470.2. [Q93009-1 ]
    UniGenei Hs.386939.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NB8 X-ray 2.30 A/B 208-560 [» ]
    1NBF X-ray 2.30 A/B/E 208-560 [» ]
    1YY6 X-ray 1.70 A 54-204 [» ]
    1YZE X-ray 2.00 A/B/C 54-205 [» ]
    2F1W X-ray 1.65 A 53-206 [» ]
    2F1X X-ray 2.30 A/B 53-200 [» ]
    2F1Y X-ray 1.70 A 53-198 [» ]
    2F1Z X-ray 3.20 A/B 43-560 [» ]
    2FOJ X-ray 1.60 A 54-205 [» ]
    2FOO X-ray 2.20 A 54-205 [» ]
    2FOP X-ray 2.10 A 54-205 [» ]
    2KVR NMR - A 537-664 [» ]
    2XXN X-ray 1.60 A 63-205 [» ]
    2YLM X-ray 2.70 A 560-1084 [» ]
    3MQR X-ray 1.80 A 54-205 [» ]
    3MQS X-ray 2.40 C 54-205 [» ]
    4JJQ X-ray 1.95 A 54-205 [» ]
    4KG9 X-ray 1.70 A 54-205 [» ]
    4M5W X-ray 2.24 A 207-560 [» ]
    4M5X X-ray 2.19 A/B 207-560 [» ]
    4PYZ X-ray 2.84 A/B 537-793 [» ]
    ProteinModelPortali Q93009.
    SMRi Q93009. Positions 63-554, 560-1083.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113622. 200 interactions.
    DIPi DIP-29053N.
    IntActi Q93009. 105 interactions.
    MINTi MINT-234628.
    STRINGi 9606.ENSP00000343535.

    Chemistry

    ChEMBLi CHEMBL2157850.

    Protein family/group databases

    MEROPSi C19.016.

    PTM databases

    PhosphoSitei Q93009.

    Polymorphism databases

    DMDMi 212276477.

    Proteomic databases

    MaxQBi Q93009.
    PaxDbi Q93009.
    PRIDEi Q93009.

    Protocols and materials databases

    DNASUi 7874.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344836 ; ENSP00000343535 ; ENSG00000187555 . [Q93009-1 ]
    ENST00000381886 ; ENSP00000371310 ; ENSG00000187555 . [Q93009-3 ]
    GeneIDi 7874.
    KEGGi hsa:7874.
    UCSCi uc002czl.2. human. [Q93009-1 ]

    Organism-specific databases

    CTDi 7874.
    GeneCardsi GC16M008985.
    H-InvDB HIX0038590.
    HGNCi HGNC:12630. USP7.
    HPAi CAB008108.
    HPA015641.
    MIMi 602519. gene.
    neXtProti NX_Q93009.
    PharmGKBi PA37255.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5077.
    HOGENOMi HOG000160240.
    HOVERGENi HBG018029.
    KOi K11838.
    OMAi AMSDGHN.
    OrthoDBi EOG75B84G.
    PhylomeDBi Q93009.
    TreeFami TF105667.

    Enzyme and pathway databases

    SignaLinki Q93009.

    Miscellaneous databases

    EvolutionaryTracei Q93009.
    GeneWikii USP7.
    GenomeRNAii 7874.
    NextBioi 30332.
    PROi Q93009.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q93009.
    Bgeei Q93009.
    CleanExi HS_USP7.
    Genevestigatori Q93009.

    Family and domain databases

    InterProi IPR002083. MATH.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR008974. TRAF-like.
    IPR028889. UCH/PAN2.
    IPR024729. USP7_ICP0-binding_dom.
    IPR029346. USP_C.
    [Graphical view ]
    Pfami PF00917. MATH. 1 hit.
    PF00443. UCH. 1 hit.
    PF14533. USP7_C2. 1 hit.
    PF12436. USP7_ICP0_bdg. 1 hit.
    [Graphical view ]
    SMARTi SM00061. MATH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49599. SSF49599. 1 hit.
    PROSITEi PS50144. MATH. 1 hit.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein."
      Everett R.D., Meredith M., Orr A., Cross A., Kathoria M., Parkinson J.
      EMBO J. 16:566-577(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Mammary cancer.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product."
      Hong S., Kim S.J., Ka S., Choi I., Kang S.
      Mol. Cell. Neurosci. 20:298-306(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 705-1102 (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH ATXN1.
    6. "Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization."
      Li M., Chen D., Shiloh A., Luo J., Nikolaev A.Y., Qin J., Gu W.
      Nature 416:648-653(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53, MUTAGENESIS OF CYS-223.
    7. "Protein interaction domains of the ubiquitin-specific protease, USP7/HAUSP."
      Holowaty M.N., Sheng Y., Nguyen T., Arrowsmith C., Frappier L.
      J. Biol. Chem. 278:47753-47761(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, INTERACTION WITH HERPESVIRUS 1 TRANS-ACTING TRANSCRIPTIONAL PROTEIN ICP0/VMW110 AND EBV EBNA1.
    8. "A dynamic role of HAUSP in the p53-Mdm2 pathway."
      Li M., Brooks C.L., Kon N., Gu W.
      Mol. Cell 13:879-886(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MDM2, MUTAGENESIS OF CYS-223.
    9. "Reciprocal activities between herpes simplex virus type 1 regulatory protein ICP0, a ubiquitin E3 ligase, and ubiquitin-specific protease USP7."
      Boutell C., Canning M., Orr A., Everett R.D.
      J. Virol. 79:12342-12354(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION, INTERACTION WITH HERPESVIRUS 1 TRANS-ACTING TRANSCRIPTIONAL PROTEIN ICP0/VMW110.
    10. Cited for: IDENTIFICATION IN A COMPLEX WITH DAXX AND MDM2, INTERACTION WITH DAXX, SUBCELLULAR LOCATION.
    11. Cited for: FUNCTION, INTERACTION WITH FOXO4, MUTAGENESIS OF CYS-223.
    12. "Biochemical characterization of USP7 reveals post-translational modification sites and structural requirements for substrate processing and subcellular localization."
      Fernandez-Montalvan A., Bouwmeester T., Joberty G., Mader R., Mahnke M., Pierrat B., Schlaeppi J.M., Worpenberg S., Gerhartz B.
      FEBS J. 274:4256-4270(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, PHOSPHORYLATION AT SER-18 AND SER-963, UBIQUITINATION AT LYS-869, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    13. "The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex."
      Song M.S., Song S.J., Kim S.Y., Oh H.J., Lim D.S.
      EMBO J. 27:1863-1874(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH DAXX; RASSF1 AND MDM2, INTERACTION WITH DAXX AND MDM2.
    14. "AAA ATPase p97 and adaptor UBXD1 suppress MDM2 ubiquitination and degradation and promote constitutive p53 turnover."
      Zweitzig D.R., Shcherbik N., Haines D.S.
      Mol. Biol. Cell 19:5029-5029(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBXN6.
    15. "The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network."
      Song M.S., Salmena L., Carracedo A., Egia A., Lo-Coco F., Teruya-Feldstein J., Pandolfi P.P.
      Nature 455:813-817(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PTEN, MUTAGENESIS OF CYS-223, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-963, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Identification of a novel higher molecular weight isoform of USP7/HAUSP that interacts with the Herpes simplex virus type-1 immediate early protein ICP0."
      Antrobus R., Boutell C.
      Virus Res. 137:64-71(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HERPESVIRUS 1 TRANS-ACTING TRANSCRIPTIONAL PROTEIN ICP0/VMW110, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, ALTERNATIVE SPLICING (ISOFORM 2).
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-869; LYS-1084 AND LYS-1096, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Daxx is reciprocally regulated by Mdm2 and Hausp."
      Tang J., Qu L., Pang M., Yang X.
      Biochem. Biophys. Res. Commun. 393:542-545(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "TSPYL5 suppresses p53 levels and function by physical interaction with USP7."
      Epping M.T., Meijer L.A., Krijgsman O., Bos J.L., Pandolfi P.P., Bernards R.
      Nat. Cell Biol. 13:102-108(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TSPYL5.
    24. "The USP7/Dnmt1 complex stimulates the DNA methylation activity of Dnmt1 and regulates the stability of UHRF1."
      Felle M., Joppien S., Nemeth A., Diermeier S., Thalhammer V., Dobner T., Kremmer E., Kappler R., Langst G.
      Nucleic Acids Res. 39:8355-8365(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DNMT1 AND UHRF1, MUTAGENESIS OF CYS-223.
    25. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "M phase phosphorylation of the epigenetic regulator UHRF1 regulates its physical association with the deubiquitylase USP7 and stability."
      Ma H., Chen H., Guo X., Wang Z., Sowa M.E., Zheng L., Hu S., Zeng P., Guo R., Diao J., Lan F., Harper J.W., Shi Y.G., Xu Y., Shi Y.
      Proc. Natl. Acad. Sci. U.S.A. 109:4828-4833(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UHRF1, MUTAGENESIS OF CYS-223.
    27. "Profiling ubiquitin linkage specificities of deubiquitinating enzymes with branched ubiquitin isopeptide probes."
      Iphofer A., Kummer A., Nimtz M., Ritter A., Arnold T., Frank R., van den Heuvel J., Kessler B.M., Jansch L., Franke R.
      ChemBioChem 13:1416-1420(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, LINKAGE SPECIFICITY.
    28. "The RNA-binding E3 ubiquitin ligase MEX-3C links ubiquitination with MHC-I mRNA degradation."
      Cano F., Bye H., Duncan L.M., Buchet-Poyau K., Billaud M., Wills M.R., Lehner P.J.
      EMBO J. 31:3596-3606(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MEX3C.
    29. Cited for: FUNCTION, INTERACTION WITH UVSSA.
    30. "Mutations in UVSSA cause UV-sensitive syndrome and destabilize ERCC6 in transcription-coupled DNA repair."
      Zhang X., Horibata K., Saijo M., Ishigami C., Ukai A., Kanno S.I., Tahara H., Neilan E.G., Honma M., Nohmi T., Yasui A., Tanaka K.
      Nat. Genet. 44:593-597(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH UVSSA.
    31. "Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde."
      Hu M., Li P., Li M., Li W., Yao T., Wu J.-W., Gu W., Cohen R.E., Shi Y.
      Cell 111:1041-1054(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 208-560 IN COMPLEX WITH UBIQUITIN, MUTAGENESIS OF CYS-223; HIS-456 AND HIS-464, INTERACTION WITH TP53.
    32. "Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization."
      Saridakis V., Sheng Y., Sarkari F., Holowaty M.N., Shire K., Nguyen T., Zhang R.G., Liao J., Lee W., Edwards A.M., Arrowsmith C.H., Frappier L.
      Mol. Cell 18:25-36(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 54-205 IN COMPLEX WITH EBNA1, INTERACTION WITH EBV EBNA1.
    33. "Structural basis of competitive recognition of p53 and MDM2 by HAUSP/USP7: implications for the regulation of the p53-MDM2 pathway."
      Hu M., Gu L., Li M., Jeffrey P.D., Gu W., Shi Y.
      PLoS Biol. 4:228-239(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 43-560 IN COMPLEX WITH TP53 AND MDM2, INTERACTION WITH TP53 AND MDM2.
    34. Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 54-205 IN COMPLEX WITH TP53 AND MDM2, INTERACTION WITH TP53 AND MDM2, MUTAGENESIS OF ASP-164 AND TRP-165.

    Entry informationi

    Entry nameiUBP7_HUMAN
    AccessioniPrimary (citable) accession number: Q93009
    Secondary accession number(s): A6NMY8, B7Z815, H0Y3G8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 159 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3