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Q9Y5T5

- UBP16_HUMAN

UniProt

Q9Y5T5 - UBP16_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 16

Gene

USP16

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome segregation when cells enter into mitosis. In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B.2 PublicationsUniRule annotation

    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).1 PublicationUniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi24 – 241Zinc 1
    Metal bindingi26 – 261Zinc 1
    Metal bindingi48 – 481Zinc 2
    Metal bindingi51 – 511Zinc 2
    Metal bindingi74 – 741Zinc 3
    Metal bindingi77 – 771Zinc 3
    Metal bindingi82 – 821Zinc 2
    Metal bindingi90 – 901Zinc 2
    Metal bindingi94 – 941Zinc 3
    Metal bindingi103 – 1031Zinc 3
    Metal bindingi116 – 1161Zinc 1
    Metal bindingi119 – 1191Zinc 1
    Active sitei205 – 2051Nucleophile
    Active sitei758 – 7581Proton acceptorUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri60 – 12566UBP-typeUniRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. histone binding Source: UniProtKB
    3. transcription coactivator activity Source: UniProtKB
    4. ubiquitin binding Source: UniProtKB
    5. ubiquitin-specific protease activity Source: UniProtKB
    6. ubiquitin thiolesterase activity Source: UniProtKB
    7. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: ProtInc
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. histone deubiquitination Source: UniProtKB
    4. histone H2A K63-linked deubiquitination Source: UniProtKB
    5. mitotic nuclear division Source: UniProtKB
    6. monoubiquitinated histone H2A deubiquitination Source: UniProtKB
    7. positive regulation of transcription, DNA-templated Source: UniProtKB
    8. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    9. positive regulation of translational elongation Source: UniProtKB
    10. protein homotetramerization Source: UniProtKB
    11. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    12. transcription, DNA-templated Source: UniProtKB-KW
    13. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiC19.021.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 16UniRule annotation (EC:3.4.19.12UniRule annotation)
    Alternative name(s):
    Deubiquitinating enzyme 16UniRule annotation
    Ubiquitin thioesterase 16UniRule annotation
    Ubiquitin-processing protease UBP-M
    Ubiquitin-specific-processing protease 16UniRule annotation
    Gene namesi
    Name:USP16UniRule annotation
    ORF Names:MSTP039
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 21

    Organism-specific databases

    HGNCiHGNC:12614. USP16.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving USP16 is a cause of Chronic myelomonocytic leukemia. Inversion inv(21) (q21;q22) with RUNX1/AML1.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi205 – 2051C → S: Loss of enzyme activity. 3 Publications

    Organism-specific databases

    PharmGKBiPA37240.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 823823Ubiquitin carboxyl-terminal hydrolase 16PRO_0000080643Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei415 – 4151Phosphoserine3 Publications
    Modified residuei552 – 5521Phosphoserine4 Publications
    Modified residuei554 – 5541Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylated at the onset of mitosis and dephosphorylated during the metaphase/anaphase transition. Phosphorylation by AURKB enhances the deubiquitinase activity.5 PublicationsUniRule annotation

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y5T5.
    PaxDbiQ9Y5T5.
    PRIDEiQ9Y5T5.

    PTM databases

    PhosphoSiteiQ9Y5T5.

    Expressioni

    Tissue specificityi

    Present in all the tissues examined including fetal brain, lung, liver, kidney, and adult heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y5T5.
    BgeeiQ9Y5T5.
    CleanExiHS_USP16.
    GenevestigatoriQ9Y5T5.

    Organism-specific databases

    HPAiHPA021140.

    Interactioni

    Subunit structurei

    Homotetramer.1 PublicationUniRule annotation

    Protein-protein interaction databases

    BioGridi115848. 16 interactions.
    IntActiQ9Y5T5. 4 interactions.

    Structurei

    Secondary structure

    1
    823
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 304
    Helixi33 – 408
    Beta strandi45 – 473
    Helixi49 – 524
    Turni63 – 653
    Beta strandi71 – 744
    Turni75 – 773
    Beta strandi80 – 823
    Beta strandi86 – 883
    Helixi90 – 967
    Beta strandi105 – 1084
    Turni109 – 1113
    Beta strandi114 – 1163
    Turni117 – 1204
    Beta strandi121 – 1233
    Helixi130 – 14213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I50NMR-A22-143[»]
    ProteinModelPortaliQ9Y5T5.
    SMRiQ9Y5T5. Positions 22-427, 629-819.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y5T5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini196 – 822627USPAdd
    BLAST

    Domaini

    The UBP-type zinc finger binds 3 zinc ions that form a pair of cross-braced ring fingers encapsulated within a third zinc finger in the primary structure. It recognizes the C-terminal tail of free ubiquitin.

    Sequence similaritiesi

    Belongs to the peptidase C19 family. USP16 subfamily.UniRule annotation
    Contains 1 UBP-type zinc finger.UniRule annotation
    Contains 1 USP domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri60 – 12566UBP-typeUniRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5560.
    HOVERGENiHBG062704.
    InParanoidiQ9Y5T5.
    KOiK11844.
    OMAiECSIQHC.
    OrthoDBiEOG7J9VNZ.
    PhylomeDBiQ9Y5T5.
    TreeFamiTF326075.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    HAMAPiMF_03062. UBP16.
    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view]
    PfamiPF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view]
    PROSITEiPS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS50271. ZF_UBP. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y5T5-1) [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

    MGKKRTKGKT VPIDDSSETL EPVCRHIRKG LEQGNLKKAL VNVEWNICQD    50
    CKTDNKVKDK AEEETEEKPS VWLCLKCGHQ GCGRNSQEQH ALKHYLTPRS 100
    EPHCLVLSLD NWSVWCYVCD NEVQYCSSNQ LGQVVDYVRK QASITTPKPA 150
    EKDNGNIELE NKKLEKESKN EQEREKKENM AKENPPMNSP CQITVKGLSN 200
    LGNTCFFNAV MQNLSQTPVL RELLKEVKMS GTIVKIEPPD LALTEPLEIN 250
    LEPPGPLTLA MSQFLNEMQE TKKGVVTPKE LFSQVCKKAV RFKGYQQQDS 300
    QELLRYLLDG MRAEEHQRVS KGILKAFGNS TEKLDEELKN KVKDYEKKKS 350
    MPSFVDRIFG GELTSMIMCD QCRTVSLVHE SFLDLSLPVL DDQSGKKSVN 400
    DKNLKKTVED EDQDSEEEKD NDSYIKERSD IPSGTSKHLQ KKAKKQAKKQ 450
    AKNQRRQQKI QGKVLHLNDI CTIDHPEDSE YEAEMSLQGE VNIKSNHISQ 500
    EGVMHKEYCV NQKDLNGQAK MIESVTDNQK STEEVDMKNI NMDNDLEVLT 550
    SSPTRNLNGA YLTEGSNGEV DISNGFKNLN LNAALHPDEI NIEILNDSHT 600
    PGTKVYEVVN EDPETAFCTL ANREVFNTDE CSIQHCLYQF TRNEKLRDAN 650
    KLLCEVCTRR QCNGPKANIK GERKHVYTNA KKQMLISLAP PVLTLHLKRF 700
    QQAGFNLRKV NKHIKFPEIL DLAPFCTLKC KNVAEENTRV LYSLYGVVEH 750
    SGTMRSGHYT AYAKARTANS HLSNLVLHGD IPQDFEMESK GQWFHISDTH 800
    VQAVPTTKVL NSQAYLLFYE RIL 823
    Length:823
    Mass (Da):93,570
    Last modified:November 1, 1999 - v1
    Checksum:iC7D4175649BA3E31
    GO
    Isoform 2 (identifier: Q9Y5T5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         150-150: Missing.

    Show »
    Length:822
    Mass (Da):93,499
    Checksum:i36FD67E22FA078AB
    GO
    Isoform 3 (identifier: Q9Y5T5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-20: MGKKRTKGKTVPIDDSSETL → MGSVAV
         150-150: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:808
    Mass (Da):91,870
    Checksum:iE4528720234CB7B7
    GO
    Isoform 4 (identifier: Q9Y5T5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-310: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:513
    Mass (Da):58,397
    Checksum:i9AD260CF2FE530A9
    GO
    Isoform 5 (identifier: Q9Y5T5-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         394-823: SGKKSVNDKN...AYLLFYERIL → VRLLNLFYSSRFFFL

    Show »
    Length:408
    Mass (Da):46,599
    Checksum:i5B3EB300F72F4E04
    GO

    Sequence cautioni

    The sequence AAG39290.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAG51175.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti141 – 1411Q → E in AAG39290. 1 PublicationCurated
    Sequence conflicti297 – 2971Q → R in BAG51175. (PubMed:14702039)Curated
    Sequence conflicti348 – 3481K → E in BAD96604. 1 PublicationCurated
    Sequence conflicti350 – 3501S → P in BAD96401. 1 PublicationCurated
    Sequence conflicti480 – 4812EY → DN in AAH30777. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti141 – 1411Q → H.2 Publications
    Corresponds to variant rs2274802 [ dbSNP | Ensembl ].
    VAR_020388

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 310310Missing in isoform 4. 1 PublicationVSP_036713Add
    BLAST
    Alternative sequencei1 – 2020MGKKR…SSETL → MGSVAV in isoform 3. 1 PublicationVSP_036714Add
    BLAST
    Alternative sequencei150 – 1501Missing in isoform 2 and isoform 3. 2 PublicationsVSP_036715
    Alternative sequencei394 – 823430SGKKS…YERIL → VRLLNLFYSSRFFFL in isoform 5. 1 PublicationVSP_036716Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126736 mRNA. Translation: AAD20949.1.
    AY333928 mRNA. Translation: AAR13293.1.
    AK023247 mRNA. Translation: BAG51175.1. Different initiation.
    AK302247 mRNA. Translation: BAG63599.1.
    AK294284 mRNA. Translation: BAG57569.1.
    AK222681 mRNA. Translation: BAD96401.1.
    AK222884 mRNA. Translation: BAD96604.1.
    AL163249 Genomic DNA. Translation: CAB90432.1.
    AF129075 Genomic DNA. No translation available.
    CH471079 Genomic DNA. Translation: EAX09927.1.
    CH471079 Genomic DNA. Translation: EAX09929.1.
    BC030777 mRNA. Translation: AAH30777.1.
    AF113219 mRNA. Translation: AAG39290.1. Different initiation.
    CCDSiCCDS13583.1. [Q9Y5T5-1]
    CCDS42912.1. [Q9Y5T5-2]
    RefSeqiNP_001001992.1. NM_001001992.1. [Q9Y5T5-2]
    NP_001027582.1. NM_001032410.1. [Q9Y5T5-1]
    NP_006438.1. NM_006447.2. [Q9Y5T5-1]
    UniGeneiHs.99819.

    Genome annotation databases

    EnsembliENST00000334352; ENSP00000334808; ENSG00000156256. [Q9Y5T5-1]
    ENST00000399975; ENSP00000382857; ENSG00000156256. [Q9Y5T5-2]
    ENST00000399976; ENSP00000382858; ENSG00000156256. [Q9Y5T5-1]
    GeneIDi10600.
    KEGGihsa:10600.
    UCSCiuc002ymw.3. human. [Q9Y5T5-1]
    uc002ymx.3. human. [Q9Y5T5-2]
    uc011acm.2. human. [Q9Y5T5-3]

    Polymorphism databases

    DMDMi6686071.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF126736 mRNA. Translation: AAD20949.1 .
    AY333928 mRNA. Translation: AAR13293.1 .
    AK023247 mRNA. Translation: BAG51175.1 . Different initiation.
    AK302247 mRNA. Translation: BAG63599.1 .
    AK294284 mRNA. Translation: BAG57569.1 .
    AK222681 mRNA. Translation: BAD96401.1 .
    AK222884 mRNA. Translation: BAD96604.1 .
    AL163249 Genomic DNA. Translation: CAB90432.1 .
    AF129075 Genomic DNA. No translation available.
    CH471079 Genomic DNA. Translation: EAX09927.1 .
    CH471079 Genomic DNA. Translation: EAX09929.1 .
    BC030777 mRNA. Translation: AAH30777.1 .
    AF113219 mRNA. Translation: AAG39290.1 . Different initiation.
    CCDSi CCDS13583.1. [Q9Y5T5-1 ]
    CCDS42912.1. [Q9Y5T5-2 ]
    RefSeqi NP_001001992.1. NM_001001992.1. [Q9Y5T5-2 ]
    NP_001027582.1. NM_001032410.1. [Q9Y5T5-1 ]
    NP_006438.1. NM_006447.2. [Q9Y5T5-1 ]
    UniGenei Hs.99819.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I50 NMR - A 22-143 [» ]
    ProteinModelPortali Q9Y5T5.
    SMRi Q9Y5T5. Positions 22-427, 629-819.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115848. 16 interactions.
    IntActi Q9Y5T5. 4 interactions.

    Protein family/group databases

    MEROPSi C19.021.

    PTM databases

    PhosphoSitei Q9Y5T5.

    Polymorphism databases

    DMDMi 6686071.

    Proteomic databases

    MaxQBi Q9Y5T5.
    PaxDbi Q9Y5T5.
    PRIDEi Q9Y5T5.

    Protocols and materials databases

    DNASUi 10600.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334352 ; ENSP00000334808 ; ENSG00000156256 . [Q9Y5T5-1 ]
    ENST00000399975 ; ENSP00000382857 ; ENSG00000156256 . [Q9Y5T5-2 ]
    ENST00000399976 ; ENSP00000382858 ; ENSG00000156256 . [Q9Y5T5-1 ]
    GeneIDi 10600.
    KEGGi hsa:10600.
    UCSCi uc002ymw.3. human. [Q9Y5T5-1 ]
    uc002ymx.3. human. [Q9Y5T5-2 ]
    uc011acm.2. human. [Q9Y5T5-3 ]

    Organism-specific databases

    CTDi 10600.
    GeneCardsi GC21P030396.
    H-InvDB HIX0023011.
    HGNCi HGNC:12614. USP16.
    HPAi HPA021140.
    MIMi 604735. gene.
    neXtProti NX_Q9Y5T5.
    PharmGKBi PA37240.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5560.
    HOVERGENi HBG062704.
    InParanoidi Q9Y5T5.
    KOi K11844.
    OMAi ECSIQHC.
    OrthoDBi EOG7J9VNZ.
    PhylomeDBi Q9Y5T5.
    TreeFami TF326075.

    Miscellaneous databases

    ChiTaRSi USP16. human.
    EvolutionaryTracei Q9Y5T5.
    GeneWikii USP16.
    GenomeRNAii 10600.
    NextBioi 40254.
    PROi Q9Y5T5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y5T5.
    Bgeei Q9Y5T5.
    CleanExi HS_USP16.
    Genevestigatori Q9Y5T5.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    HAMAPi MF_03062. UBP16.
    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR001607. Znf_UBP.
    [Graphical view ]
    Pfami PF00443. UCH. 1 hit.
    PF02148. zf-UBP. 1 hit.
    [Graphical view ]
    PROSITEi PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS50271. ZF_UBP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A mutant deubiquitinating enzyme (Ubp-M) associates with mitotic chromosomes and blocks cell division."
      Cai S.-Y., Babbitt R.W., Marchesi V.T.
      Proc. Natl. Acad. Sci. U.S.A. 96:2828-2833(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, MUTAGENESIS OF CYS-205.
    2. Grimbert P., Pawlak A., Sahali D.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    3. "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] (ISOFORMS 3 AND 4), VARIANT HIS-141.
      Tissue: Amygdala, Teratocarcinoma and Testis.
    4. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain and Liver.
    5. "The DNA sequence of human chromosome 21."
      Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A.
      , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
      Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT HIS-141.
      Tissue: Testis.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-823.
      Tissue: Aorta.
    9. "Caspase-dependent deubiquitination of monoubiquitinated nucleosomal histone H2A induced by diverse apoptogenic stimuli."
      Mimnaugh E.G., Kayastha G., McGovern N.B., Hwang S.G., Marcu M.G., Trepel J., Cai S.-Y., Marchesi V.T., Neckers L.
      Cell Death Differ. 8:1182-1196(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY FUNCTION, MUTAGENESIS OF CYS-205.
    10. "Regulation of cell cycle progression and gene expression by H2A deubiquitination."
      Joo H.-Y., Zhai L., Yang C., Nie S., Erdjument-Bromage H., Tempst P., Chang C., Wang H.
      Nature 449:1068-1072(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-205.
    11. Cited for: CHROMOSOMAL REARRANGEMENT.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415 AND SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-552 AND THR-554, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-415, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: POSSIBLE INVOLVEMENT IN DOWN SYNDROME.
    19. "Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin."
      Pai M.-T., Tzeng S.-R., Kovacs J.J., Keaton M.A., Li S.S.-C., Yao T.-P., Zhou P.
      J. Mol. Biol. 370:290-302(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 22-143, ZINC-BINDING.

    Entry informationi

    Entry nameiUBP16_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y5T5
    Secondary accession number(s): A8MU43
    , B3KN13, B4DFV8, B4DY37, D3DSD9, Q53GP7, Q53HA0, Q5VKN8, Q8NEL3, Q9H3E6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 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

    Miscellaneous

    USP16 may contribute to somatic stem cell defects observed in Down syndrome. USP16 is triplicated in Down syndrome and its overexpression may contribute to proliferation defects in stem cells. Reduction of USP16 levels results in increased proliferation capacity of Down syndrome fibroblasts (PubMed:24025767).1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 21
      Human chromosome 21: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3