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O94966

- UBP19_HUMAN

UniProt

O94966 - UBP19_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 19

Gene

USP19

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (10 Jul 2007)
      Previous versions | rss
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    Functioni

    Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic-reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing their ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non-catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked Ubiquitin chains.4 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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei506 – 5061NucleophilePROSITE-ProRule annotation
    Active sitei1165 – 11651Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri791 – 83343MYND-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. ubiquitin-specific protease activity Source: UniProtKB

    GO - Biological processi

    1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    2. negative regulation of skeletal muscle tissue development Source: UniProtKB
    3. positive regulation of cell cycle process Source: UniProtKB
    4. protein deubiquitination Source: UniProtKB
    5. regulation of cellular response to hypoxia Source: UniProtKB
    6. regulation of protein stability Source: UniProtKB
    7. response to endoplasmic reticulum stress Source: UniProtKB
    8. skeletal muscle atrophy Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiC19.024.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 19 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 19
    Ubiquitin thioesterase 19
    Ubiquitin-specific-processing protease 19
    Zinc finger MYND domain-containing protein 9
    Gene namesi
    Name:USP19
    Synonyms:KIAA0891, ZMYND9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:12617. USP19.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Single-pass membrane protein 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. endoplasmic reticulum membrane Source: UniProtKB
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37243.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13181318Ubiquitin carboxyl-terminal hydrolase 19PRO_0000080646Add
    BLAST

    Proteomic databases

    MaxQBiO94966.
    PaxDbiO94966.
    PRIDEiO94966.

    PTM databases

    PhosphoSiteiO94966.

    Expressioni

    Gene expression databases

    ArrayExpressiO94966.
    BgeeiO94966.
    CleanExiHS_USP19.
    GenevestigatoriO94966.

    Interactioni

    Subunit structurei

    Interacts with RNF123 By similarity. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts with HIF1A (via N-terminus).By similarity2 Publications

    Protein-protein interaction databases

    BioGridi116078. 58 interactions.
    IntActiO94966. 49 interactions.
    MINTiMINT-4658026.
    STRINGi9606.ENSP00000381863.

    Structurei

    Secondary structure

    1
    1318
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi276 – 2783
    Beta strandi279 – 2835
    Beta strandi287 – 2926
    Turni293 – 2953
    Beta strandi296 – 3027
    Beta strandi312 – 3154
    Beta strandi317 – 3248
    Helixi329 – 3346
    Beta strandi344 – 3529
    Turni356 – 3583
    Beta strandi360 – 3634
    Beta strandi365 – 37713

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WH0NMR-A273-393[»]
    ProteinModelPortaliO94966.
    SMRiO94966. Positions 273-402, 494-677, 996-1215.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO94966.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 12911291CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1313 – 13186LumenalSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1292 – 131221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini113 – 20290CS 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini282 – 384103CS 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini497 – 1214718USPAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 2 CS domains.PROSITE-ProRule annotation
    Contains 1 MYND-type zinc finger.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri791 – 83343MYND-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Transmembrane, Transmembrane helix, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5560.
    HOGENOMiHOG000074206.
    HOVERGENiHBG061889.
    KOiK11847.
    OMAiPQCKQHR.
    PhylomeDBiO94966.
    TreeFamiTF106276.

    Family and domain databases

    Gene3Di2.60.40.790. 2 hits.
    InterProiIPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR002893. Znf_MYND.
    [Graphical view]
    PfamiPF04969. CS. 2 hits.
    PF00443. UCH. 1 hit.
    PF01753. zf-MYND. 1 hit.
    [Graphical view]
    SUPFAMiSSF49764. SSF49764. 2 hits.
    PROSITEiPS51203. CS. 2 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS01360. ZF_MYND_1. 1 hit.
    PS50865. ZF_MYND_2. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O94966-1) [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

    MSGGASATGP RRGPPGLEDT TSKKKQKDRA NQESKDGDPR KETGSRYVAQ     50
    AGLEPLASGD PSASASHAAG ITGSRHRTRL FFPSSSGSAS TPQEEQTKEG 100
    ACEDPHDLLA TPTPELLLDW RQSAEEVIVK LRVGVGPLQL EDVDAAFTDT 150
    DCVVRFAGGQ QWGGVFYAEI KSSCAKVQTR KGSLLHLTLP KKVPMLTWPS 200
    LLVEADEQLC IPPLNSQTCL LGSEENLAPL AGEKAVPPGN DPVSPAMVRS 250
    RNPGKDDCAK EEMAVAADAA TLVDEPESMV NLAFVKNDSY EKGPDSVVVH 300
    VYVKEICRDT SRVLFREQDF TLIFQTRDGN FLRLHPGCGP HTTFRWQVKL 350
    RNLIEPEQCT FCFTASRIDI CLRKRQSQRW GGLEAPAARV GGAKVAVPTG 400
    PTPLDSTPPG GAPHPLTGQE EARAVEKDKS KARSEDTGLD SVATRTPMEH 450
    VTPKPETHLA SPKPTCMVPP MPHSPVSGDS VEEEEEEEKK VCLPGFTGLV 500
    NLGNTCFMNS VIQSLSNTRE LRDFFHDRSF EAEINYNNPL GTGGRLAIGF 550
    AVLLRALWKG THHAFQPSKL KAIVASKASQ FTGYAQHDAQ EFMAFLLDGL 600
    HEDLNRIQNK PYTETVDSDG RPDEVVAEEA WQRHKMRNDS FIVDLFQGQY 650
    KSKLVCPVCA KVSITFDPFL YLPVPLPQKQ KVLPVFYFAR EPHSKPIKFL 700
    VSVSKENSTA SEVLDSLSQS VHVKPENLRL AEVIKNRFHR VFLPSHSLDT 750
    VSPSDTLLCF ELLSSELAKE RVVVLEVQQR PQVPSVPISK CAACQRKQQS 800
    EDEKLKRCTR CYRVGYCNQL CQKTHWPDHK GLCRPENIGY PFLVSVPASR 850
    LTYARLAQLL EGYARYSVSV FQPPFQPGRM ALESQSPGCT TLLSTGSLEA 900
    GDSERDPIQP PELQLVTPMA EGDTGLPRVW AAPDRGPVPS TSGISSEMLA 950
    SGPIEVGSLP AGERVSRPEA AVPGYQHPSE AMNAHTPQFF IYKIDSSNRE 1000
    QRLEDKGDTP LELGDDCSLA LVWRNNERLQ EFVLVASKEL ECAEDPGSAG 1050
    EAARAGHFTL DQCLNLFTRP EVLAPEEAWY CPQCKQHREA SKQLLLWRLP 1100
    NVLIVQLKRF SFRSFIWRDK INDLVEFPVR NLDLSKFCIG QKEEQLPSYD 1150
    LYAVINHYGG MIGGHYTACA RLPNDRSSQR SDVGWRLFDD STVTTVDESQ 1200
    VVTRYAYVLF YRRRNSPVER PPRAGHSEHH PDLGPAAEAA ASQASRIWQE 1250
    LEAEEEPVPE GSGPLGPWGP QDWVGPLPRG PTTPDEGCLR YFVLGTVAAL 1300
    VALVLNVFYP LVSQSRWR 1318
    Length:1,318
    Mass (Da):145,651
    Last modified:July 10, 2007 - v2
    Checksum:iEA9F318D03304AA1
    GO
    Isoform 2 (identifier: O94966-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         100-114: Missing.
         202-202: L → LKKPLGTQEL...PPFVADPATQ
         573-574: IV → RL
         575-1318: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:660
    Mass (Da):71,090
    Checksum:i3DEF7C14294E7E92
    GO
    Isoform 3 (identifier: O94966-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1244-1298: ASRIWQELEA...LRYFVLGTVA → GLGPGQAPEV...PTYSNMEEVD
         1299-1318: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,281
    Mass (Da):141,413
    Checksum:i442FF7C6DE59AE94
    GO
    Isoform 4 (identifier: O94966-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         100-114: Missing.
         389-389: R → RGA
         1244-1298: ASRIWQELEA...LRYFVLGTVA → GLGPGQAPEV...PTYSNMEEVD
         1299-1318: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:1,268
    Mass (Da):140,022
    Checksum:iCD9BFE22C20EB03E
    GO
    Isoform 5 (identifier: O94966-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         202-202: L → LKKPLGTQEL...PPFVADPATQ

    Note: No experimental confirmation available.

    Show »
    Length:1,419
    Mass (Da):156,035
    Checksum:i0FCD06C7B0C80C4E
    GO
    Isoform 6 (identifier: O94966-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         202-202: L → LKKPLGTQEL...PPFVADPATQ
         389-389: R → RGA
         1244-1298: ASRIWQELEA...LRYFVLGTVA → GLGPGQAPEV...PTYSNMEEVD
         1299-1318: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,384
    Mass (Da):151,925
    Checksum:iCC8F00B6C0033058
    GO
    Isoform 7 (identifier: O94966-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         193-202: VPMLTWPSLL → KKPLGTQELV...PPFVADPATQ
         1244-1298: ASRIWQELEA...LRYFVLGTVA → GLGPGQAPEV...PTYSNMEEVD
         1299-1318: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,372
    Mass (Da):150,659
    Checksum:i982B811383529FEE
    GO

    Sequence cautioni

    The sequence AAI06030.1 differs from that shown. Reason: Frameshift at position 572.
    The sequence AAI06030.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAI42661.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAA74914.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti942 – 9421S → C in BAG57894. (PubMed:14702039)Curated
    Sequence conflicti1041 – 10411E → G in BAG62152. (PubMed:14702039)Curated
    Isoform 4 (identifier: O94966-4)
    Sequence conflicti1251 – 12511A → T in AAH82241. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361D → H.
    Corresponds to variant rs11552724 [ dbSNP | Ensembl ].
    VAR_051528

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei100 – 11415Missing in isoform 2 and isoform 4. 1 PublicationVSP_026708Add
    BLAST
    Alternative sequencei193 – 20210VPMLTWPSLL → KKPLGTQELVPGLRCQENGQ ELSPIALEPGPEPHRAKQEA RNQKRAQGRGEVGAGAGPGA QAGPSAKRAVHLCRGPEGDG SRDDPGPRGDAPPFVADPAT Q in isoform 7. 1 PublicationVSP_047057
    Alternative sequencei202 – 2021L → LKKPLGTQELVPGLRCQENG QELSPIALEPGPEPHRAKQE ARNQKRAQGRGEVGAGAGPG AQAGPSAKRAVHLCRGPEGD GSRDDPGPRGDAPPFVADPA TQ in isoform 2, isoform 5 and isoform 6. 2 PublicationsVSP_026709
    Alternative sequencei389 – 3891R → RGA in isoform 4 and isoform 6. 1 PublicationVSP_045891
    Alternative sequencei573 – 5742IV → RL in isoform 2. 1 PublicationVSP_026710
    Alternative sequencei575 – 1318744Missing in isoform 2. 1 PublicationVSP_026711Add
    BLAST
    Alternative sequencei1244 – 129855ASRIW…LGTVA → GLGPGQAPEVAPTRTAPERF APPVDRPAPTYSNMEEVD in isoform 3, isoform 4, isoform 6 and isoform 7. 2 PublicationsVSP_026712Add
    BLAST
    Alternative sequencei1299 – 131820Missing in isoform 3, isoform 4, isoform 6 and isoform 7. 2 PublicationsVSP_026713Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020698 mRNA. Translation: BAA74914.1. Different initiation.
    AK294756 mRNA. Translation: BAG57894.1.
    AK300425 mRNA. Translation: BAG62152.1.
    AC135506 Genomic DNA. No translation available.
    BC048269 mRNA. Translation: AAH48269.1.
    BC065909 mRNA. Translation: AAH65909.1.
    BC082241 mRNA. Translation: AAH82241.1.
    BC106029 mRNA. Translation: AAI06030.1. Sequence problems.
    BC142660 mRNA. Translation: AAI42661.1. Different initiation.
    BC146752 mRNA. Translation: AAI46753.1.
    CCDSiCCDS43090.1. [O94966-1]
    CCDS56254.1. [O94966-5]
    CCDS56255.1. [O94966-6]
    CCDS56256.1. [O94966-7]
    RefSeqiNP_001186089.1. NM_001199160.1. [O94966-5]
    NP_001186090.1. NM_001199161.1. [O94966-6]
    NP_001186091.1. NM_001199162.1. [O94966-7]
    NP_006668.1. NM_006677.2. [O94966-1]
    XP_005264888.1. XM_005264831.1. [O94966-4]
    UniGeneiHs.255596.
    Hs.734003.

    Genome annotation databases

    EnsembliENST00000398888; ENSP00000381863; ENSG00000172046. [O94966-1]
    ENST00000417901; ENSP00000395260; ENSG00000172046. [O94966-6]
    ENST00000434032; ENSP00000401197; ENSG00000172046. [O94966-5]
    ENST00000453664; ENSP00000400090; ENSG00000172046. [O94966-7]
    GeneIDi10869.
    KEGGihsa:10869.
    UCSCiuc003cwb.3. human. [O94966-2]
    uc003cwd.2. human. [O94966-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB020698 mRNA. Translation: BAA74914.1 . Different initiation.
    AK294756 mRNA. Translation: BAG57894.1 .
    AK300425 mRNA. Translation: BAG62152.1 .
    AC135506 Genomic DNA. No translation available.
    BC048269 mRNA. Translation: AAH48269.1 .
    BC065909 mRNA. Translation: AAH65909.1 .
    BC082241 mRNA. Translation: AAH82241.1 .
    BC106029 mRNA. Translation: AAI06030.1 . Sequence problems.
    BC142660 mRNA. Translation: AAI42661.1 . Different initiation.
    BC146752 mRNA. Translation: AAI46753.1 .
    CCDSi CCDS43090.1. [O94966-1 ]
    CCDS56254.1. [O94966-5 ]
    CCDS56255.1. [O94966-6 ]
    CCDS56256.1. [O94966-7 ]
    RefSeqi NP_001186089.1. NM_001199160.1. [O94966-5 ]
    NP_001186090.1. NM_001199161.1. [O94966-6 ]
    NP_001186091.1. NM_001199162.1. [O94966-7 ]
    NP_006668.1. NM_006677.2. [O94966-1 ]
    XP_005264888.1. XM_005264831.1. [O94966-4 ]
    UniGenei Hs.255596.
    Hs.734003.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WH0 NMR - A 273-393 [» ]
    ProteinModelPortali O94966.
    SMRi O94966. Positions 273-402, 494-677, 996-1215.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116078. 58 interactions.
    IntActi O94966. 49 interactions.
    MINTi MINT-4658026.
    STRINGi 9606.ENSP00000381863.

    Protein family/group databases

    MEROPSi C19.024.

    PTM databases

    PhosphoSitei O94966.

    Proteomic databases

    MaxQBi O94966.
    PaxDbi O94966.
    PRIDEi O94966.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000398888 ; ENSP00000381863 ; ENSG00000172046 . [O94966-1 ]
    ENST00000417901 ; ENSP00000395260 ; ENSG00000172046 . [O94966-6 ]
    ENST00000434032 ; ENSP00000401197 ; ENSG00000172046 . [O94966-5 ]
    ENST00000453664 ; ENSP00000400090 ; ENSG00000172046 . [O94966-7 ]
    GeneIDi 10869.
    KEGGi hsa:10869.
    UCSCi uc003cwb.3. human. [O94966-2 ]
    uc003cwd.2. human. [O94966-1 ]

    Organism-specific databases

    CTDi 10869.
    GeneCardsi GC03M049120.
    HGNCi HGNC:12617. USP19.
    MIMi 614471. gene.
    neXtProti NX_O94966.
    PharmGKBi PA37243.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5560.
    HOGENOMi HOG000074206.
    HOVERGENi HBG061889.
    KOi K11847.
    OMAi PQCKQHR.
    PhylomeDBi O94966.
    TreeFami TF106276.

    Miscellaneous databases

    ChiTaRSi USP19. human.
    EvolutionaryTracei O94966.
    GenomeRNAii 10869.
    NextBioi 41271.
    PROi O94966.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94966.
    Bgeei O94966.
    CleanExi HS_USP19.
    Genevestigatori O94966.

    Family and domain databases

    Gene3Di 2.60.40.790. 2 hits.
    InterProi IPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR002893. Znf_MYND.
    [Graphical view ]
    Pfami PF04969. CS. 2 hits.
    PF00443. UCH. 1 hit.
    PF01753. zf-MYND. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49764. SSF49764. 2 hits.
    PROSITEi PS51203. CS. 2 hits.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    PS01360. ZF_MYND_1. 1 hit.
    PS50865. ZF_MYND_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    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] (ISOFORMS 5 AND 7).
      Tissue: Brain.
    3. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1; 2 AND 6), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 846-1318 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-1318 (ISOFORM 4).
      Tissue: Skin and Testis.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "The ER-resident ubiquitin-specific protease 19 participates in the UPR and rescues ERAD substrates."
      Hassink G.C., Zhao B., Sompallae R., Altun M., Gastaldello S., Zinin N.V., Masucci M.G., Lindsten K.
      EMBO Rep. 10:755-761(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TOPOLOGY, SUBCELLULAR LOCATION.
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "The USP19 deubiquitinase regulates the stability of c-IAP1 and c-IAP2."
      Mei Y., Hahn A.A., Hu S., Yang X.
      J. Biol. Chem. 286:35380-35387(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BIRC2/C-IAP1; BIRC3/C-IAP2 AND XIAP/BIRC4.
    10. "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.
    11. "Ubiquitin-specific protease 19 (USP19) regulates hypoxia-inducible factor 1alpha (HIF-1alpha) during hypoxia."
      Altun M., Zhao B., Velasco K., Liu H., Hassink G., Paschke J., Pereira T., Lindsten K.
      J. Biol. Chem. 287:1962-1969(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HIF1A.
    12. "Solution structure of the CS domain of human USP19."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 273-393.

    Entry informationi

    Entry nameiUBP19_HUMAN
    AccessioniPrimary (citable) accession number: O94966
    Secondary accession number(s): A5PKX8
    , A6H8U2, B4DGT3, B4DTZ0, E7EN22, E7ETS0, E9PEG8, Q3KQW4, Q641Q9, Q6NZY8, Q86XV9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: July 10, 2007
    Last modified: October 1, 2014
    This is version 133 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, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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