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Q96PM5

- ZN363_HUMAN

UniProt

Q96PM5 - ZN363_HUMAN

Protein

RING finger and CHY zinc finger domain-containing protein 1

Gene

RCHY1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including p53/TP53, P73, HDAC1 and CDKN1B. Preferentially acts on tetrameric p53/TP53. Monoubiquitinates the translesion DNA polymerase POLH. Contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity.7 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri13 – 8068CHY-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri82 – 14463CTCHY-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri145 – 18945RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. p53 binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: UniProtKB
    6. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    2. positive regulation of protein ubiquitination Source: UniProtKB
    3. protein autoubiquitination Source: UniProtKB
    4. protein ubiquitination Source: UniProtKB
    5. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi6.3.2.19. 2681.
    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RING finger and CHY zinc finger domain-containing protein 1 (EC:6.3.2.-)
    Alternative name(s):
    Androgen receptor N-terminal-interacting protein
    CH-rich-interacting match with PLAG1
    E3 ubiquitin-protein ligase Pirh2
    RING finger protein 199
    Zinc finger protein 363
    p53-induced RING-H2 protein
    Short name:
    hPirh2
    Gene namesi
    Name:RCHY1
    Synonyms:ARNIP, CHIMP, PIRH2, RNF199, ZNF363
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:17479. RCHY1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. nuclear speck Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB
    4. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi176 – 1761M → E: Abolishes E3 ubiquitin-protein ligase activity. 1 Publication
    Mutagenesisi186 – 1861C → A: Abolishes E3 ubiquitin-protein ligase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA38240.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261RING finger and CHY zinc finger domain-containing protein 1PRO_0000056312Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei257 – 2571Phosphoserine1 Publication

    Post-translational modificationi

    Subject to ubiquitination and proteasomal degradation. Interaction with PLAGL2 or KAT5 enhances protein stability.2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96PM5.
    PaxDbiQ96PM5.
    PRIDEiQ96PM5.

    2D gel databases

    REPRODUCTION-2DPAGEQ96PM5.

    PTM databases

    PhosphoSiteiQ96PM5.

    Expressioni

    Inductioni

    Up-regulated during the S phase of the cell cycle. Expressed at low levels during G phase.

    Gene expression databases

    ArrayExpressiQ96PM5.
    BgeeiQ96PM5.
    CleanExiHS_RCHY1.
    GenevestigatoriQ96PM5.

    Organism-specific databases

    HPAiHPA030339.

    Interactioni

    Subunit structurei

    Monomer and homodimer. Interacts with AR, p53/TP53, MDM2, HDAC1, KAT5, PLAG1, PLAGL2, CDKN1B, COPE, UBE2D2 and GORAB/NTKLBP1.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AIG1Q9NVV54EBI-947779,EBI-3942989
    ARF4P180853EBI-947779,EBI-1237085
    C19orf80Q6UXH02EBI-947779,EBI-3943039
    CALM3P621582EBI-947779,EBI-397435
    HRGP041963EBI-947779,EBI-3915012
    NKD2Q969F22EBI-947779,EBI-1538629
    NLKQ9UBE85EBI-947779,EBI-366978
    TP53P046377EBI-947779,EBI-366083

    Protein-protein interaction databases

    BioGridi117406. 64 interactions.
    DIPiDIP-43981N.
    IntActiQ96PM5. 39 interactions.
    MINTiMINT-3057007.
    STRINGi9606.ENSP00000321239.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi26 – 305
    Turni32 – 343
    Beta strandi37 – 404
    Helixi41 – 477
    Beta strandi48 – 503
    Turni54 – 563
    Beta strandi59 – 624
    Turni63 – 653
    Beta strandi68 – 714
    Turni76 – 783
    Beta strandi84 – 874
    Turni88 – 914
    Beta strandi92 – 943
    Beta strandi100 – 1023
    Turni103 – 1064
    Beta strandi107 – 1104
    Turni113 – 1153
    Beta strandi116 – 1194
    Turni120 – 1234
    Beta strandi124 – 1274
    Turni128 – 1325
    Turni146 – 1494
    Turni156 – 1583
    Beta strandi159 – 1613
    Beta strandi167 – 1693
    Helixi170 – 17910
    Helixi184 – 1874
    Beta strandi217 – 2259
    Beta strandi228 – 2325
    Turni241 – 2433
    Beta strandi248 – 2514

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2JRJNMR-A143-189[»]
    2K2CNMR-A1-137[»]
    2K2DNMR-A187-261[»]
    ProteinModelPortaliQ96PM5.
    SMRiQ96PM5. Positions 1-137, 145-186, 215-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96PM5.

    Family & Domainsi

    Sequence similaritiesi

    Contains 1 CHY-type zinc finger.PROSITE-ProRule annotation
    Contains 1 CTCHY-type zinc finger.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri13 – 8068CHY-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri82 – 14463CTCHY-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri145 – 18945RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG325406.
    HOGENOMiHOG000231827.
    HOVERGENiHBG062959.
    InParanoidiQ96PM5.
    KOiK10144.
    OMAiFDMEIAA.
    OrthoDBiEOG7XH6QG.
    PhylomeDBiQ96PM5.
    TreeFamiTF323762.

    Family and domain databases

    Gene3Di2.20.28.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR004039. Rubredoxin-type_fold.
    IPR008913. Znf_CHY.
    IPR017921. Znf_CTCHY.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF05495. zf-CHY. 1 hit.
    PF13639. zf-RING_2. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS51266. ZF_CHY. 1 hit.
    PS51270. ZF_CTCHY. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96PM5-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    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

    MAATAREDGA SGQERGQRGC EHYDRGCLLK APCCDKLYTC RLCHDNNEDH    50
    QLDRFKVKEV QCINCEKIQH AQQTCEECST LFGEYYCDIC HLFDKDKKQY 100
    HCENCGICRI GPKEDFFHCL KCNLCLAMNL QGRHKCIENV SRQNCPICLE 150
    DIHTSRVVAH VLPCGHLLHR TCYEEMLKEG YRCPLCMHSA LDMTRYWRQL 200
    DDEVAQTPMP SEYQNMTVDI LCNDCNGRST VQFHILGMKC KICESYNTAQ 250
    AGGRRISLDQ Q 261
    Length:261
    Mass (Da):30,110
    Last modified:December 1, 2001 - v1
    Checksum:iAC03786F6B42A03D
    GO
    Isoform 2 (identifier: Q96PM5-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         171-179: Missing.

    Show »
    Length:252
    Mass (Da):28,983
    Checksum:i0079B97723751278
    GO
    Isoform 3 (identifier: Q96PM5-3) [UniParc]FASTAAdd to Basket

    Also known as: C

    The sequence of this isoform differs from the canonical sequence as follows:
         180-261: Missing.

    Show »
    Length:179
    Mass (Da):20,720
    Checksum:iB38F75D4374FA2F8
    GO
    Isoform 4 (identifier: Q96PM5-4) [UniParc]FASTAAdd to Basket

    Also known as: Pirh2b

    The sequence of this isoform differs from the canonical sequence as follows:
         180-261: GYRCPLCMHS...GGRRISLDQQ → YDQVLETAG

    Note: No ubiquitin protein ligase activity. Down-regulated in hepatocellular carcinoma.

    Show »
    Length:188
    Mass (Da):21,697
    Checksum:i0DEFC07DCEDBA3A7
    GO
    Isoform 5 (identifier: Q96PM5-5) [UniParc]FASTAAdd to Basket

    Also known as: Pirh2D

    The sequence of this isoform differs from the canonical sequence as follows:
         68-75: IQHAQQTC → NSTCPTDL
         76-261: Missing.

    Show »
    Length:75
    Mass (Da):8,494
    Checksum:i2FE97DE89608DE6D
    GO
    Isoform 6 (identifier: Q96PM5-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-30: MAATAREDGASGQERGQRGCEHYDRGCLLK → MAPAVKSE

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:239
    Mass (Da):27,676
    Checksum:i0DD872A14E2E217A
    GO
    Isoform 7 (identifier: Q96PM5-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         31-70: Missing.

    Note: No experimental confirmation available. Gene prediction based on partial mRNA data.

    Show »
    Length:221
    Mass (Da):25,337
    Checksum:i7B96797039B25C4D
    GO
    Isoform 8 (identifier: Q96PM5-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         31-70: Missing.
         171-179: Missing.

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:212
    Mass (Da):24,210
    Checksum:iA4EA203D3FBB7F21
    GO

    Sequence cautioni

    The sequence BAD92309.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 133SGQ → TGE in ACT35531. (PubMed:19483087)Curated
    Sequence conflicti11 – 133SGQ → TGE in ACT35532. (PubMed:19483087)Curated
    Sequence conflicti11 – 133SGQ → TGE in ACT35533. (PubMed:19483087)Curated
    Sequence conflicti11 – 133SGQ → TGE in AAK96896. 1 PublicationCurated
    Sequence conflicti142 – 1421R → Q in AAH47393. (PubMed:15489334)Curated
    Sequence conflicti220 – 2201I → F in BAD92309. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3030MAATA…GCLLK → MAPAVKSE in isoform 6. CuratedVSP_053787Add
    BLAST
    Alternative sequencei31 – 7040Missing in isoform 7 and isoform 8. CuratedVSP_053788Add
    BLAST
    Alternative sequencei68 – 758IQHAQQTC → NSTCPTDL in isoform 5. 1 PublicationVSP_053385
    Alternative sequencei76 – 261186Missing in isoform 5. 1 PublicationVSP_053386Add
    BLAST
    Alternative sequencei171 – 1799Missing in isoform 2 and isoform 8. 1 PublicationVSP_038467
    Alternative sequencei180 – 26182Missing in isoform 3. 1 PublicationVSP_038468Add
    BLAST
    Alternative sequencei180 – 26182GYRCP…SLDQQ → YDQVLETAG in isoform 4. 1 PublicationVSP_044085Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GQ250944 mRNA. Translation: ACT35531.1.
    GQ250945 mRNA. Translation: ACT35532.1.
    GQ250946 mRNA. Translation: ACT35533.1.
    AF247041 mRNA. Translation: AAL76101.1.
    AF255666 mRNA. Translation: AAK96896.1.
    AF305424 mRNA. Translation: AAL09356.1.
    AB209072 mRNA. Translation: BAD92309.1. Different initiation.
    AY888047 mRNA. Translation: AAX78233.1.
    GU937000 mRNA. Translation: ADD21555.1.
    AK091501 mRNA. Translation: BAG52375.1.
    AC096759 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX05725.1.
    BC047393 mRNA. Translation: AAH47393.1.
    CCDSiCCDS34012.1. [Q96PM5-2]
    CCDS3567.1. [Q96PM5-1]
    CCDS63990.1. [Q96PM5-8]
    CCDS63991.1. [Q96PM5-7]
    CCDS63992.1. [Q96PM5-6]
    RefSeqiNP_001009922.1. NM_001009922.2. [Q96PM5-2]
    NP_001265465.1. NM_001278536.1. [Q96PM5-7]
    NP_001265466.1. NM_001278537.1. [Q96PM5-8]
    NP_001265467.1. NM_001278538.1. [Q96PM5-6]
    NP_056251.2. NM_015436.3. [Q96PM5-1]
    UniGeneiHs.48297.

    Genome annotation databases

    EnsembliENST00000324439; ENSP00000321239; ENSG00000163743. [Q96PM5-1]
    ENST00000380840; ENSP00000370220; ENSG00000163743. [Q96PM5-7]
    ENST00000505105; ENSP00000424631; ENSG00000163743. [Q96PM5-4]
    ENST00000507014; ENSP00000424472; ENSG00000163743. [Q96PM5-8]
    ENST00000512706; ENSP00000423976; ENSG00000163743. [Q96PM5-6]
    ENST00000513257; ENSP00000421084; ENSG00000163743. [Q96PM5-2]
    GeneIDi25898.
    KEGGihsa:25898.
    UCSCiuc003hik.3. human. [Q96PM5-1]
    uc003hil.3. human. [Q96PM5-2]
    uc010iip.3. human. [Q96PM5-4]

    Polymorphism databases

    DMDMi32700008.

    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
    GQ250944 mRNA. Translation: ACT35531.1 .
    GQ250945 mRNA. Translation: ACT35532.1 .
    GQ250946 mRNA. Translation: ACT35533.1 .
    AF247041 mRNA. Translation: AAL76101.1 .
    AF255666 mRNA. Translation: AAK96896.1 .
    AF305424 mRNA. Translation: AAL09356.1 .
    AB209072 mRNA. Translation: BAD92309.1 . Different initiation.
    AY888047 mRNA. Translation: AAX78233.1 .
    GU937000 mRNA. Translation: ADD21555.1 .
    AK091501 mRNA. Translation: BAG52375.1 .
    AC096759 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX05725.1 .
    BC047393 mRNA. Translation: AAH47393.1 .
    CCDSi CCDS34012.1. [Q96PM5-2 ]
    CCDS3567.1. [Q96PM5-1 ]
    CCDS63990.1. [Q96PM5-8 ]
    CCDS63991.1. [Q96PM5-7 ]
    CCDS63992.1. [Q96PM5-6 ]
    RefSeqi NP_001009922.1. NM_001009922.2. [Q96PM5-2 ]
    NP_001265465.1. NM_001278536.1. [Q96PM5-7 ]
    NP_001265466.1. NM_001278537.1. [Q96PM5-8 ]
    NP_001265467.1. NM_001278538.1. [Q96PM5-6 ]
    NP_056251.2. NM_015436.3. [Q96PM5-1 ]
    UniGenei Hs.48297.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2JRJ NMR - A 143-189 [» ]
    2K2C NMR - A 1-137 [» ]
    2K2D NMR - A 187-261 [» ]
    ProteinModelPortali Q96PM5.
    SMRi Q96PM5. Positions 1-137, 145-186, 215-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117406. 64 interactions.
    DIPi DIP-43981N.
    IntActi Q96PM5. 39 interactions.
    MINTi MINT-3057007.
    STRINGi 9606.ENSP00000321239.

    PTM databases

    PhosphoSitei Q96PM5.

    Polymorphism databases

    DMDMi 32700008.

    2D gel databases

    REPRODUCTION-2DPAGE Q96PM5.

    Proteomic databases

    MaxQBi Q96PM5.
    PaxDbi Q96PM5.
    PRIDEi Q96PM5.

    Protocols and materials databases

    DNASUi 25898.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000324439 ; ENSP00000321239 ; ENSG00000163743 . [Q96PM5-1 ]
    ENST00000380840 ; ENSP00000370220 ; ENSG00000163743 . [Q96PM5-7 ]
    ENST00000505105 ; ENSP00000424631 ; ENSG00000163743 . [Q96PM5-4 ]
    ENST00000507014 ; ENSP00000424472 ; ENSG00000163743 . [Q96PM5-8 ]
    ENST00000512706 ; ENSP00000423976 ; ENSG00000163743 . [Q96PM5-6 ]
    ENST00000513257 ; ENSP00000421084 ; ENSG00000163743 . [Q96PM5-2 ]
    GeneIDi 25898.
    KEGGi hsa:25898.
    UCSCi uc003hik.3. human. [Q96PM5-1 ]
    uc003hil.3. human. [Q96PM5-2 ]
    uc010iip.3. human. [Q96PM5-4 ]

    Organism-specific databases

    CTDi 25898.
    GeneCardsi GC04M076405.
    HGNCi HGNC:17479. RCHY1.
    HPAi HPA030339.
    MIMi 607680. gene.
    neXtProti NX_Q96PM5.
    PharmGKBi PA38240.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG325406.
    HOGENOMi HOG000231827.
    HOVERGENi HBG062959.
    InParanoidi Q96PM5.
    KOi K10144.
    OMAi FDMEIAA.
    OrthoDBi EOG7XH6QG.
    PhylomeDBi Q96PM5.
    TreeFami TF323762.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    BRENDAi 6.3.2.19. 2681.
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi RCHY1. human.
    EvolutionaryTracei Q96PM5.
    GeneWikii RCHY1.
    GenomeRNAii 25898.
    NextBioi 35483477.
    PROi Q96PM5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96PM5.
    Bgeei Q96PM5.
    CleanExi HS_RCHY1.
    Genevestigatori Q96PM5.

    Family and domain databases

    Gene3Di 2.20.28.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR004039. Rubredoxin-type_fold.
    IPR008913. Znf_CHY.
    IPR017921. Znf_CTCHY.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF05495. zf-CHY. 1 hit.
    PF13639. zf-RING_2. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS51266. ZF_CHY. 1 hit.
    PS51270. ZF_CTCHY. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of two novel isoforms of Pirh2 ubiquitin ligase that negatively regulate p53 independent of RING finger domains."
      Corcoran C.A., Montalbano J., Sun H., He Q., Huang Y., Sheikh M.S.
      J. Biol. Chem. 284:21955-21970(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, SUBUNIT, INTERACTION WITH TP53 AND MDM2, UBIQUITINATION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
    2. Beitel L.K., Lumbroso R., Panet-Raymond V., de Tourreil A.S., Pinsky L., Trifiro M.A.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Identification of PLAG1 interacting proteins."
      Braem C.V., Kas K.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "A novel human zinc-finger protein."
      Wu H.-S., Chou C.-M., Leu J.-H., Huang C.-J.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "A novel hPirh2 splicing variant without ubiquitin protein ligase activity interacts with p53 and is down-regulated in hepatocellular carcinoma."
      Wu G., Sun M., Zhang L., Zhou J., Wang Y., Huo K.
      FEBS Lett. 584:2772-2778(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    6. "Identification of Pirh2D, an additional novel isoform of Pirh2 ubiquitin ligase."
      Shi J., Huang Y., Sheikh M.S.
      Mol. Cell. Pharmacol. 2:21-23(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), ALTERNATIVE SPLICING.
    7. "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 1).
      Tissue: Brain.
    8. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    9. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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 1).
      Tissue: Brain.
    12. "Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome."
      Logan I.R., Sapountzi V., Gaughan L., Neal D.E., Robson C.N.
      J. Biol. Chem. 279:11696-11704(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH KAT5, SUBCELLULAR LOCATION.
    13. Cited for: INTERACTION WITH GORAB, SUBCELLULAR LOCATION.
    14. "Human PIRH2 enhances androgen receptor signaling through inhibition of histone deacetylase 1 and is overexpressed in prostate cancer."
      Logan I.R., Gaughan L., McCracken S.R.C., Sapountzi V., Leung H.Y., Robson C.N.
      Mol. Cell. Biol. 26:6502-6510(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AR; KAT5 AND HDAC1, SUBCELLULAR LOCATION.
    15. "PLAGL2 controls the stability of Pirh2, an E3 ubiquitin ligase for p53."
      Zheng G., Ning J., Yang Y.-C.
      Biochem. Biophys. Res. Commun. 364:344-350(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERACTION WITH PLAGL2, PROTEASOMAL DEGRADATION.
    16. "Pirh2 promotes ubiquitin-dependent degradation of the cyclin-dependent kinase inhibitor p27Kip1."
      Hattori T., Isobe T., Abe K., Kikuchi H., Kitagawa K., Oda T., Uchida C., Kitagawa M.
      Cancer Res. 67:10789-10795(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CDKN1B.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    18. "Ubiquitylation of epsilon-COP by PIRH2 and regulation of the secretion of PSA."
      Maruyama S., Miyajima N., Bohgaki M., Tsukiyama T., Shigemura M., Nonomura K., Hatakeyama S.
      Mol. Cell. Biochem. 307:73-82(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH COPE.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. "Pirh2, a ubiquitin E3 ligase, inhibits p73 transcriptional activity by promoting its ubiquitination."
      Wu H., Zeinab R.A., Flores E.R., Leng R.P.
      Mol. Cancer Res. 9:1780-1790(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Pirh2 E3 ubiquitin ligase monoubiquitinates DNA polymerase eta to suppress translesion DNA synthesis."
      Jung Y.S., Hakem A., Hakem R., Chen X.
      Mol. Cell. Biol. 31:3997-4006(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. Cited for: STRUCTURE BY NMR OF 138-189 IN COMPLEX WITH ZINC IONS, FUNCTION, MUTAGENESIS OF MET-176 AND CYS-186, INTERACTION WITH TP53 AND UBE2D2.

    Entry informationi

    Entry nameiZN363_HUMAN
    AccessioniPrimary (citable) accession number: Q96PM5
    Secondary accession number(s): B3KRG3
    , C7E541, C7E542, C7E543, D3YRV2, E7EMC8, E7ETW5, J3KPI0, Q2KN33, Q59GN7, Q86X26, Q96PR5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 28, 2003
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 124 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3