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Q9CR50

- ZN363_MOUSE

UniProt

Q9CR50 - ZN363_MOUSE

Protein

RING finger and CHY zinc finger domain-containing protein 1

Gene

Rchy1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Jun 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. Increases AR transcription factor activity. Monoubiquitinates the translesion DNA polymerase POLH By similarity. Contributes to the regulation of the cell cycle progression.By similarity1 Publication

    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. ubiquitin-protein transferase activity Source: UniProtKB
    3. zinc ion binding Source: InterPro

    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. 3474.
    ReactomeiREACT_199115. 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
    Zinc finger protein 363
    Gene namesi
    Name:Rchy1
    Synonyms:Arnip, Chimp, Zfp363, Znf363
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1915348. Rchy1.

    Subcellular locationi

    Nucleus By similarity. Nucleus speckle By similarity. Cytoplasm By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261RING finger and CHY zinc finger domain-containing protein 1PRO_0000056313Add
    BLAST

    Post-translational modificationi

    Subject to ubiquitination and proteasomal degradation.By similarity

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    PaxDbiQ9CR50.
    PRIDEiQ9CR50.

    PTM databases

    PhosphoSiteiQ9CR50.

    Expressioni

    Tissue specificityi

    Detected in testis, liver, kidney and heart.1 Publication

    Inductioni

    Up-regulated upon p53/TP53 activation.1 Publication

    Gene expression databases

    ArrayExpressiQ9CR50.
    BgeeiQ9CR50.
    GenevestigatoriQ9CR50.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi212655. 2 interactions.

    Structurei

    Secondary structure

    1
    261
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi17 – 193
    Beta strandi26 – 316
    Turni32 – 354
    Beta strandi36 – 405
    Helixi41 – 466
    Beta strandi48 – 503
    Beta strandi54 – 563
    Beta strandi60 – 656
    Beta strandi76 – 783
    Beta strandi84 – 863
    Beta strandi88 – 903
    Beta strandi96 – 1027
    Turni103 – 1064
    Beta strandi107 – 1115
    Helixi113 – 1153
    Beta strandi116 – 1194
    Turni120 – 1234
    Beta strandi124 – 1274
    Helixi128 – 1303
    Beta strandi131 – 1344
    Turni146 – 1483
    Turni154 – 1563
    Beta strandi159 – 1613
    Beta strandi167 – 1693
    Helixi172 – 1798

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DKTNMR-A9-138[»]
    2ECMNMR-A145-186[»]
    ProteinModelPortaliQ9CR50.
    SMRiQ9CR50. Positions 10-139, 145-186, 215-261.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9CR50.

    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.
    GeneTreeiENSGT00390000008853.
    HOGENOMiHOG000231827.
    HOVERGENiHBG062959.
    InParanoidiQ9CR50.
    KOiK10144.
    OMAiCGSYNTA.
    OrthoDBiEOG7XH6QG.
    PhylomeDBiQ9CR50.
    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]

    Sequencei

    Sequence statusi: Complete.

    Q9CR50-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAATAREDGV RNLAQGPRGC EHYDRACLLK APCCDKLYTC RLCHDTNEDH    50
    QLDRFKVKEV QCINCEKLQH AQQTCEDCST LFGEYYCSIC HLFDKDKRQY 100
    HCESCGICRI GPKEDFFHCL KCNLCLTTNL RGKHKCIENV SRQNCPICLE 150
    DIHTSRVVAH VLPCGHLLHR TCYEEMLKEG YRCPLCMHSA LDMTRYWRQL 200
    DTEVAQTPMP SEYQNVTVDI LCNDCNGRST VQFHILGMKC KLCDSYNTAQ 250
    AGGRRVPVDQ Q 261
    Length:261
    Mass (Da):30,014
    Last modified:June 1, 2001 - v1
    Checksum:i219AE48A421CC10D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF071222 mRNA. Translation: AAL75940.1.
    AF276959 mRNA. Translation: AAK96899.1.
    AF305423 mRNA. Translation: AAL09355.1.
    AK018364 mRNA. Translation: BAB31179.1.
    AK018488 mRNA. Translation: BAB31236.1.
    AK078397 mRNA. Translation: BAC37254.1.
    BC057143 mRNA. Translation: AAH57143.1.
    CCDSiCCDS19424.1.
    RefSeqiNP_001258726.1. NM_001271797.1.
    NP_080833.1. NM_026557.4.
    UniGeneiMm.159453.

    Genome annotation databases

    EnsembliENSMUST00000031345; ENSMUSP00000031345; ENSMUSG00000029397.
    GeneIDi68098.
    KEGGimmu:68098.
    UCSCiuc008yby.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF071222 mRNA. Translation: AAL75940.1 .
    AF276959 mRNA. Translation: AAK96899.1 .
    AF305423 mRNA. Translation: AAL09355.1 .
    AK018364 mRNA. Translation: BAB31179.1 .
    AK018488 mRNA. Translation: BAB31236.1 .
    AK078397 mRNA. Translation: BAC37254.1 .
    BC057143 mRNA. Translation: AAH57143.1 .
    CCDSi CCDS19424.1.
    RefSeqi NP_001258726.1. NM_001271797.1.
    NP_080833.1. NM_026557.4.
    UniGenei Mm.159453.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DKT NMR - A 9-138 [» ]
    2ECM NMR - A 145-186 [» ]
    ProteinModelPortali Q9CR50.
    SMRi Q9CR50. Positions 10-139, 145-186, 215-261.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212655. 2 interactions.

    PTM databases

    PhosphoSitei Q9CR50.

    Proteomic databases

    PaxDbi Q9CR50.
    PRIDEi Q9CR50.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000031345 ; ENSMUSP00000031345 ; ENSMUSG00000029397 .
    GeneIDi 68098.
    KEGGi mmu:68098.
    UCSCi uc008yby.1. mouse.

    Organism-specific databases

    CTDi 25898.
    MGIi MGI:1915348. Rchy1.

    Phylogenomic databases

    eggNOGi NOG325406.
    GeneTreei ENSGT00390000008853.
    HOGENOMi HOG000231827.
    HOVERGENi HBG062959.
    InParanoidi Q9CR50.
    KOi K10144.
    OMAi CGSYNTA.
    OrthoDBi EOG7XH6QG.
    PhylomeDBi Q9CR50.
    TreeFami TF323762.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    BRENDAi 6.3.2.19. 3474.
    Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi RCHY1. mouse.
    EvolutionaryTracei Q9CR50.
    NextBioi 326416.
    PROi Q9CR50.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CR50.
    Bgeei Q9CR50.
    Genevestigatori Q9CR50.

    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. 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].
    2. "Identification of PLAG1 interacting proteins."
      Braem C.V., Kas K.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "A novel mouse 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].
      Strain: C57BL/6.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Colon and Egg.
    5. "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].
      Strain: C57BL/6J.
      Tissue: Mammary tumor.
    6. "Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation."
      Leng R.P., Lin Y., Ma W., Wu H., Lemmers B., Chung S., Parant J.M., Lozano G., Hakem R., Benchimol S.
      Cell 112:779-791(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TP53, INDUCTION, TISSUE SPECIFICITY.
    7. "Solution structure of the CHY zinc finger domain and of the RING domain of the RING finger and CHY zinc finger domain-containing protein 1 from Mus musculus."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 9-186.

    Entry informationi

    Entry nameiZN363_MOUSE
    AccessioniPrimary (citable) accession number: Q9CR50
    Secondary accession number(s): Q920H0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 28, 2003
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3