SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9CR50

- ZN363_MOUSE

UniProt

Q9CR50 - ZN363_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

RING finger and CHY zinc finger domain-containing protein 1

Gene
Rchy1, Arnip, Chimp, Zfp363, Znf363
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri13 – 8068CHY-typeAdd
BLAST
Zinc fingeri82 – 14463CTCHY-typeAdd
BLAST
Zinc fingeri145 – 18945RING-typeAdd
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
Complete GO annotation...

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
Complete GO annotation...

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.1 Publication

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.

Miscellaneous databases

EvolutionaryTraceiQ9CR50.

Family & Domainsi

Sequence similaritiesi

Zinc finger

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 113 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

Similar proteinsi