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Q9CR50 (ZN363_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Rchy1
Synonyms:Arnip, Chimp, Zfp363, Znf363
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length261 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Monomer and homodimer. Interacts with AR, p53/TP53, MDM2, HDAC1, KAT5, PLAG1, PLAGL2, CDKN1B, COPE, UBE2D2 and GORAB/NTKLBP1 By similarity. Ref.6

Subcellular location

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

Tissue specificity

Detected in testis, liver, kidney and heart. Ref.6

Induction

Up-regulated upon p53/TP53 activation. Ref.6

Post-translational modification

Subject to ubiquitination and proteasomal degradation By similarity.

Sequence similarities

Contains 1 CHY-type zinc finger.

Contains 1 CTCHY-type zinc finger.

Contains 1 RING-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261RING finger and CHY zinc finger domain-containing protein 1
PRO_0000056313

Regions

Zinc finger13 – 8068CHY-type
Zinc finger82 – 14463CTCHY-type
Zinc finger145 – 18945RING-type

Secondary structure

......................................... 261
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9CR50 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 219AE48A421CC10D

FASTA26130,014
        10         20         30         40         50         60 
MAATAREDGV RNLAQGPRGC EHYDRACLLK APCCDKLYTC RLCHDTNEDH QLDRFKVKEV 

        70         80         90        100        110        120 
QCINCEKLQH AQQTCEDCST LFGEYYCSIC HLFDKDKRQY HCESCGICRI GPKEDFFHCL 

       130        140        150        160        170        180 
KCNLCLTTNL RGKHKCIENV SRQNCPICLE DIHTSRVVAH VLPCGHLLHR TCYEEMLKEG 

       190        200        210        220        230        240 
YRCPLCMHSA LDMTRYWRQL DTEVAQTPMP SEYQNVTVDI LCNDCNGRST VQFHILGMKC 

       250        260 
KLCDSYNTAQ AGGRRVPVDQ Q 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001258726.1. NM_001271797.1.
NP_080833.1. NM_026557.4.
UniGeneMm.159453.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DKTNMR-A9-138[»]
2ECMNMR-A145-186[»]
ProteinModelPortalQ9CR50.
SMRQ9CR50. Positions 10-139, 145-186, 215-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212655. 1 interaction.

PTM databases

PhosphoSiteQ9CR50.

Proteomic databases

PaxDbQ9CR50.
PRIDEQ9CR50.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031345; ENSMUSP00000031345; ENSMUSG00000029397.
GeneID68098.
KEGGmmu:68098.
UCSCuc008yby.1. mouse.

Organism-specific databases

CTD25898.
MGIMGI:1915348. Rchy1.

Phylogenomic databases

eggNOGNOG325406.
GeneTreeENSGT00390000008853.
HOGENOMHOG000231827.
HOVERGENHBG062959.
InParanoidQ9CR50.
KOK10144.
OMACGSYNTA.
OrthoDBEOG7XH6QG.
PhylomeDBQ9CR50.
TreeFamTF323762.

Enzyme and pathway databases

BRENDA6.3.2.19. 3474.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ9CR50.
BgeeQ9CR50.
GenevestigatorQ9CR50.

Family and domain databases

Gene3D2.20.28.10. 1 hit.
3.30.40.10. 1 hit.
InterProIPR004039. Rubredoxin-type_fold.
IPR008913. Znf_CHY.
IPR017921. Znf_CTCHY.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF05495. zf-CHY. 1 hit.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS51266. ZF_CHY. 1 hit.
PS51270. ZF_CTCHY. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRCHY1. mouse.
EvolutionaryTraceQ9CR50.
NextBio326416.
PROQ9CR50.
SOURCESearch...

Entry information

Entry nameZN363_MOUSE
AccessionPrimary (citable) accession number: Q9CR50
Secondary accession number(s): Q920H0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot