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Q96PM5 (ZN363_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
RING finger protein 199
Zinc finger protein 363
p53-induced RING-H2 protein
Short name=hPirh2
Gene names
Name:RCHY1
Synonyms:ARNIP, CHIMP, PIRH2, RNF199, ZNF363
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Monoubiquitinates the translesion DNA polymerase POLH. Contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity. Ref.1 Ref.14 Ref.16 Ref.18 Ref.20 Ref.21 Ref.22

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. Ref.1 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.22

Subcellular location

Nucleus. Nucleus speckle. Cytoplasm Ref.1 Ref.12 Ref.13 Ref.14 Ref.16.

Induction

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

Post-translational modification

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

Sequence similarities

Contains 1 CHY-type zinc finger.

Contains 1 CTCHY-type zinc finger.

Contains 1 RING-type zinc finger.

Sequence caution

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

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of protein ubiquitination

Inferred from direct assay Ref.1. Source: UniProtKB

protein autoubiquitination

Inferred from direct assay Ref.1. Source: UniProtKB

protein ubiquitination

Inferred from direct assay Ref.22Ref.1. Source: UniProtKB

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.13. Source: HGNC

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

ubiquitin ligase complex

Inferred from direct assay Ref.22. Source: UniProtKB

   Molecular_functionp53 binding

Inferred from physical interaction Ref.22Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13Ref.22Ref.1. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.1. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.22. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96PM5-1)

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.
Isoform 2 (identifier: Q96PM5-2)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     171-179: Missing.
Isoform 3 (identifier: Q96PM5-3)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     180-261: Missing.
Isoform 4 (identifier: Q96PM5-4)

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.
Isoform 5 (identifier: Q96PM5-5)

Also known as: Pirh2D;

The sequence of this isoform differs from the canonical sequence as follows:
     68-75: IQHAQQTC → NSTCPTDL
     76-261: Missing.
Isoform 6 (identifier: Q96PM5-6)

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.
Isoform 7 (identifier: Q96PM5-7)

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.
Isoform 8 (identifier: Q96PM5-8)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 261261RING finger and CHY zinc finger domain-containing protein 1
PRO_0000056312

Regions

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

Amino acid modifications

Modified residue2571Phosphoserine Ref.17

Natural variations

Alternative sequence1 – 3030MAATA…GCLLK → MAPAVKSE in isoform 6.
VSP_053787
Alternative sequence31 – 7040Missing in isoform 7 and isoform 8.
VSP_053788
Alternative sequence68 – 758IQHAQQTC → NSTCPTDL in isoform 5.
VSP_053385
Alternative sequence76 – 261186Missing in isoform 5.
VSP_053386
Alternative sequence171 – 1799Missing in isoform 2 and isoform 8.
VSP_038467
Alternative sequence180 – 26182Missing in isoform 3.
VSP_038468
Alternative sequence180 – 26182GYRCP…SLDQQ → YDQVLETAG in isoform 4.
VSP_044085

Experimental info

Mutagenesis1761M → E: Abolishes E3 ubiquitin-protein ligase activity. Ref.22
Mutagenesis1861C → A: Abolishes E3 ubiquitin-protein ligase activity. Ref.22
Sequence conflict11 – 133SGQ → TGE in ACT35531. Ref.1
Sequence conflict11 – 133SGQ → TGE in ACT35532. Ref.1
Sequence conflict11 – 133SGQ → TGE in ACT35533. Ref.1
Sequence conflict11 – 133SGQ → TGE in AAK96896. Ref.3
Sequence conflict1421R → Q in AAH47393. Ref.11
Sequence conflict2201I → F in BAD92309. Ref.8

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (A) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: AC03786F6B42A03D

FASTA26130,110
        10         20         30         40         50         60 
MAATAREDGA SGQERGQRGC EHYDRGCLLK APCCDKLYTC RLCHDNNEDH QLDRFKVKEV 

        70         80         90        100        110        120 
QCINCEKIQH AQQTCEECST LFGEYYCDIC HLFDKDKKQY HCENCGICRI GPKEDFFHCL 

       130        140        150        160        170        180 
KCNLCLAMNL QGRHKCIENV SRQNCPICLE DIHTSRVVAH VLPCGHLLHR TCYEEMLKEG 

       190        200        210        220        230        240 
YRCPLCMHSA LDMTRYWRQL DDEVAQTPMP SEYQNMTVDI LCNDCNGRST VQFHILGMKC 

       250        260 
KICESYNTAQ AGGRRISLDQ Q 

« Hide

Isoform 2 (B) [UniParc].

Checksum: 0079B97723751278
Show »

FASTA25228,983
Isoform 3 (C) [UniParc].

Checksum: B38F75D4374FA2F8
Show »

FASTA17920,720
Isoform 4 (Pirh2b) [UniParc].

Checksum: 0DEFC07DCEDBA3A7
Show »

FASTA18821,697
Isoform 5 (Pirh2D) [UniParc].

Checksum: 2FE97DE89608DE6D
Show »

FASTA758,494
Isoform 6 [UniParc].

Checksum: 0DD872A14E2E217A
Show »

FASTA23927,676
Isoform 7 [UniParc].

Checksum: 7B96797039B25C4D
Show »

FASTA22125,337
Isoform 8 [UniParc].

Checksum: A4EA203D3FBB7F21
Show »

FASTA21224,210

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A new human gene hNTKL-BP1 interacts with hPirh2."
Zhang L., Li J., Wang C., Ma Y., Huo K.
Biochem. Biophys. Res. Commun. 330:293-297(2005) [PubMed] [Europe PMC] [Abstract]
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Molecular basis of Pirh2-mediated p53 ubiquitylation."
Sheng Y., Laister R.C., Lemak A., Wu B., Tai E., Duan S., Lukin J., Sunnerhagen M., Srisailam S., Karra M., Benchimol S., Arrowsmith C.H.
Nat. Struct. Mol. Biol. 15:1334-1342(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34012.1. [Q96PM5-2]
CCDS3567.1. [Q96PM5-1]
RefSeqNP_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]
UniGeneHs.48297.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JRJNMR-A143-189[»]
2K2CNMR-A1-137[»]
2K2DNMR-A187-261[»]
ProteinModelPortalQ96PM5.
SMRQ96PM5. Positions 1-137, 145-186, 215-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117406. 64 interactions.
DIPDIP-43981N.
IntActQ96PM5. 39 interactions.
MINTMINT-3057007.
STRING9606.ENSP00000321239.

PTM databases

PhosphoSiteQ96PM5.

Polymorphism databases

DMDM32700008.

2D gel databases

REPRODUCTION-2DPAGEQ96PM5.

Proteomic databases

MaxQBQ96PM5.
PaxDbQ96PM5.
PRIDEQ96PM5.

Protocols and materials databases

DNASU25898.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324439; ENSP00000321239; ENSG00000163743. [Q96PM5-1]
ENST00000380840; ENSP00000370220; ENSG00000163743.
ENST00000505105; ENSP00000424631; ENSG00000163743. [Q96PM5-4]
ENST00000507014; ENSP00000424472; ENSG00000163743.
ENST00000512706; ENSP00000423976; ENSG00000163743.
ENST00000513257; ENSP00000421084; ENSG00000163743. [Q96PM5-2]
GeneID25898.
KEGGhsa:25898.
UCSCuc003hik.3. human. [Q96PM5-1]
uc003hil.3. human. [Q96PM5-2]
uc010iip.3. human. [Q96PM5-4]

Organism-specific databases

CTD25898.
GeneCardsGC04M076405.
HGNCHGNC:17479. RCHY1.
HPAHPA030339.
MIM607680. gene.
neXtProtNX_Q96PM5.
PharmGKBPA38240.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG325406.
HOGENOMHOG000231827.
HOVERGENHBG062959.
InParanoidQ96PM5.
KOK10144.
OMAFDMEIAA.
OrthoDBEOG7XH6QG.
PhylomeDBQ96PM5.
TreeFamTF323762.

Enzyme and pathway databases

BRENDA6.3.2.19. 2681.
ReactomeREACT_6900. Immune System.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ96PM5.
BgeeQ96PM5.
CleanExHS_RCHY1.
GenevestigatorQ96PM5.

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. human.
EvolutionaryTraceQ96PM5.
GeneWikiRCHY1.
GenomeRNAi25898.
NextBio35483477.
PROQ96PM5.
SOURCESearch...

Entry information

Entry nameZN363_HUMAN
AccessionPrimary (citable) accession number: Q96PM5
Secondary accession number(s): B3KRG3 expand/collapse secondary AC list , C7E541, C7E542, C7E543, D3YRV2, E7EMC8, E7ETW5, J3KPI0, Q2KN33, Q59GN7, Q86X26, Q96PR5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM