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Q96PM5

- ZN363_HUMAN

UniProt

Q96PM5 - ZN363_HUMAN

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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

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 homodimerization activity Source: UniProtKB
  4. ubiquitin-protein transferase activity Source: UniProtKB
  5. 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
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. 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. nucleus Source: UniProtKB
  3. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

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

BgeeiQ96PM5.
CleanExiHS_RCHY1.
ExpressionAtlasiQ96PM5. baseline and differential.
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. 66 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.
GeneTreeiENSGT00390000008853.
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

        10         20         30         40         50
MAATAREDGA SGQERGQRGC EHYDRGCLLK APCCDKLYTC RLCHDNNEDH
60 70 80 90 100
QLDRFKVKEV QCINCEKIQH AQQTCEECST LFGEYYCDIC HLFDKDKKQY
110 120 130 140 150
HCENCGICRI GPKEDFFHCL KCNLCLAMNL QGRHKCIENV SRQNCPICLE
160 170 180 190 200
DIHTSRVVAH VLPCGHLLHR TCYEEMLKEG YRCPLCMHSA LDMTRYWRQL
210 220 230 240 250
DDEVAQTPMP SEYQNMTVDI LCNDCNGRST VQFHILGMKC KICESYNTAQ
260
AGGRRISLDQ Q
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. 66 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.
GeneTreei ENSGT00390000008853.
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

Bgeei Q96PM5.
CleanExi HS_RCHY1.
ExpressionAtlasi Q96PM5. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 125 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