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Q96PU4

- UHRF2_HUMAN

UniProt

Q96PU4 - UHRF2_HUMAN

Protein

E3 ubiquitin-protein ligase UHRF2

Gene

UHRF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131.6 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri344 – 39552PHD-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri733 – 77240RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. histone binding Source: UniProtKB
    3. ligase activity Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: HGNC
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell differentiation Source: HGNC
    3. cell proliferation Source: HGNC
    4. positive regulation of cell cycle arrest Source: UniProtKB
    5. protein autoubiquitination Source: HGNC
    6. protein ubiquitination Source: HGNC
    7. regulation of cell cycle Source: HGNC
    8. ubiquitin-dependent protein catabolic process Source: HGNC

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Cell cycle, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase UHRF2 (EC:6.3.2.-)
    Alternative name(s):
    Np95/ICBP90-like RING finger protein
    Short name:
    Np95-like RING finger protein
    Nuclear protein 97
    Nuclear zinc finger protein Np97
    RING finger protein 107
    Ubiquitin-like PHD and RING finger domain-containing protein 2
    Ubiquitin-like-containing PHD and RING finger domains protein 2
    Gene namesi
    Name:UHRF2
    Synonyms:NIRF, RNF107
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:12557. UHRF2.

    Subcellular locationi

    Nucleus 2 PublicationsPROSITE-ProRule annotation
    Note: Enriched at pericentric heterochromatin (PH). This localization is dependent on the interaction with H3K9me3 By similarity.By similarity

    GO - Cellular componenti

    1. nuclear heterochromatin Source: UniProtKB
    2. nucleus Source: HGNC

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Associated with various cancers. DNA copy number loss is found in multiple kinds of malignancies originating from the brain, breast, stomach, kidney, hematopoietic tissue and lung.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi307 – 3071K → R: No effect on autosumoylation. 1 Publication
    Mutagenesisi548 – 5481K → R: No effect on autosumoylation. 1 Publication
    Mutagenesisi735 – 7351C → S: No effect on autosumoylation, nor on ZNF131 sumoylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA37197.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 802802E3 ubiquitin-protein ligase UHRF2PRO_0000056147Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei667 – 6671Phosphoserine2 Publications
    Disulfide bondi704 – 704Interchain1 Publication

    Post-translational modificationi

    May be autoubiquitinated; which may lead to proteasomal degradation.1 Publication
    Phosphorylated. Phosphorylation may be mediated by CDK2.2 Publications
    Autosumoylated.

    Keywords - PTMi

    Disulfide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96PU4.
    PaxDbiQ96PU4.
    PeptideAtlasiQ96PU4.
    PRIDEiQ96PU4.

    PTM databases

    PhosphoSiteiQ96PU4.

    Expressioni

    Inductioni

    Up-regulated in proliferating fetal lung fibroblasts and in U-937 myeloid leukemia cells. Down-regulated in these cells by growth arrest and differentiation. In other cell types which cannot leave the cell cycle, such as tumoral HT-1080 and Hep-G2, levels are consistently up-regulated.1 Publication

    Gene expression databases

    ArrayExpressiQ96PU4.
    BgeeiQ96PU4.
    CleanExiHS_UHRF2.
    GenevestigatoriQ96PU4.

    Organism-specific databases

    HPAiHPA026633.
    HPA026697.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Binds methylated CpG containing oligonucleotides. Interacts with H3: the interaction has a preference for the 'Lys-9' trimethylated form of H3 (H3K9me3) By similarity. Interacts with PCNP, HDAC1 and CDK2 (inactive form). Component of a complex at least composed of UHRF2, CDK2 and CCNE1. Interacts directly with CCNE1; the interaction ubiquitinates CCNE1 and appears independent of CCNE1 phosphorylation. Interacts with CCND1; the interaction ubiquitinates CCND1 and appears independent of CCND1 phosphorylation. Interacts with p53/TP53 and RB1. Interacts with UBE2I.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCNA2P202482EBI-625304,EBI-457097
    CCNB1P146352EBI-625304,EBI-495332
    CCND1P243854EBI-625304,EBI-375001
    CCNE1P248644EBI-625304,EBI-519526
    CDK2P249415EBI-625304,EBI-375096
    RB1P064004EBI-625304,EBI-491274
    TP53P046373EBI-625304,EBI-366083

    Protein-protein interaction databases

    BioGridi125434. 54 interactions.
    IntActiQ96PU4. 37 interactions.
    MINTiMINT-1196856.
    STRINGi9606.ENSP00000276893.

    Structurei

    Secondary structure

    802
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 77
    Beta strandi13 – 197
    Helixi25 – 3511
    Turni40 – 423
    Beta strandi43 – 475
    Beta strandi54 – 574
    Helixi58 – 614
    Beta strandi68 – 736
    Turni332 – 3343
    Beta strandi338 – 3403
    Beta strandi343 – 3464
    Beta strandi348 – 3503
    Beta strandi359 – 3613
    Beta strandi363 – 3653
    Beta strandi368 – 3703
    Beta strandi373 – 3764
    Turni390 – 3923
    Beta strandi458 – 4614
    Helixi462 – 4676
    Beta strandi477 – 4815
    Turni482 – 4843
    Beta strandi485 – 4917
    Beta strandi502 – 5087
    Helixi532 – 5398
    Beta strandi541 – 5433
    Turni547 – 5493
    Helixi556 – 5583
    Beta strandi562 – 5676
    Helixi568 – 5725
    Beta strandi575 – 5773
    Beta strandi579 – 59719
    Turni599 – 6013
    Beta strandi602 – 61211
    Helixi622 – 6309
    Helixi694 – 7029
    Helixi704 – 7063
    Helixi707 – 7137
    Helixi714 – 7229
    Helixi723 – 7308
    Turni734 – 7363
    Beta strandi737 – 7393
    Beta strandi741 – 7455
    Beta strandi751 – 7533
    Helixi754 – 7629
    Turni769 – 7713
    Helixi785 – 79410
    Turni796 – 8016

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WY8NMR-A1-76[»]
    1Z6UX-ray2.10A/B672-802[»]
    2E6SNMR-A326-395[»]
    3OLNX-ray2.30A/B419-648[»]
    4PW5X-ray2.20A/B/E/F419-648[»]
    4PW6X-ray3.79A/B419-648[»]
    4PW7X-ray2.00A/B/E/F419-648[»]
    ProteinModelPortaliQ96PU4.
    SMRiQ96PU4. Positions 1-121, 124-395, 441-632, 688-802.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96PU4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7878Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini448 – 612165YDGPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni117 – 311195Required for interaction with histone H3By similarityAdd
    BLAST
    Regioni194 – 28895Interaction with PCNPAdd
    BLAST
    Regioni414 – 644231Methyl-CpG binding and interaction with HDAC1Add
    BLAST

    Sequence similaritiesi

    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation
    Contains 1 YDG domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri344 – 39552PHD-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri733 – 77240RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG3440.
    HOGENOMiHOG000124662.
    HOVERGENiHBG059298.
    InParanoidiQ96PU4.
    KOiK15713.
    OMAiYNVESPG.
    OrthoDBiEOG76DTRX.
    PhylomeDBiQ96PU4.
    TreeFamiTF106434.

    Family and domain databases

    Gene3Di2.30.280.10. 1 hit.
    2.30.30.30. 1 hit.
    3.30.40.10. 2 hits.
    InterProiIPR021991. DUF3590.
    IPR015947. PUA-like_domain.
    IPR014722. Rib_L2_dom2.
    IPR003105. SRA_YDG.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF12148. DUF3590. 1 hit.
    PF00628. PHD. 1 hit.
    PF02182. SAD_SRA. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view]
    SMARTiSM00249. PHD. 1 hit.
    SM00184. RING. 2 hits.
    SM00466. SRA. 1 hit.
    SM00213. UBQ. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    SSF57903. SSF57903. 1 hit.
    SSF88697. SSF88697. 1 hit.
    PROSITEiPS50053. UBIQUITIN_2. 1 hit.
    PS51015. YDG. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96PU4-1) [UniParc]FASTAAdd to Basket

    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

    MWIQVRTIDG SKTCTIEDVS RKATIEELRE RVWALFDVRP ECQRLFYRGK    50
    QLENGYTLFD YDVGLNDIIQ LLVRPDPDHL PGTSTQIEAK PCSNSPPKVK 100
    KAPRVGPSNQ PSTSARARLI DPGFGIYKVN ELVDARDVGL GAWFEAHIHS 150
    VTRASDGQSR GKTPLKNGSS CKRTNGNIKH KSKENTNKLD SVPSTSNSDC 200
    VAADEDVIYH IQYDEYPESG TLEMNVKDLR PRARTILKWN ELNVGDVVMV 250
    NYNVESPGQR GFWFDAEITT LKTISRTKKE LRVKIFLGGS EGTLNDCKII 300
    SVDEIFKIER PGAHPLSFAD GKFLRRNDPE CDLCGGDPEK KCHSCSCRVC 350
    GGKHEPNMQL LCDECNVAYH IYCLNPPLDK VPEEEYWYCP SCKTDSSEVV 400
    KAGERLKMSK KKAKMPSAST ESRRDWGRGM ACVGRTRECT IVPSNHYGPI 450
    PGIPVGSTWR FRVQVSEAGV HRPHVGGIHG RSNDGAYSLV LAGGFADEVD 500
    RGDEFTYTGS GGKNLAGNKR IGAPSADQTL TNMNRALALN CDAPLDDKIG 550
    AESRNWRAGK PVRVIRSFKG RKISKYAPEE GNRYDGIYKV VKYWPEISSS 600
    HGFLVWRYLL RRDDVEPAPW TSEGIERSRR LCLRLQYPAG YPSDKEGKKP 650
    KGQSKKQPSG TTKRPISDDD CPSASKVYKA SDSAEAIEAF QLTPQQQHLI 700
    REDCQNQKLW DEVLSHLVEG PNFLKKLEQS FMCVCCQELV YQPVTTECFH 750
    NVCKDCLQRS FKAQVFSCPA CRHDLGQNYI MIPNEILQTL LDLFFPGYSK 800
    GR 802
    Length:802
    Mass (Da):89,985
    Last modified:December 1, 2001 - v1
    Checksum:i190E26D5A347A7FA
    GO
    Isoform 2 (identifier: Q96PU4-2) [UniParc]FASTAAdd to Basket

    Also known as: a

    The sequence of this isoform differs from the canonical sequence as follows:
         500-503: DRGD → LTEL
         504-802: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:503
    Mass (Da):56,077
    Checksum:i6C81BFDFEC2FC512
    GO

    Sequence cautioni

    The sequence CAH74120.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI13295.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti287 – 2871L → M in AAH28397. (PubMed:15489334)Curated
    Sequence conflicti329 – 3291P → T in AAH28397. (PubMed:15489334)Curated
    Sequence conflicti416 – 4161P → Q in AAH28397. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti87 – 871I → N in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035961

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei500 – 5034DRGD → LTEL in isoform 2. 1 PublicationVSP_013874
    Alternative sequencei504 – 802299Missing in isoform 2. 1 PublicationVSP_013875Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB071698 mRNA. Translation: BAB68317.1.
    AF274049 mRNA. Translation: AAM33799.1.
    AL353718, AL133480 Genomic DNA. Translation: CAH74119.1.
    AL133480, AL353718 Genomic DNA. Translation: CAI13293.1.
    AL353718, AL133480 Genomic DNA. Translation: CAH74120.1. Sequence problems.
    AL133480, AL353718 Genomic DNA. Translation: CAI13295.1. Sequence problems.
    BC028397 mRNA. Translation: AAH28397.1.
    AL137728 mRNA. Translation: CAH56383.1.
    CCDSiCCDS6469.1. [Q96PU4-1]
    RefSeqiNP_690856.1. NM_152896.2. [Q96PU4-1]
    UniGeneiHs.493401.

    Genome annotation databases

    EnsembliENST00000276893; ENSP00000276893; ENSG00000147854. [Q96PU4-1]
    ENST00000468435; ENSP00000434182; ENSG00000147854. [Q96PU4-2]
    GeneIDi115426.
    KEGGihsa:115426.
    UCSCiuc003zjy.3. human. [Q96PU4-1]

    Polymorphism databases

    DMDMi67462076.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB071698 mRNA. Translation: BAB68317.1 .
    AF274049 mRNA. Translation: AAM33799.1 .
    AL353718 , AL133480 Genomic DNA. Translation: CAH74119.1 .
    AL133480 , AL353718 Genomic DNA. Translation: CAI13293.1 .
    AL353718 , AL133480 Genomic DNA. Translation: CAH74120.1 . Sequence problems.
    AL133480 , AL353718 Genomic DNA. Translation: CAI13295.1 . Sequence problems.
    BC028397 mRNA. Translation: AAH28397.1 .
    AL137728 mRNA. Translation: CAH56383.1 .
    CCDSi CCDS6469.1. [Q96PU4-1 ]
    RefSeqi NP_690856.1. NM_152896.2. [Q96PU4-1 ]
    UniGenei Hs.493401.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WY8 NMR - A 1-76 [» ]
    1Z6U X-ray 2.10 A/B 672-802 [» ]
    2E6S NMR - A 326-395 [» ]
    3OLN X-ray 2.30 A/B 419-648 [» ]
    4PW5 X-ray 2.20 A/B/E/F 419-648 [» ]
    4PW6 X-ray 3.79 A/B 419-648 [» ]
    4PW7 X-ray 2.00 A/B/E/F 419-648 [» ]
    ProteinModelPortali Q96PU4.
    SMRi Q96PU4. Positions 1-121, 124-395, 441-632, 688-802.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125434. 54 interactions.
    IntActi Q96PU4. 37 interactions.
    MINTi MINT-1196856.
    STRINGi 9606.ENSP00000276893.

    PTM databases

    PhosphoSitei Q96PU4.

    Polymorphism databases

    DMDMi 67462076.

    Proteomic databases

    MaxQBi Q96PU4.
    PaxDbi Q96PU4.
    PeptideAtlasi Q96PU4.
    PRIDEi Q96PU4.

    Protocols and materials databases

    DNASUi 115426.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000276893 ; ENSP00000276893 ; ENSG00000147854 . [Q96PU4-1 ]
    ENST00000468435 ; ENSP00000434182 ; ENSG00000147854 . [Q96PU4-2 ]
    GeneIDi 115426.
    KEGGi hsa:115426.
    UCSCi uc003zjy.3. human. [Q96PU4-1 ]

    Organism-specific databases

    CTDi 115426.
    GeneCardsi GC09P006405.
    HGNCi HGNC:12557. UHRF2.
    HPAi HPA026633.
    HPA026697.
    MIMi 615211. gene.
    neXtProti NX_Q96PU4.
    PharmGKBi PA37197.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3440.
    HOGENOMi HOG000124662.
    HOVERGENi HBG059298.
    InParanoidi Q96PU4.
    KOi K15713.
    OMAi YNVESPG.
    OrthoDBi EOG76DTRX.
    PhylomeDBi Q96PU4.
    TreeFami TF106434.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    ChiTaRSi UHRF2. human.
    EvolutionaryTracei Q96PU4.
    GeneWikii UHRF2.
    GenomeRNAii 115426.
    NextBioi 79598.
    PROi Q96PU4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96PU4.
    Bgeei Q96PU4.
    CleanExi HS_UHRF2.
    Genevestigatori Q96PU4.

    Family and domain databases

    Gene3Di 2.30.280.10. 1 hit.
    2.30.30.30. 1 hit.
    3.30.40.10. 2 hits.
    InterProi IPR021991. DUF3590.
    IPR015947. PUA-like_domain.
    IPR014722. Rib_L2_dom2.
    IPR003105. SRA_YDG.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF12148. DUF3590. 1 hit.
    PF00628. PHD. 1 hit.
    PF02182. SAD_SRA. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    SMARTi SM00249. PHD. 1 hit.
    SM00184. RING. 2 hits.
    SM00466. SRA. 1 hit.
    SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    SSF57903. SSF57903. 1 hit.
    SSF88697. SSF88697. 1 hit.
    PROSITEi PS50053. UBIQUITIN_2. 1 hit.
    PS51015. YDG. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "NIRF, a novel RING finger protein, is involved in cell-cycle regulation."
      Mori T., Li Y., Hata H., Ono K., Kochi H.
      Biochem. Biophys. Res. Commun. 296:530-536(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INDUCTION, FUNCTION, INTERACTION WITH PCNP.
      Tissue: Fetal brain.
    2. "LMO2-induced T cell leukemias overexpress a novel gene, Uhr1, containing RING and PHD zinc fingers and an ubiquitin-like domain."
      Davenport J.W., Fernandes E.R., Neale G.A.M., Goorha R.M.
      Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 2).
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 636-802 (ISOFORM 1).
      Tissue: Testis.
    6. Cited for: FUNCTION IN CELL CYCLE, PHOSPHORYLATION, INTERACTION WITH CDK2, IDENTIFICATION IN A COMPLEX WITH CDK2 AND CCNE1.
    7. "NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein."
      Mori T., Li Y., Hata H., Kochi H.
      FEBS Lett. 557:209-214(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH PCNP, FUNCTION.
    8. "ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain."
      Unoki M., Nishidate T., Nakamura Y.
      Oncogene 23:7601-7610(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HDAC1.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor."
      Mori T., Ikeda D.D., Fukushima T., Takenoshita S., Kochi H.
      Cell Cycle 10:3284-3299(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CCDN1; CCNE1; TP53 AND RB1, ASSOCIATION WITH TUMORIGENESIS.
    12. "UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131."
      Oh Y., Chung K.C.
      J. Biol. Chem. 288:9102-9111(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOSUMOYLATION, INTERACTION WITH UBE2I, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-307; LYS-548 AND CYS-735.
    13. "Solution structure of the N-terminal ubiquitin-like domain in human NP95/ICBP90-like RING finger protein (NIRF)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-76.
    14. "2.1 Angstrom crystal structure of the human ubiquitin ligase NIRF."
      Structural genomics consortium (SGC)
      Submitted (JAN-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 672-802 IN COMPLEX WITH ZINC IONS.
    15. "2.1 Angstrom crystal structure of the human ubiquitin ligase NIRF."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 672-802, SUBUNIT, DISULFIDE BOND.
    16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-87.

    Entry informationi

    Entry nameiUHRF2_HUMAN
    AccessioniPrimary (citable) accession number: Q96PU4
    Secondary accession number(s): Q5VYR1
    , Q5VYR3, Q659C8, Q8TAG7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 124 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 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3