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Q96T88

- UHRF1_HUMAN

UniProt

Q96T88 - UHRF1_HUMAN

Protein

E3 ubiquitin-protein ligase UHRF1

Gene

UHRF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Multidomain protein that acts as a key epigenetic regulator by bridging DNA methylation and chromatin modification. Specifically recognizes and binds hemimethylated DNA at replication forks via its YDG domain and recruits DNMT1 methyltransferase to ensure faithful propagation of the DNA methylation patterns through DNA replication. In addition to its role in maintenance of DNA methylation, also plays a key role in chromatin modification: through its tudor-like regions and PHD-type zinc fingers, specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3) and unmethylated at 'Arg-2' (H3R2me0), respectively, and recruits chromatin proteins. Enriched in pericentric heterochromatin where it recruits different chromatin modifiers required for this chromatin replication. Also localizes to euchromatic regions where it negatively regulates transcription possibly by impacting DNA methylation and histone modifications. Has E3 ubiquitin-protein ligase activity by mediating the ubiquitination of target proteins such as histone H3 and PML. It is still unclear how E3 ubiquitin-protein ligase activity is related to its role in chromatin in vivo. May be involved in DNA repair.9 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei316 – 3161Histone H3K4me0
    Binding sitei327 – 3271Histone H3R2me0
    Binding sitei330 – 3301Histone H3R2me0
    Binding sitei469 – 4691Methylcytosine
    Sitei479 – 4791Required to confer preferential recognition of cytosine over thymine
    Sitei489 – 4891Required to discriminate between hemimethylated DNA versus symmetrically methylated DNA
    Sitei491 – 4911Required for affinity and specificity for 5-mCpG sequence

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri310 – 36657PHD-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri724 – 76340RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
    2. hemi-methylated DNA-binding Source: UniProtKB
    3. histone binding Source: UniProtKB
    4. identical protein binding Source: BHF-UCL
    5. ligase activity Source: UniProtKB-KW
    6. methylated histone binding Source: UniProtKB
    7. methyl-CpG binding Source: UniProtKB
    8. nucleosomal histone binding Source: BHF-UCL
    9. protein binding Source: UniProtKB
    10. sequence-specific DNA binding transcription factor activity Source: ProtInc
    11. ubiquitin-protein transferase activity Source: UniProtKB
    12. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell proliferation Source: BHF-UCL
    3. DNA repair Source: UniProtKB-KW
    4. histone monoubiquitination Source: BHF-UCL
    5. histone ubiquitination Source: UniProtKB
    6. maintenance of DNA methylation Source: UniProtKB
    7. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    8. positive regulation of cellular protein metabolic process Source: BHF-UCL
    9. positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity Source: BHF-UCL
    10. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    11. protein autoubiquitination Source: UniProtKB
    12. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
    13. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Ligase, Repressor

    Keywords - Biological processi

    Cell cycle, DNA damage, DNA repair, Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ96T88.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase UHRF1 (EC:6.3.2.-)
    Alternative name(s):
    Inverted CCAAT box-binding protein of 90 kDa
    Nuclear protein 95
    Nuclear zinc finger protein Np95
    Short name:
    HuNp95
    Short name:
    hNp95
    RING finger protein 106
    Transcription factor ICBP90
    Ubiquitin-like PHD and RING finger domain-containing protein 1
    Short name:
    hUHRF1
    Ubiquitin-like-containing PHD and RING finger domains protein 1
    Gene namesi
    Name:UHRF1
    Synonyms:ICBP90, NP95, RNF106
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Unplaced

    Organism-specific databases

    HGNCiHGNC:12556. UHRF1.

    Subcellular locationi

    Nucleus 5 PublicationsPROSITE-ProRule annotation
    Note: Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions.

    GO - Cellular componenti

    1. euchromatin Source: UniProtKB
    2. heterochromatin Source: UniProtKB
    3. nuclear chromatin Source: UniProtKB
    4. nuclear matrix Source: BHF-UCL
    5. nucleus Source: BHF-UCL
    6. replication fork Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Defects in UHRF1 may be a cause of cancers. Overexpressed in many different forms of human cancers, including bladder, breast, cervical, colorectal and prostate cancers, as well as pancreatic adenocarcinomas, rhabdomyosarcomas and gliomas. Plays an important role in the correlation of histone modification and gene silencing in cancer progression. Expression is associated with a poor prognosis in patients with various cancers, suggesting that it participates in cancer progression.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi142 – 1421D → A: Impaired binding to histone H3 without affecting the protein folding; when associated with A-153. 1 Publication
    Mutagenesisi145 – 1451D → A: Impaired binding to histone H3. 1 Publication
    Mutagenesisi152 – 1521F → A: Impaired binding to histone H3. 1 Publication
    Mutagenesisi153 – 1531E → A: Impaired binding to histone H3 without affecting the protein folding; when associated with A-142. 1 Publication
    Mutagenesisi188 – 1881Y → A: Impaired binding to histone H3. 2 Publications
    Mutagenesisi190 – 1901D → A: Slightly impaired binding to histone H3. 1 Publication
    Mutagenesisi191 – 1911Y → A: Impaired binding to histone H3. 1 Publication
    Mutagenesisi295 – 2962RR → AA: Disrupts the simultaneous binding to H3R2me0 and H3K9me3.
    Mutagenesisi298 – 2981S → A: Diminishes phosphorylation by PKA. 1 Publication
    Mutagenesisi330 – 3301Q → A or K: Does not affect ability to bind histone H3 peptide. 1 Publication
    Mutagenesisi334 – 3352DE → AA: Abolishes binding to histone H3. 3 Publications
    Mutagenesisi334 – 3341D → A: Impaired binding to histone H3. 3 Publications
    Mutagenesisi337 – 3371D → A: Impaired binding to histone H3. 3 Publications
    Mutagenesisi433 – 4331R → A: Does not affect ability to bind DNA. 1 Publication
    Mutagenesisi443 – 4431R → A: Decreased ability to bind DNA. 1 Publication
    Mutagenesisi448 – 4481G → D: Decreased affinity for DNA. 1 Publication
    Mutagenesisi466 – 4661Y → G: Decreased ability to bind DNA. 1 Publication
    Mutagenesisi469 – 4691D → G: Abolishes ability to bind hemimethylated DNA.
    Mutagenesisi489 – 4891N → A: Abolishes specificity to hemimethylated DNA. 1 Publication
    Mutagenesisi491 – 4911R → A: Decreased binding to methylated DNA but does not affect ability to bind DNA. 2 Publications
    Mutagenesisi639 – 6391S → A: Prevents phosphorylation by CDK1 during M phase, leading to increased stability. 1 Publication
    Mutagenesisi639 – 6391S → D: Mimics phosphorylation; impaired interaction with USP7, leading to decreased stability. 1 Publication
    Mutagenesisi651 – 6511S → A: No effect on in vitro phosphorylation by PKA. 1 Publication
    Mutagenesisi666 – 6661S → A: No effect on in vitro phosphorylation by PKA. 1 Publication
    Mutagenesisi741 – 7411H → A: Abolishes E3 ubiquitin-protein ligase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA37196.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 793793E3 ubiquitin-protein ligase UHRF1PRO_0000056144Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei76 – 761Phosphoserine3 Publications
    Modified residuei91 – 911Phosphoserine2 Publications
    Modified residuei287 – 2871Phosphoserine6 Publications
    Modified residuei298 – 2981Phosphoserine; by PKA2 Publications
    Cross-linki385 – 385Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei399 – 3991N6-acetyllysine1 Publication
    Modified residuei546 – 5461N6-acetyllysine1 Publication
    Modified residuei639 – 6391Phosphoserine; by CDK15 Publications
    Modified residuei651 – 6511Phosphoserine2 Publications
    Modified residuei707 – 7071Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylation at Ser-298 of the linker region decreases the binding to H3K9me3. Phosphorylation at Ser-639 by CDK1 during M phase impairs interaction with USP7, preventing deubiquitination and leading to degradation by the proteasome.6 Publications
    Ubiquitinated; which leads to proteasomal degradation. Autoubiquitinated; interaction with USP7 leads to deubiquitination and prevents degradation. Ubiquitination and degradation takes place during M phase, when phosphorylation at Ser-639 prevents intereaction with USP7 and subsequent deubiquitination. Polyubiquitination may be stimulated by DNA damage.8 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ96T88.
    PaxDbiQ96T88.
    PRIDEiQ96T88.

    PTM databases

    PhosphoSiteiQ96T88.

    Expressioni

    Tissue specificityi

    Expressed in thymus, bone marrow, testis, lung and heart. Overexpressed in breast cancer.3 Publications

    Developmental stagei

    Expressed in fetal thymus, liver and kidney.1 Publication

    Inductioni

    Up-regulated in proliferating cells, and down-regulated in quiescent cells. Down-regulated upon adriamycin-induced DNA damage, in a p53/TP53 and CDKN1A-dependent way. Induced by E2F1 transcription factor.4 Publications

    Gene expression databases

    CleanExiHS_UHRF1.
    GenevestigatoriQ96T88.

    Interactioni

    Subunit structurei

    Interacts with DNMT3A and DNMT3B By similarity. Interacts with DNMT1; the interaction is direct. Interacts with USP7; leading to its deubiquitination. Interacts with histone H3. Interacts with HDAC1, but not with HDAC2. Interacts with UHRF1BP1. Interacts with PML. Interacts with EHMT2. Binds hemimethylated CpG containing oligonucleotides.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DNMT1P2635812EBI-1548946,EBI-719459
    DNMT3AQ9Y6K17EBI-1548946,EBI-923653
    DNMT3BQ9UBC37EBI-1548946,EBI-80125

    Protein-protein interaction databases

    BioGridi118893. 42 interactions.
    IntActiQ96T88. 6 interactions.
    MINTiMINT-2815626.
    STRINGi9606.ENSP00000381295.

    Structurei

    Secondary structure

    793
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1 – 77
    Beta strandi13 – 197
    Helixi25 – 3612
    Helixi40 – 423
    Beta strandi43 – 475
    Turni58 – 625
    Beta strandi68 – 736
    Turni127 – 1293
    Beta strandi140 – 1445
    Turni146 – 1483
    Beta strandi151 – 16111
    Beta strandi164 – 1674
    Turni179 – 1813
    Beta strandi182 – 1909
    Helixi192 – 1943
    Beta strandi196 – 2005
    Helixi201 – 2033
    Beta strandi204 – 2063
    Beta strandi210 – 2123
    Helixi214 – 2163
    Beta strandi222 – 2276
    Beta strandi229 – 2313
    Beta strandi237 – 24812
    Beta strandi253 – 2608
    Beta strandi262 – 27211
    Helixi274 – 2763
    Beta strandi277 – 2793
    Beta strandi283 – 2864
    Turni303 – 3075
    Beta strandi309 – 3113
    Turni314 – 3163
    Turni319 – 3213
    Beta strandi323 – 3253
    Helixi327 – 3293
    Beta strandi330 – 3323
    Turni334 – 3363
    Beta strandi339 – 3413
    Helixi342 – 3443
    Beta strandi345 – 3473
    Beta strandi354 – 3563
    Turni361 – 3633
    Beta strandi417 – 4193
    Beta strandi429 – 4324
    Helixi433 – 4386
    Turni439 – 4424
    Beta strandi448 – 4525
    Turni453 – 4553
    Beta strandi456 – 4627
    Beta strandi473 – 4797
    Turni487 – 4893
    Helixi503 – 5119
    Beta strandi512 – 5143
    Turni518 – 5203
    Helixi527 – 5293
    Beta strandi533 – 5386
    Helixi539 – 5446
    Beta strandi546 – 5483
    Beta strandi550 – 56819
    Beta strandi572 – 58211
    Helixi592 – 60110
    Helixi611 – 6177
    Helixi678 – 6869
    Helixi688 – 6903
    Helixi691 – 6999
    Beta strandi706 – 7083
    Helixi710 – 72112
    Turni725 – 7273
    Beta strandi728 – 7303
    Beta strandi732 – 7365
    Beta strandi742 – 7443
    Helixi745 – 7539
    Turni760 – 7623
    Helixi776 – 78510
    Turni787 – 7926

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FAZX-ray2.00A/B1-76[»]
    2L3RNMR-A126-285[»]
    2LGGNMR-A298-366[»]
    2LGKNMR-A298-366[»]
    2LGLNMR-A298-366[»]
    2PB7X-ray1.90A408-643[»]
    3ASKX-ray2.90A/B/C/D134-367[»]
    3ASLX-ray1.41A298-367[»]
    3BI7X-ray1.70A414-617[»]
    3CLZX-ray2.20A/B/C/D414-617[»]
    3DB3X-ray2.40A126-285[»]
    3DB4X-ray2.40A126-285[»]
    3DWHX-ray1.95A414-617[»]
    3FL2X-ray1.75A672-793[»]
    3SHBX-ray1.80A298-366[»]
    3SOUX-ray1.80A/B298-367[»]
    3SOWX-ray1.95A/B298-367[»]
    3SOXX-ray2.65A/B298-367[»]
    3T6RX-ray1.95A/B299-364[»]
    3ZVYX-ray1.95A/B296-367[»]
    3ZVZX-ray1.45B314-367[»]
    4GY5X-ray2.96A/B/C/D134-366[»]
    ProteinModelPortaliQ96T88.
    SMRiQ96T88. Positions 1-76, 126-367, 377-617, 675-793.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96T88.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7878Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST
    Domaini419 – 582164YDGPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni133 – 20977Tudor-like 1Add
    BLAST
    Regioni216 – 28368Tudor-like 2Add
    BLAST
    Regioni296 – 3016Linker
    Regioni333 – 3375Histone H3R2me0 binding
    Regioni353 – 3553Histone H3R2me0 binding
    Regioni445 – 4462Required to promote base flippingBy similarity
    Regioni463 – 4642Methylcytosine binding
    Regioni466 – 4694Required for formation of a 5-methylcytosine-binding pocket
    Regioni478 – 4814Required for formation of a 5-methylcytosine-binding pocket

    Domaini

    The tudor-like regions specifically recognize and bind histone H3 unmethylated at 'Arg-2' (H3R2me0), while the PHD-type zinc finger specifically recognizes and binds histone H3 trimethylated at 'Lys-9' (H3K9me3). The tudor-like regions simultaneously recognizes H3K9me3 through a conserved aromatic cage in the first tudor-like subdomain and unmodified H3K4 (H3K4me0) within a groove between the tandem subdomains (PubMed:21489993, PubMed:21777816 and PubMed:22100450). The linker region plays a role in the formation of a histone H3-binding hole between the reader modules formed by the tudor-like regions and the PHD-type zinc finger by making extended contacts with the tandem tudor-like regions (PubMed:22837395).1 Publication
    The YDG domain (also named SRA domain) specifically recognizes and binds hemimethylated DNA at replication forks (DNA that is only methylated on the mother strand of replicating DNA) (PubMed:17673620). It contains a binding pocket that accommodates the 5-methylcytosine that is flipped out of the duplex DNA. 2 specialized loops reach through the resulting gap in the DNA from both the major and the minor grooves to read the other 3 bases of the CpG duplex. The major groove loop confers both specificity for the CpG dinucleotide and discrimination against methylation of deoxycytidine of the complementary strand (PubMed:18772889). The YDG domain also recognizes and binds 5-hydroxymethylcytosine (5hmC) (PubMed:21731699).3 Publications
    The RING finger is required for ubiquitin ligase activity.By similarity

    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 fingeri310 – 36657PHD-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri724 – 76340RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG3440.
    HOGENOMiHOG000124662.
    HOVERGENiHBG059298.
    InParanoidiQ96T88.
    KOiK10638.
    PhylomeDBiQ96T88.

    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. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96T88-1) [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

    MWIQVRTMDG RQTHTVDSLS RLTKVEELRR KIQELFHVEP GLQRLFYRGK    50
    QMEDGHTLFD YEVRLNDTIQ LLVRQSLVLP HSTKERDSEL SDTDSGCCLG 100
    QSESDKSSTH GEAAAETDSR PADEDMWDET ELGLYKVNEY VDARDTNMGA 150
    WFEAQVVRVT RKAPSRDEPC SSTSRPALEE DVIYHVKYDD YPENGVVQMN 200
    SRDVRARART IIKWQDLEVG QVVMLNYNPD NPKERGFWYD AEISRKRETR 250
    TARELYANVV LGDDSLNDCR IIFVDEVFKI ERPGEGSPMV DNPMRRKSGP 300
    SCKHCKDDVN RLCRVCACHL CGGRQDPDKQ LMCDECDMAF HIYCLDPPLS 350
    SVPSEDEWYC PECRNDASEV VLAGERLRES KKKAKMASAT SSSQRDWGKG 400
    MACVGRTKEC TIVPSNHYGP IPGIPVGTMW RFRVQVSESG VHRPHVAGIH 450
    GRSNDGAYSL VLAGGYEDDV DHGNFFTYTG SGGRDLSGNK RTAEQSCDQK 500
    LTNTNRALAL NCFAPINDQE GAEAKDWRSG KPVRVVRNVK GGKNSKYAPA 550
    EGNRYDGIYK VVKYWPEKGK SGFLVWRYLL RRDDDEPGPW TKEGKDRIKK 600
    LGLTMQYPEG YLEALANRER EKENSKREEE EQQEGGFASP RTGKGKWKRK 650
    SAGGGPSRAG SPRRTSKKTK VEPYSLTAQQ SSLIREDKSN AKLWNEVLAS 700
    LKDRPASGSP FQLFLSKVEE TFQCICCQEL VFRPITTVCQ HNVCKDCLDR 750
    SFRAQVFSCP ACRYDLGRSY AMQVNQPLQT VLNQLFPGYG NGR 793
    Length:793
    Mass (Da):89,814
    Last modified:December 1, 2001 - v1
    Checksum:iE65B15657525C89F
    GO
    Isoform 2 (identifier: Q96T88-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MGVFAVPPLSSDTM

    Note: No experimental confirmation available.

    Show »
    Length:806
    Mass (Da):91,116
    Checksum:iBFE365939E846398
    GO

    Sequence cautioni

    The sequence BAB15177.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti383 – 3831K → E in BAF82078. (PubMed:14702039)Curated
    Sequence conflicti383 – 3831K → N in AAF28469. (PubMed:10646863)Curated
    Sequence conflicti457 – 4571A → S in AAF28469. (PubMed:10646863)Curated
    Sequence conflicti675 – 6751S → N in BAF82078. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti240 – 2401D → H.1 Publication
    Corresponds to variant rs17886098 [ dbSNP | Ensembl ].
    VAR_022554
    Natural varianti379 – 3791E → K.2 Publications
    Corresponds to variant rs17885791 [ dbSNP | Ensembl ].
    VAR_022555
    Natural varianti638 – 6381A → T.2 Publications
    Corresponds to variant rs17883331 [ dbSNP | Ensembl ].
    VAR_022556
    Natural varianti642 – 6421T → M.1 Publication
    Corresponds to variant rs17884843 [ dbSNP | Ensembl ].
    VAR_022557
    Natural varianti713 – 7131L → F.1 Publication
    Corresponds to variant rs17883563 [ dbSNP | Ensembl ].
    VAR_022558

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MGVFAVPPLSSDTM in isoform 2. 1 PublicationVSP_044394

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129507 mRNA. Translation: AAF28469.1.
    AB177623 mRNA. Translation: BAF36719.1.
    AB177624 mRNA. Translation: BAF36720.1.
    AB075601 mRNA. Translation: BAC20576.1.
    AF274048 mRNA. Translation: AAK55744.1.
    EF560733 mRNA. Translation: ABQ59043.1.
    AK025578 mRNA. Translation: BAB15177.1. Different initiation.
    AK289389 mRNA. Translation: BAF82078.1.
    AK314579 mRNA. Translation: BAG37156.1.
    AY787925 Genomic DNA. Translation: AAV40831.1.
    AC027319 Genomic DNA. No translation available.
    AC053467 Genomic DNA. Translation: AAF64067.1.
    CH471139 Genomic DNA. Translation: EAW69187.1.
    BC113875 mRNA. Translation: AAI13876.2.
    RefSeqiNP_001041666.1. NM_001048201.2. [Q96T88-1]
    NP_001276979.1. NM_001290050.1. [Q96T88-1]
    NP_001276980.1. NM_001290051.1. [Q96T88-1]
    NP_001276981.1. NM_001290052.1. [Q96T88-1]
    NP_037414.3. NM_013282.4.
    UniGeneiHs.108106.

    Genome annotation databases

    GeneIDi29128.
    KEGGihsa:29128.
    UCSCiuc002mbo.3. human. [Q96T88-1]

    Polymorphism databases

    DMDMi67462077.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF129507 mRNA. Translation: AAF28469.1 .
    AB177623 mRNA. Translation: BAF36719.1 .
    AB177624 mRNA. Translation: BAF36720.1 .
    AB075601 mRNA. Translation: BAC20576.1 .
    AF274048 mRNA. Translation: AAK55744.1 .
    EF560733 mRNA. Translation: ABQ59043.1 .
    AK025578 mRNA. Translation: BAB15177.1 . Different initiation.
    AK289389 mRNA. Translation: BAF82078.1 .
    AK314579 mRNA. Translation: BAG37156.1 .
    AY787925 Genomic DNA. Translation: AAV40831.1 .
    AC027319 Genomic DNA. No translation available.
    AC053467 Genomic DNA. Translation: AAF64067.1 .
    CH471139 Genomic DNA. Translation: EAW69187.1 .
    BC113875 mRNA. Translation: AAI13876.2 .
    RefSeqi NP_001041666.1. NM_001048201.2. [Q96T88-1 ]
    NP_001276979.1. NM_001290050.1. [Q96T88-1 ]
    NP_001276980.1. NM_001290051.1. [Q96T88-1 ]
    NP_001276981.1. NM_001290052.1. [Q96T88-1 ]
    NP_037414.3. NM_013282.4.
    UniGenei Hs.108106.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FAZ X-ray 2.00 A/B 1-76 [» ]
    2L3R NMR - A 126-285 [» ]
    2LGG NMR - A 298-366 [» ]
    2LGK NMR - A 298-366 [» ]
    2LGL NMR - A 298-366 [» ]
    2PB7 X-ray 1.90 A 408-643 [» ]
    3ASK X-ray 2.90 A/B/C/D 134-367 [» ]
    3ASL X-ray 1.41 A 298-367 [» ]
    3BI7 X-ray 1.70 A 414-617 [» ]
    3CLZ X-ray 2.20 A/B/C/D 414-617 [» ]
    3DB3 X-ray 2.40 A 126-285 [» ]
    3DB4 X-ray 2.40 A 126-285 [» ]
    3DWH X-ray 1.95 A 414-617 [» ]
    3FL2 X-ray 1.75 A 672-793 [» ]
    3SHB X-ray 1.80 A 298-366 [» ]
    3SOU X-ray 1.80 A/B 298-367 [» ]
    3SOW X-ray 1.95 A/B 298-367 [» ]
    3SOX X-ray 2.65 A/B 298-367 [» ]
    3T6R X-ray 1.95 A/B 299-364 [» ]
    3ZVY X-ray 1.95 A/B 296-367 [» ]
    3ZVZ X-ray 1.45 B 314-367 [» ]
    4GY5 X-ray 2.96 A/B/C/D 134-366 [» ]
    ProteinModelPortali Q96T88.
    SMRi Q96T88. Positions 1-76, 126-367, 377-617, 675-793.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118893. 42 interactions.
    IntActi Q96T88. 6 interactions.
    MINTi MINT-2815626.
    STRINGi 9606.ENSP00000381295.

    Chemistry

    ChEMBLi CHEMBL2424510.

    PTM databases

    PhosphoSitei Q96T88.

    Polymorphism databases

    DMDMi 67462077.

    Proteomic databases

    MaxQBi Q96T88.
    PaxDbi Q96T88.
    PRIDEi Q96T88.

    Protocols and materials databases

    DNASUi 29128.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 29128.
    KEGGi hsa:29128.
    UCSCi uc002mbo.3. human. [Q96T88-1 ]

    Organism-specific databases

    CTDi 29128.
    GeneCardsi GC19P004910.
    HGNCi HGNC:12556. UHRF1.
    MIMi 607990. gene.
    neXtProti NX_Q96T88.
    PharmGKBi PA37196.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3440.
    HOGENOMi HOG000124662.
    HOVERGENi HBG059298.
    InParanoidi Q96T88.
    KOi K10638.
    PhylomeDBi Q96T88.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    SignaLinki Q96T88.

    Miscellaneous databases

    EvolutionaryTracei Q96T88.
    GeneWikii UHRF1.
    GenomeRNAii 29128.
    NextBioi 35463698.
    PROi Q96T88.
    SOURCEi Search...

    Gene expression databases

    CleanExi HS_UHRF1.
    Genevestigatori Q96T88.

    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. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ICBP90, a novel human CCAAT binding protein, involved in the regulation of topoisomerase IIa expression."
      Hopfner R., Mousli M., Jeltsch J.-M., Voulgaris A., Lutz Y., Marin C., Bellocq J.-P., Oudet P., Bronner C.
      Cancer Res. 60:121-128(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, DNA-BINDING, INDUCTION, FUNCTION.
      Tissue: Thymus.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "LMO2-induced T cell leukemias overexpress Np95, a gene 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).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    5. "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), VARIANTS LYS-379 AND THR-638.
    6. NIEHS SNPs program
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-240; LYS-379; THR-638; MET-642 AND PHE-713.
    7. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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).
    10. "ICBP90 belongs to a new family of proteins with an expression that is deregulated in cancer cells."
      Mousli M., Hopfner R., Abbady A.-Q., Monte D., Jeanblanc M., Oudet P., Louis B., Bronner C.
      Br. J. Cancer 89:120-127(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, TISSUE SPECIFICITY.
    11. Cited for: PHOSPHORYLATION, PHOSPHORYLATION AT SER-298, MUTAGENESIS OF SER-298; SER-651 AND SER-666.
    12. "Down-regulation of nuclear protein ICBP90 by p53/p21Cip1/WAF1-dependent DNA-damage checkpoint signals contributes to cell cycle arrest at G1/S transition."
      Arima Y., Hirota T., Bronner C., Mousli M., Fujiwara T., Niwa S., Ishikawa H., Saya H.
      Genes Cells 9:131-142(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, UBIQUITINATION, FUNCTION.
    13. "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, INDUCTION, TISSUE SPECIFICITY, DNA-BINDING, INTERACTION WITH HDAC1 AND UHRF1BP1.
    14. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-385.
      Tissue: Mammary cancer.
    17. "UHRF1 plays a role in maintaining DNA methylation in mammalian cells."
      Bostick M., Kim J.K., Esteve P.O., Clark A., Pradhan S., Jacobsen S.E.
      Science 317:1760-1764(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DNMT1.
    18. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "ICBP90, a novel methyl K9 H3 binding protein linking protein ubiquitination with heterochromatin formation."
      Karagianni P., Amazit L., Qin J., Wong J.
      Mol. Cell. Biol. 28:705-717(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOUBIQUITINATION.
    20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-91 AND SER-707, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    21. "UHRF1 is a novel molecular marker for diagnosis and the prognosis of bladder cancer."
      Unoki M., Kelly J.D., Neal D.E., Ponder B.A., Nakamura Y., Hamamoto R.
      Br. J. Cancer 101:98-105(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CANCER.
    22. "UHRF1 binds G9a and participates in p21 transcriptional regulation in mammalian cells."
      Kim J.K., Esteve P.O., Jacobsen S.E., Pradhan S.
      Nucleic Acids Res. 37:493-505(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EHMT2.
    23. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    24. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-399 AND LYS-546, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. "The multi-domain protein Np95 connects DNA methylation and histone modification."
      Rottach A., Frauer C., Pichler G., Bonapace I.M., Spada F., Leonhardt H.
      Nucleic Acids Res. 38:1796-1804(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-188 AND TYR-191.
    26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76; SER-287; SER-639 AND SER-707, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "The USP7/Dnmt1 complex stimulates the DNA methylation activity of Dnmt1 and regulates the stability of UHRF1."
      Felle M., Joppien S., Nemeth A., Diermeier S., Thalhammer V., Dobner T., Kremmer E., Kappler R., Langst G.
      Nucleic Acids Res. 39:8355-8365(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOUBIQUITINATION, DEUBIQUITINATION BY USP7, INTERACTION WITH USP7 AND DNMT1.
    29. "Recognition of 5-hydroxymethylcytosine by the Uhrf1 SRA domain."
      Frauer C., Hoffmann T., Bultmann S., Casa V., Cardoso M.C., Antes I., Leonhardt H.
      PLoS ONE 6:E21306-E21306(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: HYDROXYMETHYLCYTOSINE-BINDING.
    30. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287 AND SER-651, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. "The epigenetic regulator UHRF1 promotes ubiquitination-mediated degradation of the tumor-suppressor protein promyelocytic leukemia protein."
      Guan D., Factor D., Liu Y., Wang Z., Kao H.Y.
      Oncogene 32:3819-3828(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PML, MUTAGENESIS OF HIS-741.
    32. "UHRF1 coordinates peroxisome proliferator activated receptor gamma (PPARG) epigenetic silencing and mediates colorectal cancer progression."
      Sabatino L., Fucci A., Pancione M., Carafa V., Nebbioso A., Pistore C., Babbio F., Votino C., Laudanna C., Ceccarelli M., Altucci L., Bonapace I.M., Colantuoni V.
      Oncogene 31:5061-5072(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CANCER.
    33. Cited for: INVOLVEMENT IN CANCER.
    34. "M phase phosphorylation of the epigenetic regulator UHRF1 regulates its physical association with the deubiquitylase USP7 and stability."
      Ma H., Chen H., Guo X., Wang Z., Sowa M.E., Zheng L., Hu S., Zeng P., Guo R., Diao J., Lan F., Harper J.W., Shi Y.G., Xu Y., Shi Y.
      Proc. Natl. Acad. Sci. U.S.A. 109:4828-4833(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOUBIQUITINATION, DEUBIQUITINATION BY USP7, INTERACTION WITH USP7, PHOSPHORYLATION AT SER-639, MUTAGENESIS OF SER-639.
    35. "Ubiquitin-like domain of human nuclear zinc finger protein NP95."
      Structural genomics consortium (SGC)
      Submitted (JAN-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-76.
    36. "Expression, purification, crystallization and preliminary crystallographic study of the SRA domain of the human UHRF1 protein."
      Delagoutte B., Lallous N., Birck C., Oudet P., Samama J.P.
      Acta Crystallogr. F 64:922-925(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 408-643.
    37. "Structure and hemimethylated CpG binding of the SRA domain from human UHRF1."
      Qian C., Li S., Jakoncic J., Zeng L., Walsh M.J., Zhou M.M.
      J. Biol. Chem. 283:34490-34494(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 414-617, MUTAGENESIS OF ARG-433; ARG-443; TYR-466 AND ARG-491.
    38. "Structural basis for recognition of hemi-methylated DNA by the SRA domain of human UHRF1."
      Avvakumov G.V., Walker J.R., Xue S., Li Y., Duan S., Bronner C., Arrowsmith C.H., Dhe-Paganon S.
      Nature 455:822-825(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 414-617 IN COMPLEX WITH HEMIMETHYLATED DNA, MUTAGENESIS OF GLY-448; ASN-489 AND ARG-491.
    39. "Crystal structure of PHD domain of UHRF1 and insights into recognition of unmodified histone H3 arginine residue 2."
      Hu L., Li Z., Wang P., Lin Y., Xu Y.
      Cell Res. 21:1374-1378(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 298-366, MUTAGENESIS OF ASP-334 AND ASP-337.
    40. "Structural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD finger."
      Wang C., Shen J., Yang Z., Chen P., Zhao B., Hu W., Lan W., Tong X., Wu H., Li G., Cao C.
      Cell Res. 21:1379-1382(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 298-366, MUTAGENESIS OF ASP-334 AND ASP-337.
    41. Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 126-285, STRUCTURE BY NMR OF 126-285, MUTAGENESIS OF ASP-142; ASP-145; PHE-152; GLU-153; TYR-188 AND ASP-190.
    42. "PHD finger recognition of unmodified histone H3R2 links UHRF1 to regulation of euchromatic gene expression."
      Rajakumara E., Wang Z., Ma H., Hu L., Chen H., Lin Y., Guo R., Wu F., Li H., Lan F., Shi Y.G., Xu Y., Patel D.J., Shi Y.
      Mol. Cell 43:275-284(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 298-367 IN COMPLEX WITH ZINC AND HISTONE H3 PEPTIDE, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 334-ASP-GLU-335.
    43. "The PHD finger of human UHRF1 reveals a new subgroup of unmethylated histone H3 tail readers."
      Lallous N., Legrand P., McEwen A.G., Ramon-Maiques S., Samama J.P., Birck C.
      PLoS ONE 6:E27599-E27599(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 314-367, MUTAGENESIS OF GLN-330; ASP-334 AND ASP-337.
    44. "UHRF1 double tudor domain and the adjacent PHD finger act together to recognize K9me3-containing histone H3 tail."
      Xie S., Jakoncic J., Qian C.
      J. Mol. Biol. 415:318-328(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 299-364 IN COMPLEX WITH HISTONE H3 PEPTIDE.
    45. "Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1."
      Arita K., Isogai S., Oda T., Unoki M., Sugita K., Sekiyama N., Kuwata K., Hamamoto R., Tochio H., Sato M., Ariyoshi M., Shirakawa M.
      Proc. Natl. Acad. Sci. U.S.A. 109:12950-12955(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 134-367 IN COMPLEX WITH ZINC AND HISTONE H3 PEPTIDE, PHOSPHORYLATION AT SER-298, MUTAGENESIS OF 295-ARG-ARG-296.

    Entry informationi

    Entry nameiUHRF1_HUMAN
    AccessioniPrimary (citable) accession number: Q96T88
    Secondary accession number(s): A0JBR2
    , A8K024, B2RBA9, Q2HIX7, Q8J022, Q9H6S6, Q9P115, Q9P1U7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 127 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 19
      Human chromosome 19: 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