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Q96T88 (UHRF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
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 names
Name:UHRF1
Synonyms:ICBP90, NP95, RNF106
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length793 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.12 Ref.13 Ref.17 Ref.19 Ref.22 Ref.28 Ref.31 Ref.42

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.13 Ref.17 Ref.22 Ref.28 Ref.31 Ref.34

Subcellular location

Nucleus. Note: Localizes to replication foci. Enriched in pericentric heterochromatin. Also localizes to euchromatic regions. Ref.1 Ref.17 Ref.19 Ref.22 Ref.42

Tissue specificity

Expressed in thymus, bone marrow, testis, lung and heart. Overexpressed in breast cancer. Ref.1 Ref.10 Ref.13

Developmental stage

Expressed in fetal thymus, liver and kidney. Ref.1

Induction

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. Ref.1 Ref.10 Ref.12 Ref.13

Domain

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 (Ref.41, Ref.42 and Ref.44). 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 (Ref.45).

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) (Ref.17). 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 (Ref.38). The YDG domain also recognizes and binds 5-hydroxymethylcytosine (5hmC) (Ref.29).

The RING finger is required for ubiquitin ligase activity By similarity.

Post-translational modification

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.

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. Ref.12 Ref.19 Ref.28 Ref.34

Involvement in disease

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.

Sequence similarities

Contains 1 PHD-type zinc finger.

Contains 1 RING-type zinc finger.

Contains 1 ubiquitin-like domain.

Contains 1 YDG domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell cycle
DNA damage
DNA repair
Transcription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionChromatin regulator
Ligase
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell proliferation

Inferred from expression pattern Ref.13. Source: BHF-UCL

histone monoubiquitination

Inferred from sequence or structural similarity. Source: BHF-UCL

histone ubiquitination

Inferred from direct assay Ref.19. Source: UniProtKB

maintenance of DNA methylation

Inferred from mutant phenotype Ref.17. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.42. Source: UniProtKB

positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity

Inferred by curator Ref.1. Source: BHF-UCL

positive regulation of cellular protein metabolic process

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred by curator Ref.1. Source: BHF-UCL

protein autoubiquitination

Inferred from direct assay Ref.19Ref.28. Source: UniProtKB

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.31. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componenteuchromatin

Inferred from direct assay Ref.42. Source: UniProtKB

heterochromatin

Inferred from direct assay Ref.19Ref.41Ref.42. Source: UniProtKB

nuclear chromatin

Inferred from direct assay Ref.17. Source: UniProtKB

nuclear matrix

Inferred from sequence or structural similarity. Source: BHF-UCL

nucleus

Inferred from direct assay Ref.1. Source: BHF-UCL

replication fork

Inferred from direct assay Ref.17. Source: UniProtKB

   Molecular_functioncore promoter proximal region sequence-specific DNA binding

Inferred from direct assay Ref.1. Source: BHF-UCL

hemi-methylated DNA-binding

Inferred from direct assay Ref.17. Source: UniProtKB

histone binding

Inferred from direct assay Ref.42. Source: UniProtKB

identical protein binding

Inferred from sequence or structural similarity. Source: BHF-UCL

methyl-CpG binding

Inferred from direct assay PubMed 21029866. Source: UniProtKB

methylated histone binding

Inferred from direct assay Ref.19PubMed 21029866Ref.41. Source: UniProtKB

nucleosomal histone binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.17Ref.28Ref.31. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Traceable author statement PubMed 1868030. Source: ProtInc

ubiquitin-protein transferase activity

Inferred from direct assay Ref.19Ref.28Ref.31. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.42. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96T88-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96T88-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGVFAVPPLSSDTM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 793793E3 ubiquitin-protein ligase UHRF1
PRO_0000056144

Regions

Domain1 – 7878Ubiquitin-like
Domain419 – 582164YDG
Zinc finger310 – 36657PHD-type
Zinc finger724 – 76340RING-type
Region133 – 20977Tudor-like 1
Region216 – 28368Tudor-like 2
Region296 – 3016Linker
Region333 – 3375Histone H3R2me0 binding
Region353 – 3553Histone H3R2me0 binding
Region445 – 4462Required to promote base flipping By similarity
Region463 – 4642Methylcytosine binding
Region466 – 4694Required for formation of a 5-methylcytosine-binding pocket
Region478 – 4814Required for formation of a 5-methylcytosine-binding pocket

Sites

Binding site3161Histone H3K4me0
Binding site3271Histone H3R2me0
Binding site3301Histone H3R2me0
Binding site4691Methylcytosine
Site4791Required to confer preferential recognition of cytosine over thymine
Site4891Required to discriminate between hemimethylated DNA versus symmetrically methylated DNA
Site4911Required for affinity and specificity for 5-mCpG sequence

Amino acid modifications

Modified residue761Phosphoserine Ref.20 Ref.26
Modified residue911Phosphoserine Ref.20
Modified residue2871Phosphoserine Ref.14 Ref.18 Ref.23 Ref.26 Ref.30
Modified residue2981Phosphoserine; by PKA Ref.11 Ref.45
Modified residue3991N6-acetyllysine Ref.24
Modified residue5461N6-acetyllysine Ref.24
Modified residue6391Phosphoserine; by CDK1 Ref.14 Ref.15 Ref.26 Ref.34
Modified residue6511Phosphoserine Ref.30
Modified residue7071Phosphoserine Ref.20 Ref.26
Cross-link385Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.16

Natural variations

Alternative sequence11M → MGVFAVPPLSSDTM in isoform 2.
VSP_044394
Natural variant2401D → H. Ref.6
Corresponds to variant rs17886098 [ dbSNP | Ensembl ].
VAR_022554
Natural variant3791E → K. Ref.5 Ref.6
Corresponds to variant rs17885791 [ dbSNP | Ensembl ].
VAR_022555
Natural variant6381A → T. Ref.5 Ref.6
Corresponds to variant rs17883331 [ dbSNP | Ensembl ].
VAR_022556
Natural variant6421T → M. Ref.6
Corresponds to variant rs17884843 [ dbSNP | Ensembl ].
VAR_022557
Natural variant7131L → F. Ref.6
Corresponds to variant rs17883563 [ dbSNP | Ensembl ].
VAR_022558

Experimental info

Mutagenesis1421D → A: Impaired binding to histone H3 without affecting the protein folding; when associated with A-153. Ref.41 Ref.42 Ref.45
Mutagenesis1451D → A: Impaired binding to histone H3. Ref.41 Ref.42 Ref.45
Mutagenesis1521F → A: Impaired binding to histone H3. Ref.41 Ref.42 Ref.45
Mutagenesis1531E → A: Impaired binding to histone H3 without affecting the protein folding; when associated with A-142. Ref.41 Ref.42 Ref.45
Mutagenesis1881Y → A: Impaired binding to histone H3. Ref.25 Ref.41 Ref.42 Ref.45
Mutagenesis1901D → A: Slightly impaired binding to histone H3. Ref.41 Ref.42 Ref.45
Mutagenesis1911Y → A: Impaired binding to histone H3. Ref.25 Ref.42 Ref.45
Mutagenesis295 – 2962RR → AA: Disrupts the simultaneous binding to H3R2me0 and H3K9me3. Ref.42 Ref.45
Mutagenesis2981S → A: Diminishes phosphorylation by PKA. Ref.11 Ref.42 Ref.45
Mutagenesis3301Q → A or K: Does not affect ability to bind histone H3 peptide. Ref.42 Ref.43 Ref.45
Mutagenesis334 – 3352DE → AA: Abolishes binding to histone H3. Ref.39 Ref.40 Ref.42 Ref.43 Ref.45
Mutagenesis3341D → A: Impaired binding to histone H3. Ref.39 Ref.40 Ref.42 Ref.43 Ref.45
Mutagenesis3371D → A: Impaired binding to histone H3. Ref.39 Ref.40 Ref.42 Ref.43 Ref.45
Mutagenesis4331R → A: Does not affect ability to bind DNA. Ref.37 Ref.42 Ref.45
Mutagenesis4431R → A: Decreased ability to bind DNA. Ref.37 Ref.42 Ref.45
Mutagenesis4481G → D: Decreased affinity for DNA. Ref.38 Ref.42 Ref.45
Mutagenesis4661Y → G: Decreased ability to bind DNA. Ref.37 Ref.42 Ref.45
Mutagenesis4691D → G: Abolishes ability to bind hemimethylated DNA. Ref.42 Ref.45
Mutagenesis4891N → A: Abolishes specificity to hemimethylated DNA. Ref.38 Ref.42 Ref.45
Mutagenesis4911R → A: Decreased binding to methylated DNA but does not affect ability to bind DNA. Ref.37 Ref.38 Ref.42 Ref.45
Mutagenesis6391S → A: Prevents phosphorylation by CDK1 during M phase, leading to increased stability. Ref.34 Ref.42 Ref.45
Mutagenesis6391S → D: Mimics phosphorylation; impaired interaction with USP7, leading to decreased stability. Ref.34 Ref.42 Ref.45
Mutagenesis6511S → A: No effect on in vitro phosphorylation by PKA. Ref.11 Ref.42 Ref.45
Mutagenesis6661S → A: No effect on in vitro phosphorylation by PKA. Ref.11 Ref.42 Ref.45
Mutagenesis7411H → A: Abolishes E3 ubiquitin-protein ligase activity. Ref.31 Ref.42 Ref.45
Sequence conflict3831K → E in BAF82078. Ref.5
Sequence conflict3831K → N in AAF28469. Ref.1
Sequence conflict4571A → S in AAF28469. Ref.1
Sequence conflict6751S → N in BAF82078. Ref.5

Secondary structure

................................................................................................................................... 793
Helix Strand Turn

Details...

Sequences

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

Last modified December 1, 2001. Version 1.
Checksum: E65B15657525C89F

FASTA79389,814
        10         20         30         40         50         60 
MWIQVRTMDG RQTHTVDSLS RLTKVEELRR KIQELFHVEP GLQRLFYRGK QMEDGHTLFD 

        70         80         90        100        110        120 
YEVRLNDTIQ LLVRQSLVLP HSTKERDSEL SDTDSGCCLG QSESDKSSTH GEAAAETDSR 

       130        140        150        160        170        180 
PADEDMWDET ELGLYKVNEY VDARDTNMGA WFEAQVVRVT RKAPSRDEPC SSTSRPALEE 

       190        200        210        220        230        240 
DVIYHVKYDD YPENGVVQMN SRDVRARART IIKWQDLEVG QVVMLNYNPD NPKERGFWYD 

       250        260        270        280        290        300 
AEISRKRETR TARELYANVV LGDDSLNDCR IIFVDEVFKI ERPGEGSPMV DNPMRRKSGP 

       310        320        330        340        350        360 
SCKHCKDDVN RLCRVCACHL CGGRQDPDKQ LMCDECDMAF HIYCLDPPLS SVPSEDEWYC 

       370        380        390        400        410        420 
PECRNDASEV VLAGERLRES KKKAKMASAT SSSQRDWGKG MACVGRTKEC TIVPSNHYGP 

       430        440        450        460        470        480 
IPGIPVGTMW RFRVQVSESG VHRPHVAGIH GRSNDGAYSL VLAGGYEDDV DHGNFFTYTG 

       490        500        510        520        530        540 
SGGRDLSGNK RTAEQSCDQK LTNTNRALAL NCFAPINDQE GAEAKDWRSG KPVRVVRNVK 

       550        560        570        580        590        600 
GGKNSKYAPA EGNRYDGIYK VVKYWPEKGK SGFLVWRYLL RRDDDEPGPW TKEGKDRIKK 

       610        620        630        640        650        660 
LGLTMQYPEG YLEALANRER EKENSKREEE EQQEGGFASP RTGKGKWKRK SAGGGPSRAG 

       670        680        690        700        710        720 
SPRRTSKKTK VEPYSLTAQQ SSLIREDKSN AKLWNEVLAS LKDRPASGSP FQLFLSKVEE 

       730        740        750        760        770        780 
TFQCICCQEL VFRPITTVCQ HNVCKDCLDR SFRAQVFSCP ACRYDLGRSY AMQVNQPLQT 

       790 
VLNQLFPGYG NGR 

« Hide

Isoform 2 [UniParc].

Checksum: BFE365939E846398
Show »

FASTA80691,116

References

« Hide 'large scale' references
[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]"Isolation and characterization of a novel human radiosusceptibility gene, NP95."
Muto M., Fujimori A., Nenoi M., Daino K., Matsuda Y., Kuroiwa A., Kubo E., Kanari Y., Utsuno M., Tsuji H., Ukai H., Mita K., Takahagi M., Tatsumi K.
Radiat. Res. 166:723-733(2006) [PubMed] [Europe PMC] [Abstract]
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]"Phosphorylation of ICBP90 by protein kinase A enhances topoisomerase IIalpha expression."
Trotzier M.-A., Bronner C., Bathami K., Mathieu E., Abbady A.-Q., Jeanblanc M., Muller C.D., Rochette-Egly C., Mousli M.
Biochem. Biophys. Res. Commun. 319:590-595(2004) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"The SRA protein UHRF1 promotes epigenetic crosstalks and is involved in prostate cancer progression."
Babbio F., Pistore C., Curti L., Castiglioni I., Kunderfranco P., Brino L., Oudet P., Seiler R., Thalman G.N., Roggero E., Sarti M., Pinton S., Mello-Grand M., Chiorino G., Catapano C.V., Carbone G.M., Bonapace I.M.
Oncogene 31:4878-4887(2012) [PubMed] [Europe PMC] [Abstract]
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]"Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein."
Nady N., Lemak A., Walker J.R., Avvakumov G.V., Kareta M.S., Achour M., Xue S., Duan S., Allali-Hassani A., Zuo X., Wang Y.X., Bronner C., Chedin F., Arrowsmith C.H., Dhe-Paganon S.
J. Biol. Chem. 286:24300-24311(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_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.
UniGeneHs.108106.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ96T88.
SMRQ96T88. Positions 1-76, 126-367, 377-617, 675-793.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118893. 33 interactions.
IntActQ96T88. 6 interactions.
MINTMINT-2815626.
STRING9606.ENSP00000381295.

Chemistry

ChEMBLCHEMBL2424510.

PTM databases

PhosphoSiteQ96T88.

Polymorphism databases

DMDM67462077.

Proteomic databases

MaxQBQ96T88.
PaxDbQ96T88.
PRIDEQ96T88.

Protocols and materials databases

DNASU29128.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29128.
KEGGhsa:29128.
UCSCuc002mbo.3. human. [Q96T88-1]

Organism-specific databases

CTD29128.
GeneCardsGC19P004910.
HGNCHGNC:12556. UHRF1.
MIM607990. gene.
neXtProtNX_Q96T88.
PharmGKBPA37196.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3440.
HOGENOMHOG000124662.
HOVERGENHBG059298.
InParanoidQ96T88.
KOK10638.
PhylomeDBQ96T88.

Enzyme and pathway databases

SignaLinkQ96T88.
UniPathwayUPA00143.

Gene expression databases

CleanExHS_UHRF1.
GenevestigatorQ96T88.

Family and domain databases

Gene3D2.30.280.10. 1 hit.
2.30.30.30. 1 hit.
3.30.40.10. 2 hits.
InterProIPR021991. 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]
PfamPF12148. DUF3590. 1 hit.
PF00628. PHD. 1 hit.
PF02182. SAD_SRA. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
SM00466. SRA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
SSF57903. SSF57903. 1 hit.
SSF88697. SSF88697. 1 hit.
PROSITEPS50053. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ96T88.
GeneWikiUHRF1.
GenomeRNAi29128.
NextBio35463698.
PROQ96T88.
SOURCESearch...

Entry information

Entry nameUHRF1_HUMAN
AccessionPrimary (citable) accession number: Q96T88
Secondary accession number(s): A0JBR2 expand/collapse secondary AC list , A8K024, B2RBA9, Q2HIX7, Q8J022, Q9H6S6, Q9P115, Q9P1U7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM