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E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) (Nuclear zinc finger protein Np95) (XNp95) (RING-type E3 ubiquitin transferase UHRF1) (Ubiquitin-like PHD and RING finger domain-containing protein 1) (Ubiquitin-like-containing PHD and RING finger domains protein 1)

 UHRF1_XENLA             Reviewed;         772 AA.
B6CHA3;
31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 1.
22-NOV-2017, entry version 57.
RecName: Full=E3 ubiquitin-protein ligase UHRF1;
EC=2.3.2.27;
AltName: Full=Nuclear zinc finger protein Np95;
Short=XNp95;
AltName: Full=RING-type E3 ubiquitin transferase UHRF1;
AltName: Full=Ubiquitin-like PHD and RING finger domain-containing protein 1;
AltName: Full=Ubiquitin-like-containing PHD and RING finger domains protein 1;
Name=uhrf1; Synonyms=np95;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Lindsay H.D.;
"Xenopus Homolog of XNp95.";
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
-!- 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. However, it is
still unclear how E3 ubiquitin-protein ligase activity is related
to its role in chromatin in vivo.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00358}. Note=Localizes to replication foci. Enriched in
pericentric heterochromatin. Also localizes to euchromatic regions
(By similarity). {ECO:0000250}.
-!- 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). {ECO:0000250}.
-!- DOMAIN: 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).
{ECO:0000250}.
-!- DOMAIN: The RING finger is required for ubiquitin ligase activity.
{ECO:0000250}.
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EMBL; EU177101; ABY28114.1; -; mRNA.
RefSeq; NP_001129236.1; NM_001135764.1.
RefSeq; XP_018091852.1; XM_018236363.1.
UniGene; Xl.23750; -.
ProteinModelPortal; B6CHA3; -.
SMR; B6CHA3; -.
BioGrid; 101600; 2.
IntAct; B6CHA3; 1.
GeneID; 432234; -.
KEGG; xla:432234; -.
CTD; 432234; -.
Xenbase; XB-GENE-5821540; uhrf1.
HOVERGEN; HBG059298; -.
KO; K10638; -.
UniPathway; UPA00143; -.
GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISS:UniProtKB.
GO; GO:0005657; C:replication fork; ISS:UniProtKB.
GO; GO:0044729; F:hemi-methylated DNA-binding; ISS:UniProtKB.
GO; GO:0042393; F:histone binding; ISS:UniProtKB.
GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0016574; P:histone ubiquitination; ISS:UniProtKB.
GO; GO:0010216; P:maintenance of DNA methylation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.30.280.10; -; 1.
Gene3D; 2.30.30.30; -; 1.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR015947; PUA-like_sf.
InterPro; IPR014722; Rib_L2_dom2.
InterPro; IPR036987; SRA-YDG_sf.
InterPro; IPR003105; SRA_YDG.
InterPro; IPR021991; TTD_dom.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
Pfam; PF00628; PHD; 1.
Pfam; PF02182; SAD_SRA; 1.
Pfam; PF12148; TTD; 1.
Pfam; PF00240; ubiquitin; 1.
SMART; SM00249; PHD; 1.
SMART; SM00184; RING; 2.
SMART; SM00466; SRA; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF57903; SSF57903; 1.
SUPFAM; SSF88697; SSF88697; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
PROSITE; PS51015; YDG; 1.
PROSITE; PS01359; ZF_PHD_1; 1.
PROSITE; PS50016; ZF_PHD_2; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
2: Evidence at transcript level;
Cell cycle; Chromatin regulator; DNA-binding; Metal-binding; Nucleus;
Repeat; Repressor; Transcription; Transcription regulation;
Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 772 E3 ubiquitin-protein ligase UHRF1.
/FTId=PRO_0000419989.
DOMAIN 1 77 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
DOMAIN 417 580 YDG. {ECO:0000255|PROSITE-
ProRule:PRU00358}.
ZN_FING 297 364 PHD-type. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 703 742 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 129 205 Tudor-like 1.
REGION 212 281 Tudor-like 2.
REGION 291 299 Linker. {ECO:0000250}.
REGION 331 335 Histone H3R2me0 binding. {ECO:0000250}.
REGION 351 353 Histone H3R2me0 binding. {ECO:0000250}.
REGION 443 444 Required to promote base flipping.
{ECO:0000250}.
REGION 461 462 Methylcytosine binding. {ECO:0000250}.
REGION 464 467 Required for formation of a 5-
methylcytosine-binding pocket.
{ECO:0000250}.
REGION 476 479 Required for formation of a 5-
methylcytosine-binding pocket.
{ECO:0000250}.
BINDING 314 314 Histone H3K4me0. {ECO:0000250}.
BINDING 325 325 Histone H3R2me0. {ECO:0000250}.
BINDING 328 328 Histone H3R2me0. {ECO:0000250}.
BINDING 467 467 Methylcytosine. {ECO:0000250}.
SITE 477 477 Required to confer preferential
recognition of cytosine over thymine.
{ECO:0000250}.
SITE 487 487 Required to discriminate between
hemimethylated DNA versus symmetrically
methylated DNA. {ECO:0000250}.
SITE 489 489 Required for affinity and specificity for
5-mCpG sequence. {ECO:0000250}.
SEQUENCE 772 AA; 86974 MW; 202D7F91C7CEFBCD CRC64;
MWIQVRTMDG RDTRRIDSLS KLTKVDDLRD RIQQLFGVAL ESQRLFYRGK QMENGHTLFD
YSVGLNDIVQ LLVRQIPDSF PTKHKECELS DASAGCGSGQ RDSDSGSGEG AMDVDGQSIS
IIGENVGTSL YKKNDLVDAR DLNMGAWFEA QIVNVSKKVG PYGTLPEVSD TSVTSDAIIY
HVKYEDYPEN GVVQLTCKDV RLRARTTLPW HEIKVGQVVM VNYNPDEPKE RGYWYDAEIL
RKHESKKIKE IYAKVLLGDA GDSLNDCRIR FVNEIYKIEE PGSTYLNTES PQKRQNGPEC
KHCKDNPKRA CRMCACCICG GKQDPEKQLL CDECDLAFHI YCLKPPLSVI PQDEDWYCPD
CRNDASEVVL AGEKLKESKK KARMASANSS SQRDWGKGMA CVGRSRECTI VPSNHYGPIP
GVPVGTLWKF RVQVSESGVH RPHVAGIHGR SNDGSYSLVL AGGYEDDVDN GNEFTYTGSG
GRDLSGNKRT AEQSCDQKLS NMNRALALNC SAPINDKEGS IAKDWRAGKP VRVVRNSKGR
KHSKYAPEEG NRYDGIYKVV KYWPEKGKSG FLVWRYLLRR DDYEPAPWSK EGKERIKKLG
LTMQYPDGYL ETLASKEREK ENKTEDEPID SPSKGKRKRN SDNEQTAAKS IPKKMKVASY
KLTLEQKTLI KQDVLNAKLW SEVMLFLKEG PKFVNKVEET FLCICCQEVV YEPVTTECHH
NICKGCLDRS FKALVHSCPA CRHDLGKNYP LNVNKPLQAI LSQLFPGYES GR


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