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Protein Page:
UHRF1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
UHRF1 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. 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. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin ligase; Transcription factor; Ligase; EC 6.3.2.-; EC 6.3.2.19; DNA binding protein; Ubiquitin conjugating system
Cellular Component: heterochromatin; euchromatin; nuclear matrix; nuclear chromatin; replication fork; nucleus
Molecular Function: identical protein binding; protein binding; methyl-CpG binding; nucleosomal histone binding; zinc ion binding; histone binding; ubiquitin-protein ligase activity; transcription factor activity; methylated histone residue binding; ligase activity
Biological Process: histone monoubiquitination; cell proliferation; protein autoubiquitination; maintenance of DNA methylation; transcription, DNA-dependent; protein ubiquitination during ubiquitin-dependent protein catabolic process; histone ubiquitination; positive regulation of cellular protein metabolic process; positive regulation of transcription from RNA polymerase II promoter; negative regulation of transcription from RNA polymerase II promoter; cell cycle; DNA repair
Reference #:  Q96T88 (UniProtKB)
Alt. Names/Synonyms: E3 ubiquitin-protein ligase UHRF1; FLJ21925; hNP95; HuNp95; ICBP90; Inverted CCAAT box-binding protein of 90 kDa; MGC138707; NP95; Nuclear protein 95; Nuclear zinc finger protein Np95; RING finger protein 106; RNF106; Transcription factor ICBP90; Ubiquitin-like PHD and RING finger domain-containing protein 1; ubiquitin-like with PHD and ring finger domains 1; ubiquitin-like, containing PHD and RING finger domains, 1; Ubiquitin-like-containing PHD and RING finger domains protein 1; UHRF1
Gene Symbols: UHRF1
Molecular weight: 89,814 Da
Basal Isoelectric point: 7.66  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

UHRF1

Protein Structure Not Found.


STRING  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene  |  InnateDB


Sites Implicated In
intracellular localization: S661‑p
molecular association, regulation: S95‑p
protein degradation: S95‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 3 T13-p RTMDGRQtHTVDSLS
0 1 K24 DSLSRLTKVEELRRK
0 7 K50-ub QRLFYRGkQMEDGHT
0 1 T68-p YEVRLNDtIQLLVRQ
0 8 S76-p IQLLVRQsLVLPHST
0 1 K84-ub LVLPHSTkERDsELs
0 2 S88-p HSTkERDsELsDtDs
0 10 S91-p kERDsELsDtDsGCC
0 3 T93-p RDsELsDtDsGCCLG
1 7 S95-p sELsDtDsGCCLGQS
0 3 T109 SESDKSSTHGEAAAE
0 1 T117-p HGEAAAEtDSRPADE
0 5 R120 AAAEtDSRPADEDMW
0 1 K136-ub ETELGLYkVNEYVDA
0 2 S165-p RVTRKAPsRDEPCSS
0 1 K187 EDVIYHVKYDDYPEN
0 10 N200 ENGVVQMNSRDVRAR
0 1 R202 GVVQMNSRDVRARAR
0 3 K233-ub NYNPDNPkERGFWYD
0 4 S265-p NVVLGDDsLNDCRII
0 12 S287-p IERPGEGsPMVDNPM
0 7 - gap
0 3 - gap
1 0 S298-p DNPMRRKsGPSCkHC
0 6 K303-ub RKsGPSCkHCKDDVN
0 4 D346 AFHIYCLDPPLSSVP
0 3 S368-p PECRNDAsEVVLAGE
0 4 R376 EVVLAGERLRESKKK
1 1 K385-ub RESKKKAkMASATSS
0 2 S393-p MASATSSsQRDWGkG
0 1 K399-ac SsQRDWGkGMACVGR
0 4 K399-ub SsQRDWGkGMACVGR
0 1 R406 kGMACVGRTKECTIV
0 1 Y418-p TIVPSNHyGPIPGIP
0 1 T492-p DLSGNKRtAEQsCDQ
0 1 S496-p NKRtAEQsCDQKLTN
0 1 A514 ALALNCFAPINDQEG
0 4 Q519 CFAPINDQEGAEAkD
0 5 K525-ub DQEGAEAkDWRSGKP
0 1 K546-ac VKGGKNSkYAPAEGN
0 3 K560-ub NRYDGIYkVVkYWPE
0 2 K563-ub DGIYkVVkYWPEKGk
0 2 K570-ub kYWPEKGkSGFLVWR
0 1 K592-ub DEPGPWTkEGKDRIK
0 5 K600-ub EGKDRIKkLGLTMQY
0 1 K622 LANREREKENSkREE
0 1 K626-ub EREKENSkREEEEQQ
0 1 E631 NSkREEEEQQEGGFA
1 10 S639-p QQEGGFAsPRTGKGK
0 2 S651-p KGKWKRKsAGGGPSR
0 1 S657 KsAGGGPSRAGsPRR
1 7 S661-p GGPSRAGsPRRTSKK
0 1 K670-ub RRTSKKTkVEPYSLT
0 1 S682-p SLTAQQSsLIREDKS
0 4 K692-ub REDKSNAkLWNEVLA
0 1 K702-ub NEVLASLkDRPAsGs
0 4 S707-p SLkDRPAsGsPFQLF
0 2 S709-p kDRPAsGsPFQLFLS
  mouse

► Hide Isoforms
 
T13 RTMDGKETHTVNSLS
K24-ub NSLSRLTkVQELRKK
K50 QRLFYRGKQMEDGHT
T68 YDVRLNDTIQLLVRQ
S76-p IQLLVRQsLALPLST
K84 LALPLSTKERDsELs
S88-p LSTKERDsELsDsDs
S91-p KERDsELsDsDsGYG
S93-p RDsELsDsDsGYGVG
S95-p sELsDsDsGYGVGHS
T109-p SESDKSStHGEGAAE
A117 HGEGAAEADDkTVWE
K120-ub GAAEADDkTVWEDTD
K132 DTDLGLYKVNEYVDV
S161-p QVQKRALsEDEPCSS
K183-ub DDIMYHVkYDDYPEH
K196-ub EHGVDIVkAkNVRAR
K198-ub GVDIVkAkNVRARAR
R229 NYNVDYPRKRGFWYD
S261-p NIRLLNDsQLNNCRI
R284 IELPKERRPLIAsPs
S289-p ERRPLIAsPsQPPPA
S291-p RPLIAsPsQPPPALR
S303 ALRNTGKSGPSCRFC
R308 GKSGPSCRFCKDDEN
K351-ub AFHLYCLkPPLTSVP
S373-p PSCRTDSsEVVQAGE
K381-ub EVVQAGEkLKESKKK
K390 KESKKKAKMASATSS
S398 MASATSSSRRDWGkG
K404 SSRRDWGKGMACVGr
K404-ub SSRRDWGkGMACVGr
R411-m2 kGMACVGrTTECTIV
F423 TIVPANHFGPIPGVP
T497 DLSGNKRTAGQSSDQ
S501 NKRTAGQSSDQKLTN
S519-p ALALNCHsPINEkGA
K524-ub CHsPINEkGAEAEDW
E529 NEkGAEAEDWRQGKP
K550 MKGGKHSKYAPAEGN
K564-ub NRYDGIYkVVKYWPE
K567 DGIYkVVKYWPERGk
K574-ub KYWPERGkSGFLVWR
R596 TEPEPWTREGKDRTR
Q604 EGKDRTRQLGLTMQY
K622-ub YLEALANkEKSRKRP
R626 LANkEKSRKRPAkAL
K631-ub KSRKRPAkALEQGPS
S639 ALEQGPSSSKTGKSK
S649 TGKSKQKSTGPTLss
S655-p KSTGPTLssPRASKK
S656-p STGPTLssPRASKKS
K664 PRASKKSKLEPYTLS
N676 TLSEQQANLIKEDKG
K686 KEDKGNAKLWDDVLT
Q696 DDVLTSLQDGPYQIF
- gap
- gap
  UHRF1 iso2  
T13 RTMDGKETHTVNSLS
K24 NSLSRLTKVQELRKK
K50 QRLFYRGKQMEDGHT
T68 YDVRLNDTIQLLVRQ
S76 IQLLVRQSLALPLST
K84 LALPLSTKERDSELS
S88 LSTKERDSELSDSDS
S91 KERDSELSDSDSGYG
S93 RDSELSDSDSGYGVG
S95 SELSDSDSGYGVGHS
T109 SESDKSSTHGEGAAE
A117 HGEGAAEADDKTVWE
K120 GAAEADDKTVWEDTD
K132 DTDLGLYKVNEYVDV
S161 QVQKRALSEDEPCSS
K183 DDIMYHVKYDDYPEH
K196 EHGVDIVKAKNVRAR
K198 GVDIVKAKNVRARAR
R229 NYNVDYPRKRGFWYD
S261 NIRLLNDSQLNNCRI
R284 IELPKERRPLIAsPs
S289-p ERRPLIAsPsQRKSG
S291-p RPLIAsPsQRKSGPS
S295 AsPsQRKSGPSCRFC
R300 RKSGPSCRFCKDDEN
K343 AFHLYCLKPPLTSVP
S365 PSCRTDSSEVVQAGE
K373 EVVQAGEKLKESKKK
K382 KESKKKAKMASATSS
S390 MASATSSSRRDWGKG
K396 SSRRDWGKGMACVGR
K396 SSRRDWGKGMACVGR
R403 KGMACVGRTTECTIV
F415 TIVPANHFGPIPGVP
T489 DLSGNKRTAGQSSDQ
S493 NKRTAGQSSDQKLTN
S511 ALALNCHSPINEKGA
K516 CHSPINEKGAEAEDW
E521 NEKGAEAEDWRQGKP
K542 MKGGKHSKYAPAEGN
K556 NRYDGIYKVVKYWPE
K559 DGIYKVVKYWPERGK
K566 KYWPERGKSGFLVWR
R588 TEPEPWTREGKDRTR
Q596 EGKDRTRQLGLTMQY
K614 YLEALANKEKSRKRP
R618 LANKEKSRKRPAKAL
K623 KSRKRPAKALEQGPS
S631 ALEQGPSSSKTGKSK
S641 TGKSKQKSTGPTLSS
S647 KSTGPTLSSPRASKK
S648 STGPTLSSPRASKKS
K656 PRASKKSKLEPYTLS
N668 TLSEQQANLIKEDKG
K678 KEDKGNAKLWDDVLT
Q688 DDVLTSLQDGPYQIF
- gap
- gap
  rat

 
T13 RTMDGKETHTVNSLS
K24 NSLSRLTKVQELRKK
K50 QRLFYRGKQMEDGHT
T68 YDVRLNDTIQLLVRQ
S76 IQLLVRQSLALPLST
K84 LALPLSTKERDSELS
S88 LSTKERDSELSDSDS
S91 KERDSELSDSDSGYG
S93 RDSELSDSDSGYGVG
S95 SELSDSDSGYGVGHS
T109 SESDKSSTHGEGTAD
G117 HGEGTADGDDKTVWE
K120 GTADGDDKTVWEDTD
K132 DTDLGLYKVNEYVDV
S161 QVQKKALSEEEPCSS
K183 DDIMYHIKYDDYPEH
K196 EHGVDIVKAKNVRAR
K198 GVDIVKAKNVRARAR
R229 NYNVDYPRKRGFWYD
S261 NVMLLNDSQLNNCRI
S284 IELPNERSPLIGSPS
S289 ERSPLIGSPSRRKSG
S291 SPLIGSPSRRKSGPS
S295 GSPSRRKSGPSCQYC
Q300 RKSGPSCQYCKDDEN
Q343 AFHLYCLQPPLTCVP
S365 PSCRTDSSEVVQAGE
K373 EVVQAGEKLKKSKKK
K382 KKSKKKAKMASATSS
S390 MASATSSSRRDWGKG
K396 SSRRDWGKGMACVGR
K396 SSRRDWGKGMACVGR
R403 KGMACVGRTTECTIV
F415 TIVPANHFGPIPGVP
T489 DLSGNKRTAGQSSDQ
S493 NKRTAGQSSDQKLTN
S511 ALALNCHSPINEKGA
K516 CHSPINEKGAEAEDW
E521 NEKGAEAEDWRQGKP
K542 MKGGKHSKYAPAEGN
K556 NRYDGIYKVVKYWPE
K559 DGIYKVVKYWPEKGK
K566 KYWPEKGKSGFIVWR
R588 TEPEPWTREGKDRTR
Q596 EGKDRTRQLGLTMQY
K614 YLEALANKEKNRKRP
R618 LANKEKNRKRPAKAL
K623 KNRKRPAKALEQGPS
S631 ALEQGPSSSKIGKSK
S641 IGKSKRKSTGPATTs
T647 KSTGPATTsPRVSKK
S648-p STGPATTsPRVSKKS
K656 PRVSKKSKLEPYTLP
N668 TLPLQQANLIKEDKG
K678 KEDKGNAKLWDDVLS
Q688 DDVLSSLQDGPYQIF
- gap
- gap
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