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Q96T88

- UHRF1_HUMAN

UniProt

Q96T88 - UHRF1_HUMAN

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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

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. sequence-specific DNA binding transcription factor activity Source: ProtInc
  10. ubiquitin-protein transferase activity Source: UniProtKB
  11. 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
Complete GO annotation...

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 heterochromatin Source: Ensembl
  5. nuclear matrix Source: BHF-UCL
  6. nucleus Source: BHF-UCL
  7. replication fork Source: UniProtKB
Complete GO annotation...

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. 1 Publication
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. 1 Publication
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 – 761Phosphoserine2 Publications
Modified residuei91 – 911Phosphoserine1 Publication
Modified residuei287 – 2871Phosphoserine5 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 CDK14 Publications
Modified residuei651 – 6511Phosphoserine1 Publication
Modified residuei707 – 7071Phosphoserine2 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.
ExpressionAtlasiQ96T88. differential.
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. 47 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[»]
4QQDX-ray2.28A/B126-285[»]
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.
GeneTreeiENSGT00390000008296.
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

        10         20         30         40         50
MWIQVRTMDG RQTHTVDSLS RLTKVEELRR KIQELFHVEP GLQRLFYRGK
60 70 80 90 100
QMEDGHTLFD YEVRLNDTIQ LLVRQSLVLP HSTKERDSEL SDTDSGCCLG
110 120 130 140 150
QSESDKSSTH GEAAAETDSR PADEDMWDET ELGLYKVNEY VDARDTNMGA
160 170 180 190 200
WFEAQVVRVT RKAPSRDEPC SSTSRPALEE DVIYHVKYDD YPENGVVQMN
210 220 230 240 250
SRDVRARART IIKWQDLEVG QVVMLNYNPD NPKERGFWYD AEISRKRETR
260 270 280 290 300
TARELYANVV LGDDSLNDCR IIFVDEVFKI ERPGEGSPMV DNPMRRKSGP
310 320 330 340 350
SCKHCKDDVN RLCRVCACHL CGGRQDPDKQ LMCDECDMAF HIYCLDPPLS
360 370 380 390 400
SVPSEDEWYC PECRNDASEV VLAGERLRES KKKAKMASAT SSSQRDWGKG
410 420 430 440 450
MACVGRTKEC TIVPSNHYGP IPGIPVGTMW RFRVQVSESG VHRPHVAGIH
460 470 480 490 500
GRSNDGAYSL VLAGGYEDDV DHGNFFTYTG SGGRDLSGNK RTAEQSCDQK
510 520 530 540 550
LTNTNRALAL NCFAPINDQE GAEAKDWRSG KPVRVVRNVK GGKNSKYAPA
560 570 580 590 600
EGNRYDGIYK VVKYWPEKGK SGFLVWRYLL RRDDDEPGPW TKEGKDRIKK
610 620 630 640 650
LGLTMQYPEG YLEALANRER EKENSKREEE EQQEGGFASP RTGKGKWKRK
660 670 680 690 700
SAGGGPSRAG SPRRTSKKTK VEPYSLTAQQ SSLIREDKSN AKLWNEVLAS
710 720 730 740 750
LKDRPASGSP FQLFLSKVEE TFQCICCQEL VFRPITTVCQ HNVCKDCLDR
760 770 780 790
SFRAQVFSCP ACRYDLGRSY AMQVNQPLQT VLNQLFPGYG NGR
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.
CCDSiCCDS74262.1. [Q96T88-2]
CCDS74263.1. [Q96T88-1]
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

EnsembliENST00000612630; ENSP00000484739; ENSG00000276043. [Q96T88-1]
ENST00000615884; ENSP00000478601; ENSG00000276043. [Q96T88-1]
ENST00000616255; ENSP00000478348; ENSG00000276043. [Q96T88-1]
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 .
CCDSi CCDS74262.1. [Q96T88-2 ]
CCDS74263.1. [Q96T88-1 ]
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 [» ]
4QQD X-ray 2.28 A/B 126-285 [» ]
ProteinModelPortali Q96T88.
SMRi Q96T88. Positions 1-76, 126-367, 377-617, 675-793.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118893. 47 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

Ensembli ENST00000612630 ; ENSP00000484739 ; ENSG00000276043 . [Q96T88-1 ]
ENST00000615884 ; ENSP00000478601 ; ENSG00000276043 . [Q96T88-1 ]
ENST00000616255 ; ENSP00000478348 ; ENSG00000276043 . [Q96T88-1 ]
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.
GeneTreei ENSGT00390000008296.
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.
ExpressionAtlasi Q96T88. differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 128 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

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