Q96T88 (UHRF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	UHRF1
Synonyms:	ICBP90, NP95, RNF106

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	793 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Cell cycle DNA damage DNA repair Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Chromatin regulator Ligase Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	euchromatin 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 replication fork Inferred from direct assay Ref.17. Source: UniProtKB
Molecular_function	core 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 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 residue binding Inferred from direct assay Ref.19PubMed 21029866Ref.41. Source: UniProtKB nucleosomal histone binding Inferred from sequence or structural similarity. Source: BHF-UCL sequence-specific DNA binding transcription factor activity Traceable author statement PubMed 1868030. Source: ProtInc ubiquitin-protein ligase 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

With	Entry	#Exp.	IntAct	Notes
DNMT1	P26358	10	EBI-1548946,EBI-719459

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 793

793

E3 ubiquitin-protein ligase UHRF1

PRO_0000056144

Regions

Domain

1 – 78

78

Ubiquitin-like

Domain

419 – 582

164

YDG

Zinc finger

310 – 366

57

PHD-type

Zinc finger

724 – 763

40

RING-type

Region

133 – 209

77

Tudor-like 1

Region

216 – 283

68

Tudor-like 2

Region

296 – 301

6

Linker

Region

333 – 337

5

Histone H3R2me0 binding

Region

353 – 355

3

Histone H3R2me0 binding

Region

445 – 446

2

Required to promote base flipping By similarity

Region

463 – 464

2

Methylcytosine binding

Region

466 – 469

4

Required for formation of a 5-methylcytosine-binding pocket

Region

478 – 481

4

Required for formation of a 5-methylcytosine-binding pocket

Sites

Binding site

316

1

Histone H3K4me0

Binding site

327

1

Histone H3R2me0

Binding site

330

1

Histone H3R2me0

Binding site

469

1

Methylcytosine

Site

479

1

Required to confer preferential recognition of cytosine over thymine

Site

489

1

Required to discriminate between hemimethylated DNA versus symmetrically methylated DNA

Site

491

1

Required for affinity and specificity for 5-mCpG sequence

Amino acid modifications

Modified residue

76

1

Phosphoserine Ref.20 Ref.26

Modified residue

91

1

Phosphoserine Ref.20

Modified residue

287

1

Phosphoserine Ref.14 Ref.18 Ref.23 Ref.26 Ref.30

Modified residue

298

1

Phosphoserine; by PKA Ref.11 Ref.45

Modified residue

399

1

N6-acetyllysine Ref.24

Modified residue

546

1

N6-acetyllysine Ref.24

Modified residue

639

1

Phosphoserine; by CDK1 Ref.14 Ref.15 Ref.26 Ref.34

Modified residue

651

1

Phosphoserine Ref.30

Modified residue

707

1

Phosphoserine Ref.20 Ref.26

Cross-link

385

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.16

Natural variations

Alternative sequence

1

1

M → MGVFAVPPLSSDTM in isoform 2.

VSP_044394

Natural variant

240

1

D → H. Ref.6
Corresponds to variant rs17886098 [ dbSNP | Ensembl ].

VAR_022554

Natural variant

379

1

E → K. Ref.5 Ref.6
Corresponds to variant rs17885791 [ dbSNP | Ensembl ].

VAR_022555

Natural variant

638

1

A → T. Ref.5 Ref.6
Corresponds to variant rs17883331 [ dbSNP | Ensembl ].

VAR_022556

Natural variant

642

1

T → M. Ref.6
Corresponds to variant rs17884843 [ dbSNP | Ensembl ].

VAR_022557

Natural variant

713

1

L → F. Ref.6
Corresponds to variant rs17883563 [ dbSNP | Ensembl ].

VAR_022558

Experimental info

Mutagenesis

142

1

D → A: Impaired binding to histone H3 without affecting the protein folding; when associated with A-153. Ref.41 Ref.42 Ref.45

Mutagenesis

145

1

D → A: Impaired binding to histone H3. Ref.41 Ref.42 Ref.45

Mutagenesis

152

1

F → A: Impaired binding to histone H3. Ref.41 Ref.42 Ref.45

Mutagenesis

153

1

E → A: Impaired binding to histone H3 without affecting the protein folding; when associated with A-142. Ref.41 Ref.42 Ref.45

Mutagenesis

188

1

Y → A: Impaired binding to histone H3. Ref.25 Ref.41 Ref.42 Ref.45

Mutagenesis

190

1

D → A: Slightly impaired binding to histone H3. Ref.41 Ref.42 Ref.45

Mutagenesis

191

1

Y → A: Impaired binding to histone H3. Ref.25 Ref.42 Ref.45

Mutagenesis

295 – 296

2

RR → AA: Disrupts the simultaneous binding to H3R2me0 and H3K9me3. Ref.42 Ref.45

Mutagenesis

298

1

S → A: Diminishes phosphorylation by PKA. Ref.11 Ref.42 Ref.45

Mutagenesis

330

1

Q → A or K: Does not affect ability to bind histone H3 peptide. Ref.42 Ref.43 Ref.45

Mutagenesis

334 – 335

2

DE → AA: Abolishes binding to histone H3. Ref.39 Ref.40 Ref.42 Ref.43 Ref.45

Mutagenesis

334

1

D → A: Impaired binding to histone H3. Ref.39 Ref.40 Ref.42 Ref.43 Ref.45

Mutagenesis

337

1

D → A: Impaired binding to histone H3. Ref.39 Ref.40 Ref.42 Ref.43 Ref.45

Mutagenesis

433

1

R → A: Does not affect ability to bind DNA. Ref.37 Ref.42 Ref.45

Mutagenesis

443

1

R → A: Decreased ability to bind DNA. Ref.37 Ref.42 Ref.45

Mutagenesis

448

1

G → D: Decreased affinity for DNA. Ref.38 Ref.42 Ref.45

Mutagenesis

466

1

Y → G: Decreased ability to bind DNA. Ref.37 Ref.42 Ref.45

Mutagenesis

469

1

D → G: Abolishes ability to bind hemimethylated DNA. Ref.42 Ref.45

Mutagenesis

489

1

N → A: Abolishes specificity to hemimethylated DNA. Ref.38 Ref.42 Ref.45

Mutagenesis

491

1

R → A: Decreased binding to methylated DNA but does not affect ability to bind DNA. Ref.37 Ref.38 Ref.42 Ref.45

Mutagenesis

639

1

S → A: Prevents phosphorylation by CDK1 during M phase, leading to increased stability. Ref.34 Ref.42 Ref.45

Mutagenesis

639

1

S → D: Mimics phosphorylation; impaired interaction with USP7, leading to decreased stability. Ref.34 Ref.42 Ref.45

Mutagenesis

651

1

S → A: No effect on in vitro phosphorylation by PKA. Ref.11 Ref.42 Ref.45

Mutagenesis

666

1

S → A: No effect on in vitro phosphorylation by PKA. Ref.11 Ref.42 Ref.45

Mutagenesis

741

1

H → A: Abolishes E3 ubiquitin-protein ligase activity. Ref.31 Ref.42 Ref.45

Sequence conflict

383

1

K → E in BAF82078. Ref.5

Sequence conflict

383

1

K → N in AAF28469. Ref.1

Sequence conflict

457

1

A → S in AAF28469. Ref.1

Sequence conflict

675

1

S → N in BAF82078. Ref.5

Secondary structure

1

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793

Helix Strand Turn

Details...

Beta strand

1 – 7

7

Beta strand

13 – 19

7

Helix

25 – 36

12

Helix

40 – 42

3

Beta strand

43 – 47

5

Turn

58 – 62

5

Beta strand

68 – 73

6

Turn

127 – 129

3

Beta strand

140 – 144

5

Turn

146 – 148

3

Beta strand

151 – 161

11

Beta strand

164 – 167

4

Turn

179 – 181

3

Beta strand

182 – 190

9

Helix

192 – 194

3

Beta strand

196 – 200

5

Helix

201 – 203

3

Beta strand

204 – 206

3

Beta strand

210 – 212

3

Helix

214 – 216

3

Beta strand

222 – 227

6

Beta strand

229 – 231

3

Beta strand

237 – 248

12

Beta strand

253 – 260

8

Beta strand

262 – 272

11

Helix

274 – 276

3

Beta strand

277 – 279

3

Beta strand

283 – 286

4

Turn

303 – 307

5

Beta strand

309 – 311

3

Turn

314 – 316

3

Turn

319 – 321

3

Beta strand

323 – 325

3

Helix

327 – 329

3

Beta strand

330 – 332

3

Turn

334 – 336

3

Beta strand

339 – 341

3

Helix

342 – 344

3

Beta strand

345 – 347

3

Beta strand

354 – 356

3

Turn

361 – 363

3

Beta strand

417 – 419

3

Beta strand

429 – 432

4

Helix

433 – 438

6

Turn

439 – 442

4

Beta strand

448 – 452

5

Turn

453 – 455

3

Beta strand

456 – 462

7

Beta strand

473 – 479

7

Turn

487 – 489

3

Helix

503 – 511

9

Beta strand

512 – 514

3

Turn

518 – 520

3

Helix

527 – 529

3

Beta strand

533 – 538

6

Helix

539 – 544

6

Beta strand

546 – 548

3

Beta strand

550 – 568

19

Beta strand

572 – 582

11

Helix

592 – 601

10

Helix

611 – 617

7

Helix

678 – 686

9

Helix

688 – 690

3

Helix

691 – 699

9

Beta strand

706 – 708

3

Helix

710 – 721

12

Turn

725 – 727

3

Beta strand

728 – 730

3

Beta strand

732 – 736

5

Beta strand

742 – 744

3

Helix

745 – 753

9

Turn

760 – 762

3

Helix

776 – 785

10

Turn

787 – 792

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: E65B15657525C89F	FASTA	793	89,814
	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
	Isoform 2 [UniParc]. Checksum: BFE365939E846398	FASTA	806	91,116
	10 20 30 40 50 60 MGVFAVPPLS SDTMWIQVRT MDGRQTHTVD SLSRLTKVEE LRRKIQELFH VEPGLQRLFY 70 80 90 100 110 120 RGKQMEDGHT LFDYEVRLND TIQLLVRQSL VLPHSTKERD SELSDTDSGC CLGQSESDKS 130 140 150 160 170 180 STHGEAAAET DSRPADEDMW DETELGLYKV NEYVDARDTN MGAWFEAQVV RVTRKAPSRD 190 200 210 220 230 240 EPCSSTSRPA LEEDVIYHVK YDDYPENGVV QMNSRDVRAR ARTIIKWQDL EVGQVVMLNY 250 260 270 280 290 300 NPDNPKERGF WYDAEISRKR ETRTARELYA NVVLGDDSLN DCRIIFVDEV FKIERPGEGS 310 320 330 340 350 360 PMVDNPMRRK SGPSCKHCKD DVNRLCRVCA CHLCGGRQDP DKQLMCDECD MAFHIYCLDP 370 380 390 400 410 420 PLSSVPSEDE WYCPECRNDA SEVVLAGERL RESKKKAKMA SATSSSQRDW GKGMACVGRT 430 440 450 460 470 480 KECTIVPSNH YGPIPGIPVG TMWRFRVQVS ESGVHRPHVA GIHGRSNDGA YSLVLAGGYE 490 500 510 520 530 540 DDVDHGNFFT YTGSGGRDLS GNKRTAEQSC DQKLTNTNRA LALNCFAPIN DQEGAEAKDW 550 560 570 580 590 600 RSGKPVRVVR NVKGGKNSKY APAEGNRYDG IYKVVKYWPE KGKSGFLVWR YLLRRDDDEP 610 620 630 640 650 660 GPWTKEGKDR IKKLGLTMQY PEGYLEALAN REREKENSKR EEEEQQEGGF ASPRTGKGKW 670 680 690 700 710 720 KRKSAGGGPS RAGSPRRTSK KTKVEPYSLT AQQSSLIRED KSNAKLWNEV LASLKDRPAS 730 740 750 760 770 780 GSPFQLFLSK VEETFQCICC QELVFRPITT VCQHNVCKDC LDRSFRAQVF SCPACRYDLG 790 800 RSYAMQVNQP LQTVLNQLFP GYGNGR

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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 0:0-0(2012) [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

NIEHS-SNPs

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.

IPI

IPI00797945.

RefSeq

NP_001041666.1. NM_001048201.1.
NP_037414.3. NM_013282.3.

UniGene

Hs.108106.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q96T88.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96T88. 3 interactions.

MINT

MINT-2815626.

STRING

9606.ENSP00000381295.

PTM databases

PhosphoSite

Q96T88.

Polymorphism databases

DMDM

67462077.

Proteomic databases

PaxDb

Q96T88.

PRIDE

Q96T88.

Protocols and materials databases

DNASU

29128.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

29128.

KEGG

hsa:29128.

UCSC

uc002mbo.3. human.

Organism-specific databases

CTD

29128.

GeneCards

GC19P004910.

HGNC

HGNC:12556. UHRF1.

MIM

607990. gene.

neXtProt

NX_Q96T88.

PharmGKB

PA37196.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3440.

HOGENOM

HOG000124662.

HOVERGEN

HBG059298.

InParanoid

Q96T88.

KO

K10638.

OrthoDB

EOG408N7M.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

CleanEx

HS_UHRF1.

Genevestigator

Q96T88.

GermOnline

ENSG00000034063. Homo sapiens.

Family and domain databases

Gene3D

2.30.280.10. 1 hit.
2.30.30.30. 1 hit.
3.30.40.10. 2 hits.

InterPro

IPR021991. DUF3590.
IPR014722. Rib_L2_dom2.
IPR003105. SRA_YDG.
IPR000626. Ubiquitin.
IPR019955. Ubiquitin_supergroup.
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]

Pfam

PF12148. DUF3590. 1 hit.
PF00628. PHD. 1 hit.
PF00240. ubiquitin. 1 hit.
PF02182. YDG_SRA. 1 hit.
[Graphical view]

SMART

SM00249. PHD. 1 hit.
SM00184. RING. 2 hits.
SM00466. SRA. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]

SUPFAM

SSF57903. FYVE_PHD_ZnF. 1 hit.

PROSITE

PS00299. UBIQUITIN_1. False negative.
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]

ProtoNet

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Other

EvolutionaryTrace

Q96T88.

GenomeRNAi

29128.

NextBio

35463698.

SOURCE

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Entry information

Entry name

UHRF1_HUMAN

Accession

Primary (citable) accession number: Q96T88
Secondary accession number(s): A0JBR2 , 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:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.