Q96PU4 (UHRF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase UHRF2
EC=6.3.2.-

Alternative name(s):
Np95/ICBP90-like RING finger protein
Short name=Np95-like RING finger protein
Nuclear protein 97
Nuclear zinc finger protein Np97
RING finger protein 107
Ubiquitin-like PHD and RING finger domain-containing protein 2
Ubiquitin-like-containing PHD and RING finger domains protein 2

Gene names

Name:	UHRF2
Synonyms:	NIRF, RNF107

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	802 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. Appears to contribute to tumorigenesis. Ref.1 Ref.6 Ref.7 Ref.8 Ref.11
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Homodimer; disulfide-linked. Binds methylated CpG containing oligonucleotides. Interacts with H3: the interaction has a preference for the 'Lys-9' trimethylated form of H3 (H3K9me3) By similarity. Interacts with PCNP, HDAC1 and CDK2 (inactive form). Component of a complex at least composed of UHRF2, CDK2 and CCNE1. Interacts directly with CCNE1; the interaction ubiquitinates CCNE1 and appears independent of CCNE1 phosphorylation. Interacts with CCND1; the interaction ubiquitinates CCND1 and appears independent of CCND1 phosphorylation. Interacts with p53/TP53 and RB1. Ref.1 Ref.6 Ref.7 Ref.8 Ref.11 Ref.14
Subcellular location	Nucleus. Note: Enriched at pericentric heterochromatin (PH). This localization is dependent on the interaction with H3K9me3 By similarity. Ref.1
Induction	Up-regulated in proliferating fetal lung fibroblasts and in U-937 myeloid leukemia cells. Down-regulated in these cells by growth arrest and differentiation. In other cell types which cannot leave the cell cycle, such as tumoral HT-1080 and Hep-G2, levels are consistently up-regulated. Ref.1
Post-translational modification	May be autoubiquitinated; which may lead to proteasomal degradation. Phosphorylated. Phosphorylation may be mediated by CDK2. Ref.6
Involvement in disease	Associated with various cancers. DNA copy number loss is found in multiple kinds of malignancies originating from the brain, breast, stomach, kidney, hematopoietic tissue and lung.
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 CAH74120.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI13295.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell cycle Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Ligase
PTM	Disulfide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from expression pattern Ref.1. Source: HGNC cell proliferation Inferred from expression pattern Ref.1. Source: HGNC positive regulation of cell cycle arrest Inferred from direct assay Ref.6. Source: UniProtKB protein autoubiquitination Inferred from direct assay Ref.7. Source: HGNC ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.7. Source: HGNC
Cellular_component	nuclear heterochromatin Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW histone binding Inferred from sequence or structural similarity. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay Ref.7. Source: HGNC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCNA2	P20248	2	EBI-625304,EBI-457097
CCNB1	P14635	2	EBI-625304,EBI-495332
CCND1	P24385	4	EBI-625304,EBI-375001
CCNE1	P24864	4	EBI-625304,EBI-519526
CDK2	P24941	5	EBI-625304,EBI-375096
RB1	P06400	4	EBI-625304,EBI-491274
TP53	P04637	3	EBI-625304,EBI-366083

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q96PU4-1)

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: Q96PU4-2)

Also known as: a;

The sequence of this isoform differs from the canonical sequence as follows:
     500-503: DRGD → LTEL
     504-802: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 802

802

E3 ubiquitin-protein ligase UHRF2

PRO_0000056147

Regions

Domain

1 – 78

78

Ubiquitin-like

Domain

448 – 612

165

YDG

Zinc finger

344 – 395

52

PHD-type

Zinc finger

733 – 772

40

RING-type

Region

117 – 311

195

Required for interaction with histone H3 By similarity

Region

194 – 288

95

Interaction with PCNP

Region

414 – 644

231

Methyl-CpG binding and interaction with HDAC1

Amino acid modifications

Modified residue

667

1

Phosphoserine Ref.9

Disulfide bond

704

Interchain Ref.14

Natural variations

Alternative sequence

500 – 503

4

DRGD → LTEL in isoform 2.

VSP_013874

Alternative sequence

504 – 802

299

Missing in isoform 2.

VSP_013875

Natural variant

87

1

I → N in a colorectal cancer sample; somatic mutation. Ref.15

VAR_035961

Experimental info

Sequence conflict

287

1

L → M in AAH28397. Ref.4

Sequence conflict

329

1

P → T in AAH28397. Ref.4

Sequence conflict

416

1

P → Q in AAH28397. Ref.4

Secondary structure

1

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802

Helix Strand Turn

Details...

Beta strand

1 – 7

7

Beta strand

13 – 19

7

Helix

25 – 35

11

Turn

40 – 42

3

Beta strand

43 – 47

5

Beta strand

54 – 57

4

Helix

58 – 61

4

Beta strand

68 – 73

6

Turn

332 – 334

3

Beta strand

338 – 340

3

Beta strand

343 – 346

4

Beta strand

348 – 350

3

Beta strand

359 – 361

3

Beta strand

363 – 365

3

Beta strand

368 – 370

3

Beta strand

373 – 376

4

Turn

390 – 392

3

Beta strand

458 – 461

4

Helix

462 – 467

6

Beta strand

477 – 481

5

Turn

482 – 484

3

Beta strand

485 – 493

9

Beta strand

502 – 508

7

Helix

532 – 540

9

Beta strand

541 – 543

3

Turn

547 – 549

3

Helix

556 – 558

3

Beta strand

562 – 567

6

Helix

568 – 570

3

Turn

571 – 573

3

Beta strand

579 – 597

19

Turn

599 – 601

3

Beta strand

604 – 612

9

Helix

622 – 630

9

Helix

694 – 702

9

Helix

704 – 706

3

Helix

707 – 713

7

Helix

714 – 722

9

Helix

723 – 730

8

Turn

734 – 736

3

Beta strand

737 – 739

3

Beta strand

741 – 745

5

Beta strand

751 – 753

3

Helix

754 – 762

9

Turn

769 – 771

3

Helix

785 – 794

10

Turn

796 – 801

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 190E26D5A347A7FA	FASTA	802	89,985
	10 20 30 40 50 60 MWIQVRTIDG SKTCTIEDVS RKATIEELRE RVWALFDVRP ECQRLFYRGK QLENGYTLFD 70 80 90 100 110 120 YDVGLNDIIQ LLVRPDPDHL PGTSTQIEAK PCSNSPPKVK KAPRVGPSNQ PSTSARARLI 130 140 150 160 170 180 DPGFGIYKVN ELVDARDVGL GAWFEAHIHS VTRASDGQSR GKTPLKNGSS CKRTNGNIKH 190 200 210 220 230 240 KSKENTNKLD SVPSTSNSDC VAADEDVIYH IQYDEYPESG TLEMNVKDLR PRARTILKWN 250 260 270 280 290 300 ELNVGDVVMV NYNVESPGQR GFWFDAEITT LKTISRTKKE LRVKIFLGGS EGTLNDCKII 310 320 330 340 350 360 SVDEIFKIER PGAHPLSFAD GKFLRRNDPE CDLCGGDPEK KCHSCSCRVC GGKHEPNMQL 370 380 390 400 410 420 LCDECNVAYH IYCLNPPLDK VPEEEYWYCP SCKTDSSEVV KAGERLKMSK KKAKMPSAST 430 440 450 460 470 480 ESRRDWGRGM ACVGRTRECT IVPSNHYGPI PGIPVGSTWR FRVQVSEAGV HRPHVGGIHG 490 500 510 520 530 540 RSNDGAYSLV LAGGFADEVD RGDEFTYTGS GGKNLAGNKR IGAPSADQTL TNMNRALALN 550 560 570 580 590 600 CDAPLDDKIG AESRNWRAGK PVRVIRSFKG RKISKYAPEE GNRYDGIYKV VKYWPEISSS 610 620 630 640 650 660 HGFLVWRYLL RRDDVEPAPW TSEGIERSRR LCLRLQYPAG YPSDKEGKKP KGQSKKQPSG 670 680 690 700 710 720 TTKRPISDDD CPSASKVYKA SDSAEAIEAF QLTPQQQHLI REDCQNQKLW DEVLSHLVEG 730 740 750 760 770 780 PNFLKKLEQS FMCVCCQELV YQPVTTECFH NVCKDCLQRS FKAQVFSCPA CRHDLGQNYI 790 800 MIPNEILQTL LDLFFPGYSK GR
	Isoform 2 (a) [UniParc]. Checksum: 6C81BFDFEC2FC512	FASTA	503	56,077
	10 20 30 40 50 60 MWIQVRTIDG SKTCTIEDVS RKATIEELRE RVWALFDVRP ECQRLFYRGK QLENGYTLFD 70 80 90 100 110 120 YDVGLNDIIQ LLVRPDPDHL PGTSTQIEAK PCSNSPPKVK KAPRVGPSNQ PSTSARARLI 130 140 150 160 170 180 DPGFGIYKVN ELVDARDVGL GAWFEAHIHS VTRASDGQSR GKTPLKNGSS CKRTNGNIKH 190 200 210 220 230 240 KSKENTNKLD SVPSTSNSDC VAADEDVIYH IQYDEYPESG TLEMNVKDLR PRARTILKWN 250 260 270 280 290 300 ELNVGDVVMV NYNVESPGQR GFWFDAEITT LKTISRTKKE LRVKIFLGGS EGTLNDCKII 310 320 330 340 350 360 SVDEIFKIER PGAHPLSFAD GKFLRRNDPE CDLCGGDPEK KCHSCSCRVC GGKHEPNMQL 370 380 390 400 410 420 LCDECNVAYH IYCLNPPLDK VPEEEYWYCP SCKTDSSEVV KAGERLKMSK KKAKMPSAST 430 440 450 460 470 480 ESRRDWGRGM ACVGRTRECT IVPSNHYGPI PGIPVGSTWR FRVQVSEAGV HRPHVGGIHG 490 500 RSNDGAYSLV LAGGFADEVL TEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"NIRF, a novel RING finger protein, is involved in cell-cycle regulation." Mori T., Li Y., Hata H., Ono K., Kochi H. Biochem. Biophys. Res. Commun. 296:530-536(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INDUCTION, FUNCTION, INTERACTION WITH PCNP. Tissue: Fetal brain.
[2]	"LMO2-induced T cell leukemias overexpress a novel gene, Uhr1, 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).
[3]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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). Tissue: Brain.
[5]	"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] OF 636-802 (ISOFORM 1). Tissue: Testis.
[6]	"NIRF induces G1 arrest and associates with Cdk2." Li Y., Mori T., Hata H., Homma Y., Kochi H. Biochem. Biophys. Res. Commun. 319:464-468(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN CELL CYCLE, PHOSPHORYLATION, INTERACTION WITH CDK2, IDENTIFICATION IN A COMPLEX WITH CDK2 AND CCNE1.
[7]	"NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein." Mori T., Li Y., Hata H., Kochi H. FEBS Lett. 557:209-214(2004) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, INTERACTION WITH PCNP, FUNCTION.
[8]	"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, INTERACTION WITH HDAC1.
[9]	"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-667, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor." Mori T., Ikeda D.D., Fukushima T., Takenoshita S., Kochi H. Cell Cycle 10:3284-3299(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CCDN1; CCNE1; TP53 AND RB1, ASSOCIATION WITH TUMORIGENESIS.
[12]	"Solution structure of the N-terminal ubiquitin-like domain in human NP95/ICBP90-like RING finger protein (NIRF)." RIKEN structural genomics initiative (RSGI) Submitted (AUG-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-76.
[13]	"2.1 Angstrom crystal structure of the human ubiquitin ligase NIRF." Structural genomics consortium (SGC) Submitted (JAN-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 672-802 IN COMPLEX WITH ZINC IONS.
[14]	"2.1 Angstrom crystal structure of the human ubiquitin ligase NIRF." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 672-802, SUBUNIT, DISULFIDE BOND.
[15]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-87.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB071698 mRNA. Translation: BAB68317.1.
AF274049 mRNA. Translation: AAM33799.1.
AL353718, AL133480 Genomic DNA. Translation: CAH74119.1.
AL133480, AL353718 Genomic DNA. Translation: CAI13293.1.
AL353718, AL133480 Genomic DNA. Translation: CAH74120.1. Sequence problems.
AL133480, AL353718 Genomic DNA. Translation: CAI13295.1. Sequence problems.
BC028397 mRNA. Translation: AAH28397.1.
AL137728 mRNA. Translation: CAH56383.1.

IPI

IPI00044681.
IPI00395464.

RefSeq

NP_690856.1. NM_152896.2.

UniGene

Hs.493401.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WY8	NMR	-	A	1-76	[»]
1Z6U	X-ray	2.10	A/B	672-802	[»]
2E6S	NMR	-	A	326-395	[»]
3OLN	X-ray	2.30	A/B	419-648	[»]

ProteinModelPortal

Q96PU4.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96PU4. 36 interactions.

MINT

MINT-1196856.

STRING

9606.ENSP00000276893.

PTM databases

PhosphoSite

Q96PU4.

Polymorphism databases

DMDM

67462076.

Proteomic databases

PaxDb

Q96PU4.

PeptideAtlas

Q96PU4.

PRIDE

Q96PU4.

Protocols and materials databases

DNASU

115426.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000276893; ENSP00000276893; ENSG00000147854.
ENST00000450508; ENSP00000399217; ENSG00000147854.
ENST00000468435; ENSP00000434182; ENSG00000147854.

GeneID

115426.

KEGG

hsa:115426.

UCSC

uc003zjy.3. human.

Organism-specific databases

CTD

115426.

GeneCards

GC09P006405.

HGNC

HGNC:12557. UHRF2.

HPA

HPA026633.
HPA026697.

neXtProt

NX_Q96PU4.

PharmGKB

PA37197.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3440.

HOGENOM

HOG000124662.

HOVERGEN

HBG059298.

InParanoid

Q96PU4.

KO

K15713.

OMA

VNHNSKE.

OrthoDB

EOG408N7M.

Enzyme and pathway databases

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q96PU4.

Bgee

Q96PU4.

CleanEx

HS_UHRF2.

Genevestigator

Q96PU4.

GermOnline

ENSG00000147854. 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. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

UHRF2. human.

EvolutionaryTrace

Q96PU4.

GenomeRNAi

115426.

NextBio

79598.

Entry information

Entry name

UHRF2_HUMAN

Accession

Primary (citable) accession number: Q96PU4
Secondary accession number(s): Q5VYR1 , Q5VYR3, Q659C8, Q8TAG7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 110 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.