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Protein

E3 ubiquitin-protein ligase UHRF2

Gene

UHRF2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131.6 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri344 – 395PHD-typePROSITE-ProRule annotationAdd BLAST52
Zinc fingeri733 – 772RING-typePROSITE-ProRule annotationAdd BLAST40

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • histone binding Source: UniProtKB
  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: MGI
  • ubiquitin-protein transferase activity Source: HGNC
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell differentiation Source: HGNC
  • cell proliferation Source: HGNC
  • maintenance of DNA methylation Source: GO_Central
  • positive regulation of cell cycle arrest Source: UniProtKB
  • protein autoubiquitination Source: HGNC
  • protein ubiquitination Source: HGNC
  • regulation of cell cycle Source: HGNC
  • regulation of methylation-dependent chromatin silencing Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000147854-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:UHRF2
Synonyms:NIRF, RNF107
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:12557. UHRF2.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation2 Publications

  • Note: Enriched at pericentric heterochromatin (PH). This localization is dependent on the interaction with H3K9me3 (By similarity).By similarity

GO - Cellular componenti

  • nuclear heterochromatin Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi307K → R: No effect on autosumoylation. 1 Publication1
Mutagenesisi548K → R: No effect on autosumoylation. 1 Publication1
Mutagenesisi735C → S: No effect on autosumoylation, nor on ZNF131 sumoylation. 1 Publication1

Organism-specific databases

DisGeNETi115426.
OpenTargetsiENSG00000147854.
PharmGKBiPA37197.

Polymorphism and mutation databases

BioMutaiUHRF2.
DMDMi67462076.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000561471 – 802E3 ubiquitin-protein ligase UHRF2Add BLAST802

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei667PhosphoserineCombined sources1
Disulfide bondi704Interchain1 Publication

Post-translational modificationi

May be autoubiquitinated; which may lead to proteasomal degradation.1 Publication
Phosphorylated. Phosphorylation may be mediated by CDK2.1 Publication
Autosumoylated.

Keywords - PTMi

Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96PU4.
MaxQBiQ96PU4.
PaxDbiQ96PU4.
PeptideAtlasiQ96PU4.
PRIDEiQ96PU4.

PTM databases

iPTMnetiQ96PU4.
PhosphoSitePlusiQ96PU4.

Expressioni

Inductioni

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.1 Publication

Gene expression databases

BgeeiENSG00000147854.
CleanExiHS_UHRF2.
ExpressionAtlasiQ96PU4. baseline and differential.
GenevisibleiQ96PU4. HS.

Organism-specific databases

HPAiHPA026633.
HPA026697.

Interactioni

Subunit structurei

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. Interacts with UBE2I.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNA2P202482EBI-625304,EBI-457097
CCNB1P146352EBI-625304,EBI-495332
CCND1P243854EBI-625304,EBI-375001
CCNE1P248644EBI-625304,EBI-519526
CDK2P249415EBI-625304,EBI-375096
RB1P064004EBI-625304,EBI-491274
TP53P046373EBI-625304,EBI-366083

GO - Molecular functioni

Protein-protein interaction databases

BioGridi125434. 58 interactors.
IntActiQ96PU4. 37 interactors.
MINTiMINT-1196856.
STRINGi9606.ENSP00000276893.

Structurei

Secondary structure

1802
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 7Combined sources7
Beta strandi13 – 19Combined sources7
Helixi25 – 35Combined sources11
Turni40 – 42Combined sources3
Beta strandi43 – 47Combined sources5
Beta strandi54 – 57Combined sources4
Helixi58 – 61Combined sources4
Beta strandi68 – 73Combined sources6
Beta strandi132 – 136Combined sources5
Turni138 – 140Combined sources3
Beta strandi143 – 153Combined sources11
Beta strandi206 – 213Combined sources8
Helixi217 – 219Combined sources3
Beta strandi222 – 224Combined sources3
Helixi226 – 228Combined sources3
Beta strandi229 – 231Combined sources3
Helixi239 – 241Combined sources3
Beta strandi247 – 252Combined sources6
Beta strandi262 – 273Combined sources12
Beta strandi275 – 277Combined sources3
Beta strandi279 – 286Combined sources8
Beta strandi293 – 298Combined sources6
Turni318 – 320Combined sources3
Turni332 – 336Combined sources5
Beta strandi338 – 340Combined sources3
Turni343 – 345Combined sources3
Turni348 – 350Combined sources3
Beta strandi356 – 360Combined sources5
Beta strandi363 – 365Combined sources3
Beta strandi368 – 370Combined sources3
Turni371 – 373Combined sources3
Beta strandi374 – 376Combined sources3
Turni390 – 392Combined sources3
Beta strandi458 – 461Combined sources4
Helixi462 – 467Combined sources6
Beta strandi477 – 481Combined sources5
Turni482 – 484Combined sources3
Beta strandi485 – 491Combined sources7
Beta strandi502 – 508Combined sources7
Helixi532 – 539Combined sources8
Beta strandi541 – 543Combined sources3
Turni547 – 549Combined sources3
Helixi556 – 558Combined sources3
Beta strandi562 – 567Combined sources6
Helixi568 – 572Combined sources5
Beta strandi575 – 577Combined sources3
Beta strandi579 – 597Combined sources19
Turni599 – 601Combined sources3
Beta strandi602 – 612Combined sources11
Helixi622 – 630Combined sources9
Helixi694 – 702Combined sources9
Helixi704 – 706Combined sources3
Helixi707 – 713Combined sources7
Helixi714 – 722Combined sources9
Helixi723 – 730Combined sources8
Turni734 – 736Combined sources3
Beta strandi737 – 739Combined sources3
Beta strandi741 – 745Combined sources5
Beta strandi751 – 753Combined sources3
Helixi754 – 762Combined sources9
Turni769 – 771Combined sources3
Helixi785 – 794Combined sources10
Turni796 – 801Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WY8NMR-A1-76[»]
1Z6UX-ray2.10A/B672-802[»]
2E6SNMR-A326-395[»]
3OLNX-ray2.30A/B419-648[»]
4PW5X-ray2.20A/B/E/F419-648[»]
4PW6X-ray3.79A/B419-648[»]
4PW7X-ray2.00A/B/E/F419-648[»]
4TVRX-ray2.29A109-395[»]
ProteinModelPortaliQ96PU4.
SMRiQ96PU4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96PU4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 78Ubiquitin-likePROSITE-ProRule annotationAdd BLAST78
Domaini448 – 612YDGPROSITE-ProRule annotationAdd BLAST165

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni117 – 311Required for interaction with histone H3By similarityAdd BLAST195
Regioni194 – 288Interaction with PCNPAdd BLAST95
Regioni414 – 644Methyl-CpG binding and interaction with HDAC11 PublicationAdd BLAST231

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)DescriptionActionsGraphical viewLength
Zinc fingeri344 – 395PHD-typePROSITE-ProRule annotationAdd BLAST52
Zinc fingeri733 – 772RING-typePROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IFAP. Eukaryota.
COG3440. LUCA.
GeneTreeiENSGT00390000008296.
HOGENOMiHOG000124662.
HOVERGENiHBG059298.
InParanoidiQ96PU4.
KOiK15713.
OMAiCRFCSCC.
OrthoDBiEOG091G06BT.
PhylomeDBiQ96PU4.
TreeFamiTF106434.

Family and domain databases

Gene3Di2.30.280.10. 1 hit.
2.30.30.30. 1 hit.
3.30.40.10. 2 hits.
InterProiIPR015947. PUA-like_domain.
IPR014722. Rib_L2_dom2.
IPR003105. SRA_YDG.
IPR021991. TTD_dom.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_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]
PfamiPF00628. PHD. 1 hit.
PF02182. SAD_SRA. 1 hit.
PF12148. TTD. 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. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96PU4-1) [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
MWIQVRTIDG SKTCTIEDVS RKATIEELRE RVWALFDVRP ECQRLFYRGK
60 70 80 90 100
QLENGYTLFD YDVGLNDIIQ LLVRPDPDHL PGTSTQIEAK PCSNSPPKVK
110 120 130 140 150
KAPRVGPSNQ PSTSARARLI DPGFGIYKVN ELVDARDVGL GAWFEAHIHS
160 170 180 190 200
VTRASDGQSR GKTPLKNGSS CKRTNGNIKH KSKENTNKLD SVPSTSNSDC
210 220 230 240 250
VAADEDVIYH IQYDEYPESG TLEMNVKDLR PRARTILKWN ELNVGDVVMV
260 270 280 290 300
NYNVESPGQR GFWFDAEITT LKTISRTKKE LRVKIFLGGS EGTLNDCKII
310 320 330 340 350
SVDEIFKIER PGAHPLSFAD GKFLRRNDPE CDLCGGDPEK KCHSCSCRVC
360 370 380 390 400
GGKHEPNMQL LCDECNVAYH IYCLNPPLDK VPEEEYWYCP SCKTDSSEVV
410 420 430 440 450
KAGERLKMSK KKAKMPSAST ESRRDWGRGM ACVGRTRECT IVPSNHYGPI
460 470 480 490 500
PGIPVGSTWR FRVQVSEAGV HRPHVGGIHG RSNDGAYSLV LAGGFADEVD
510 520 530 540 550
RGDEFTYTGS GGKNLAGNKR IGAPSADQTL TNMNRALALN CDAPLDDKIG
560 570 580 590 600
AESRNWRAGK PVRVIRSFKG RKISKYAPEE GNRYDGIYKV VKYWPEISSS
610 620 630 640 650
HGFLVWRYLL RRDDVEPAPW TSEGIERSRR LCLRLQYPAG YPSDKEGKKP
660 670 680 690 700
KGQSKKQPSG TTKRPISDDD CPSASKVYKA SDSAEAIEAF QLTPQQQHLI
710 720 730 740 750
REDCQNQKLW DEVLSHLVEG PNFLKKLEQS FMCVCCQELV YQPVTTECFH
760 770 780 790 800
NVCKDCLQRS FKAQVFSCPA CRHDLGQNYI MIPNEILQTL LDLFFPGYSK

GR
Length:802
Mass (Da):89,985
Last modified:December 1, 2001 - v1
Checksum:i190E26D5A347A7FA
GO
Isoform 2 (identifier: Q96PU4-2) [UniParc]FASTAAdd to basket
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.
Show »
Length:503
Mass (Da):56,077
Checksum:i6C81BFDFEC2FC512
GO

Sequence cautioni

The sequence CAH74120 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI13295 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti287L → M in AAH28397 (PubMed:15489334).Curated1
Sequence conflicti329P → T in AAH28397 (PubMed:15489334).Curated1
Sequence conflicti416P → Q in AAH28397 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03596187I → N in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs147971931dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_013874500 – 503DRGD → LTEL in isoform 2. 1 Publication4
Alternative sequenceiVSP_013875504 – 802Missing in isoform 2. 1 PublicationAdd BLAST299

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6469.1. [Q96PU4-1]
RefSeqiNP_690856.1. NM_152896.2. [Q96PU4-1]
UniGeneiHs.493401.

Genome annotation databases

EnsembliENST00000276893; ENSP00000276893; ENSG00000147854. [Q96PU4-1]
ENST00000468435; ENSP00000434182; ENSG00000147854. [Q96PU4-2]
GeneIDi115426.
KEGGihsa:115426.
UCSCiuc003zjy.4. human. [Q96PU4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS6469.1. [Q96PU4-1]
RefSeqiNP_690856.1. NM_152896.2. [Q96PU4-1]
UniGeneiHs.493401.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WY8NMR-A1-76[»]
1Z6UX-ray2.10A/B672-802[»]
2E6SNMR-A326-395[»]
3OLNX-ray2.30A/B419-648[»]
4PW5X-ray2.20A/B/E/F419-648[»]
4PW6X-ray3.79A/B419-648[»]
4PW7X-ray2.00A/B/E/F419-648[»]
4TVRX-ray2.29A109-395[»]
ProteinModelPortaliQ96PU4.
SMRiQ96PU4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125434. 58 interactors.
IntActiQ96PU4. 37 interactors.
MINTiMINT-1196856.
STRINGi9606.ENSP00000276893.

PTM databases

iPTMnetiQ96PU4.
PhosphoSitePlusiQ96PU4.

Polymorphism and mutation databases

BioMutaiUHRF2.
DMDMi67462076.

Proteomic databases

EPDiQ96PU4.
MaxQBiQ96PU4.
PaxDbiQ96PU4.
PeptideAtlasiQ96PU4.
PRIDEiQ96PU4.

Protocols and materials databases

DNASUi115426.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000276893; ENSP00000276893; ENSG00000147854. [Q96PU4-1]
ENST00000468435; ENSP00000434182; ENSG00000147854. [Q96PU4-2]
GeneIDi115426.
KEGGihsa:115426.
UCSCiuc003zjy.4. human. [Q96PU4-1]

Organism-specific databases

CTDi115426.
DisGeNETi115426.
GeneCardsiUHRF2.
HGNCiHGNC:12557. UHRF2.
HPAiHPA026633.
HPA026697.
MIMi615211. gene.
neXtProtiNX_Q96PU4.
OpenTargetsiENSG00000147854.
PharmGKBiPA37197.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFAP. Eukaryota.
COG3440. LUCA.
GeneTreeiENSGT00390000008296.
HOGENOMiHOG000124662.
HOVERGENiHBG059298.
InParanoidiQ96PU4.
KOiK15713.
OMAiCRFCSCC.
OrthoDBiEOG091G06BT.
PhylomeDBiQ96PU4.
TreeFamiTF106434.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000147854-MONOMER.

Miscellaneous databases

ChiTaRSiUHRF2. human.
EvolutionaryTraceiQ96PU4.
GeneWikiiUHRF2.
GenomeRNAii115426.
PROiQ96PU4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000147854.
CleanExiHS_UHRF2.
ExpressionAtlasiQ96PU4. baseline and differential.
GenevisibleiQ96PU4. HS.

Family and domain databases

Gene3Di2.30.280.10. 1 hit.
2.30.30.30. 1 hit.
3.30.40.10. 2 hits.
InterProiIPR015947. PUA-like_domain.
IPR014722. Rib_L2_dom2.
IPR003105. SRA_YDG.
IPR021991. TTD_dom.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_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]
PfamiPF00628. PHD. 1 hit.
PF02182. SAD_SRA. 1 hit.
PF12148. TTD. 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. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiUHRF2_HUMAN
AccessioniPrimary (citable) accession number: Q96PU4
Secondary accession number(s): Q5VYR1
, Q5VYR3, Q659C8, Q8TAG7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 1, 2001
Last modified: November 2, 2016
This is version 143 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 9
    Human chromosome 9: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.