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Q96PU4

- UHRF2_HUMAN

UniProt

Q96PU4 - UHRF2_HUMAN

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Protein

E3 ubiquitin-protein ligase UHRF2

Gene

UHRF2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri344 – 39552PHD-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri733 – 77240RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. histone binding Source: UniProtKB
  3. ligase activity Source: UniProtKB-KW
  4. ubiquitin-protein transferase activity Source: HGNC
  5. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell differentiation Source: HGNC
  3. cell proliferation Source: HGNC
  4. positive regulation of cell cycle arrest Source: UniProtKB
  5. protein autoubiquitination Source: HGNC
  6. protein ubiquitination Source: HGNC
  7. regulation of cell cycle Source: HGNC
  8. ubiquitin-dependent protein catabolic process Source: HGNC
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

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
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:12557. UHRF2.

Subcellular locationi

Nucleus 2 PublicationsPROSITE-ProRule annotation
Note: Enriched at pericentric heterochromatin (PH). This localization is dependent on the interaction with H3K9me3 (By similarity).By similarity

GO - Cellular componenti

  1. nuclear heterochromatin Source: UniProtKB
  2. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi307 – 3071K → R: No effect on autosumoylation. 1 Publication
Mutagenesisi548 – 5481K → R: No effect on autosumoylation. 1 Publication
Mutagenesisi735 – 7351C → S: No effect on autosumoylation, nor on ZNF131 sumoylation. 1 Publication

Organism-specific databases

PharmGKBiPA37197.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 802802E3 ubiquitin-protein ligase UHRF2PRO_0000056147Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei667 – 6671Phosphoserine1 Publication
Disulfide bondi704 – 704Interchain1 Publication

Post-translational modificationi

May be autoubiquitinated; which may lead to proteasomal degradation.1 Publication
Phosphorylated. Phosphorylation may be mediated by CDK2.2 Publications
Autosumoylated.

Keywords - PTMi

Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ96PU4.
PaxDbiQ96PU4.
PeptideAtlasiQ96PU4.
PRIDEiQ96PU4.

PTM databases

PhosphoSiteiQ96PU4.

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

BgeeiQ96PU4.
CleanExiHS_UHRF2.
ExpressionAtlasiQ96PU4. baseline and differential.
GenevestigatoriQ96PU4.

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

Protein-protein interaction databases

BioGridi125434. 55 interactions.
IntActiQ96PU4. 37 interactions.
MINTiMINT-1196856.
STRINGi9606.ENSP00000276893.

Structurei

Secondary structure

802
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 77Combined sources
Beta strandi13 – 197Combined sources
Helixi25 – 3511Combined sources
Turni40 – 423Combined sources
Beta strandi43 – 475Combined sources
Beta strandi54 – 574Combined sources
Helixi58 – 614Combined sources
Beta strandi68 – 736Combined sources
Turni332 – 3343Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi343 – 3464Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi359 – 3613Combined sources
Beta strandi363 – 3653Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi373 – 3764Combined sources
Turni390 – 3923Combined sources
Beta strandi458 – 4614Combined sources
Helixi462 – 4676Combined sources
Beta strandi477 – 4815Combined sources
Turni482 – 4843Combined sources
Beta strandi485 – 4917Combined sources
Beta strandi502 – 5087Combined sources
Helixi532 – 5398Combined sources
Beta strandi541 – 5433Combined sources
Turni547 – 5493Combined sources
Helixi556 – 5583Combined sources
Beta strandi562 – 5676Combined sources
Helixi568 – 5725Combined sources
Beta strandi575 – 5773Combined sources
Beta strandi579 – 59719Combined sources
Turni599 – 6013Combined sources
Beta strandi602 – 61211Combined sources
Helixi622 – 6309Combined sources
Helixi694 – 7029Combined sources
Helixi704 – 7063Combined sources
Helixi707 – 7137Combined sources
Helixi714 – 7229Combined sources
Helixi723 – 7308Combined sources
Turni734 – 7363Combined sources
Beta strandi737 – 7393Combined sources
Beta strandi741 – 7455Combined sources
Beta strandi751 – 7533Combined sources
Helixi754 – 7629Combined sources
Turni769 – 7713Combined sources
Helixi785 – 79410Combined sources
Turni796 – 8016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ96PU4.
SMRiQ96PU4. Positions 1-121, 124-395, 439-642, 688-802.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96PU4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7878Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Domaini448 – 612165YDGPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni117 – 311195Required for interaction with histone H3By similarityAdd
BLAST
Regioni194 – 28895Interaction with PCNPAdd
BLAST
Regioni414 – 644231Methyl-CpG binding and interaction with HDAC1Add
BLAST

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 fingeri344 – 39552PHD-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri733 – 77240RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG3440.
GeneTreeiENSGT00390000008296.
HOGENOMiHOG000124662.
HOVERGENiHBG059298.
InParanoidiQ96PU4.
KOiK15713.
OMAiYNVESPG.
OrthoDBiEOG76DTRX.
PhylomeDBiQ96PU4.
TreeFamiTF106434.

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. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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 CAH74120.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI13295.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti287 – 2871L → M in AAH28397. (PubMed:15489334)Curated
Sequence conflicti329 – 3291P → T in AAH28397. (PubMed:15489334)Curated
Sequence conflicti416 – 4161P → Q in AAH28397. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti87 – 871I → N in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035961

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei500 – 5034DRGD → LTEL in isoform 2. 1 PublicationVSP_013874
Alternative sequencei504 – 802299Missing in isoform 2. 1 PublicationVSP_013875Add
BLAST

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.3. human. [Q96PU4-1]

Polymorphism databases

DMDMi67462076.

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 .
CCDSi CCDS6469.1. [Q96PU4-1 ]
RefSeqi NP_690856.1. NM_152896.2. [Q96PU4-1 ]
UniGenei Hs.493401.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
4PW5 X-ray 2.20 A/B/E/F 419-648 [» ]
4PW6 X-ray 3.79 A/B 419-648 [» ]
4PW7 X-ray 2.00 A/B/E/F 419-648 [» ]
ProteinModelPortali Q96PU4.
SMRi Q96PU4. Positions 1-121, 124-395, 439-642, 688-802.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125434. 55 interactions.
IntActi Q96PU4. 37 interactions.
MINTi MINT-1196856.
STRINGi 9606.ENSP00000276893.

PTM databases

PhosphoSitei Q96PU4.

Polymorphism databases

DMDMi 67462076.

Proteomic databases

MaxQBi Q96PU4.
PaxDbi Q96PU4.
PeptideAtlasi Q96PU4.
PRIDEi Q96PU4.

Protocols and materials databases

DNASUi 115426.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000276893 ; ENSP00000276893 ; ENSG00000147854 . [Q96PU4-1 ]
ENST00000468435 ; ENSP00000434182 ; ENSG00000147854 . [Q96PU4-2 ]
GeneIDi 115426.
KEGGi hsa:115426.
UCSCi uc003zjy.3. human. [Q96PU4-1 ]

Organism-specific databases

CTDi 115426.
GeneCardsi GC09P006405.
HGNCi HGNC:12557. UHRF2.
HPAi HPA026633.
HPA026697.
MIMi 615211. gene.
neXtProti NX_Q96PU4.
PharmGKBi PA37197.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3440.
GeneTreei ENSGT00390000008296.
HOGENOMi HOG000124662.
HOVERGENi HBG059298.
InParanoidi Q96PU4.
KOi K15713.
OMAi YNVESPG.
OrthoDBi EOG76DTRX.
PhylomeDBi Q96PU4.
TreeFami TF106434.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi UHRF2. human.
EvolutionaryTracei Q96PU4.
GeneWikii UHRF2.
GenomeRNAii 115426.
NextBioi 79598.
PROi Q96PU4.
SOURCEi Search...

Gene expression databases

Bgeei Q96PU4.
CleanExi HS_UHRF2.
ExpressionAtlasi Q96PU4. baseline and differential.
Genevestigatori Q96PU4.

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. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 636-802 (ISOFORM 1).
    Tissue: Testis.
  6. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. 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. "UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131."
    Oh Y., Chung K.C.
    J. Biol. Chem. 288:9102-9111(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOSUMOYLATION, INTERACTION WITH UBE2I, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-307; LYS-548 AND CYS-735.
  13. "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.
  14. "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.
  15. "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.
  16. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-87.

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 26, 2014
This is version 126 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

External Data

Dasty 3