GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

HUMAN:TP53B

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) TP53BP1
Protein Name(s) Tumor suppressor p53-binding protein 1

53BP1 p53-binding protein 1 p53BP1

External Links
UniProt Q12888
EMBL AF078776
AB210025
BX537418
AY904026
AC018924
BC112161
U09477
CCDS CCDS10096.1
CCDS45250.1
CCDS45251.1
PIR I38604
RefSeq NP_001135451.1
NP_001135452.1
NP_005648.1
XP_005254691.1
UniGene Hs.440968
Hs.584887
PDB 1GZH
1KZY
1XNI
2G3R
2IG0
2LVM
3LGF
3LGL
3LH0
4CRI
4RG2
PDBsum 1GZH
1KZY
1XNI
2G3R
2IG0
2LVM
3LGF
3LGL
3LH0
4CRI
4RG2
ProteinModelPortal Q12888
SMR Q12888
BioGrid 113011
DIP DIP-5978N
IntAct Q12888
MINT MINT-276057
STRING 9606.ENSP00000371475
BindingDB Q12888
ChEMBL CHEMBL2424509
PhosphoSite Q12888
DMDM 8928568
MaxQB Q12888
PaxDb Q12888
PRIDE Q12888
Ensembl ENST00000263801
ENST00000382044
ENST00000450115
GeneID 7158
KEGG hsa:7158
UCSC uc001zrr.4
uc001zrs.3
CTD 7158
GeneCards GC15M043699
HGNC HGNC:11999
HPA CAB004083
HPA008788
HPA022133
MIM 605230
neXtProt NX_Q12888
PharmGKB PA36680
eggNOG NOG264535
GeneTree ENSGT00390000011891
HOGENOM HOG000231961
HOVERGEN HBG060882
InParanoid Q12888
OMA PEIPFQA
OrthoDB EOG7RZ5P1
PhylomeDB Q12888
TreeFam TF350227
Reactome REACT_97
ChiTaRS TP53BP1
EvolutionaryTrace Q12888
GeneWiki TP53BP1
GenomeRNAi 7158
NextBio 28010
PMAP-CutDB Q12888
PRO PR:Q12888
Proteomes UP000005640
Bgee Q12888
CleanEx HS_TP53BP1
ExpressionAtlas Q12888
Genevestigator Q12888
GO GO:0000777
GO:0005737
GO:0005654
GO:0005634
GO:0005657
GO:0003684
GO:0035064
GO:0002039
GO:0001102
GO:0001104
GO:0042162
GO:0006974
GO:0006281
GO:0006302
GO:0000724
GO:0051091
GO:0045944
GO:0045893
GO:0006366
Gene3D 2.30.30.30
3.40.50.10190
InterPro IPR015125
IPR001357
IPR014722
Pfam PF09038
SMART SM00292
SUPFAM SSF52113
PROSITE PS50172

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0035861

site of double-strand break

PMID:23333306[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006303

double-strand break repair via nonhomologous end joining

PMID:23333306[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:2000042

negative regulation of double-strand break repair via homologous recombination

PMID:23333306[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:2000042

negative regulation of double-strand break repair via homologous recombination

PMID:23345425[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045830

positive regulation of isotype switching

PMID:23345425[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051260

protein homooligomerization

PMID:23345425[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045830

positive regulation of isotype switching

PMID:23760478[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006303

double-strand break repair via nonhomologous end joining

PMID:23760478[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0035861

site of double-strand break

PMID:23760478[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0061649

ubiquitin modification-dependent histone binding

PMID:23760478[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0035064

methylated histone binding

PMID:23760478[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:28241136[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006303

double-strand break repair via nonhomologous end joining

PMID:28241136[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0035064

methylated histone binding

PMID:28241136[4]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0035861

site of double-strand break

PMID:28241136[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:28241136[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0002039

p53 binding

PMID:14985081[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P04637

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:9748285[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

PMID:9748285[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0051091

positive regulation of DNA-binding transcription factor activity

PMID:17805299[7]

ECO:0000305

curator inference used in manual assertion

GO:0045944

P

Seeded From UniProt

complete

involved_in

GO:0045944

positive regulation of transcription by RNA polymerase II

PMID:17805299[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0002039

p53 binding

PMID:17805299[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P04637

F

Seeded From UniProt

complete

enables

GO:0003712

transcription coregulator activity

PMID:17805299[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0001102

RNA polymerase II activating transcription factor binding

PMID:17805299[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P04637

F

Seeded From UniProt

complete

colocalizes_with

GO:0000781

chromosome, telomeric region

PMID:15149599[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0045893

positive regulation of transcription, DNA-templated

PMID:9748285[6]

ECO:0000303

author statement without traceable support used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0035064

methylated histone binding

PMID:22373579[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0045944

positive regulation of transcription by RNA polymerase II

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001809041
SGD:S000002625
UniProtKB:Q12888

P

Seeded From UniProt

complete

enables

GO:0042393

histone binding

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001809041
SGD:S000002625

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1351320
PANTHER:PTN001809041
PomBase:SPBC342.05
RGD:1308039
UniProtKB:Q12888

C

Seeded From UniProt

complete

involved_in

GO:0000077

DNA damage checkpoint

PMID:21873635[10]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001809041
SGD:S000002625
UniProtKB:A0A1D8PNH8

P

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:17500065[11]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016604

nuclear body

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0071481

cellular response to X-ray

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:F1M842
ensembl:ENSRNOP00000019025

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:F1M842
ensembl:ENSRNOP00000019025

C

Seeded From UniProt

complete

involved_in

GO:2000042

negative regulation of double-strand break repair via homologous recombination

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

P

Seeded From UniProt

complete

part_of

GO:1990391

DNA repair complex

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

C

Seeded From UniProt

complete

involved_in

GO:0045830

positive regulation of isotype switching

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

P

Seeded From UniProt

complete

enables

GO:0043565

sequence-specific DNA binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

F

Seeded From UniProt

complete

enables

GO:0042162

telomeric DNA binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

F

Seeded From UniProt

complete

part_of

GO:0035861

site of double-strand break

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

C

Seeded From UniProt

complete

enables

GO:0035064

methylated histone binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

F

Seeded From UniProt

complete

part_of

GO:0016604

nuclear body

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

C

Seeded From UniProt

complete

involved_in

GO:0006303

double-strand break repair via nonhomologous end joining

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

P

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

P

Seeded From UniProt

complete

part_of

GO:0005657

replication fork

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

C

Seeded From UniProt

complete

enables

GO:0003684

damaged DNA binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

F

Seeded From UniProt

complete

part_of

GO:0000784

nuclear chromosome, telomeric region

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

C

Seeded From UniProt

complete

part_of

GO:0000776

kinetochore

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P70399
ensembl:ENSMUSP00000106278

C

Seeded From UniProt

complete

involved_in

GO:0006303

double-strand break repair via nonhomologous end joining

Reactome:R-HSA-5693571

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

Reactome:R-HSA-69891
Reactome:R-HSA-5693599
Reactome:R-HSA-5693566
Reactome:R-HSA-5693551
Reactome:R-HSA-5686900
Reactome:R-HSA-5686704
Reactome:R-HSA-5686685
Reactome:R-HSA-5684071
Reactome:R-HSA-5684052
Reactome:R-HSA-5683801
Reactome:R-HSA-5683735
Reactome:R-HSA-5683425
Reactome:R-HSA-5683405
Reactome:R-HSA-5683385
Reactome:R-HSA-5683384
Reactome:R-HSA-2997723

ECO:0000304

author statement supported by traceable reference used in manual assertion
















C

Seeded From UniProt

complete

part_of

GO:0005694

chromosome

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0158
UniProtKB-SubCell:SL-0468

C

Seeded From UniProt

complete

part_of

GO:0000775

chromosome, centromeric region

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0137

C

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0234

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0238

F

Seeded From UniProt

complete

part_of

GO:0000776

kinetochore

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0995

C

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0227

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

part_of

GO:0000777

condensed chromosome kinetochore

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0149

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 Escribano-Díaz, C et al. (2013) A cell cycle-dependent regulatory circuit composed of 53BP1-RIF1 and BRCA1-CtIP controls DNA repair pathway choice. Mol. Cell 49 872-83 PubMed GONUTS page
  2. 2.0 2.1 2.2 Lottersberger, F et al. (2013) Role of 53BP1 oligomerization in regulating double-strand break repair. Proc. Natl. Acad. Sci. U.S.A. 110 2146-51 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 Fradet-Turcotte, A et al. (2013) 53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark. Nature 499 50-4 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 4.4 Drané, P et al. (2017) TIRR regulates 53BP1 by masking its histone methyl-lysine binding function. Nature 543 211-216 PubMed GONUTS page
  5. Cao, Y et al. (2004) Hepatitis C virus core protein interacts with p53-binding protein, 53BP2/Bbp/ASPP2, and inhibits p53-mediated apoptosis. Biochem. Biophys. Res. Commun. 315 788-95 PubMed GONUTS page
  6. 6.0 6.1 6.2 Iwabuchi, K et al. (1998) Stimulation of p53-mediated transcriptional activation by the p53-binding proteins, 53BP1 and 53BP2. J. Biol. Chem. 273 26061-8 PubMed GONUTS page
  7. 7.0 7.1 7.2 7.3 7.4 Huang, J et al. (2007) p53 is regulated by the lysine demethylase LSD1. Nature 449 105-8 PubMed GONUTS page
  8. Herbig, U et al. (2004) Telomere shortening triggers senescence of human cells through a pathway involving ATM, p53, and p21(CIP1), but not p16(INK4a). Mol. Cell 14 501-13 PubMed GONUTS page
  9. Mallette, FA et al. (2012) RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1 recruitment to DNA damage sites. EMBO J. 31 1865-78 PubMed GONUTS page
  10. 10.0 10.1 10.2 10.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  11. Cho, YW et al. (2007) PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex. J. Biol. Chem. 282 20395-406 PubMed GONUTS page