Property Report: isogroup BRCA1 [Human]

Proteome Database

Property Report

E	Experimentally determined
S	Predicted by sequence similarity
P	Predicted by analysis other than seq. similarity
K	Predicted by BioKnowledge^TM Transfer by BIOBASE
see	Indicates references that mention and cite a finding, but do not demonstrate it directly.

Human BRCA1	Gene Ontology: Molecular Function

DNA binding [15, E; 6, E]
->nucleic acid binding->binding

estrogen receptor binding [1, E]
->steroid hormone receptor binding->nuclear hormone receptor binding->hormone receptor binding->receptor binding->protein binding->binding

NF-kappaB binding [2, E]
->transcription factor binding->protein binding->binding

protein binding [11, E; 13, E]
->binding

protein heterodimerization activity [3, E]
->protein dimerization activity->protein binding->binding

protein N-terminus binding [4, E]
->protein binding->binding

transcription activator activity [10, E; 12, E]
->transcription regulator activity

transcription coactivator activity [9, E; 15, E; 7, E]
->transcription activator activity->transcription regulator activity
->transcription cofactor activity->transcription factor binding->protein binding->binding
->transcription cofactor activity->transcription regulator activity

transcription cofactor activity [8, E]
->transcription factor binding->protein binding->binding
->transcription regulator activity

transcription corepressor activity [5, E]
->transcription cofactor activity->transcription factor binding->protein binding->binding
->transcription cofactor activity->transcription regulator activity
->transcription repressor activity->transcription regulator activity

transcription repressor activity [14, E]
->transcription regulator activity

tubulin binding [16, E]
->cytoskeletal protein binding->protein binding->binding

ubiquitin-protein ligase activity [4, E]
->small conjugating protein ligase activity->acid-amino acid ligase activity->ligase activity, forming carbon-nitrogen bonds->ligase activity->catalytic activity

zinc ion binding [18, S; 17, E]
->transition metal ion binding->cation binding->ion binding->binding
->transition metal ion binding->metal ion binding->ion binding->binding

References [hide] (18 entries)

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[1] PMID 15674350 . Structural determinants of the BRCA1 : estrogen receptor interaction. Oncogene 24(11) 1831-46 (2005)
[2] PMID 12700228 . BRCA1 augments transcription by the NF-kappaB transcription factor by binding to the Rel domain of the p65/RelA subunit. Journal Of Biological Chemistry 278(29) 26333-41. (2003)
[3] PMID 12890688 . The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. Journal Of Biological Chemistry 278(37) 34743-6. (2003)
[4] PMID 11278247 . The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation. Journal Of Biological Chemistry 276(18) 14537-40. (2001)
[5] PMID 11244506 . Role of direct interaction in BRCA1 inhibition of estrogen receptor activity. Oncogene 20(1) 77-87. (2001)

[1] PMID 15674350 . Structural determinants of the BRCA1 : estrogen receptor interaction. Oncogene 24(11) 1831-46 (2005)
[2] PMID 12700228 . BRCA1 augments transcription by the NF-kappaB transcription factor by binding to the Rel domain of the p65/RelA subunit. Journal Of Biological Chemistry 278(29) 26333-41. (2003)
[3] PMID 12890688 . The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin. Journal Of Biological Chemistry 278(37) 34743-6. (2003)
[4] PMID 11278247 . The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation. Journal Of Biological Chemistry 276(18) 14537-40. (2001)
[5] PMID 11244506 . Role of direct interaction in BRCA1 inhibition of estrogen receptor activity. Oncogene 20(1) 77-87. (2001)
[6] PMID 11353843 . From the Cover: Direct DNA binding by Brca1. Proceedings Of The National Academy Of Sciences Of The United States Of America 98(11) 6086-91. (2001)
[7] PMID 10725406 . BRCA1 interaction with RNA polymerase II reveals a role for hRPB2 and hRPB10alpha in activated transcription. Proceedings Of The National Academy Of Sciences Of The United States Of America 97(7) 3148-53. (2000)
[8] PMID 10945975 . BRCA1 physically and functionally interacts with ATF1. Journal Of Biological Chemistry 275(46) 36230-7 (2000)
[9] PMID 10655477 . CBP/p300 interact with and function as transcriptional coactivators of BRCA1. Proceedings Of The National Academy Of Sciences Of The United States Of America 97(3) 1020-5. (2000)
[10] PMID 11016938 . A functional comparison of BRCA1 C-terminal domains in transcription activation and chromatin remodeling. Journal Of Biological Chemistry 275(51) 40169-73. (2000)
[11] PMID 10910365 . Functional link of BRCA1 and ataxia telangiectasia gene product in DNA damage response. Nature 406(6792) 210-5 (2000)
[12] PMID 11175350 . Transactivation of the p21 promoter by BRCA1 splice variants in mammary epithelial cells: evidence for both common and distinct activities of wildtype and mutant forms. Oncogene 19(54) 6351-6360. (2000)
[13] PMID 10426999 . Association of BRCA1 with the hRad50-hMre11-p95 complex and the DNA damage response. Science 285(5428) 747-50 (1999)
[14] PMID 10334989 . BRCA1 inhibition of estrogen receptor signaling in transfected cells. Science 284(5418) 1354-6 (1999)
[15] PMID 9662397 . BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A. Nature Genetics 19(3) 254-6 (1998)
[16] PMID 9789027 . BRCA1 is associated with the centrosome during mitosis. Proceedings Of The National Academy Of Sciences Of The United States Of America 95(22) 12983-8. (1998)
[17] PMID 9254622 . Sequential metal binding by the RING finger domain of BRCA1. Biochemistry 36(33) 10240-5. (1997)
[18] PMID 8944023 . Identification of a RING protein that can interact in vivo with the BRCA1 gene product. Nature Genetics 14(4) 430-40 (1996)

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