Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

Exploring the link between MORF4L1 and risk of breast cancer.

Martrat G, Maxwell CM, Tominaga E, Porta-de-la-Riva M, Bonifaci N, Gomez-Baldo L, Bogliolo M, Lazaro C, Blanco I, Brunet J, Aguilar H, Fernandez-Rodriguez J, Seal S, Renwick A, Rahman N, Kuehl J, Neveling K, Schindler D, Ramirez MJ, Castella M, Hernandez G, , Easton DF, Peock S, Cook M, Oliver CT, Frost D, Platte R, Evans DG, Lalloo F, Eeles R, Izatt L, Chu C, Davidson R, Ong KR, Cook J, Douglas F, Hodgson S, Brewer C, Morrison PJ, Porteous M, Peterlongo P, Manoukian S, Peissel B, Zaffaroni D, Roversi G, Barile M, Viel A, Pasini B, Ottini L, Putignano AL, Savarese A, Bernard L, Radice P, Healey S, Spurdle A, Chen X, Beesley J, , Rookus MA, Verhoef S, Tilanus-Linthorst MA, Vreeswijk MP, Asperen CJ, Bodmer D, Ausems MG, van Os TA, Blok MJ, Meijers-Heijboer HE, Hogervorst FB, , Goldgar DE, Buys S, John EM, Miron A, Southey M, Daly MB, , , Harbst K, Borg A, Rantala J, Barbany-Bustinza G, Ehrencrona H, Stenmark-Askmalm M, Kaufman B, Laitman Y, Milgrom R, Friedman E, Domchek SM, Nathanson KL, Rebbeck TR, Johannsson OT, Couch FJ, Wang X, Fredericksen Z, Cuadras D, Moreno V, Pientka FK, Depping R, Caldes T, Osorio A, Benitez J, Bueren J, Heikkinen T, Nevanlinna H, Hamann U, Torres D, Caligo MA, Godwin AK, Imyanitov EN, Janavicius R, , Sinilnikova OM, Stoppa-Lyonnet D, Mazoyer S, Verny-Pierre C, Castera L, de Pauw A, Bignon YJ, Uhrhammer N, Peyrat JP, Vennin P, Ferrer SF, Collonge-Rame MA, Mortemousque I, McGuffog L, Chenevix-Trench G, Pereira-Smith OM, Antoniou AC, Ceron J, Tominaga K, Surralles J, Pujana MA

Proteins encoded by Fanconi anemia (FA) and/or breast cancer (BrCa) susceptibility genes cooperate in a common DNA damage repair signaling pathway. To gain deeper insight into this pathway and its influence on cancer risk, we searched for novel components through protein physical interaction screens.Protein physical interactions were screened using the yeast two-hybrid system. Co-affinity purifications and endogenous co-immunoprecipitation assays were ... [more]

Breast Cancer Res. Apr. 05, 2011; 13(2);R40 [Pubmed: 21466675]

Throughput

High Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
BLM MLH1	Affinity Capture-MS Affinity Capture-MS An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.	Meetei AR (2003)	Low	-	BioGRID	-
BLM MLH1	Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Langland G (2001)	Low	-	BioGRID	244027
BLM MLH1	Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Meetei AR (2003)	Low	-	BioGRID	-
MLH1 BLM	Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Pedrazzi G (2001)	Low	-	BioGRID	-
MLH1 BLM	Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex.	Havugimana PC (2022)	High	-	BioGRID	3443350
MLH1 BLM	Co-purification Co-purification An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.	Wang Y (2000)	Low	-	BioGRID	243974
BLM MLH1	Far Western Far Western An interaction is detected between a protein immobilized on a membrane and a purified protein probe.	Freire R (2001)	Low	-	BioGRID	-
BLM MLH1	Far Western Far Western An interaction is detected between a protein immobilized on a membrane and a purified protein probe.	Langland G (2001)	Low	-	BioGRID	244026
BLM MLH1	Far Western Far Western An interaction is detected between a protein immobilized on a membrane and a purified protein probe.	Pedrazzi G (2001)	Low	-	BioGRID	-
MLH1 BLM	Protein-peptide Protein-peptide An interaction is detected between a protein and a peptide derived from an interaction partner. This includes phage display experiments.	Dherin C (2009)	Low	-	BioGRID	-
BLM MLH1	Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.	Langland G (2001)	Low	-	BioGRID	244024
MLH1 BLM	Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.	Dherin C (2009)	Low	-	BioGRID	-
BLM MLH1	Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.	Langland G (2001)	Low	-	BioGRID	244025
BLM MLH1	Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.	Pedrazzi G (2001)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

BLM

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

MLH1