BioPAX pathway converted from "FA core complex assembles at DNA interstrand crosslinks (ICLs)" in the Reactome database.FA core complex assembles at DNA interstrand crosslinks (ICLs)

FA core complex assembles at DNA interstrand crosslinks (ICLs)

In addition to FANCM, FAAP24, APITD1 (MHF1) and STRA13 (MHF2), the FA core complex also includes FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FAAP20 and FAAP100 (Singh et al. 2010, Yan et al. 2010, Leung et al. 2012). While FANCA, FANCB, FANCC, FANCE, FANCF, FANCG and FANCL, and probably FAAP20 and FAAP100, can assemble a complex in the nucleoplasm, they are unable to load onto DNA in the absence of FANCM and FAAP24 (Kim et al. 2008, Yan et al. 2010, Leung et al. 2012).

Authored: Orlic-Milacic, Marija, 2015-06-29Reviewed: Fugger, Kasper, 2015-08-20Edited: Orlic-Milacic, Marija, 2015-06-29

Reactome DB_ID: 419545

nucleoplasmGO0005654

UniProt:Q0VG06 FAAP100

FAAP100

FAAP100C17orf70FUNCTION Plays a role in Fanconi anemia-associated DNA damage response network. Regulates FANCD2 monoubiquitination and the stability of the FA core complex. Induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed.SUBUNIT Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9, FANCM, FAAP24 and FAAP100. Forms a subcomplex with FANCB and FANCL.

Reactomehttp://www.reactome.orgHomo sapiens

NCBI Taxonomy9606UniProtQ0VG06

Chain Coordinates

EQUAL

881

EQUAL

Reactome DB_ID: 419520

UniProt:Q9NW38 FANCL

FANCL

FANCLPHF9FUNCTION Ubiquitin ligase protein that mediates monoubiquitination of FANCD2 in the presence of UBE2T, a key step in the DNA damage pathway (PubMed:12973351, PubMed:16916645, PubMed:17938197, PubMed:19111657, PubMed:24389026). Also mediates monoubiquitination of FANCI (PubMed:19589784). May stimulate the ubiquitin release from UBE2W. May be required for proper primordial germ cell proliferation in the embryonic stage, whereas it is probably not needed for spermatogonial proliferation after birth.PATHWAY Protein modification; protein ubiquitination.SUBUNIT Interacts with GGN (By similarity). Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM (PubMed:12973351, PubMed:15502827, PubMed:16116422, PubMed:22343915). The complex is not found in FA patients. In complex with FANCF, FANCA and FANCG, but not with FANCC, nor FANCE, interacts with HES1; this interaction may be essential for the stability and nuclear localization of FA core complex proteins (PubMed:18550849). Interacts with FANCI (PubMed:21775430). Directly interacts (via the RING-type zinc finger) with UBE2T and UBE2W (PubMed:16916645, PubMed:17938197, PubMed:19111657, PubMed:21775430, PubMed:24389026).DOMAIN The UBC-RWD region (URD) region mediates interaction with FANCI and FANCD2.PTM The RING-type zinc finger domain is monoubiquitinated in the presence of UBE2T and UBE2W.CAUTION Although PubMed:12724401 reports that it contains a PHD-type zinc finger, it contains a RING-type zinc finger. Moreover, PHD-type zinc fingers do not have any ubiquitin ligase activity.

UniProtQ9NW38

EQUAL

375

EQUAL

Reactome DB_ID: 419543

UniProt:Q9HB96 FANCE

FANCE

FANCEFACEFUNCTION As part of the Fanconi anemia (FA) complex functions in DNA cross-links repair. Required for the nuclear accumulation of FANCC and provides a critical bridge between the FA complex and FANCD2.SUBUNIT Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. The complex is not found in FA patients. Interacts with FANCC and FANCD2.PTM Phosphorylated. Phosphorylation by CHEK1 at Thr-346 and Ser-374 regulates its function in DNA cross-links repair.PTM Ubiquitinated. Phosphorylation by CHEK1 induces polyubiquitination and degradation.

UniProtQ9HB96

EQUAL

536

EQUAL

Reactome DB_ID: 419530

UniProt:Q00597 FANCC

FANCC

FACFANCCFACCFUNCTION DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Upon IFNG induction, may facilitate STAT1 activation by recruiting STAT1 to IFNGR1.SUBUNIT Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. This complex may also include HSP70. The complex is not found in FA patients. Interacts with ZBTB32. Upon IFNG induction, interacts with STAT1. Interacts with CDK1. Interacts with EIF2AK2; interaction between FA variants and EIF2AK2 may lead to augmented EIF2AK2 activation and cell death.TISSUE SPECIFICITY Ubiquitous.DEVELOPMENTAL STAGE Expression increases during S phase, is maximal at the G2/M transition, and declines during M phase (at protein level).

UniProtQ00597

EQUAL

558

EQUAL

Reactome DB_ID: 6785090

FANCM:FAAP24:APITD1:STRA13:ICL-DNA [nucleoplasm]

FANCM:FAAP24:APITD1:STRA13:ICL-DNA

Reactome DB_ID: 6785088

FANCM:FAAP24 [nucleoplasm]

FANCM:FAAP24

Reactome DB_ID: 419533

UniProt:Q9BTP7 FAAP24

FAAP24

C19orf40FAAP24FUNCTION Plays a role in DNA repair through recruitment of the FA core complex to damaged DNA. Regulates FANCD2 monoubiquitination upon DNA damage. Induces chromosomal instability as well as hypersensitivity to DNA cross-linking agents, when repressed. Targets FANCM/FAAP24 complex to the DNA, preferentially to single strand DNA.SUBUNIT Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9, FANCM and FAAP24. Interacts with FANCM.DOMAIN The C-terminal region is distantly related to RuvA domain 2, a DNA-binding domain.

UniProtQ9BTP7

EQUAL

215

EQUAL

Reactome DB_ID: 419535

UniProt:Q8IYD8 FANCM

FANCM

FANCMKIAA1596FUNCTION DNA-dependent ATPase component of the Fanconi anemia (FA) core complex (PubMed:16116422). Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:16116422, PubMed:19423727, PubMed:20347428, PubMed:20347429, PubMed:29231814). In complex with CENPS and CENPX, binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA) and Holliday junction substrates (PubMed:20347428, PubMed:20347429). Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX (PubMed:20347429). In complex with FAAP24, efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates (PubMed:17289582). In vitro, on its own, strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA (PubMed:16116434).SUBUNIT Component of the Fanconi anemia (FA) core complex, which consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FAAP24 and FAAP100 (PubMed:16116422, PubMed:16116434, PubMed:17289582). The FA core complex associates with Bloom syndrome (BLM) complex, which consists of at least BLM, DNA topoisomerase 3-alpha/TOP3A, RMI1/BLAP75, RPA1/RPA70 and RPA2/RPA32. This supercomplex between FA and BLM complexes has been called BRAFT (PubMed:20347428). Forms a discrete complex with CENPS and CENPX, called FANCM-MHF; this interaction stimulates DNA binding and replication fork remodeling by FANCM and stabilizes the binding partners (PubMed:20347428, PubMed:20347429). Forms a heterodimer with FAAP24; this interaction increases FANCM single-stranded DNA-binding activity (PubMed:17289582, PubMed:20347428).TISSUE SPECIFICITY Expressed in germ cells of fetal and adult ovaries. In fetal ovaries, it is present in oogonia but expression is stronger in pachytene stage oocytes. Expressed in oocytes arrested at the diplotene stage of prophase I during the last trimester of pregnancy and in adults (PubMed:29231814). Expressed in the testis (PubMed:30075111).DEVELOPMENTAL STAGE Expressed throughout ovarian development (5-32 weeks post-fertilization (wpf)). Expression tends to be higher at 14 and 17 wpf.PTM Phosphorylated; hyperphosphorylated in response to genotoxic stress.SIMILARITY Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily.

UniProtQ8IYD8

EQUAL

2048

EQUAL

Reactome Database ID Release 756785088Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=6785088ReactomeR-HSA-6785088

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-6785088.1

Reactome DB_ID: 6785117

ICL-DNA [nucleoplasm]

ICL-DNA

DNA with interstrand crosslink

Reactome DB_ID: 6785093

APITD1:STRA13 octamer [nucleoplasm]

APITD1:STRA13 octamer

MHF octamerMHF1:MHF2 octamer

Reactome DB_ID: 6785091

APITD1:STRA13 [nucleoplasm]

APITD1:STRA13

MHFMHF1:MHF2

Reactome DB_ID: 5633510

UniProt:Q8N2Z9 CENPS

CENPS

MHF1APITD1FAAP16CENPSFUNCTION DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:20347428, PubMed:20347429). In complex with CENPX (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM (PubMed:20347428, PubMed:20347429). In complex with CENPX and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks (PubMed:20347428). In complex with CENPT, CENPW and CENPX (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression (PubMed:19620631). As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure (PubMed:20347428, PubMed:22304917). DNA-binding function is fulfilled in the presence of CENPX, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own (PubMed:20347428, PubMed:20347429).SUBUNIT Heterodimer with CENPX, sometimes called MHF; this interaction stabilizes both partners (PubMed:19620631, PubMed:20347428, PubMed:20347429, PubMed:24522885). MHF heterodimers can assemble to form tetrameric structures (PubMed:22304917). MHF also coassemble with CENPT-CENPW heterodimers at centromeres to form the tetrameric CENP-T-W-S-X complex (PubMed:22304917, PubMed:24522885). Forms a discrete complex with FANCM and CENPX, called FANCM-MHF; this interaction, probably mediated by direct binding between CENPS and FANCM, leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling (PubMed:20347428, PubMed:20347429). Recruited by FANCM to the Fanconi anemia (FA) core complex, which consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FAAP24 and FAAP100. The FA core complex associates with Bloom syndrome (BLM) complex, which consists of at least BLM, DNA topoisomerase 3-alpha (TOP3A), RMI1/BLAP75, RPA1/RPA70 and RPA2/RPA32. The super complex between FA and BLM is called BRAFT (PubMed:20347428, PubMed:20347429). Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex, composed of at least CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU (PubMed:16622419).TISSUE SPECIFICITY Ubiquitously expressed.DEVELOPMENTAL STAGE Expression varies across the cell cycle, with highest levels in G2 phase (at protein level). No statistically significant changes at the transcript level.SIMILARITY Belongs to the TAF9 family. CENP-S/MHF1 subfamily.

UniProtQ8N2Z9

EQUAL

138

EQUAL

Reactome DB_ID: 5633522

UniProt:A8MT69 CENPX

CENPX

MHF2CENPXSTRA13FAAP10FUNCTION DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:20347428, PubMed:20347429). In complex with CENPS (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPS and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks (PubMed:20347428, PubMed:20347429). In complex with CENPS, CENPT and CENPW (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression (PubMed:19620631). As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure (PubMed:20347428, PubMed:20347429). DNA-binding function is fulfilled in the presence of CENPS, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own (PubMed:20347429).SUBUNIT Heterodimer with CENPX, sometimes called MHF; this interaction stabilizes both partners (PubMed:19620631, PubMed:20347428, PubMed:20347429, PubMed:24522885). MHF heterodimers can assemble to form tetrameric structures (PubMed:22304917). MHF also coassemble with CENPT-CENPW heterodimers at centromeres to form the tetrameric CENP-T-W-S-X complex (PubMed:22304917, PubMed:24522885). Forms a discrete complex with FANCM and CENPX, called FANCM-MHF; this interaction, probably mediated by direct binding between CENPS and FANCM, leads to synergistic activation of double-stranded DNA binding and strongly stimulates FANCM-mediated DNA remodeling (PubMed:20347428, PubMed:20347429). Recruited by FANCM to the Fanconi anemia (FA) core complex, which consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL, FANCM, FAAP24 and FAAP100. The FA core complex associates with Bloom syndrome (BLM) complex, which consists of at least BLM, DNA topoisomerase 3-alpha (TOP3A), RMI1/BLAP75, RPA1/RPA70 and RPA2/RPA32. The super complex between FA and BLM is called BRAFT (PubMed:20347428, PubMed:20347429).DEVELOPMENTAL STAGE Expression varies across the cell cycle, with highest levels in S phase (at protein level). No statistically significant changes at the transcript level.SIMILARITY Belongs to the CENP-X/MHF2 family.

UniProtA8MT69

EQUAL

Reactome Database ID Release 756785091Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=6785091ReactomeR-HSA-6785091

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-6785091.1Reactome Database ID Release 756785093Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=6785093ReactomeR-HSA-6785093

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-6785093.1Reactome Database ID Release 756785090Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=6785090ReactomeR-HSA-6785090

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-6785090.1

Reactome DB_ID: 6783321

UniProt:Q6NZ36 FAAP20

FAAP20

C1orf86FP7162FAAP20FUNCTION Component of the Fanconi anemia (FA) complex required to recruit the FA complex to DNA interstrand cross-links (ICLs) and promote ICLs repair. Following DNA damage recognizes and binds 'Lys-63'-linked ubiquitin generated by RNF8 at ICLs and recruits other components of the FA complex. Promotes translesion synthesis via interaction with REV1.SUBUNIT Component of the Fanconi anemia (FA) complex. Interacts with FANCA; interaction is direct. Interacts with REV1. Reported to bind monoubiquitinated REV1; however it binds better to non-ubiquitinated REV1 (PubMed:22266823).DOMAIN The UBZ2-type zinc finger binds both 'Lys-48'- and 'Lys-63'-linked polyubiquitin with preference for 'Lys-63'-linked polyubiquitin.CAUTION According to a report, ubiquitin-binding is dispensable for function (PubMed:22396592). However, such data are not confirmed by PubMed:22705371.

UniProtQ6NZ36

EQUAL

180

EQUAL

Reactome DB_ID: 419541

UniProt:O15360 FANCA

FANCA

FANCHFAAFANCAFACAFUNCTION DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be involved in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability.SUBUNIT Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. The complex is not found in FA patients. In complex with FANCF, FANCG and FANCL, but not with FANCC, nor FANCE, interacts with HES1; this interaction may be essential for the stability and nuclear localization of FA core complex proteins. The complex with FANCC and FANCG may also include EIF2AK2 and HSP70. Interacts with FAAP20/C1orf86; interaction is direct.PTM Phosphorylation is required for the formation of the nuclear complex. Not phosphorylated in cells derived from groups A, B, C, E, F, G, and H.

UniProtO15360

EQUAL

1455

EQUAL

Reactome DB_ID: 419528

UniProt:Q8NB91 FANCB

FANCB

FANCBFUNCTION DNA repair protein required for FANCD2 ubiquitination.SUBUNIT Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. The complex is not found in FA patients.

UniProtQ8NB91

EQUAL

859

EQUAL

Reactome DB_ID: 419537

UniProt:Q9NPI8 FANCF

FANCF

FANCFFUNCTION DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability (By similarity).SUBUNIT Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. The complex is not found in FA patients. In complex with FANCA, FANCG and FANCL, but not with FANCC, nor FANCE, interacts with HES1; this interaction may be essential for the stability and nuclear localization of FA core complex proteins.

UniProtQ9NPI8

EQUAL

374

EQUAL

Reactome DB_ID: 419532

UniProt:O15287 FANCG

FANCG

XRCC9FANCGFUNCTION DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability. Candidate tumor suppressor gene.SUBUNIT Belongs to the multisubunit FA complex composed of FANCA, FANCB, FANCC, FANCE, FANCF, FANCG, FANCL/PHF9 and FANCM. The complex is not found in FA patients. In complex with FANCF, FANCA and FANCL, but not with FANCC, nor FANCE, interacts with HES1; this interaction may be essential for the stability and nuclear localization of FA core complex proteins. The complex with FANCC and FANCG may also include EIF2AK2 and HSP70. When phosphorylated at Ser-7, forms a complex with BRCA2, FANCD2 and XRCC3.TISSUE SPECIFICITY Highly expressed in testis and thymus. Found in lymphoblasts.

UniProtO15287

EQUAL

622

EQUAL

Reactome DB_ID: 6785124

FA Core Complex:ICL-DNA [nucleoplasm]

FA Core Complex:ICL-DNA

Reactome DB_ID: 6785123

FA Core Complex [nucleoplasm]

FA Core Complex

Reactome DB_ID: 419545

EQUAL

881

EQUAL

Reactome DB_ID: 419520

EQUAL

375

EQUAL

Reactome DB_ID: 6785088

Reactome DB_ID: 419543

EQUAL

536

EQUAL

Reactome DB_ID: 419530

EQUAL

558

EQUAL

Reactome DB_ID: 6783321

EQUAL

180

EQUAL

Reactome DB_ID: 419541

EQUAL

1455

EQUAL

Reactome DB_ID: 419528

EQUAL

859

EQUAL

Reactome DB_ID: 419537

EQUAL

374

EQUAL

Reactome DB_ID: 419532

EQUAL

622

EQUAL

Reactome DB_ID: 6785093

Reactome Database ID Release 756785123Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=6785123ReactomeR-HSA-6785123

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-6785123.1

Reactome DB_ID: 6785117

Reactome Database ID Release 756785124Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=6785124ReactomeR-HSA-6785124

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-6785124.1Reactome Database ID Release 756785126Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=6785126ReactomeR-HSA-6785126

Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-HSA-6785126.218174376Pubmed2008Cell cycle-dependent chromatin loading of the Fanconi anemia core complex by FANCM/FAAP24Kim, Jung MinKee, YounghoonGurtan, AllanD'Andrea, Alan DBlood 111:5215-2222396592Pubmed2012Fanconi anemia (FA) binding protein FAAP20 stabilizes FA complementation group A (FANCA) and participates in interstrand cross-link repairLeung, Justin Wai ChungWang, YucaiFong, Ka WingHuen, Michael Shing YanLi, LeiChen, JProc. Natl. Acad. Sci. U.S.A. 109:4491-620347429Pubmed2010MHF1-MHF2, a histone-fold-containing protein complex, participates in the Fanconi anemia pathway via FANCMSingh, Thiyam RamsingSaro, DorinaAli, Abdullah MahmoodZheng, Xiao-FengDu, Chang-huKillen, Michael WSachpatzidis, AristidisWahengbam, KebolaPierce, Andrew JXiong, YongSung, PMeetei, Amom RuhikantaMol. Cell 37:879-8620347428Pubmed2010A histone-fold complex and FANCM form a conserved DNA-remodeling complex to maintain genome stabilityYan, ZhijiangDelannoy, MathieuLing, CDaee, DanielleOsman, FekretMuniandy, Parameswary AShen, XiOostra, Anneke BDu, HansenSteltenpool, JurgenLin, TiSchuster, BeatriceDécaillet, ChantalStasiak, AndrzejStasiak, Alicja ZStone, StacieHoatlin, Maureen ESchindler, DetlevWoodcock, CLJoenje, HansSen, Ranjande Winter, Johan PLi, LeiSeidman, Michael MWhitby, Matthew CMyung, KyungjaeConstantinou, AngelosWang, WeidongMol. Cell 37:865-78