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Protein

BRCA1-A complex subunit Abraxas

Gene

FAM175A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in DNA damage response and double-strand break (DSB) repair. Component of the BRCA1-A complex, acting as a central scaffold protein that assembles the various components of the complex and mediates the recruitment of BRCA1. The BRCA1-A complex specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesion sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at DSBs. This complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX.7 Publications

GO - Molecular functioni

  • polyubiquitin binding Source: UniProtKB

GO - Biological processi

  • chromatin modification Source: UniProtKB-KW
  • DNA repair Source: Reactome
  • double-strand break repair Source: UniProtKB
  • double-strand break repair via homologous recombination Source: Reactome
  • double-strand break repair via nonhomologous end joining Source: Reactome
  • G2 DNA damage checkpoint Source: UniProtKB
  • positive regulation of DNA repair Source: UniProtKB
  • response to ionizing radiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiR-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-69473. G2/M DNA damage checkpoint.

Names & Taxonomyi

Protein namesi
Recommended name:
BRCA1-A complex subunit Abraxas
Alternative name(s):
Coiled-coil domain-containing protein 98
Protein FAM175A
Gene namesi
Name:FAM175A
Synonyms:ABRA1, CCDC98
ORF Names:UNQ496/PRO1013
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:25829. FAM175A.

Subcellular locationi

GO - Cellular componenti

  • BRCA1-A complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Breast cancer (BC)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.
See also OMIM:114480
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti361 – 3611R → Q in BC; results in reduced DSB repair efficiency; primarily localizes to the cytoplasm and has reduced nuclear localization; does not affect interaction with BRCA1; results in highly reduced interaction with UIMC1/RAP80. 2 Publications
Corresponds to variant rs201627097 [ dbSNP | Ensembl ].
VAR_071865

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi400 – 4001F → D: No effect on formation of a heterotetramer with BRCA1. 1 Publication
Mutagenesisi402 – 4021E → R: Decreases formation of a heterotetramer with BRCA1. 1 Publication
Mutagenesisi403 – 4031Y → A: No effect on formation of a heterotetramer with BRCA1. 1 Publication
Mutagenesisi404 – 4041S → A: No effect on homodimerization. Mildly decreased recruitment of BRCA1 to sites of DNA damage. 1 Publication
Mutagenesisi404 – 4041S → D: Permits formation of a heterotetramer with BRCA1. 1 Publication
Mutagenesisi404 – 4041S → P: Abolishes formation of a heterotetramer with BRCA1. Does not affect interaction with a first BRCA1 chain. 1 Publication
Mutagenesisi406 – 4061S → A: Abolishes phosphorylation of the pSXXF motif and the interaction with BRCA1 but does not affect the interaction with UIMC1/RAP80. Strongly decreases recruitment of BRCA1 to sites of DNA damage. No effect on homodimerization. 4 Publications

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiFAM175A.
MIMi114480. phenotype.
PharmGKBiPA162387308.

Polymorphism and mutation databases

BioMutaiFAM175A.
DMDMi126215684.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409BRCA1-A complex subunit AbraxasPRO_0000278575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphoserineBy similarity
Modified residuei386 – 3861PhosphoserineCombined sources
Modified residuei387 – 3871PhosphoserineCombined sources
Modified residuei390 – 3901PhosphothreonineCombined sources
Modified residuei404 – 4041Phosphoserine1 Publication
Modified residuei406 – 4061PhosphoserineCombined sources4 Publications

Post-translational modificationi

Phosphorylation of Ser-406 of the pSXXF motif by ATM or ATR constitutes a specific recognition motif for the BRCT domain of BRCA1 (PubMed:17643121, PubMed:17525340, PubMed:17643122). Ionizing radiation promotes rapid phosphorylation at Ser-404 and Ser-406 by ATM; this promotes recruitment of BRCA1 to sites of DNA damage (PubMed:26778126).4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6UWZ7.
MaxQBiQ6UWZ7.
PaxDbiQ6UWZ7.
PRIDEiQ6UWZ7.

PTM databases

iPTMnetiQ6UWZ7.
PhosphoSiteiQ6UWZ7.

Expressioni

Gene expression databases

BgeeiQ6UWZ7.
CleanExiHS_FAM175A.
ExpressionAtlasiQ6UWZ7. baseline and differential.
GenevisibleiQ6UWZ7. HS.

Organism-specific databases

HPAiHPA037653.
HPA037654.

Interactioni

Subunit structurei

Component of the ARISC complex, at least composed of UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1 (PubMed:24075985). Component of the BRCA1-A complex, at least composed of BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1. In the complex, interacts directly with UIMC1/RAP80, BRCC3/BRCC36 and BRE/BRCC45. Interacts directly (when phosphorylated at Ser-406) with BRCA1. Homodimer. The homodimer interacts directly (when phosphorylated at Ser-404 and Ser-406) with two BRCA1 chains, giving rise to a heterotetramer. Binds polyubiquitin.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRCA1P3839810EBI-1263451,EBI-349905
UIMC1Q96RL19EBI-1263451,EBI-725300

GO - Molecular functioni

  • polyubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi123911. 19 interactions.
DIPiDIP-29615N.
IntActiQ6UWZ7. 8 interactions.
STRINGi9606.ENSP00000369857.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JLUX-ray3.50B399-409[»]
4U4AX-ray3.51D/E/F399-409[»]
4Y18X-ray3.50I/J/K/L/M/N/O/P399-409[»]
4Y2GX-ray2.50B403-409[»]
ProteinModelPortaliQ6UWZ7.
SMRiQ6UWZ7. Positions 10-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni11 – 121111MPN-likeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili206 – 26055Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi406 – 4094pSXXF motifCurated

Domaini

The MPN-like region is similar to the MPN (JAB/Mov34) domain. Its presence reveals similarities between the structure of the 19S proteasome and the BRCA1-A complexes.1 Publication

Sequence similaritiesi

Belongs to the FAM175 family. Abraxas subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG59. Eukaryota.
ENOG4110D5E. LUCA.
GeneTreeiENSGT00530000063424.
HOGENOMiHOG000112448.
HOVERGENiHBG095943.
InParanoidiQ6UWZ7.
OrthoDBiEOG7J9VPJ.
PhylomeDBiQ6UWZ7.
TreeFamiTF331751.

Family and domain databases

InterProiIPR023238. FAM175.
IPR023239. FAM175_BRCA1-A_cplx_Abraxas_su.
[Graphical view]
PRINTSiPR02052. ABRAXAS.
PR02051. PROTEINF175.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6UWZ7-1) [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
MEGESTSAVL SGFVLGALAF QHLNTDSDTE GFLLGEVKGE AKNSITDSQM
60 70 80 90 100
DDVEVVYTID IQKYIPCYQL FSFYNSSGEV NEQALKKILS NVKKNVVGWY
110 120 130 140 150
KFRRHSDQIM TFRERLLHKN LQEHFSNQDL VFLLLTPSII TESCSTHRLE
160 170 180 190 200
HSLYKPQKGL FHRVPLVVAN LGMSEQLGYK TVSGSCMSTG FSRAVQTHSS
210 220 230 240 250
KFFEEDGSLK EVHKINEMYA SLQEELKSIC KKVEDSEQAV DKLVKDVNRL
260 270 280 290 300
KREIEKRRGA QIQAAREKNI QKDPQENIFL CQALRTFFPN SEFLHSCVMS
310 320 330 340 350
LKNRHVSKSS CNYNHHLDVV DNLTLMVEHT DIPEASPAST PQIIKHKALD
360 370 380 390 400
LDDRWQFKRS RLLDTQDKRS KADTGSSNQD KASKMSSPET DEEIEKMKGF

GEYSRSPTF
Length:409
Mass (Da):46,663
Last modified:February 20, 2007 - v2
Checksum:iA1ACA4F759BD1AEE
GO
Isoform 2 (identifier: Q6UWZ7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-109: Missing.

Show »
Length:300
Mass (Da):34,447
Checksum:iA22EF29B4B0FCAFF
GO

Sequence cautioni

The sequence AAH39573.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti239 – 2391A → T.
Corresponds to variant rs12642536 [ dbSNP | Ensembl ].
VAR_030790
Natural varianti348 – 3481A → T Common polymorphism not associated with susceptibility to breast cancer. 3 Publications
Corresponds to variant rs12642536 [ dbSNP | Ensembl ].
VAR_054054
Natural varianti361 – 3611R → Q in BC; results in reduced DSB repair efficiency; primarily localizes to the cytoplasm and has reduced nuclear localization; does not affect interaction with BRCA1; results in highly reduced interaction with UIMC1/RAP80. 2 Publications
Corresponds to variant rs201627097 [ dbSNP | Ensembl ].
VAR_071865
Natural varianti373 – 3731D → N Common polymorphism not associated with susceptibility to breast cancer. 3 Publications
Corresponds to variant rs13125836 [ dbSNP | Ensembl ].
VAR_054055

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 109109Missing in isoform 2. VSP_058196Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358576 mRNA. Translation: AAQ88939.1.
EF531340 mRNA. Translation: ABP87396.1.
CH471057 Genomic DNA. Translation: EAX05942.1.
BC039573 mRNA. Translation: AAH39573.1. Different initiation.
AK022704 mRNA. Translation: BAB14189.1.
AK023676 mRNA. Translation: BAB14635.1.
CCDSiCCDS3605.2. [Q6UWZ7-1]
RefSeqiNP_620775.2. NM_139076.2.
UniGeneiHs.334772.

Genome annotation databases

EnsembliENST00000321945; ENSP00000369857; ENSG00000163322. [Q6UWZ7-1]
GeneIDi84142.
KEGGihsa:84142.
UCSCiuc003hou.3. human. [Q6UWZ7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY358576 mRNA. Translation: AAQ88939.1.
EF531340 mRNA. Translation: ABP87396.1.
CH471057 Genomic DNA. Translation: EAX05942.1.
BC039573 mRNA. Translation: AAH39573.1. Different initiation.
AK022704 mRNA. Translation: BAB14189.1.
AK023676 mRNA. Translation: BAB14635.1.
CCDSiCCDS3605.2. [Q6UWZ7-1]
RefSeqiNP_620775.2. NM_139076.2.
UniGeneiHs.334772.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JLUX-ray3.50B399-409[»]
4U4AX-ray3.51D/E/F399-409[»]
4Y18X-ray3.50I/J/K/L/M/N/O/P399-409[»]
4Y2GX-ray2.50B403-409[»]
ProteinModelPortaliQ6UWZ7.
SMRiQ6UWZ7. Positions 10-261.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123911. 19 interactions.
DIPiDIP-29615N.
IntActiQ6UWZ7. 8 interactions.
STRINGi9606.ENSP00000369857.

PTM databases

iPTMnetiQ6UWZ7.
PhosphoSiteiQ6UWZ7.

Polymorphism and mutation databases

BioMutaiFAM175A.
DMDMi126215684.

Proteomic databases

EPDiQ6UWZ7.
MaxQBiQ6UWZ7.
PaxDbiQ6UWZ7.
PRIDEiQ6UWZ7.

Protocols and materials databases

DNASUi84142.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000321945; ENSP00000369857; ENSG00000163322. [Q6UWZ7-1]
GeneIDi84142.
KEGGihsa:84142.
UCSCiuc003hou.3. human. [Q6UWZ7-1]

Organism-specific databases

CTDi84142.
GeneCardsiFAM175A.
HGNCiHGNC:25829. FAM175A.
HPAiHPA037653.
HPA037654.
MalaCardsiFAM175A.
MIMi114480. phenotype.
611143. gene.
neXtProtiNX_Q6UWZ7.
PharmGKBiPA162387308.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IG59. Eukaryota.
ENOG4110D5E. LUCA.
GeneTreeiENSGT00530000063424.
HOGENOMiHOG000112448.
HOVERGENiHBG095943.
InParanoidiQ6UWZ7.
OrthoDBiEOG7J9VPJ.
PhylomeDBiQ6UWZ7.
TreeFamiTF331751.

Enzyme and pathway databases

ReactomeiR-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693571. Nonhomologous End-Joining (NHEJ).
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-69473. G2/M DNA damage checkpoint.

Miscellaneous databases

GenomeRNAii84142.
NextBioi73456.
PROiQ6UWZ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ6UWZ7.
CleanExiHS_FAM175A.
ExpressionAtlasiQ6UWZ7. baseline and differential.
GenevisibleiQ6UWZ7. HS.

Family and domain databases

InterProiIPR023238. FAM175.
IPR023239. FAM175_BRCA1-A_cplx_Abraxas_su.
[Graphical view]
PRINTSiPR02052. ABRAXAS.
PR02051. PROTEINF175.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Abraxas and RAP80 form a BRCA1 protein complex required for the DNA damage response."
    Wang B., Matsuoka S., Ballif B.A., Zhang D., Smogorzewska A., Giyi S., Elledge S.J.
    Science 316:1194-1198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1 AND UIMC1, PHOSPHORYLATION AT SER-406, MUTAGENESIS OF SER-406.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-373.
  3. 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 1).
    Tissue: Testis.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT THR-348.
    Tissue: Placenta.
  6. "CCDC98 targets BRCA1 to DNA damage sites."
    Liu Z., Wu J., Yu X.
    Nat. Struct. Mol. Biol. 14:716-720(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1 AND UIMC1, PHOSPHORYLATION AT SER-406, MUTAGENESIS OF SER-406.
  7. "CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage response."
    Kim H., Huang J., Chen J.
    Nat. Struct. Mol. Biol. 14:710-715(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1 AND UIMC1, PHOSPHORYLATION AT SER-406, MUTAGENESIS OF SER-406.
  8. "Ubc13/Rnf8 ubiquitin ligases control foci formation of the Rap80/Abraxas/Brca1/Brcc36 complex in response to DNA damage."
    Wang B., Elledge S.J.
    Proc. Natl. Acad. Sci. U.S.A. 104:20759-20763(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-387; THR-390 AND SER-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "MERIT40 controls BRCA1-Rap80 complex integrity and recruitment to DNA double-strand breaks."
    Shao G., Patterson-Fortin J., Messick T.E., Feng D., Shanbhag N., Wang Y., Greenberg R.A.
    Genes Dev. 23:740-754(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX.
  12. "NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control."
    Wang B., Hurov K., Hofmann K., Elledge S.J.
    Genes Dev. 23:729-739(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BRCA1-A COMPLEX, DOMAIN MPN-LIKE, INTERACTION WITH UIMC1; BRCC3; BRE; BABAM1 AND BRCA1, UBIQUITIN-BINDING.
  13. "MERIT40 facilitates BRCA1 localization and DNA damage repair."
    Feng L., Huang J., Chen J.
    Genes Dev. 23:719-728(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE BRCA1-A COMPLEX, INTERACTION WITH UIMC1; BRCC3; BRE AND BRCA1.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-390 AND SER-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-387; THR-390 AND SER-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-387 AND THR-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: IDENTIFICATION IN THE ARISC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  18. "Preliminary crystallographic studies of BRCA1 BRCT-ABRAXAS complex."
    Badgujar D.C., Sawant U., Vikrant X., Yadav L., Hosur M.V., Varma A.K.
    Acta Crystallogr. F 69:1401-1404(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 399-409 IN COMPLEX WITH BRCA1, INTERACTION WITH BRCA1.
  19. "Structure of BRCA1-BRCT/Abraxas complex reveals phosphorylation-dependent BRCT dimerization at DNA damage sites."
    Wu Q., Paul A., Su D., Mehmood S., Foo T.K., Ochi T., Bunting E.L., Xia B., Robinson C.V., Wang B., Blundell T.L.
    Mol. Cell 0:0-0(2016) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 403-409 IN COMPLEX WITH BRCA1, INTERACTION WITH BRCA1, SUBUNIT, FUNCTION, PHOSPHORYLATION AT SER-404 AND SER-406, MUTAGENESIS OF PHE-400; GLU-402; TYR-403; SER-404 AND SER-406.
  20. "Analysis of the genes coding for the BRCA1-interacting proteins, RAP80 and Abraxas (CCDC98), in high-risk, non-BRCA1/2, multiethnic breast cancer cases."
    Novak D.J., Sabbaghian N., Maillet P., Chappuis P.O., Foulkes W.D., Tischkowitz M.
    Breast Cancer Res. Treat. 117:453-459(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-348 AND ASN-373.
  21. Cited for: FUNCTION, VARIANTS THR-348 AND ASN-373, VARIANT BC GLN-361, CHARACTERIZATION OF VARIANT BC GLN-361.
  22. "Mislocalization of BRCA1-complex due to ABRAXAS Arg361Gln mutation."
    Kumar R.V., Siddiqui Q., Singh N., Waghmare S.K., Varma A.K.
    J. Biomol. Struct. Dyn. 33:1291-1301(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT BC GLN-361.

Entry informationi

Entry nameiF175A_HUMAN
AccessioniPrimary (citable) accession number: Q6UWZ7
Secondary accession number(s): A5JJ07, Q9H8I1, Q9H9N4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: February 20, 2007
Last modified: May 11, 2016
This is version 101 of the entry and version 2 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 4
    Human chromosome 4: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.