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Protein

BRCA1-A complex subunit Abraxas

Gene

Fam175a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiR-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-MMU-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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1917931. Fam175a.

Subcellular locationi

  • Nucleus By similarity

  • Note: Localizes at sites of DNA damage at double-strand breaks (DSBs).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407BRCA1-A complex subunit AbraxasPRO_0000278576Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481PhosphoserineCombined sources
Modified residuei384 – 3841PhosphoserineBy similarity
Modified residuei385 – 3851PhosphoserineBy similarity
Modified residuei394 – 3941PhosphoserineCombined sources
Modified residuei404 – 4041PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation of Ser-404 of the pSXXF motif by ATM or ATR constitutes a specific recognition motif for the BRCT domain of BRCA1.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BPZ8.
MaxQBiQ8BPZ8.
PaxDbiQ8BPZ8.
PRIDEiQ8BPZ8.

PTM databases

PhosphoSiteiQ8BPZ8.

Expressioni

Gene expression databases

BgeeiQ8BPZ8.
ExpressionAtlasiQ8BPZ8. baseline and differential.
GenevisibleiQ8BPZ8. MM.

Interactioni

Subunit structurei

Component of the ARISC complex, at least composed of UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1. Component of the BRCA1-A complex, at least composed of the 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. Homodimer. Interacts directly (when phosphorylated at Ser-404) with BRCA1. The phosphorylated homodimer can interact directly with two BRCA1 chains, giving rise to a heterotetramer. Binds polyubiquitin.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000055895.

Structurei

3D structure databases

ProteinModelPortaliQ8BPZ8.
SMRiQ8BPZ8. Positions 7-258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili209 – 25951Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi404 – 4074pSXXF motifCurated

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi382 – 3854Poly-Ser

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.By similarity

Sequence similaritiesi

Belongs to the FAM175 family. Abraxas subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG59. Eukaryota.
ENOG4110D5E. LUCA.
GeneTreeiENSGT00530000063424.
HOGENOMiHOG000112448.
HOVERGENiHBG095943.
InParanoidiQ8BPZ8.
OMAiSFYNSAG.
OrthoDBiEOG7J9VPJ.
PhylomeDBiQ8BPZ8.
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: Q8BPZ8-1) [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
MEGESTLGVL SGFVLGALTF HHLNTDSDTE GFLLGEMKGE AKNSITDSQM
60 70 80 90 100
DNVKVVYTID IQKYIPCYRL FSFYNSLGEV NEHALKKVLS NVRKTVVGWY
110 120 130 140 150
KFRRHSDQIM TFREQLLHRN LQTHLSSPEL VFLLLTPSIT TESCSTHCLE
160 170 180 190 200
HALYKPQRGL FHRVPLVVTN LGMSDQLGYK TEPASCTSTV FSRAVRTHSS
210 220 230 240 250
QFFNEDGSLK EVHKINEMYA AVQEELKSIC QKVEQSEREV EKLLMDVNQL
260 270 280 290 300
KEVRRTQQAR ATGAGEKNVQ RNPQENILLC QALRTFFPES EVLHSCVISL
310 320 330 340 350
KNRHISPSGC NVNHHVDVVD QLTLMVEYVY SPEASPVPTA QLRKRKALDT
360 370 380 390 400
HDQGSVKRPR LLETESRPSV AASRSRHQDK ASSSSLDIDI EMGSPEDDAD

YPRSPTF
Length:407
Mass (Da):46,039
Last modified:March 1, 2003 - v1
Checksum:iFB8B05A197A2BC64
GO
Isoform 2 (identifier: Q8BPZ8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     228-261: SICQKVEQSEREVEKLLMDVNQLKEVRRTQQARA → CRLRPEEALVPMDLEAQLRAALVYAKKLNKVNEK
     262-407: Missing.

Show »
Length:261
Mass (Da):29,688
Checksum:iE87E9CB73AFE37FF
GO

Sequence cautioni

The sequence AAH29845.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC25434.1 differs from that shown. Reason: Frameshift at positions 4 and 227. Curated
The sequence BAE39607.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421K → E in BAE39607 (PubMed:16141072).Curated
Sequence conflicti211 – 2111E → G in BAC25434 (PubMed:16141072).Curated
Sequence conflicti351 – 3511H → Q in AAH29845 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei228 – 26134SICQK…QQARA → CRLRPEEALVPMDLEAQLRA ALVYAKKLNKVNEK in isoform 2. 1 PublicationVSP_023335Add
BLAST
Alternative sequencei262 – 407146Missing in isoform 2. 1 PublicationVSP_023336Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014420 mRNA. Translation: BAC25434.1. Frameshift.
AK042001 mRNA. Translation: BAC31129.1.
AK042339 mRNA. Translation: BAC31229.1.
AK051816 mRNA. Translation: BAC34780.1.
AK167540 mRNA. Translation: BAE39607.1. Different initiation.
BC029845 mRNA. Translation: AAH29845.1. Different initiation.
CCDSiCCDS19469.1. [Q8BPZ8-1]
RefSeqiNP_765993.1. NM_172405.3. [Q8BPZ8-1]
UniGeneiMm.486560.

Genome annotation databases

EnsembliENSMUST00000044535; ENSMUSP00000047692; ENSMUSG00000035234. [Q8BPZ8-2]
ENSMUST00000055245; ENSMUSP00000055895; ENSMUSG00000035234. [Q8BPZ8-1]
ENSMUST00000117364; ENSMUSP00000114050; ENSMUSG00000035234. [Q8BPZ8-1]
ENSMUST00000200657; ENSMUSP00000143465; ENSMUSG00000035234. [Q8BPZ8-1]
GeneIDi70681.
KEGGimmu:70681.
UCSCiuc008yid.1. mouse. [Q8BPZ8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014420 mRNA. Translation: BAC25434.1. Frameshift.
AK042001 mRNA. Translation: BAC31129.1.
AK042339 mRNA. Translation: BAC31229.1.
AK051816 mRNA. Translation: BAC34780.1.
AK167540 mRNA. Translation: BAE39607.1. Different initiation.
BC029845 mRNA. Translation: AAH29845.1. Different initiation.
CCDSiCCDS19469.1. [Q8BPZ8-1]
RefSeqiNP_765993.1. NM_172405.3. [Q8BPZ8-1]
UniGeneiMm.486560.

3D structure databases

ProteinModelPortaliQ8BPZ8.
SMRiQ8BPZ8. Positions 7-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000055895.

PTM databases

PhosphoSiteiQ8BPZ8.

Proteomic databases

EPDiQ8BPZ8.
MaxQBiQ8BPZ8.
PaxDbiQ8BPZ8.
PRIDEiQ8BPZ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044535; ENSMUSP00000047692; ENSMUSG00000035234. [Q8BPZ8-2]
ENSMUST00000055245; ENSMUSP00000055895; ENSMUSG00000035234. [Q8BPZ8-1]
ENSMUST00000117364; ENSMUSP00000114050; ENSMUSG00000035234. [Q8BPZ8-1]
ENSMUST00000200657; ENSMUSP00000143465; ENSMUSG00000035234. [Q8BPZ8-1]
GeneIDi70681.
KEGGimmu:70681.
UCSCiuc008yid.1. mouse. [Q8BPZ8-1]

Organism-specific databases

CTDi84142.
MGIiMGI:1917931. Fam175a.

Phylogenomic databases

eggNOGiENOG410IG59. Eukaryota.
ENOG4110D5E. LUCA.
GeneTreeiENSGT00530000063424.
HOGENOMiHOG000112448.
HOVERGENiHBG095943.
InParanoidiQ8BPZ8.
OMAiSFYNSAG.
OrthoDBiEOG7J9VPJ.
PhylomeDBiQ8BPZ8.
TreeFamiTF331751.

Enzyme and pathway databases

ReactomeiR-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-MMU-69473. G2/M DNA damage checkpoint.

Miscellaneous databases

NextBioi332079.
PROiQ8BPZ8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BPZ8.
ExpressionAtlasiQ8BPZ8. baseline and differential.
GenevisibleiQ8BPZ8. MM.

Family and domain databases

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

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Eye, Placenta and Thymus.
  2. "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).
    Strain: Czech II.
    Tissue: Mammary tumor.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Testis.

Entry informationi

Entry nameiF175A_MOUSE
AccessioniPrimary (citable) accession number: Q8BPZ8
Secondary accession number(s): Q3TJ88
, Q8BFV6, Q8BT69, Q8K2T7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: March 1, 2003
Last modified: April 13, 2016
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.