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Q3UI43 (BABA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
BRISC and BRCA1-A complex member 1
Alternative name(s):
Mediator of RAP80 interactions and targeting subunit of 40 kDa
New component of the BRCA1-A complex
Gene names
Name:Babam1
Synonyms:Merit40, Nba1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length333 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. In the BRCA1-A complex, it is required for the complex integrity and its localization at DSBs. Probably also plays a role as a component of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin. In these 2 complexes, it is probably required to maintain the stability of BRE/BRCC45 and help the 'Lys-63'-linked deubiquitinase activity mediated by BRCC3/BRCC36 component By similarity.

Subunit structure

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 BRCA1-A complex, interacts directly with FAM175A/Abraxas and BRE/BRCC45. Component of the BRISC complex, at least composed of the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and BABAM1/NBA1 By similarity.

Subcellular location

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

Domain

The VWFA-like region is similar to the VWFA domain. Its presence reveals similarities between the structure of the 19S proteasome and the BRCA1-A complexes By similarity.

Sequence similarities

Belongs to the BABAM1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 333333BRISC and BRCA1-A complex member 1
PRO_0000288459

Regions

Region99 – 302204VWFA-like

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue331Phosphoserine By similarity
Modified residue531Phosphoserine By similarity

Experimental info

Sequence conflict231T → P in AAH05692. Ref.2
Sequence conflict481S → N in AAH05692. Ref.2
Sequence conflict1201S → T in BAC36785. Ref.1
Sequence conflict3151A → S in AAH05692. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q3UI43 [UniParc].

Last modified October 11, 2005. Version 1.
Checksum: 5309BA609EA07FF8

FASTA33336,793
        10         20         30         40         50         60 
MEVAEANSPT EEEEEEEEEG EETISEPRPH TRSNPEGAED RALGAQASVG SRSEGEGEAA 

        70         80         90        100        110        120 
TADGGAASVP GAGPKPWQVP ASASEVQIRT PRVNCPEKVI ICLDLSEEMS VPKLESFNGS 

       130        140        150        160        170        180 
RTNALNVSQK MVEMFVRTKH KIDKSHEFAL VVVNDDSAWL SGLTSDPREL CSCLYDLETA 

       190        200        210        220        230        240 
SCSTFNLEGL FSLIQQKTEL PVTENVQTIP PPYVVRTILV YSRPPCQPQF SLTEPMKKMF 

       250        260        270        280        290        300 
QCPYFFFDIV YIHNGTEEKE EDMSWKDMFA FMGSLDTKGA SYKYEVALAG PALELHNCMA 

       310        320        330 
KLLAHPLQRP CQTHASYSLL EEDEEAGEEE ATV 

« Hide

References

[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. expand/collapse author list , 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].
Strain: C57BL/6J.
Tissue: Head, Heart and Olfactory bulb.
[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].
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK003366 mRNA. Translation: BAB22740.1.
AK077402 mRNA. Translation: BAC36785.1.
AK078265 mRNA. Translation: BAC37197.1.
AK147083 mRNA. Translation: BAE27663.1.
BC005692 mRNA. Translation: AAH05692.1.
IPIIPI00165711.
RefSeqNP_080912.2. NM_026636.2.
UniGeneMm.21749.

3D structure databases

ProteinModelPortalQ3UI43.
ModBaseSearch...

PTM databases

PhosphoSiteQ3UI43.

Proteomic databases

PaxDbQ3UI43.
PRIDEQ3UI43.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002473; ENSMUSP00000002473; ENSMUSG00000031820.
GeneID68251.
KEGGmmu:68251.
UCSCuc009mdb.2. mouse.

Organism-specific databases

CTD29086.
MGIMGI:1915501. Babam1.

Phylogenomic databases

eggNOGNOG76997.
GeneTreeENSGT00390000016934.
InParanoidQ9CTJ4.
OMAVQIRTPR.
OrthoDBEOG40P477.

Gene expression databases

BgeeQ3UI43.
CleanExMM_5430437P03RIK.
GenevestigatorQ3UI43.

Family and domain databases

InterProIPR026126. BABAM1.
[Graphical view]
PANTHERPTHR15660. PTHR15660. 1 hit.
ProtoNetSearch...

Other

NextBio326830.
SOURCESearch...

Entry information

Entry nameBABA1_MOUSE
AccessionPrimary (citable) accession number: Q3UI43
Secondary accession number(s): Q8C5Q8, Q99JU2, Q9CTJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 11, 2005
Last modified: May 1, 2013
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families