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Q864S8 (BRCA2_FELCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Breast cancer type 2 susceptibility protein homolog
Alternative name(s):
Fanconi anemia group D1 protein homolog
Gene names
Name:BRCA2
Synonyms:FANCD1
OrganismFelis catus (Cat) (Felis silvestris catus) [Complete proteome]
Taxonomic identifier9685 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Feliformia › Felidae › Felinae › Felis

Protein attributes

Sequence length3372 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in double-strand break repair and/or homologous recombination. Binds RAD51 and potentiates recombinational DNA repair by promoting assembly of RAD51 onto single-stranded DNA (ssDNA). Acts by targeting RAD51 to ssDNA over double-stranded DNA, enabling RAD51 to displace replication protein-A (RPA) from ssDNA and stabilizing RAD51-ssDNA filaments by blocking ATP hydrolysis. May participate in S phase checkpoint activation. Binds selectively to ssDNA, and to ssDNA in tailed duplexes and replication fork structures. In concert with NPM1, regulates centrosome duplication By similarity.

Subunit structure

Monomer and dimer. Interacts with RAD51; regulates RAD51 recruitment and function at sites of DNA repair. Interacts with DSS1. Interacts with both nonubiquitinated and monoubiquitinated FANCD2; this complex also includes XRCC3 and phosphorylated FANCG By similarity. Interacts with WDR16. Interacts with USP11. Interacts with DMC1. Part of a trimeric complex containing BRCA1, BRCA2 and PALB2. Interacts with PALB2. Interacts with BRCA1 only in the presence of PALB2 which serves as the bridging protein. Interacts with ROCK2 and NPM1 By similarity.

Post-translational modification

Phosphorylation by CHEK1 and CHEK2 regulates interaction with RAD51. Phosphorylation at Ser-3236 by CDK1 and CDK2 is low in S phase when recombination is active, but increases as cells progress towards mitosis; this phosphorylation prevents homologous recombination-dependent repair during S phase and G2 by inhibiting RAD51 binding By similarity.

Ubiquitinated in the absence of DNA damage; this does not lead to proteasomal degradation. In contrast, ubiquitination in response to DNA damage leads to proteasomal degradation By similarity.

Sequence similarities

Contains 7 BRCA2 repeats.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
   DiseaseTumor suppressor
   DomainRepeat
   LigandDNA-binding
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcell cycle cytokinesis

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome duplication

Inferred from sequence or structural similarity. Source: UniProtKB

double-strand break repair

Inferred from sequence or structural similarity. Source: UniProtKB

double-strand break repair via homologous recombination

Inferred from electronic annotation. Source: InterPro

negative regulation of mammary gland epithelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

nucleotide-excision repair

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-dependent

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of S phase of mitotic cell cycle

Inferred from electronic annotation. Source: InterPro

   Cellular_componentBRCA2-MAGE-D1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

centrosome

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

secretory granule

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functiongamma-tubulin binding

Inferred from sequence or structural similarity. Source: UniProtKB

single-stranded DNA binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 33723372Breast cancer type 2 susceptibility protein homolog
PRO_0000227014

Regions

Repeat994 – 102835BRCA2 1
Repeat1208 – 124235BRCA2 2
Repeat1417 – 145135BRCA2 3
Repeat1518 – 155235BRCA2 4
Repeat1663 – 169735BRCA2 5
Repeat1925 – 195935BRCA2 6
Repeat1995 – 202935BRCA2 7
Region1 – 4040Interaction with PALB2 By similarity
Region630 – 992363Interaction with NPM1 By similarity

Amino acid modifications

Modified residue32361Phosphoserine; by CDK1 and CDK2 By similarity
Modified residue33311Phosphothreonine; by CHEK1 and CHEK2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q864S8 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 37F23DA23CA94665

FASTA3,372377,345
        10         20         30         40         50         60 
MPIGCKERPT FFEIFRTRCN KADLGPISLN WFEELCLEAP PYNSEPTEES GYKISYEPNL 

        70         80         90        100        110        120 
FKTPQRKPCH QLASTPIIFK EQGLIPPIYQ QSPLKELGKD ITNSKHRSCC TMKSKMDQTN 

       130        140        150        160        170        180 
DVTSPPLNSC LSESPLLRST HVTPQREKSV VCGSLFHTPK LTKGQTPKRI SESLGAEVDP 

       190        200        210        220        230        240 
DMSWSSSLAT PPTLSSTVLI VRDEEASAAV FPNDTTAIFK SYFCNHDESL KKNDRFIPSG 

       250        260        270        280        290        300 
PDSENKSQRE AKSQGLGKMV GNSCDKVNSC KDPFGNSTLN VLEDGVRERV ADVSEEDSFP 

       310        320        330        340        350        360 
LCVPKCKTRN LQKIKTSKTR KNIFNETTDE CKEAKKQMKE NKHSFVSEME ANASDPLDSN 

       370        380        390        400        410        420 
VTNQKPFGNG SDKISKEVVL SSASESCHLT LSGLNGTHME KLPLLCISSC DQNNSEKDLI 

       430        440        450        460        470        480 
TTEKECTNFI ILEDSLPQIS GVPKCTEKIL NEEIVVNKID EGQCLESHED SILAVKQAVF 

       490        500        510        520        530        540 
ETSLIASPLQ GIRKSIFRIR ESPEETFSAV FSNNITDPNF KEEHEASESV LEKHSICSQK 

       550        560        570        580        590        600 
EDSLSTSSLD NGSWPATIKH TSVALKNSGL ISTLKKKTKK FIYVVNDETS YQGLKTQKDQ 

       610        620        630        640        650        660 
QSGLMNYSAQ FEANVLEGPL TFANADSGLL HSSVKKTCLQ NDSKEPILSL TNSFGTLLRK 

       670        680        690        700        710        720 
VSNKGSSSPN NKIISQDLDY KEAKIKKEKL QSFISTETNC LSSLQEKHCE DDTKSQRVAD 

       730        740        750        760        770        780 
RKEEILPAVS QPSVPYSEVE DSGIHFQTLK SFSSDPDKSS QLTPHPRDPP SNPVGLSRGR 

       790        800        810        820        830        840 
ESYEVSETLK CKNHEAGFEL TKTMENSQEI HVLNEHAKKA KLLSTEKYVT EASPSMKVPF 

       850        860        870        880        890        900 
NQNAHLTIIQ KDQKETTLIS KITMNPNSEE LFPDGDNFVF KITKERNVPV LGSIKELQDS 

       910        920        930        940        950        960 
DLCCVKEPVL ENSTMVVYTD MDDKQAAKVS ITKGFDSSNI DDLTEKDRNS IKQQLRMTLD 

       970        980        990       1000       1010       1020 
QDSKSDITLD SDMKSNGNND YMDNWARLSD PILNHNFGNG FRTASNKEIK LSEHNIKKSK 

      1030       1040       1050       1060       1070       1080 
MLFKDIEERY PTNLACIEIV NTPLESQEKL SKPHILDPQS INTVSGCVQS SAYVSDSENR 

      1090       1100       1110       1120       1130       1140 
HTTPPTLSLK RDFDSNHNLT PSQKAEITEL STILEESGSQ FEFTQFRKPS HLKQKNPCEM 

      1150       1160       1170       1180       1190       1200 
PEKHLTISNT TPEEQKDGHL RLTINALSIS QGDSSKKFEG IIGGKQKLAC LSKTSCNKSA 

      1210       1220       1230       1240       1250       1260 
SGHLTGKNEV EFRGFYSARG TKLNVCSEAL QKAKKLFSDL ENISEETSVE VDRSFSSSKC 

      1270       1280       1290       1300       1310       1320 
NGSVSMFKKE NCNNEKKLNE KNNKYRLILQ NNIEMTTGIF VAEDTEGYKR NIENKANKYT 

      1330       1340       1350       1360       1370       1380 
DASRNVYNFR EADGSDSSKN DTVYIHKEEN GLPYIDQHDI DLKLSSQFIK EGNTQIKEGL 

      1390       1400       1410       1420       1430       1440 
SDLTCLEVVK AEETLHVNTS NKEHLTANTM GRITKDFDIF DVSFQTASGK NIRVSRASLN 

      1450       1460       1470       1480       1490       1500 
KVTNLLDQKC TEEELNNFAD SLNSELLSGI DINKADISHH GEMEILKKRQ MKESDLTGTE 

      1510       1520       1530       1540       1550       1560 
NKSLTLQQRP EYEIKKIKEP TILGFHTASG KRIEIAKESL DKVKNLFDEQ EQDKSEMTNF 

      1570       1580       1590       1600       1610       1620 
SHRGTKMSKG REECEGGLRL ACKTIEITPA SKEEEMQKPL EKNLVSNEIV VVPRLLSDNL 

      1630       1640       1650       1660       1670       1680 
YKQTENLKIP NRASLKVKVH ENTGKETAKK PTTCTNQSTY SATENSALSF YTGHGRKISV 

      1690       1700       1710       1720       1730       1740 
SQSSILEVKK WLRGGELDDQ PEKTVYNISE YLPKSKVDNS GIEPVVRNVG ERENTSVSEI 

      1750       1760       1770       1780       1790       1800 
MFTVREADTD PQSVNEDICV QRLVTNFSCK KENTAIKVTV SDSNNFDSTQ KLNSDSNDAV 

      1810       1820       1830       1840       1850       1860 
PVYTTASSER VLVAHETKVA EGFTENCSMA IKQTTKSKPG KIVAGYRKAP DDSEDTICPN 

      1870       1880       1890       1900       1910       1920 
SLDGAECSSP SHKDFAETQS EQTPQLNQSI SGFKKRSEIP PHQINLKTSD ICKLSTGKRL 

      1930       1940       1950       1960       1970       1980 
QSISYTNACG IFSTASGKCV QVSDAALQKA RQVFSKVEDS AKQPFSKVSF KHNEDHSDKF 

      1990       2000       2010       2020       2030       2040 
TREENTMIHT PQNLLSSAFS GFSTASGKQV PVSESALCKV KGILEEFDVM RTECGPQRSP 

      2050       2060       2070       2080       2090       2100 
TSRQDVSKMP PPSCVENKTP KHSVNSKLEK AYNKEFKLSS NSKIENGSSE NHSVQVSPYP 

      2110       2120       2130       2140       2150       2160 
SQFKQDKQLI QGNKASLVEN IHLLEKEQAL PKNIKWKLET EAFPNLPLKT DTAIHSTDSK 

      2170       2180       2190       2200       2210       2220 
DPENYFETET VEIAKAFMED GELTDADLLS HARHFLPTCQ HSEETLVSNS RRGKRRGVLV 

      2230       2240       2250       2260       2270       2280 
SVGEPPIKRN LLNEFDRIIK NQEKSLKASK STPDGIIKDR SLFMHHISLE PVTCGPFSTT 

      2290       2300       2310       2320       2330       2340 
KKRQEIQNPN FTAPGQKFLS KSHFYEHLAL EKSSSNVSIS GQPFCTVPAT RSEKRGHSIT 

      2350       2360       2370       2380       2390       2400 
PSKPVKVFVP PFKTKSRFLQ DEQHISKNTH VEENKQKPNN IDEHSSGDSK NNINNSEIHQ 

      2410       2420       2430       2440       2450       2460 
LNKNNSSQAA TMVFTKCEKE PLDLIASLQN ARDIQDMRIR EKRKQHIFPQ PGSLFLAKTS 

      2470       2480       2490       2500       2510       2520 
TVPRISLRVA VEGRVPSACS HKQLYMYGVS KHCVKINSKN AESFQFHTQD YFGKEVQWAK 

      2530       2540       2550       2560       2570       2580 
EGIQLADGGW LIPSNDGKAG KEEFYRALCD TPGVDPNLIS RIWVYNHYRW IIWKLAAMEF 

      2590       2600       2610       2620       2630       2640 
AFPKEFANRC LSPERVLLQL KYRYDMEIDR SKRSAIKKIM ERDDTAAKTL VLCISETISS 

      2650       2660       2670       2680       2690       2700 
STDLSETSGS KTSGVGTKNV GIVELTDGWY AIKAQLDPPL LALVKKGRLT VGHKIIIHGA 

      2710       2720       2730       2740       2750       2760 
ELAGSPDACT PLEAPESLIL KISANSTRPA CWYAKLGFFP DPRPFPLPLS SLFSDGGNVG 

      2770       2780       2790       2800       2810       2820 
CVDVVIQRTY PIQWMEKTPS GLCIFRNERE EEREATKYAE AQQKKLEVLF NKIQAEFEKH 

      2830       2840       2850       2860       2870       2880 
DENITKRCVP LRALTRQQVC ALQDGAELYE AVKNAPDPAS LEAYFSEEQI RALNNHRQML 

      2890       2900       2910       2920       2930       2940 
NDKKQAQIQL EFRKAMESAE QGEQMLPRDV TTVWKMRIIS YGKKEKDSVT LSIWRPSSDL 

      2950       2960       2970       2980       2990       3000 
YSLLTEGKRY RIYHLATSQS KSKSERAHIQ LTATKKTQYQ QLPASDELLF QVYQPREPLY 

      3010       3020       3030       3040       3050       3060 
FNKLLDPDFQ PPCSEVDLIG FVVSVVKKIG FAPLVYLSDE CHNLLAIKVW TDLNEDIVKP 

      3070       3080       3090       3100       3110       3120 
HTLIAASNLQ WRPESKSGIP TLFAGDFSRF SASPKEGHFQ ETFHKMKNTI ENVETFCNDA 

      3130       3140       3150       3160       3170       3180 
ENKLVHILNA NSPKVSTPMK DYASEPHTIQ TVLGLGNKLS MSSPNSEMNY QSPLSLCKPK 

      3190       3200       3210       3220       3230       3240 
AKSVPTPGSA QMTSKSCYKG ERELDDPKTC KKRKALDFLS RLPLPPPVSP ICTFVSPAAQ 

      3250       3260       3270       3280       3290       3300 
KAFQPPRSCG TKYETPIKKR ELNSPQMTPL KFNDTSLVES DSIADEELAL INTQALLSGL 

      3310       3320       3330       3340       3350       3360 
AGEDQLMSLN DSPRTAPTSS KDYVRPKSYP TAPGIRDCEN PQASTEGGEP DVQDTDTVKR 

      3370 
SSMRLQRRQQ QT

« Hide

References

[1]"Properties of the tumor suppressor gene brca2 in the cat."
Oonuma T., Morimatsu M., Ochiai K., Syuto B.
J. Vet. Med. Sci. 65:1123-1126(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB107955 mRNA. Translation: BAC75821.2.
RefSeqNP_001009858.1. NM_001009858.1.

3D structure databases

ProteinModelPortalQ864S8.
SMRQ864S8. Positions 1520-1552, 2423-3128.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID493878.
KEGGfca:493878.

Organism-specific databases

CTD675.

Phylogenomic databases

HOVERGENHBG050731.
KOK08775.

Family and domain databases

Gene3D2.40.50.140. 4 hits.
InterProIPR015525. BRCA2.
IPR015187. BRCA2_OB_1.
IPR015188. BRCA2_OB_3.
IPR002093. BRCA2_repeat.
IPR015252. DNA_recomb/repair_BRCA2_hlx.
IPR012340. NA-bd_OB-fold.
IPR015205. Tower.
[Graphical view]
PANTHERPTHR11289. PTHR11289. 1 hit.
PfamPF09169. BRCA-2_helical. 1 hit.
PF09103. BRCA-2_OB1. 1 hit.
PF09104. BRCA-2_OB3. 1 hit.
PF00634. BRCA2. 7 hits.
PF09121. Tower. 1 hit.
[Graphical view]
PIRSFPIRSF002397. BRCA2. 1 hit.
SUPFAMSSF81872. BRCA2_helical. 1 hit.
SSF50249. Nucleic_acid_OB. 3 hits.
PROSITEPS50138. BRCA2_REPEAT. 7 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameBRCA2_FELCA
AccessionPrimary (citable) accession number: Q864S8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: January 4, 2005
Last modified: May 1, 2013
This is version 58 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents