BRAP2_CAEEL
ID BRAP2_CAEEL Reviewed; 590 AA.
AC Q95QN6;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=BRCA1-associated protein homolog 2 {ECO:0000312|WormBase:EEED8.16};
GN Name=brap-2 {ECO:0000312|WormBase:EEED8.16};
GN ORFNames=EEED8.16 {ECO:0000312|WormBase:EEED8.16};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=20207739; DOI=10.1074/jbc.m110.107011;
RA Koon J.C., Kubiseski T.J.;
RT "Developmental arrest of Caenorhabditis elegans BRAP-2 mutant exposed to
RT oxidative stress is dependent on BRC-1.";
RL J. Biol. Chem. 285:13437-13443(2010).
CC -!- FUNCTION: Controls the stress response to increased levels of reactive
CC oxygen species by modulating the brc-1-dependent expression of cki-1.
CC {ECO:0000269|PubMed:20207739}.
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DR EMBL; FO081042; CCD68743.1; -; Genomic_DNA.
DR RefSeq; NP_495016.1; NM_062615.5.
DR AlphaFoldDB; Q95QN6; -.
DR SMR; Q95QN6; -.
DR BioGRID; 39261; 2.
DR DIP; DIP-24711N; -.
DR IntAct; Q95QN6; 1.
DR STRING; 6239.EEED8.16; -.
DR iPTMnet; Q95QN6; -.
DR EPD; Q95QN6; -.
DR PaxDb; Q95QN6; -.
DR PeptideAtlas; Q95QN6; -.
DR EnsemblMetazoa; EEED8.16.1; EEED8.16.1; WBGene00017144.
DR GeneID; 173917; -.
DR KEGG; cel:CELE_EEED8.16; -.
DR UCSC; EEED8.16; c. elegans.
DR CTD; 173917; -.
DR WormBase; EEED8.16; CE28903; WBGene00017144; brap-2.
DR eggNOG; KOG0804; Eukaryota.
DR GeneTree; ENSGT00500000044909; -.
DR HOGENOM; CLU_009969_3_0_1; -.
DR InParanoid; Q95QN6; -.
DR OMA; GIIHLYK; -.
DR OrthoDB; 659103at2759; -.
DR PhylomeDB; Q95QN6; -.
DR Reactome; R-CEL-5675221; Negative regulation of MAPK pathway.
DR SignaLink; Q95QN6; -.
DR PRO; PR:Q95QN6; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00017144; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR CDD; cd12718; RRM_BRAP2; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR011422; BRAP2.
DR InterPro; IPR034932; BRAP2_RRM.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF07576; BRAP2; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 4: Predicted;
KW Metal-binding; Reference proteome; Stress response; Zinc; Zinc-finger.
FT CHAIN 1..590
FT /note="BRCA1-associated protein homolog 2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000056324"
FT ZN_FING 260..297
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 294..386
FT /note="UBP-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 27..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
SQ SEQUENCE 590 AA; 67414 MW; 56EA3FEEBD7D9CE8 CRC64;
MSSLYVPLVL RLEVRDRTKI VQSFIDDSKA GSESPLAGER TRQRLVKKGN TPPKKELKGR
EEDPPIGVMS SEPSHNYHKG RRTYSEVVIE SLDGEKLVDS SSSVAGTSEK SGGRSVSEGP
PDQVAYYSGN PLTEKTEGIM HFYKYNDEKL TKVAQCRMLC MYAVPAQVEV REIISFMCIS
LPMIVSIKVV RDPAPNQYML IIKFKEHNDA VTFYEEFNNC PFNDLESYCC TLFFVDRIEC
TTSNDLFSSD DTSLTELPTC AVCLERMDDS VLAILCNHSF HARCLEQWAD NTCPVCRYVQ
SPEVVAEQRC NDCGMSNDLW ICLICGNIGC GRYAEQHAQR HWELTSHTYS LKVGGERVWD
YAGDNYVHRL IENGADGKLV EYQRESNASF DDKNQKGGDK LEGIKLEYTL LLTSQLEDQR
KYFEGLRHDM EQTMSKMEKT AYAQVENLEH QLTERSTELK SLKGDLDDTV TARKVAEKRA
TQTNEKVNKL ANELKDEREI NQMLRKDQQV WKGQVEKLIE SQKTARTEYE KKIEDLQSQV
NDLLMHFETQ NKLKEQLDAG KITQEEITES QVELDSSSSS SRKLNRKKKK
