UBXN1_HUMAN
ID UBXN1_HUMAN Reviewed; 297 AA.
AC Q04323; Q9BV93; Q9BVV5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=UBX domain-containing protein 1;
DE AltName: Full=SAPK substrate protein 1;
DE AltName: Full=UBA/UBX 33.3 kDa protein;
GN Name=UBXN1; Synonyms=SAKS1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Pollard K.M.;
RL Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 220-231 AND 276-285, PHOSPHORYLATION AT SER-200, AND
RP INTERACTION WITH VCP.
RX PubMed=15362974; DOI=10.1042/bj20041498;
RA McNeill H., Knebel A., Arthur J.S., Cuenda A., Cohen P.;
RT "A novel UBA and UBX domain protein that binds polyubiquitin and VCP and is
RT a substrate for SAPKs.";
RL Biochem. J. 384:391-400(2004).
RN [4]
RP PROTEIN SEQUENCE OF 220-231, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [5]
RP UBIQUITIN-BINDING, AND INTERACTION WITH VCP.
RX PubMed=18775313; DOI=10.1016/j.cell.2008.06.048;
RA Alexandru G., Graumann J., Smith G.T., Kolawa N.J., Fang R., Deshaies R.J.;
RT "UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha
RT turnover.";
RL Cell 134:804-816(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP UBIQUITIN-BINDING, DOMAIN UBA, INTERACTION WITH BRCA1 AND BARD1,
RP MUTAGENESIS OF MET-13 AND ARG-219, AND FUNCTION.
RX PubMed=20351172; DOI=10.1128/mcb.01056-09;
RA Wu-Baer F., Ludwig T., Baer R.;
RT "The UBXN1 protein associates with autoubiquitinated forms of the BRCA1
RT tumor suppressor and inhibits its enzymatic function.";
RL Mol. Cell. Biol. 30:2787-2798(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAVS.
RX PubMed=23545497; DOI=10.1016/j.celrep.2013.02.027;
RA Wang P., Yang L., Cheng G., Yang G., Xu Z., You F., Sun Q., Lin R.,
RA Fikrig E., Sutton R.E.;
RT "UBXN1 interferes with Rig-I-like receptor-mediated antiviral immune
RT response by targeting MAVS.";
RL Cell Rep. 3:1057-1070(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-229, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207 AND SER-270, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP FUNCTION, AND INTERACTION WITH BIRC2.
RX PubMed=25681446; DOI=10.1074/jbc.m114.631689;
RA Wang Y.B., Tan B., Mu R., Chang Y., Wu M., Tu H.Q., Zhang Y.C., Guo S.S.,
RA Qin X.H., Li T., Li W.H., Li A.L., Zhang X.M., Li H.Y.;
RT "Ubiquitin-associated domain-containing ubiquitin regulatory X (UBX)
RT protein UBXN1 is a negative regulator of nuclear factor kappaB (NF-kappaB)
RT signaling.";
RL J. Biol. Chem. 290:10395-10405(2015).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP FUNCTION, AND INTERACTION WITH CUL1.
RX PubMed=28152074; DOI=10.1371/journal.ppat.1006187;
RA Hu Y., O'Boyle K., Auer J., Raju S., You F., Wang P., Fikrig E.,
RA Sutton R.E.;
RT "Multiple UBXN family members inhibit retrovirus and lentivirus production
RT and canonical NFkappaBeta signaling by stabilizing IkappaBalpha.";
RL PLoS Pathog. 13:E1006187-E1006187(2017).
RN [18]
RP INTERACTION WITH NIPAH VIRUS PROTEIN V (MICROBIAL INFECTION).
RX PubMed=29769705; DOI=10.1038/s41598-018-25815-9;
RA Uchida S., Horie R., Sato H., Kai C., Yoneda M.;
RT "Possible role of the Nipah virus V protein in the regulation of the
RT interferon beta induction by interacting with UBX domain-containing
RT protein1.";
RL Sci. Rep. 8:7682-7682(2018).
CC -!- FUNCTION: Ubiquitin-binding protein that plays a role in the modulation
CC of innate immune response. Blocks both the RIG-I-like receptors (RLR)
CC and NF-kappa-B pathways. Following viral infection, UBXN1 is induced
CC and recruited to the RLR component MAVS. In turn, interferes with MAVS
CC oligomerization, and disrupts the MAVS/TRAF3/TRAF6 signalosome. This
CC function probably serves as a brake to prevent excessive RLR signaling
CC (PubMed:23545497). Interferes with the TNFalpha-triggered NF-kappa-B
CC pathway by interacting with cellular inhibitors of apoptosis proteins
CC (cIAPs) and thereby inhibiting their recruitment to TNFR1
CC (PubMed:25681446). Prevents also the activation of NF-kappa-B by
CC associating with CUL1 and thus inhibiting NF-kappa-B inhibitor
CC alpha/NFKBIA degradation that remains bound to NF-kappa-B
CC (PubMed:28152074). Interacts with the BRCA1-BARD1 heterodimer and
CC regulates its activity. Specifically binds 'Lys-6'-linked polyubiquitin
CC chains. Interaction with autoubiquitinated BRCA1 leads to the
CC inhibition of the E3 ubiquitin-protein ligase activity of the BRCA1-
CC BARD1 heterodimer (PubMed:20351172). Component of a complex required to
CC couple deglycosylation and proteasome-mediated degradation of misfolded
CC proteins in the endoplasmic reticulum that are retrotranslocated in the
CC cytosol. {ECO:0000269|PubMed:20351172, ECO:0000269|PubMed:23545497,
CC ECO:0000269|PubMed:25681446, ECO:0000269|PubMed:28152074}.
CC -!- SUBUNIT: Interacts with MAVS; this interaction prevents MAVS
CC oligomerization and thus disrupts the RLR signaling pathway
CC (PubMed:23545497). Interacts with CUL1; this interaction inhibits CUL1-
CC mediated degradation of NF-kappa-B inhibitors (PubMed:28152074).
CC Interacts with BIRC2/c-IAP1; this interaction prevents TNFalpha-
CC stimulated RIP1 ubiquitination and subsequent NF-kappa-B activation
CC (PubMed:25681446). Component of a complex required to couple
CC retrotranslocation, ubiquitination and deglycosylation composed of
CC NGLY1, SAKS1, AMFR, VCP and RAD23B. Interacts with HOMER2 (By
CC similarity). Interacts directly with VCP. Interacts with BRCA1 and
CC BARD1; interaction takes place when BRCA1 is not autoubiquitinated but
CC is strongly enhanced in the presence of autoubiquitinated BRCA1.
CC {ECO:0000250|UniProtKB:Q922Y1, ECO:0000269|PubMed:15362974,
CC ECO:0000269|PubMed:18775313, ECO:0000269|PubMed:20351172,
CC ECO:0000269|PubMed:23545497, ECO:0000269|PubMed:25681446,
CC ECO:0000269|PubMed:28152074}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminal UBX domain)
CC with nipah virus protein V. {ECO:0000269|PubMed:29769705}.
CC -!- INTERACTION:
CC Q04323; V9HW80: HEL-S-70; NbExp=3; IntAct=EBI-1058647, EBI-10175326;
CC Q04323; Q9Y263: PLAA; NbExp=5; IntAct=EBI-1058647, EBI-1994037;
CC Q04323; Q9HCM9: TRIM39; NbExp=3; IntAct=EBI-1058647, EBI-739510;
CC Q04323; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-1058647, EBI-10180829;
CC Q04323; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-1058647, EBI-741480;
CC Q04323; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-1058647, EBI-10173939;
CC Q04323; Q8WU02; NbExp=3; IntAct=EBI-1058647, EBI-747182;
CC Q04323-2; O00154-4: ACOT7; NbExp=3; IntAct=EBI-11530712, EBI-12007918;
CC Q04323-2; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-11530712, EBI-25840379;
CC Q04323-2; Q08426: EHHADH; NbExp=3; IntAct=EBI-11530712, EBI-2339219;
CC Q04323-2; P04792: HSPB1; NbExp=3; IntAct=EBI-11530712, EBI-352682;
CC Q04323-2; Q9UBY9: HSPB7; NbExp=3; IntAct=EBI-11530712, EBI-739361;
CC Q04323-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-11530712, EBI-10975473;
CC Q04323-2; P02545: LMNA; NbExp=3; IntAct=EBI-11530712, EBI-351935;
CC Q04323-2; Q9Y263: PLAA; NbExp=3; IntAct=EBI-11530712, EBI-1994037;
CC Q04323-2; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-11530712, EBI-5452779;
CC Q04323-2; O60260-5: PRKN; NbExp=3; IntAct=EBI-11530712, EBI-21251460;
CC Q04323-2; P54725: RAD23A; NbExp=3; IntAct=EBI-11530712, EBI-746453;
CC Q04323-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-11530712, EBI-396669;
CC Q04323-2; P37840: SNCA; NbExp=3; IntAct=EBI-11530712, EBI-985879;
CC Q04323-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-11530712, EBI-947187;
CC Q04323-2; O76024: WFS1; NbExp=3; IntAct=EBI-11530712, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23545497}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q04323-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q04323-2; Sequence=VSP_020367;
CC -!- DOMAIN: The UBA domain specifically recognizes and binds 'Lys-6'-linked
CC polyubiquitin chains. {ECO:0000269|PubMed:20351172}.
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DR EMBL; M68864; AAA36396.1; -; mRNA.
DR EMBL; BC000902; AAH00902.1; -; mRNA.
DR EMBL; BC001372; AAH01372.1; -; mRNA.
DR EMBL; BC040129; AAH40129.1; -; mRNA.
DR CCDS; CCDS66105.1; -. [Q04323-1]
DR CCDS; CCDS8029.1; -. [Q04323-2]
DR PIR; S27965; S27965.
DR RefSeq; NP_001273006.1; NM_001286077.1. [Q04323-1]
DR RefSeq; NP_001273007.1; NM_001286078.1.
DR RefSeq; NP_056937.2; NM_015853.4. [Q04323-2]
DR RefSeq; XP_005274090.1; XM_005274033.4. [Q04323-2]
DR RefSeq; XP_016873363.1; XM_017017874.1. [Q04323-1]
DR AlphaFoldDB; Q04323; -.
DR SMR; Q04323; -.
DR BioGRID; 119239; 195.
DR DIP; DIP-29467N; -.
DR IntAct; Q04323; 75.
DR MINT; Q04323; -.
DR STRING; 9606.ENSP00000294119; -.
DR MEROPS; X36.001; -.
DR GlyGen; Q04323; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q04323; -.
DR MetOSite; Q04323; -.
DR PhosphoSitePlus; Q04323; -.
DR BioMuta; UBXN1; -.
DR DMDM; 30923268; -.
DR EPD; Q04323; -.
DR jPOST; Q04323; -.
DR MassIVE; Q04323; -.
DR MaxQB; Q04323; -.
DR PaxDb; Q04323; -.
DR PeptideAtlas; Q04323; -.
DR PRIDE; Q04323; -.
DR ProteomicsDB; 58240; -. [Q04323-1]
DR ProteomicsDB; 58241; -. [Q04323-2]
DR Antibodypedia; 1591; 126 antibodies from 22 providers.
DR DNASU; 51035; -.
DR Ensembl; ENST00000294119.6; ENSP00000294119.2; ENSG00000162191.14. [Q04323-2]
DR Ensembl; ENST00000301935.10; ENSP00000303991.5; ENSG00000162191.14. [Q04323-1]
DR GeneID; 51035; -.
DR KEGG; hsa:51035; -.
DR MANE-Select; ENST00000301935.10; ENSP00000303991.5; NM_001286077.2; NP_001273006.1.
DR UCSC; uc001nuj.5; human. [Q04323-1]
DR CTD; 51035; -.
DR DisGeNET; 51035; -.
DR GeneCards; UBXN1; -.
DR HGNC; HGNC:18402; UBXN1.
DR HPA; ENSG00000162191; Low tissue specificity.
DR MIM; 616378; gene.
DR neXtProt; NX_Q04323; -.
DR OpenTargets; ENSG00000162191; -.
DR PharmGKB; PA162408336; -.
DR VEuPathDB; HostDB:ENSG00000162191; -.
DR eggNOG; KOG2689; Eukaryota.
DR GeneTree; ENSGT00940000156457; -.
DR InParanoid; Q04323; -.
DR OMA; AQHFPRK; -.
DR PhylomeDB; Q04323; -.
DR TreeFam; TF313944; -.
DR PathwayCommons; Q04323; -.
DR Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR SignaLink; Q04323; -.
DR SIGNOR; Q04323; -.
DR BioGRID-ORCS; 51035; 21 hits in 1082 CRISPR screens.
DR ChiTaRS; UBXN1; human.
DR GenomeRNAi; 51035; -.
DR Pharos; Q04323; Tbio.
DR PRO; PR:Q04323; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q04323; protein.
DR Bgee; ENSG00000162191; Expressed in mucosa of stomach and 208 other tissues.
DR ExpressionAtlas; Q04323; baseline and differential.
DR Genevisible; Q04323; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:BHF-UCL.
DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0071796; F:K6-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IDA:UniProtKB.
DR GO; GO:1904855; F:proteasome regulatory particle binding; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IDA:BHF-UCL.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:BHF-UCL.
DR GO; GO:1904293; P:negative regulation of ERAD pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:1903094; P:negative regulation of protein K48-linked deubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:2000157; P:negative regulation of ubiquitin-specific protease activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; NAS:UniProtKB.
DR CDD; cd14302; UBA_UBXN1; 1.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041923; UBA_UBXN1.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Host-virus interaction; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..297
FT /note="UBX domain-containing protein 1"
FT /id="PRO_0000211023"
FT DOMAIN 2..42
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 211..293
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 41..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..297
FT /note="Interaction with BRCA1"
FT /evidence="ECO:0000269|PubMed:20351172"
FT COILED 87..172
FT /evidence="ECO:0000255"
FT COMPBIAS 84..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 200
FT /note="Phosphoserine; by MAPK12"
FT /evidence="ECO:0000269|PubMed:15362974"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 283..297
FT /note="LVPSAVLIVAKKCPS -> MAARLETRTRNWGSREACLGKGGMQREGAL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020367"
FT VARIANT 56
FT /note="L -> F (in dbSNP:rs11543359)"
FT /id="VAR_057370"
FT MUTAGEN 13
FT /note="M->T: Abolishes binding to 'Lys-6'-linked
FT polyubiquitin chains and ability to inhibit E3 ubiquitin-
FT protein ligase activity of the BRCA1-BARD1 heterodimer."
FT /evidence="ECO:0000269|PubMed:20351172"
FT MUTAGEN 219
FT /note="R->A: Does not affect binding to 'Lys-6'-linked
FT polyubiquitin chains and ability to inhibit E3 ubiquitin-
FT protein ligase activity of the BRCA1-BARD1 heterodimer."
FT /evidence="ECO:0000269|PubMed:20351172"
FT CONFLICT 76
FT /note="G -> A (in Ref. 1; AAA36396)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="E -> AE (in Ref. 1; AAA36396)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="K -> N (in Ref. 1; AAA36396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 33325 MW; E4E0C8BBAC93F2BB CRC64;
MAELTALESL IEMGFPRGRA EKALALTGNQ GIEAAMDWLM EHEDDPDVDE PLETPLGHIL
GREPTSSEQG GLEGSGSAAG EGKPALSEEE RQEQTKRMLE LVAQKQRERE EREEREALER
ERQRRRQGQE LSAARQRLQE DEMRRAAEER RREKAEELAA RQRVREKIER DKAERAKKYG
GSVGSQPPPV APEPGPVPSS PSQEPPTKRE YDQCRIQVRL PDGTSLTQTF RAREQLAAVR
LYVELHRGEE LGGGQDPVQL LSGFPRRAFS EADMERPLQE LGLVPSAVLI VAKKCPS
