Full text data of UBXN1
UBXN1
(SAKS1)
[Confidence: low (only semi-automatic identification from reviews)]
UBX domain-containing protein 1 (SAPK substrate protein 1; UBA/UBX 33.3 kDa protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UBX domain-containing protein 1 (SAPK substrate protein 1; UBA/UBX 33.3 kDa protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q04323
ID UBXN1_HUMAN Reviewed; 297 AA.
AC Q04323; Q9BV93; Q9BVV5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-MAY-2003, sequence version 2.
DT 22-JAN-2014, entry version 108.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT project: 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,
RP AND 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
RT and is a substrate for SAPKs.";
RL Biochem. J. 384:391-400(2004).
RN [4]
RP PROTEIN SEQUENCE OF 220-231, AND 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.,
RA Deshaies R.J.;
RT "UBXD7 binds multiple ubiquitin ligases and implicates p97 in
RT HIF1alpha turnover.";
RL Cell 134:804-816(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND MASS
RP SPECTROMETRY.
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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND MASS
RP SPECTROMETRY.
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, AND
RP MUTAGENESIS OF MET-13 AND ARG-219.
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
RT BRCA1 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Ubiquitin-binding protein that interacts with the BRCA1-
CC BARD1 heterodimer, and regulates its activity. Specifically binds
CC 'Lys-6'-linked polyubiquitin chains. Interaction with
CC autoubiquitinated BRCA1, leads to inhibit the E3 ubiquitin-protein
CC ligase activity of the BRCA1-BARD1 heterodimer. Component of a
CC complex required to couple deglycosylation and proteasome-mediated
CC degradation of misfolded proteins in the endoplasmic reticulum
CC that are retrotranslocated in the cytosol.
CC -!- SUBUNIT: 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
CC but is strongly enhanced in the presence of autoubiquitinated
CC BRCA1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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 Note=No experimental confirmation available;
CC -!- DOMAIN: The UBA domain specifically recognizes and binds 'Lys-6'-
CC linked polyubiquitin chains.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -!- SIMILARITY: Contains 1 UBX domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; S27965; S27965.
DR RefSeq; NP_001273006.1; NM_001286077.1.
DR RefSeq; NP_001273007.1; NM_001286078.1.
DR RefSeq; NP_056937.2; NM_015853.4.
DR RefSeq; XP_005274090.1; XM_005274033.1.
DR UniGene; Hs.351296; -.
DR ProteinModelPortal; Q04323; -.
DR SMR; Q04323; 2-55.
DR DIP; DIP-29467N; -.
DR IntAct; Q04323; 30.
DR STRING; 9606.ENSP00000294119; -.
DR PhosphoSite; Q04323; -.
DR DMDM; 30923268; -.
DR PaxDb; Q04323; -.
DR PeptideAtlas; Q04323; -.
DR PRIDE; Q04323; -.
DR DNASU; 51035; -.
DR Ensembl; ENST00000294119; ENSP00000294119; ENSG00000162191.
DR Ensembl; ENST00000301935; ENSP00000303991; ENSG00000162191.
DR GeneID; 51035; -.
DR KEGG; hsa:51035; -.
DR UCSC; uc001nul.2; human.
DR CTD; 51035; -.
DR GeneCards; GC11M062477; -.
DR H-InvDB; HIX0009719; -.
DR HGNC; HGNC:18402; UBXN1.
DR HPA; HPA012669; -.
DR neXtProt; NX_Q04323; -.
DR PharmGKB; PA162408336; -.
DR eggNOG; COG5207; -.
DR HOGENOM; HOG000188321; -.
DR HOVERGEN; HBG082310; -.
DR OMA; QWLEDNQ; -.
DR OrthoDB; EOG7SR4PG; -.
DR ChiTaRS; UBXN1; human.
DR GenomeRNAi; 51035; -.
DR NextBio; 53592; -.
DR PRO; PR:Q04323; -.
DR ArrayExpress; Q04323; -.
DR Bgee; Q04323; -.
DR CleanEx; HS_UBXN1; -.
DR Genevestigator; Q04323; -.
DR GO; GO:0034098; C:Cdc48p-Npl4p-Ufd1p AAA ATPase complex; IDA:BHF-UCL.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0071796; F:K6-linked polyubiquitin binding; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:BHF-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; NAS:UniProtKB.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR000449; UBA/Ts_N.
DR InterPro; IPR001012; UBX.
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 PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 297 UBX domain-containing protein 1.
FT /FTId=PRO_0000211023.
FT DOMAIN 1 42 UBA.
FT DOMAIN 211 293 UBX.
FT REGION 43 297 Interaction with BRCA1.
FT COILED 87 172 Potential.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 199 199 Phosphoserine.
FT MOD_RES 200 200 Phosphoserine; by MAPK12.
FT MOD_RES 270 270 Phosphoserine.
FT VAR_SEQ 283 297 LVPSAVLIVAKKCPS -> MAARLETRTRNWGSREACLGKG
FT GMQREGAL (in isoform 2).
FT /FTId=VSP_020367.
FT VARIANT 56 56 L -> F (in dbSNP:rs11543359).
FT /FTId=VAR_057370.
FT MUTAGEN 13 13 M->T: Abolishes binding to 'Lys-6'-linked
FT polyubiquitin chains and ability to
FT inhibit E3 ubiquitin-protein ligase
FT activity of the BRCA1-BARD1 heterodimer.
FT MUTAGEN 219 219 R->A: Does not affect binding to 'Lys-6'-
FT linked polyubiquitin chains and ability
FT to inhibit E3 ubiquitin-protein ligase
FT activity of the BRCA1-BARD1 heterodimer.
FT CONFLICT 76 76 G -> A (in Ref. 1; AAA36396).
FT CONFLICT 148 148 E -> AE (in Ref. 1; AAA36396).
FT CONFLICT 154 154 K -> N (in Ref. 1; AAA36396).
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
//
ID UBXN1_HUMAN Reviewed; 297 AA.
AC Q04323; Q9BV93; Q9BVV5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-MAY-2003, sequence version 2.
DT 22-JAN-2014, entry version 108.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT project: 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,
RP AND 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
RT and is a substrate for SAPKs.";
RL Biochem. J. 384:391-400(2004).
RN [4]
RP PROTEIN SEQUENCE OF 220-231, AND 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.,
RA Deshaies R.J.;
RT "UBXD7 binds multiple ubiquitin ligases and implicates p97 in
RT HIF1alpha turnover.";
RL Cell 134:804-816(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND MASS
RP SPECTROMETRY.
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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND MASS
RP SPECTROMETRY.
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, AND
RP MUTAGENESIS OF MET-13 AND ARG-219.
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
RT BRCA1 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Ubiquitin-binding protein that interacts with the BRCA1-
CC BARD1 heterodimer, and regulates its activity. Specifically binds
CC 'Lys-6'-linked polyubiquitin chains. Interaction with
CC autoubiquitinated BRCA1, leads to inhibit the E3 ubiquitin-protein
CC ligase activity of the BRCA1-BARD1 heterodimer. Component of a
CC complex required to couple deglycosylation and proteasome-mediated
CC degradation of misfolded proteins in the endoplasmic reticulum
CC that are retrotranslocated in the cytosol.
CC -!- SUBUNIT: 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
CC but is strongly enhanced in the presence of autoubiquitinated
CC BRCA1.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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 Note=No experimental confirmation available;
CC -!- DOMAIN: The UBA domain specifically recognizes and binds 'Lys-6'-
CC linked polyubiquitin chains.
CC -!- SIMILARITY: Contains 1 UBA domain.
CC -!- SIMILARITY: Contains 1 UBX domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; S27965; S27965.
DR RefSeq; NP_001273006.1; NM_001286077.1.
DR RefSeq; NP_001273007.1; NM_001286078.1.
DR RefSeq; NP_056937.2; NM_015853.4.
DR RefSeq; XP_005274090.1; XM_005274033.1.
DR UniGene; Hs.351296; -.
DR ProteinModelPortal; Q04323; -.
DR SMR; Q04323; 2-55.
DR DIP; DIP-29467N; -.
DR IntAct; Q04323; 30.
DR STRING; 9606.ENSP00000294119; -.
DR PhosphoSite; Q04323; -.
DR DMDM; 30923268; -.
DR PaxDb; Q04323; -.
DR PeptideAtlas; Q04323; -.
DR PRIDE; Q04323; -.
DR DNASU; 51035; -.
DR Ensembl; ENST00000294119; ENSP00000294119; ENSG00000162191.
DR Ensembl; ENST00000301935; ENSP00000303991; ENSG00000162191.
DR GeneID; 51035; -.
DR KEGG; hsa:51035; -.
DR UCSC; uc001nul.2; human.
DR CTD; 51035; -.
DR GeneCards; GC11M062477; -.
DR H-InvDB; HIX0009719; -.
DR HGNC; HGNC:18402; UBXN1.
DR HPA; HPA012669; -.
DR neXtProt; NX_Q04323; -.
DR PharmGKB; PA162408336; -.
DR eggNOG; COG5207; -.
DR HOGENOM; HOG000188321; -.
DR HOVERGEN; HBG082310; -.
DR OMA; QWLEDNQ; -.
DR OrthoDB; EOG7SR4PG; -.
DR ChiTaRS; UBXN1; human.
DR GenomeRNAi; 51035; -.
DR NextBio; 53592; -.
DR PRO; PR:Q04323; -.
DR ArrayExpress; Q04323; -.
DR Bgee; Q04323; -.
DR CleanEx; HS_UBXN1; -.
DR Genevestigator; Q04323; -.
DR GO; GO:0034098; C:Cdc48p-Npl4p-Ufd1p AAA ATPase complex; IDA:BHF-UCL.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0071796; F:K6-linked polyubiquitin binding; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:BHF-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; NAS:UniProtKB.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR000449; UBA/Ts_N.
DR InterPro; IPR001012; UBX.
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 PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 297 UBX domain-containing protein 1.
FT /FTId=PRO_0000211023.
FT DOMAIN 1 42 UBA.
FT DOMAIN 211 293 UBX.
FT REGION 43 297 Interaction with BRCA1.
FT COILED 87 172 Potential.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 199 199 Phosphoserine.
FT MOD_RES 200 200 Phosphoserine; by MAPK12.
FT MOD_RES 270 270 Phosphoserine.
FT VAR_SEQ 283 297 LVPSAVLIVAKKCPS -> MAARLETRTRNWGSREACLGKG
FT GMQREGAL (in isoform 2).
FT /FTId=VSP_020367.
FT VARIANT 56 56 L -> F (in dbSNP:rs11543359).
FT /FTId=VAR_057370.
FT MUTAGEN 13 13 M->T: Abolishes binding to 'Lys-6'-linked
FT polyubiquitin chains and ability to
FT inhibit E3 ubiquitin-protein ligase
FT activity of the BRCA1-BARD1 heterodimer.
FT MUTAGEN 219 219 R->A: Does not affect binding to 'Lys-6'-
FT linked polyubiquitin chains and ability
FT to inhibit E3 ubiquitin-protein ligase
FT activity of the BRCA1-BARD1 heterodimer.
FT CONFLICT 76 76 G -> A (in Ref. 1; AAA36396).
FT CONFLICT 148 148 E -> AE (in Ref. 1; AAA36396).
FT CONFLICT 154 154 K -> N (in Ref. 1; AAA36396).
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
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