UBAC1_HUMAN
ID UBAC1_HUMAN Reviewed; 405 AA.
AC Q9BSL1; O75500; Q9UMW7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Ubiquitin-associated domain-containing protein 1;
DE Short=UBA domain-containing protein 1;
DE AltName: Full=E3 ubiquitin-protein ligase subunit KPC2;
DE AltName: Full=Glialblastoma cell differentiation-related protein 1;
DE AltName: Full=Kip1 ubiquitination-promoting complex protein 2;
GN Name=UBAC1; Synonyms=GBDR1, KPC2, UBADC1;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Endothelial cell;
RX PubMed=10857748; DOI=10.1006/geno.2000.6176;
RA Li C., Rodriguez M., Adamson J.W., Banerjee D.;
RT "Identification of a glialblastoma cell differentiation factor-related gene
RT mRNA in human microvascular endothelial cells.";
RL Genomics 65:243-252(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Lymph;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 75-405.
RC TISSUE=Glioblastoma;
RA Jin H.L., Hu S.N., Li G.T., Tu C., Zhong N., Yuan J.G., Qiang B.Q.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=15531880; DOI=10.1038/ncb1194;
RA Kamura T., Hara T., Matsumoto M., Ishida N., Okumura F., Hatakeyama S.,
RA Yoshida M., Nakayama K., Nakayama K.;
RT "Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1) at G1
RT phase.";
RL Nat. Cell Biol. 6:1229-1235(2004).
RN [6]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH THE PROTEASOME.
RX PubMed=15746103; DOI=10.1074/jbc.m500866200;
RA Kotoshiba S., Kamura T., Hara T., Ishida N., Nakayama K.;
RT "Molecular dissection of the interaction between p27 and Kip1
RT ubiquitylation-promoting complex, the ubiquitin ligase that regulates
RT proteolysis of p27 in G1 phase.";
RL J. Biol. Chem. 280:17694-17700(2005).
RN [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP STRUCTURE BY NMR OF 172-241.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the first UBA domain in the human ubiquitin
RT associated domain containing 1 (UBADC1).";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Non-catalytic subunit of the KPC complex that acts as E3
CC ubiquitin-protein ligase. Required for poly-ubiquitination and
CC proteasome-mediated degradation of CDKN1B during G1 phase of the cell
CC cycle. {ECO:0000269|PubMed:15531880, ECO:0000269|PubMed:15746103}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Component of the KPC complex composed of RNF123/KPC1 and
CC UBAC1/KPC2. Interacts with RNF123 via its N-terminal domain. Interacts
CC with the proteasome via its N-terminal domain.
CC {ECO:0000269|PubMed:15531880, ECO:0000269|PubMed:15746103}.
CC -!- INTERACTION:
CC Q9BSL1; A0A0S2Z5Q7: ALS2; NbExp=3; IntAct=EBI-749370, EBI-25928834;
CC Q9BSL1; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-749370, EBI-2875665;
CC Q9BSL1; P54253: ATXN1; NbExp=6; IntAct=EBI-749370, EBI-930964;
CC Q9BSL1; Q96M89-2: CCDC138; NbExp=3; IntAct=EBI-749370, EBI-10972887;
CC Q9BSL1; Q15038: DAZAP2; NbExp=7; IntAct=EBI-749370, EBI-724310;
CC Q9BSL1; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-749370, EBI-25840379;
CC Q9BSL1; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-749370, EBI-11978259;
CC Q9BSL1; P42858: HTT; NbExp=26; IntAct=EBI-749370, EBI-466029;
CC Q9BSL1; P24592: IGFBP6; NbExp=3; IntAct=EBI-749370, EBI-947015;
CC Q9BSL1; O60333-2: KIF1B; NbExp=3; IntAct=EBI-749370, EBI-10975473;
CC Q9BSL1; Q7L590-2: MCM10; NbExp=3; IntAct=EBI-749370, EBI-10233517;
CC Q9BSL1; Q09327: MGAT3; NbExp=3; IntAct=EBI-749370, EBI-18058216;
CC Q9BSL1; Q9NWW9: PLAAT2; NbExp=3; IntAct=EBI-749370, EBI-12253270;
CC Q9BSL1; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-749370, EBI-373552;
CC Q9BSL1; P78424: POU6F2; NbExp=3; IntAct=EBI-749370, EBI-12029004;
CC Q9BSL1; P60891: PRPS1; NbExp=3; IntAct=EBI-749370, EBI-749195;
CC Q9BSL1; P49810: PSEN2; NbExp=3; IntAct=EBI-749370, EBI-2010251;
CC Q9BSL1; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-749370, EBI-396669;
CC Q9BSL1; Q9NWF9: RNF216; NbExp=3; IntAct=EBI-749370, EBI-723313;
CC Q9BSL1; P37840: SNCA; NbExp=3; IntAct=EBI-749370, EBI-985879;
CC Q9BSL1; Q8N0X7: SPART; NbExp=3; IntAct=EBI-749370, EBI-2643803;
CC Q9BSL1; Q9C040: TRIM2; NbExp=10; IntAct=EBI-749370, EBI-749840;
CC Q9BSL1; Q9HCM9: TRIM39; NbExp=3; IntAct=EBI-749370, EBI-739510;
CC Q9BSL1; P0CG47: UBB; NbExp=4; IntAct=EBI-749370, EBI-413034;
CC Q9BSL1; P0CG48: UBC; NbExp=3; IntAct=EBI-749370, EBI-3390054;
CC Q9BSL1; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-749370, EBI-947187;
CC Q9BSL1; P09936: UCHL1; NbExp=3; IntAct=EBI-749370, EBI-714860;
CC Q9BSL1; O76024: WFS1; NbExp=3; IntAct=EBI-749370, EBI-720609;
CC Q9BSL1; Q96DA0: ZG16B; NbExp=3; IntAct=EBI-749370, EBI-953824;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10857748,
CC ECO:0000269|PubMed:15531880}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10857748}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC21559.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF176796; AAD51084.1; -; mRNA.
DR EMBL; AL355574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004967; AAH04967.1; -; mRNA.
DR EMBL; BC011822; AAH11822.1; -; mRNA.
DR EMBL; AF068195; AAC21559.1; ALT_INIT; mRNA.
DR CCDS; CCDS35177.1; -.
DR RefSeq; NP_057256.2; NM_016172.2.
DR PDB; 2DAI; NMR; -; A=172-241.
DR PDBsum; 2DAI; -.
DR AlphaFoldDB; Q9BSL1; -.
DR SMR; Q9BSL1; -.
DR BioGRID; 115691; 109.
DR CORUM; Q9BSL1; -.
DR DIP; DIP-47279N; -.
DR IntAct; Q9BSL1; 77.
DR MINT; Q9BSL1; -.
DR STRING; 9606.ENSP00000360821; -.
DR BindingDB; Q9BSL1; -.
DR GlyGen; Q9BSL1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BSL1; -.
DR PhosphoSitePlus; Q9BSL1; -.
DR BioMuta; UBAC1; -.
DR DMDM; 74752306; -.
DR EPD; Q9BSL1; -.
DR jPOST; Q9BSL1; -.
DR MassIVE; Q9BSL1; -.
DR MaxQB; Q9BSL1; -.
DR PaxDb; Q9BSL1; -.
DR PeptideAtlas; Q9BSL1; -.
DR PRIDE; Q9BSL1; -.
DR ProteomicsDB; 78913; -.
DR Antibodypedia; 18666; 209 antibodies from 28 providers.
DR DNASU; 10422; -.
DR Ensembl; ENST00000371756.4; ENSP00000360821.3; ENSG00000130560.9.
DR GeneID; 10422; -.
DR KEGG; hsa:10422; -.
DR MANE-Select; ENST00000371756.4; ENSP00000360821.3; NM_016172.3; NP_057256.2.
DR UCSC; uc004cgt.3; human.
DR CTD; 10422; -.
DR DisGeNET; 10422; -.
DR GeneCards; UBAC1; -.
DR HGNC; HGNC:30221; UBAC1.
DR HPA; ENSG00000130560; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 608129; gene.
DR neXtProt; NX_Q9BSL1; -.
DR OpenTargets; ENSG00000130560; -.
DR PharmGKB; PA162407814; -.
DR VEuPathDB; HostDB:ENSG00000130560; -.
DR eggNOG; ENOG502QQQ6; Eukaryota.
DR GeneTree; ENSGT00390000014658; -.
DR HOGENOM; CLU_035938_0_0_1; -.
DR InParanoid; Q9BSL1; -.
DR OMA; LHVCTME; -.
DR OrthoDB; 1163759at2759; -.
DR PhylomeDB; Q9BSL1; -.
DR TreeFam; TF324579; -.
DR PathwayCommons; Q9BSL1; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9BSL1; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 10422; 8 hits in 1081 CRISPR screens.
DR ChiTaRS; UBAC1; human.
DR EvolutionaryTrace; Q9BSL1; -.
DR GeneWiki; UBAC1; -.
DR GenomeRNAi; 10422; -.
DR Pharos; Q9BSL1; Tbio.
DR PRO; PR:Q9BSL1; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9BSL1; protein.
DR Bgee; ENSG00000130560; Expressed in gastrocnemius and 194 other tissues.
DR ExpressionAtlas; Q9BSL1; baseline and differential.
DR Genevisible; Q9BSL1; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd14303; UBA1_KPC2; 1.
DR CDD; cd14304; UBA2_KPC2; 1.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041926; UBA1_UBAC1.
DR InterPro; IPR041927; UBA2_UBAC1.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00627; UBA; 2.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00165; UBA; 2.
DR SUPFAM; SSF46934; SSF46934; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..405
FT /note="Ubiquitin-associated domain-containing protein 1"
FT /id="PRO_0000250449"
FT DOMAIN 14..98
FT /note="Ubiquitin-like"
FT DOMAIN 187..231
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 288..328
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 353..392
FT /note="STI1"
FT REGION 101..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VARIANT 374
FT /note="E -> D (in dbSNP:rs11103231)"
FT /id="VAR_027562"
FT CONFLICT 244
FT /note="Q -> R (in Ref. 4; AAC21559)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="Missing (in Ref. 1; AAD51084)"
FT /evidence="ECO:0000305"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:2DAI"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:2DAI"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:2DAI"
FT HELIX 221..230
FT /evidence="ECO:0007829|PDB:2DAI"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:2DAI"
SQ SEQUENCE 405 AA; 45338 MW; 5FC8EC84A8602CBE CRC64;
MFVQEEKIFA GKVLRLHICA SDGAEWLEEA TEDTSVEKLK ERCLKHCAHG SLEDPKSITH
HKLIHAASER VLSDARTILE ENIQDQDVLL LIKKRAPSPL PKMADVSAEE KKKQDQKAPD
KEAILRATAN LPSYNMDRAA VQTNMRDFQT ELRKILVSLI EVAQKLLALN PDAVELFKKA
NAMLDEDEDE RVDEAALRQL TEMGFPENRA TKALQLNHMS VPQAMEWLIE HAEDPTIDTP
LPGQAPPEAE GATAAASEAA AGASATDEEA RDELTEIFKK IRRKREFRAD ARAVISLMEM
GFDEKEVIDA LRVNNNQQNA ACEWLLGDRK PSPEELDKGI DPDSPLFQAI LDNPVVQLGL
TNPKTLLAFE DMLENPLNST QWMNDPETGP VMLQISRIFQ TLNRT
