ID   UBAC1_RAT               Reviewed;         409 AA.
AC   Q5XIR9;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
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=Kip1 ubiquitination-promoting complex protein 2;
GN   Name=Ubac1; Synonyms=Kpc2, Ubadc1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
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 (By similarity). {ECO:0000250}.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; BC083603; AAH83603.1; -; mRNA.
DR   RefSeq; NP_001007743.1; NM_001007742.1.
DR   AlphaFoldDB; Q5XIR9; -.
DR   SMR; Q5XIR9; -.
DR   STRING; 10116.ENSRNOP00000024352; -.
DR   iPTMnet; Q5XIR9; -.
DR   PhosphoSitePlus; Q5XIR9; -.
DR   jPOST; Q5XIR9; -.
DR   PaxDb; Q5XIR9; -.
DR   PRIDE; Q5XIR9; -.
DR   Ensembl; ENSRNOT00000024352; ENSRNOP00000024352; ENSRNOG00000017983.
DR   GeneID; 362087; -.
DR   KEGG; rno:362087; -.
DR   UCSC; RGD:1359542; rat.
DR   CTD; 10422; -.
DR   RGD; 1359542; Ubac1.
DR   eggNOG; ENOG502QQQ6; Eukaryota.
DR   GeneTree; ENSGT00390000014658; -.
DR   HOGENOM; CLU_035938_0_0_1; -.
DR   InParanoid; Q5XIR9; -.
DR   OMA; LHVCTME; -.
DR   OrthoDB; 1163759at2759; -.
DR   PhylomeDB; Q5XIR9; -.
DR   TreeFam; TF324579; -.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q5XIR9; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000017983; Expressed in skeletal muscle tissue and 20 other tissues.
DR   Genevisible; Q5XIR9; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   Acetylation; Cytoplasm; Reference proteome; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN           1..409
FT                   /note="Ubiquitin-associated domain-containing protein 1"
FT                   /id="PRO_0000250451"
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          292..332
FT                   /note="UBA 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          357..396
FT                   /note="STI1"
FT   REGION          235..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BSL1"
SQ   SEQUENCE   409 AA;  45546 MW;  73FF7C00C0554929 CRC64;
     MFVQEEKIFA GKVLRLHICA ADGSEWLEEA TEDTSVEKLK ESCLKHGAHG SLEDPKNVTH
     HKLIHAASER VLSDSKTILE ENIQDQDVLL LIKKRAPSPI PKMADVSAEE KKKQEQKAPD
     KDAILRATAN LPACSTDRTA VQTTMRDFQT ELRKILVSLI EVAQKLLALN PDAVELFKKA
     NAMLDEDEDE RVDETALRQL TEMGFPESRA SKALRLNHMS VPQAMEWLIE HSEDPAIDTP
     LPGHAAQAEA SAAAATSSSS SEAAVGTSVE DEESRDELTE IFKKIRRKKE FRADARAVIS
     LMEMGFDEKE VIDALRVNNN QQNAACEWLL GDRKPSPEEL DQGIDPNSPL FQAILDNPVV
     QLGLTNPKTL LAFEDMLENP LNSTQWMNDP ETGPVMLQIS RIFQTLNRT