Full text data of UBAC1
UBAC1
(GBDR1, KPC2, UBADC1)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Ubiquitin-associated domain-containing protein 1; UBA domain-containing protein 1 (E3 ubiquitin-protein ligase subunit KPC2; Glialblastoma cell differentiation-related protein 1; Kip1 ubiquitination-promoting complex protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-associated domain-containing protein 1; UBA domain-containing protein 1 (E3 ubiquitin-protein ligase subunit KPC2; Glialblastoma cell differentiation-related protein 1; Kip1 ubiquitination-promoting complex protein 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BSL1
ID UBAC1_HUMAN Reviewed; 405 AA.
AC Q9BSL1; O75500; Q9UMW7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 109.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP 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
RT gene 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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
RT project: 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.,
RA Hatakeyama S., Yoshida M., Nakayama K., Nakayama K.;
RT "Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1)
RT at G1 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.,
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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal 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
CC cell cycle.
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.
CC Interacts with the proteasome via its N-terminal domain.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Contains 1 STI1 domain.
CC -!- SIMILARITY: Contains 2 UBA domains.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC21559.1; Type=Erroneous initiation;
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; AF176796; AAD51084.1; -; mRNA.
DR EMBL; AL355574; CAI14118.1; -; Genomic_DNA.
DR EMBL; BC004967; AAH04967.1; -; mRNA.
DR EMBL; BC011822; AAH11822.1; -; mRNA.
DR EMBL; AF068195; AAC21559.1; ALT_INIT; mRNA.
DR RefSeq; NP_057256.2; NM_016172.2.
DR UniGene; Hs.9194; -.
DR PDB; 2DAI; NMR; -; A=172-241.
DR PDBsum; 2DAI; -.
DR ProteinModelPortal; Q9BSL1; -.
DR SMR; Q9BSL1; 172-326.
DR DIP; DIP-47279N; -.
DR IntAct; Q9BSL1; 5.
DR STRING; 9606.ENSP00000360821; -.
DR MEROPS; C19.M01; -.
DR PhosphoSite; Q9BSL1; -.
DR DMDM; 74752306; -.
DR PaxDb; Q9BSL1; -.
DR PeptideAtlas; Q9BSL1; -.
DR PRIDE; Q9BSL1; -.
DR DNASU; 10422; -.
DR Ensembl; ENST00000371756; ENSP00000360821; ENSG00000130560.
DR GeneID; 10422; -.
DR KEGG; hsa:10422; -.
DR UCSC; uc004cgt.3; human.
DR CTD; 10422; -.
DR GeneCards; GC09M138824; -.
DR HGNC; HGNC:30221; UBAC1.
DR HPA; HPA005651; -.
DR MIM; 608129; gene.
DR neXtProt; NX_Q9BSL1; -.
DR PharmGKB; PA162407814; -.
DR eggNOG; NOG85584; -.
DR HOGENOM; HOG000231457; -.
DR HOVERGEN; HBG053148; -.
DR InParanoid; Q9BSL1; -.
DR KO; K12174; -.
DR OMA; HHKLIHA; -.
DR OrthoDB; EOG7060QJ; -.
DR PhylomeDB; Q9BSL1; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q9BSL1; -.
DR GeneWiki; UBAC1; -.
DR GenomeRNAi; 10422; -.
DR NextBio; 39500; -.
DR PRO; PR:Q9BSL1; -.
DR Bgee; Q9BSL1; -.
DR CleanEx; HS_UBAC1; -.
DR Genevestigator; Q9BSL1; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR000449; UBA/Ts_N.
DR Pfam; PF00627; UBA; 2.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00165; UBA; 2.
DR SUPFAM; SSF46934; SSF46934; 2.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS50053; UBIQUITIN_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; Polymorphism;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1 405 Ubiquitin-associated domain-containing
FT protein 1.
FT /FTId=PRO_0000250449.
FT DOMAIN 14 98 Ubiquitin-like.
FT DOMAIN 187 231 UBA 1.
FT DOMAIN 288 328 UBA 2.
FT DOMAIN 353 392 STI1.
FT MOD_RES 1 1 N-acetylmethionine.
FT VARIANT 374 374 E -> D (in dbSNP:rs11103231).
FT /FTId=VAR_027562.
FT CONFLICT 244 244 Q -> R (in Ref. 4; AAC21559).
FT CONFLICT 269 269 Missing (in Ref. 1; AAD51084).
FT STRAND 189 191
FT HELIX 194 203
FT HELIX 207 216
FT HELIX 221 230
FT HELIX 231 233
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
//
ID UBAC1_HUMAN Reviewed; 405 AA.
AC Q9BSL1; O75500; Q9UMW7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 109.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP 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
RT gene 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.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA 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.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA 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.,
RA Rogers J., 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
RT project: 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.,
RA Hatakeyama S., Yoshida M., Nakayama K., Nakayama K.;
RT "Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1)
RT at G1 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.,
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).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal 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
CC cell cycle.
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.
CC Interacts with the proteasome via its N-terminal domain.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Contains 1 STI1 domain.
CC -!- SIMILARITY: Contains 2 UBA domains.
CC -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC21559.1; Type=Erroneous initiation;
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; AF176796; AAD51084.1; -; mRNA.
DR EMBL; AL355574; CAI14118.1; -; Genomic_DNA.
DR EMBL; BC004967; AAH04967.1; -; mRNA.
DR EMBL; BC011822; AAH11822.1; -; mRNA.
DR EMBL; AF068195; AAC21559.1; ALT_INIT; mRNA.
DR RefSeq; NP_057256.2; NM_016172.2.
DR UniGene; Hs.9194; -.
DR PDB; 2DAI; NMR; -; A=172-241.
DR PDBsum; 2DAI; -.
DR ProteinModelPortal; Q9BSL1; -.
DR SMR; Q9BSL1; 172-326.
DR DIP; DIP-47279N; -.
DR IntAct; Q9BSL1; 5.
DR STRING; 9606.ENSP00000360821; -.
DR MEROPS; C19.M01; -.
DR PhosphoSite; Q9BSL1; -.
DR DMDM; 74752306; -.
DR PaxDb; Q9BSL1; -.
DR PeptideAtlas; Q9BSL1; -.
DR PRIDE; Q9BSL1; -.
DR DNASU; 10422; -.
DR Ensembl; ENST00000371756; ENSP00000360821; ENSG00000130560.
DR GeneID; 10422; -.
DR KEGG; hsa:10422; -.
DR UCSC; uc004cgt.3; human.
DR CTD; 10422; -.
DR GeneCards; GC09M138824; -.
DR HGNC; HGNC:30221; UBAC1.
DR HPA; HPA005651; -.
DR MIM; 608129; gene.
DR neXtProt; NX_Q9BSL1; -.
DR PharmGKB; PA162407814; -.
DR eggNOG; NOG85584; -.
DR HOGENOM; HOG000231457; -.
DR HOVERGEN; HBG053148; -.
DR InParanoid; Q9BSL1; -.
DR KO; K12174; -.
DR OMA; HHKLIHA; -.
DR OrthoDB; EOG7060QJ; -.
DR PhylomeDB; Q9BSL1; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q9BSL1; -.
DR GeneWiki; UBAC1; -.
DR GenomeRNAi; 10422; -.
DR NextBio; 39500; -.
DR PRO; PR:Q9BSL1; -.
DR Bgee; Q9BSL1; -.
DR CleanEx; HS_UBAC1; -.
DR Genevestigator; Q9BSL1; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR InterPro; IPR006636; STI1_HS-bd.
DR InterPro; IPR009060; UBA-like.
DR InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR InterPro; IPR000449; UBA/Ts_N.
DR Pfam; PF00627; UBA; 2.
DR SMART; SM00727; STI1; 1.
DR SMART; SM00165; UBA; 2.
DR SUPFAM; SSF46934; SSF46934; 2.
DR PROSITE; PS50030; UBA; 2.
DR PROSITE; PS50053; UBIQUITIN_2; FALSE_NEG.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm; Polymorphism;
KW Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1 405 Ubiquitin-associated domain-containing
FT protein 1.
FT /FTId=PRO_0000250449.
FT DOMAIN 14 98 Ubiquitin-like.
FT DOMAIN 187 231 UBA 1.
FT DOMAIN 288 328 UBA 2.
FT DOMAIN 353 392 STI1.
FT MOD_RES 1 1 N-acetylmethionine.
FT VARIANT 374 374 E -> D (in dbSNP:rs11103231).
FT /FTId=VAR_027562.
FT CONFLICT 244 244 Q -> R (in Ref. 4; AAC21559).
FT CONFLICT 269 269 Missing (in Ref. 1; AAD51084).
FT STRAND 189 191
FT HELIX 194 203
FT HELIX 207 216
FT HELIX 221 230
FT HELIX 231 233
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
//
MIM
608129
*RECORD*
*FIELD* NO
608129
*FIELD* TI
*608129 UBIQUITIN-ASSOCIATED DOMAIN-CONTAINING PROTEIN 1; UBAC1
;;UBA DOMAIN-CONTAINING PROTEIN 1;;
read moreGLIOBLASTOMA DIFFERENTIATION-RELATED PROTEIN 1; GBDR1;;
KIP1 UBIQUITINATION-PROMOTING COMPLEX 2; KPC2
*FIELD* TX
CLONING
By differential display analysis of untreated and EPO (133170)-treated
primary human microvascular endothelial cells (HMVECs), followed by
HMVEC cDNA library screening, Li et al. (2000) cloned GBDR1. The deduced
404-amino acid protein has a calculated molecular mass of about 44.4 kD.
GBDR1 contains a C-terminal helix-loop-helix motif and an SRC (190090)
homology-3 (SH3) domain. It has several putative phosphorylation sites,
including 8 CK2 (see 115440) sites, as well as 1 N-glycosylation site
and 2 N-myristoylation sites. The 5-prime untranslated region of the
transcript contains a CpG island, and the 3-prime region contains 2 mRNA
instability motifs. Northern blot analysis detected a 1.9-kb transcript
expressed in both resting and EPO-stimulated HMVECs and human umbilical
vein endothelial cells (HUVECs). Northern blot analysis of a
multiple-tissue panel detected ubiquitous GBDR1 expression, with highest
levels in heart and skeletal muscle and lowest level in lung. Western
blot analysis of HMVEC lysates detected GBDR1 at an apparent molecular
mass of about 46 kD. Cell fractionation revealed GBDR1 in the membrane
fraction, and detergent treatment indicated that GBDR1 associates with
nuclear membranes. In HMVECs, GBDR1 showed a punctate cytoplasmic
distribution and a variable number of nuclear speckles.
By searching an EST database for sequences similar to rabbit Kpc2,
followed by PCR of a human liver cDNA library, Kamura et al. (2004)
cloned UBAC1, which they called KPC2. The deduced protein contains an
N-terminal ubiquitin-like (UBL) domain and 2 C-terminal
ubiquitin-associated (UBA) domains.
GENE FUNCTION
Although differential screening indicated that GBDR1 was upregulated
following EPO treatment of HMVECs, Li et al. (2000) were unable to
confirm upregulation by Northern blot analysis. However, EPO treatment
increased the amount of GBDR1 in the nuclear compartment of
immunostained HMVECs. In vitro phosphorylation assays determined that
GBDR1 is a substrate for CK2, and Li et al. (2000) noted that 2 CK2
phosphorylation sites are near a putative nuclear localization signal.
Kamura et al. (2004) found that KPC2 interacted with the proteasome
through its UBL domain and with polyubiquitinated proteins through its
UBA domains. By immunoprecipitation analysis, they showed that
epitope-tagged KPC2 interacted directly with KPC1 (RNF123; 614472) and
that the complex exhibited pronounced E3 ubiquitin ligase activity
toward p27(KIP1) (CDKN1B; 600778), but not other substrates, in the
presence of E1 (UBA1; 314370), and E2 (UBCH5A, or UBE2D1; 602961)
enzymes. Both mono- and polyubiquitinated forms of p27(KIP1) were
detected, and polyubiquitination required either UBC4 (UBE2D2; 602962)
or UBCH5A. The E3 activity of KPC1 toward p27(KIP1) was greater in the
absence of PKC2. Overexpression and knockdown studies with mouse
fibroblasts revealed that the KPC complex functioned in the cytoplasm,
ubiquitinated p27(KIP1) during G1 phase of the cell cycle, and required
nuclear export of p27(KIP1) by Crm1 (XPO1; 602559).
MAPPING
By somatic cell hybrid analysis and Southern blot analysis, Li et al.
(2000) mapped the single-copy UBAC1 gene to chromosome 9.
Hartz (2011) mapped the UBAC1 gene to chromosome 9q34.3 based on an
alignment of the UBAC1 sequence (GenBank GENBANK AF068195) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/24/2011.
2. Kamura, T.; Hara, T.; Matsumoto, M.; Ishida, N.; Okumura, F.; Hatakeyama,
S.; Yoshida, M.; Nakayama, K.; Nakayama, K. I.: Cytoplasmic ubiquitin
ligase KPC regulates proteolysis of p27(Kip1) at G1 phase. Nature
Cell Biol. 6: 1229-1235, 2004.
3. Li, C.; Rodriguez, M.; Adamson, J. W.; Banerjee, D.: Identification
of a glialblastoma cell differentiation factor-related gene mRNA in
human microvascular endothelial cells. Genomics 65: 243-252, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 10/24/2011
*FIELD* CD
Patricia A. Hartz: 9/29/2003
*FIELD* ED
mgross: 02/06/2012
terry: 10/24/2011
alopez: 3/30/2009
mgross: 9/29/2003
*RECORD*
*FIELD* NO
608129
*FIELD* TI
*608129 UBIQUITIN-ASSOCIATED DOMAIN-CONTAINING PROTEIN 1; UBAC1
;;UBA DOMAIN-CONTAINING PROTEIN 1;;
read moreGLIOBLASTOMA DIFFERENTIATION-RELATED PROTEIN 1; GBDR1;;
KIP1 UBIQUITINATION-PROMOTING COMPLEX 2; KPC2
*FIELD* TX
CLONING
By differential display analysis of untreated and EPO (133170)-treated
primary human microvascular endothelial cells (HMVECs), followed by
HMVEC cDNA library screening, Li et al. (2000) cloned GBDR1. The deduced
404-amino acid protein has a calculated molecular mass of about 44.4 kD.
GBDR1 contains a C-terminal helix-loop-helix motif and an SRC (190090)
homology-3 (SH3) domain. It has several putative phosphorylation sites,
including 8 CK2 (see 115440) sites, as well as 1 N-glycosylation site
and 2 N-myristoylation sites. The 5-prime untranslated region of the
transcript contains a CpG island, and the 3-prime region contains 2 mRNA
instability motifs. Northern blot analysis detected a 1.9-kb transcript
expressed in both resting and EPO-stimulated HMVECs and human umbilical
vein endothelial cells (HUVECs). Northern blot analysis of a
multiple-tissue panel detected ubiquitous GBDR1 expression, with highest
levels in heart and skeletal muscle and lowest level in lung. Western
blot analysis of HMVEC lysates detected GBDR1 at an apparent molecular
mass of about 46 kD. Cell fractionation revealed GBDR1 in the membrane
fraction, and detergent treatment indicated that GBDR1 associates with
nuclear membranes. In HMVECs, GBDR1 showed a punctate cytoplasmic
distribution and a variable number of nuclear speckles.
By searching an EST database for sequences similar to rabbit Kpc2,
followed by PCR of a human liver cDNA library, Kamura et al. (2004)
cloned UBAC1, which they called KPC2. The deduced protein contains an
N-terminal ubiquitin-like (UBL) domain and 2 C-terminal
ubiquitin-associated (UBA) domains.
GENE FUNCTION
Although differential screening indicated that GBDR1 was upregulated
following EPO treatment of HMVECs, Li et al. (2000) were unable to
confirm upregulation by Northern blot analysis. However, EPO treatment
increased the amount of GBDR1 in the nuclear compartment of
immunostained HMVECs. In vitro phosphorylation assays determined that
GBDR1 is a substrate for CK2, and Li et al. (2000) noted that 2 CK2
phosphorylation sites are near a putative nuclear localization signal.
Kamura et al. (2004) found that KPC2 interacted with the proteasome
through its UBL domain and with polyubiquitinated proteins through its
UBA domains. By immunoprecipitation analysis, they showed that
epitope-tagged KPC2 interacted directly with KPC1 (RNF123; 614472) and
that the complex exhibited pronounced E3 ubiquitin ligase activity
toward p27(KIP1) (CDKN1B; 600778), but not other substrates, in the
presence of E1 (UBA1; 314370), and E2 (UBCH5A, or UBE2D1; 602961)
enzymes. Both mono- and polyubiquitinated forms of p27(KIP1) were
detected, and polyubiquitination required either UBC4 (UBE2D2; 602962)
or UBCH5A. The E3 activity of KPC1 toward p27(KIP1) was greater in the
absence of PKC2. Overexpression and knockdown studies with mouse
fibroblasts revealed that the KPC complex functioned in the cytoplasm,
ubiquitinated p27(KIP1) during G1 phase of the cell cycle, and required
nuclear export of p27(KIP1) by Crm1 (XPO1; 602559).
MAPPING
By somatic cell hybrid analysis and Southern blot analysis, Li et al.
(2000) mapped the single-copy UBAC1 gene to chromosome 9.
Hartz (2011) mapped the UBAC1 gene to chromosome 9q34.3 based on an
alignment of the UBAC1 sequence (GenBank GENBANK AF068195) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Hartz, P. A.: Personal Communication. Baltimore, Md. 10/24/2011.
2. Kamura, T.; Hara, T.; Matsumoto, M.; Ishida, N.; Okumura, F.; Hatakeyama,
S.; Yoshida, M.; Nakayama, K.; Nakayama, K. I.: Cytoplasmic ubiquitin
ligase KPC regulates proteolysis of p27(Kip1) at G1 phase. Nature
Cell Biol. 6: 1229-1235, 2004.
3. Li, C.; Rodriguez, M.; Adamson, J. W.; Banerjee, D.: Identification
of a glialblastoma cell differentiation factor-related gene mRNA in
human microvascular endothelial cells. Genomics 65: 243-252, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 10/24/2011
*FIELD* CD
Patricia A. Hartz: 9/29/2003
*FIELD* ED
mgross: 02/06/2012
terry: 10/24/2011
alopez: 3/30/2009
mgross: 9/29/2003