UBXN1_RAT
ID UBXN1_RAT Reviewed; 297 AA.
AC Q499N6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=UBX domain-containing protein 1;
DE AltName: Full=SAPK substrate protein 1;
GN Name=Ubxn1; Synonyms=Saks1;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
CC -!- FUNCTION: Ubiquitin-binding protein that interacts with the BRCA1-BARD1
CC heterodimer, and regulates its activity. Specifically binds 'Lys-6'-
CC linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1,
CC leads to inhibit the E3 ubiquitin-protein ligase activity of the BRCA1-
CC BARD1 heterodimer. Component of a complex required to couple
CC deglycosylation and proteasome-mediated degradation of misfolded
CC proteins in the endoplasmic reticulum that are retrotranslocated in the
CC cytosol (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a complex required to couple retrotranslocation,
CC ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP
CC and RAD23B. Interacts with HOMER2 (By similarity). Interacts directly
CC with VCP. Interacts with BRCA1 and BARD1; interaction takes place when
CC BRCA1 is not autoubiquitinated bur is strongly enhanced in the presence
CC of autoubiquitinated BRCA1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The UBA domain specifically recognizes and binds 'Lys-6'-linked
CC polyubiquitin chains. {ECO:0000250}.
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DR EMBL; AABR03002578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006231037.2; XM_006230975.2.
DR AlphaFoldDB; Q499N6; -.
DR SMR; Q499N6; -.
DR IntAct; Q499N6; 1.
DR STRING; 10116.ENSRNOP00000026651; -.
DR iPTMnet; Q499N6; -.
DR PhosphoSitePlus; Q499N6; -.
DR jPOST; Q499N6; -.
DR PaxDb; Q499N6; -.
DR PRIDE; Q499N6; -.
DR GeneID; 293719; -.
DR UCSC; RGD:1309471; rat.
DR CTD; 51035; -.
DR RGD; 1309471; Ubxn1.
DR VEuPathDB; HostDB:ENSRNOG00000019666; -.
DR eggNOG; KOG2689; Eukaryota.
DR HOGENOM; CLU_047594_1_0_1; -.
DR InParanoid; Q499N6; -.
DR OMA; AQHFPRK; -.
DR OrthoDB; 1297214at2759; -.
DR PhylomeDB; Q499N6; -.
DR TreeFam; TF313944; -.
DR Reactome; R-RNO-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR PRO; PR:Q499N6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019666; Expressed in quadriceps femoris and 20 other tissues.
DR Genevisible; Q499N6; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; ISO:RGD.
DR GO; GO:0071796; F:K6-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:RGD.
DR GO; GO:1904855; F:proteasome regulatory particle binding; ISO:RGD.
DR GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:1904293; P:negative regulation of ERAD pathway; ISO:RGD.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:1903094; P:negative regulation of protein K48-linked deubiquitination; ISO:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:2000157; P:negative regulation of ubiquitin-specific protease activity; ISO:RGD.
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 3: Inferred from homology;
KW Acetylation; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT CHAIN 2..297
FT /note="UBX domain-containing protein 1"
FT /id="PRO_0000248998"
FT DOMAIN 2..42
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 209..291
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 38..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..297
FT /note="Interaction with BRCA1"
FT /evidence="ECO:0000250"
FT COILED 86..172
FT /evidence="ECO:0000255"
FT COMPBIAS 84..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 200
FT /note="Phosphoserine; by MAPK12"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
SQ SEQUENCE 297 AA; 33582 MW; ABF2A4F385293DCA CRC64;
MAELTALESL IEMGFPRGRA EKALALTGNQ GIEAAMDWLM EHEDDPDVDE PLETPLSHIL
GREPTPSEQV GPEGSGSAAG ESKPVLTEEE RQEQTKRMLE LVAQKQRERE EREEREALER
EKQRRRQGQE LSAARQKLQE DEIRRAAEER RREKAEELAA RQRVREKIER DKAERAQKYG
GTVGSRSSPP ATDPGPVPSS PRQEPPTKRE YDQCRIQVRL PDGTSLTQTF RAREQLAAVR
LYVELHRGEE PGQDQDPVQL LSGFPRRAFS EADMERPLQE LGLVPSAVLI VAKKCPS
