UBXN7_MOUSE
ID UBXN7_MOUSE Reviewed; 467 AA.
AC Q6P5G6; Q6ZQ44;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=UBX domain-containing protein 7;
GN Name=Ubxn7; Synonyms=Kiaa0794, Ubxd7;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-467.
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; SER-266 AND SER-373, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Ubiquitin-binding adapter that links a subset of NEDD8-
CC associated cullin ring ligases (CRLs) to the segregase VCP/p97, to
CC regulate turnover of their ubiquitination substrates (By similarity).
CC {ECO:0000250|UniProtKB:O94888}.
CC -!- SUBUNIT: Interacts with neddylated CUL2, ubiquitinated HIF1A, and
CC VCP/p97. {ECO:0000250|UniProtKB:O94888}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O94888}.
CC -!- DOMAIN: The UIM (ubiquitin-interacting motif) is required to engage the
CC NEDD8 modification on cullins. {ECO:0000250|UniProtKB:O94888}.
CC -!- DOMAIN: The UBX domain mediates interaction with VCP/p97.
CC {ECO:0000250|UniProtKB:O94888}.
CC -!- DOMAIN: The UBA domain is required for binding ubiquitinated-protein
CC substrates. {ECO:0000250|UniProtKB:O94888}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH62904.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC062904; AAH62904.1; ALT_INIT; mRNA.
DR EMBL; AK129218; BAC98028.1; -; mRNA.
DR RefSeq; XP_006522142.1; XM_006522079.3.
DR AlphaFoldDB; Q6P5G6; -.
DR SMR; Q6P5G6; -.
DR BioGRID; 230246; 31.
DR STRING; 10090.ENSMUSP00000110804; -.
DR iPTMnet; Q6P5G6; -.
DR EPD; Q6P5G6; -.
DR jPOST; Q6P5G6; -.
DR MaxQB; Q6P5G6; -.
DR PaxDb; Q6P5G6; -.
DR PeptideAtlas; Q6P5G6; -.
DR PRIDE; Q6P5G6; -.
DR ProteomicsDB; 298188; -.
DR Antibodypedia; 66084; 32 antibodies from 11 providers.
DR Ensembl; ENSMUST00000232137; ENSMUSP00000156376; ENSMUSG00000053774.
DR GeneID; 224111; -.
DR UCSC; uc007yyq.2; mouse.
DR CTD; 26043; -.
DR MGI; MGI:2146388; Ubxn7.
DR VEuPathDB; HostDB:ENSMUSG00000053774; -.
DR eggNOG; KOG0260; Eukaryota.
DR eggNOG; KOG1364; Eukaryota.
DR GeneTree; ENSGT00390000018687; -.
DR InParanoid; Q6P5G6; -.
DR PhylomeDB; Q6P5G6; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR BioGRID-ORCS; 224111; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ubxn7; mouse.
DR PRO; PR:Q6P5G6; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q6P5G6; protein.
DR Bgee; ENSMUSG00000053774; Expressed in cleaving embryo and 224 other tissues.
DR ExpressionAtlas; Q6P5G6; baseline and differential.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR006577; UAS.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR017346; UBX_7/2.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00789; UBX; 1.
DR PIRSF; PIRSF037991; UCP037991_UBX7/2; 1.
DR SMART; SM00594; UAS; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT CHAIN 2..467
FT /note="UBX domain-containing protein 7"
FT /id="PRO_0000211036"
FT DOMAIN 2..54
FT /note="UBA"
FT REPEAT 263..282
FT /note="ubiquitin-interacting motif (UIM)"
FT DOMAIN 386..463
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 57..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..346
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:O94888"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 84
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O94888"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O94888"
SQ SEQUENCE 467 AA; 52164 MW; B96E22396EA6B4FD CRC64;
MAAHGGSAAS SALKGLIQQF TAITGASESV GKHMLEACNN NLEMAVTMFL DGGGIAEEPS
TSSASVSTVR PHTEEEVRAP IPQKQEILVE PEPLFGVRQE QELRNGGAID KKLTTLADLF
RPPIDLMHKG SFETAKECGQ MQNKWLMINI QNVQDFACQC LNRDVWSNEA VKNIIREHFI
FWQVYHDSEE GQRYIQFYKL GDFPYVSILD PRTGQKLVEW HQLDVSSFLD QVTGFLGEHG
QLDGLSSSPP KKCARSESLI DASEDSQLEA AIRASLQETH FDSAQAKQDS RSDEESESEL
FSGSEEFISV CGSDEEEEVE NLAKSRKSPH KDLGHRKEEN RRPLTEPPAR TEPGTATNHQ
GLPSMDSEVL EMSPEKSDGI VEGIDVNGPK AQLMLRYPDG KREQITLPEQ AKLLALVKHV
QSKGYPNERF ELLTNFPRRK LSHLDYDITL QEAGLCPQET VFVQERN
