ID   UBXN7_HUMAN             Reviewed;         489 AA.
AC   O94888; D3DXB3; Q6ZP77; Q86X20; Q8N327;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   27-MAR-2024, entry version 184.
DE   RecName: Full=UBX domain-containing protein 7;
GN   Name=UBXN7; Synonyms=KIAA0794, UBXD7;
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 [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA   Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XI. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 5:277-286(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-489.
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA   Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J.,
RA   Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT   "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT   network: indicating the involvement of ribonucleoside-diphosphate reductase
RT   M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT   transduction.";
RL   Mol. Cell. Proteomics 6:1952-1967(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 AND SER-288, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-288, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [15]
RP   FUNCTION, UIM MOTIF, UBA DOMAIN, MUTAGENESIS OF SER-288; SER-297 AND
RP   PRO-459, AND INTERACTION WITH CUL2; HIF1A AND VCP.
RX   PubMed=22537386; DOI=10.1186/1741-7007-10-36;
RA   Bandau S., Knebel A., Gage Z.O., Wood N.T., Alexandru G.;
RT   "UBXN7 docks on neddylated cullin complexes using its UIM motif and causes
RT   HIF1alpha accumulation.";
RL   BMC Biol. 10:36-36(2012).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-288 AND THR-306, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [17]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-84 AND LYS-134, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [18]
RP   STRUCTURE BY NMR OF 376-487.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the UBX domain of KIAA0794 protein.";
RL   Submitted (NOV-2004) to the PDB data bank.
RN   [19]
RP   STRUCTURE BY NMR OF 5-54.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the novel identified UBA-like domain in the N-
RT   terminal of human FAS associated factor 1 protein.";
RL   Submitted (JUN-2006) to the PDB data bank.
RN   [20]
RP   STRUCTURE BY NMR OF 131-270.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the UAS domain of human UBX domain-containing
RT   protein 7.";
RL   Submitted (OCT-2006) to the PDB data bank.
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.
CC       {ECO:0000269|PubMed:22537386}.
CC   -!- SUBUNIT: Interacts with neddylated CUL2, ubiquitinated HIF1A, and
CC       VCP/p97. {ECO:0000269|PubMed:22537386}.
CC   -!- INTERACTION:
CC       O94888; Q6UXS0: CLEC19A; NbExp=3; IntAct=EBI-1993627, EBI-12192919;
CC       O94888; O43186: CRX; NbExp=3; IntAct=EBI-1993627, EBI-748171;
CC       O94888; Q13616: CUL1; NbExp=8; IntAct=EBI-1993627, EBI-359390;
CC       O94888; Q13617: CUL2; NbExp=20; IntAct=EBI-1993627, EBI-456179;
CC       O94888; Q13618: CUL3; NbExp=6; IntAct=EBI-1993627, EBI-456129;
CC       O94888; Q13619: CUL4A; NbExp=7; IntAct=EBI-1993627, EBI-456106;
CC       O94888; Q13620: CUL4B; NbExp=3; IntAct=EBI-1993627, EBI-456067;
CC       O94888; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-1993627, EBI-3867333;
CC       O94888; Q15038: DAZAP2; NbExp=3; IntAct=EBI-1993627, EBI-724310;
CC       O94888; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-1993627, EBI-11978259;
CC       O94888; Q16665: HIF1A; NbExp=3; IntAct=EBI-1993627, EBI-447269;
CC       O94888; P50221: MEOX1; NbExp=3; IntAct=EBI-1993627, EBI-2864512;
CC       O94888; Q15843: NEDD8; NbExp=2; IntAct=EBI-1993627, EBI-716247;
CC       O94888; Q13952-2: NFYC; NbExp=3; IntAct=EBI-1993627, EBI-11956831;
CC       O94888; Q02548: PAX5; NbExp=3; IntAct=EBI-1993627, EBI-296331;
CC       O94888; P26367: PAX6; NbExp=3; IntAct=EBI-1993627, EBI-747278;
CC       O94888; Q04864-2: REL; NbExp=3; IntAct=EBI-1993627, EBI-10829018;
CC       O94888; Q9Y4K3: TRAF6; NbExp=3; IntAct=EBI-1993627, EBI-359276;
CC       O94888; Q9HCM9-2: TRIM39; NbExp=3; IntAct=EBI-1993627, EBI-11523450;
CC       O94888; Q9BVG3: TRIM62; NbExp=3; IntAct=EBI-1993627, EBI-6929619;
CC       O94888; Q9BZR9: TRIM8; NbExp=3; IntAct=EBI-1993627, EBI-2340370;
CC       O94888; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-1993627, EBI-741480;
CC       O94888; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-1993627, EBI-947187;
CC       O94888; P55072: VCP; NbExp=18; IntAct=EBI-1993627, EBI-355164;
CC       O94888; Q8ND25: ZNRF1; NbExp=5; IntAct=EBI-1993627, EBI-2129250;
CC       O94888; Q9WTX6: Cul1; Xeno; NbExp=3; IntAct=EBI-1993627, EBI-1551052;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22537386}.
CC   -!- DOMAIN: The UIM (ubiquitin-interacting motif) is required to engage the
CC       NEDD8 modification on cullins. {ECO:0000269|PubMed:22537386}.
CC   -!- DOMAIN: The UBX domain mediates interaction with VCP/p97.
CC       {ECO:0000269|PubMed:22537386}.
CC   -!- DOMAIN: The UBA domain is required for binding ubiquitinated-protein
CC       substrates. {ECO:0000269|PubMed:22537386}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA34514.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC85247.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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DR   EMBL; AB018337; BAA34514.1; ALT_INIT; mRNA.
DR   EMBL; AK129880; BAC85247.1; ALT_SEQ; mRNA.
DR   EMBL; CH471191; EAW53652.1; -; Genomic_DNA.
DR   EMBL; CH471191; EAW53654.1; -; Genomic_DNA.
DR   EMBL; BC028986; AAH28986.1; -; mRNA.
DR   CCDS; CCDS43191.1; -.
DR   RefSeq; NP_056377.1; NM_015562.1.
DR   PDB; 1WJ4; NMR; -; A=377-487.
DR   PDB; 2DAL; NMR; -; A=6-54.
DR   PDB; 2DLX; NMR; -; A=131-270.
DR   PDB; 5X3P; X-ray; 2.00 A; A/B/C=410-489.
DR   PDB; 5X4L; X-ray; 2.40 A; C/D=410-489.
DR   PDBsum; 1WJ4; -.
DR   PDBsum; 2DAL; -.
DR   PDBsum; 2DLX; -.
DR   PDBsum; 5X3P; -.
DR   PDBsum; 5X4L; -.
DR   AlphaFoldDB; O94888; -.
DR   SMR; O94888; -.
DR   BioGRID; 117507; 183.
DR   ComplexPortal; CPX-8101; VCP-NPL4-UFD1-UBXN7 AAA ATPase complex.
DR   DIP; DIP-47029N; -.
DR   IntAct; O94888; 68.
DR   STRING; 9606.ENSP00000296328; -.
DR   GlyGen; O94888; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O94888; -.
DR   MetOSite; O94888; -.
DR   PhosphoSitePlus; O94888; -.
DR   BioMuta; UBXN7; -.
DR   EPD; O94888; -.
DR   jPOST; O94888; -.
DR   MassIVE; O94888; -.
DR   MaxQB; O94888; -.
DR   PaxDb; 9606-ENSP00000296328; -.
DR   PeptideAtlas; O94888; -.
DR   ProteomicsDB; 50526; -.
DR   Pumba; O94888; -.
DR   Antibodypedia; 66084; 37 antibodies from 12 providers.
DR   DNASU; 26043; -.
DR   Ensembl; ENST00000296328.9; ENSP00000296328.4; ENSG00000163960.12.
DR   GeneID; 26043; -.
DR   KEGG; hsa:26043; -.
DR   MANE-Select; ENST00000296328.9; ENSP00000296328.4; NM_015562.2; NP_056377.1.
DR   UCSC; uc003fwm.5; human.
DR   AGR; HGNC:29119; -.
DR   CTD; 26043; -.
DR   DisGeNET; 26043; -.
DR   GeneCards; UBXN7; -.
DR   HGNC; HGNC:29119; UBXN7.
DR   HPA; ENSG00000163960; Low tissue specificity.
DR   MIM; 616379; gene.
DR   neXtProt; NX_O94888; -.
DR   OpenTargets; ENSG00000163960; -.
DR   PharmGKB; PA162408447; -.
DR   VEuPathDB; HostDB:ENSG00000163960; -.
DR   eggNOG; KOG0260; Eukaryota.
DR   eggNOG; KOG1364; Eukaryota.
DR   GeneTree; ENSGT00390000018687; -.
DR   HOGENOM; CLU_021255_3_0_1; -.
DR   InParanoid; O94888; -.
DR   OMA; CAFPRKS; -.
DR   OrthoDB; 5482878at2759; -.
DR   PhylomeDB; O94888; -.
DR   TreeFam; TF323635; -.
DR   PathwayCommons; O94888; -.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR   SignaLink; O94888; -.
DR   BioGRID-ORCS; 26043; 15 hits in 1172 CRISPR screens.
DR   ChiTaRS; UBXN7; human.
DR   EvolutionaryTrace; O94888; -.
DR   GenomeRNAi; 26043; -.
DR   Pharos; O94888; Tbio.
DR   PRO; PR:O94888; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; O94888; Protein.
DR   Bgee; ENSG00000163960; Expressed in endometrium epithelium and 204 other cell types or tissues.
DR   ExpressionAtlas; O94888; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IDA:BHF-UCL.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0043130; F:ubiquitin binding; IDA:BHF-UCL.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:BHF-UCL.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd02958; UAS; 1.
DR   CDD; cd14345; UBA_UBXD7; 1.
DR   CDD; cd01773; UBX_UBXN7; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   PANTHER; PTHR23322; FAS-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR23322:SF6; UBX DOMAIN-CONTAINING PROTEIN 7; 1.
DR   Pfam; PF13899; Thioredoxin_7; 1.
DR   Pfam; PF14555; UBA_4; 1.
DR   Pfam; PF00789; UBX; 1.
DR   PIRSF; PIRSF037991; UCP037991_UBX7/2; 1.
DR   SMART; SM00594; UAS; 1.
DR   SMART; SM00166; UBX; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50033; UBX; 1.
DR   Genevisible; O94888; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   CHAIN           2..489
FT                   /note="UBX domain-containing protein 7"
FT                   /id="PRO_0000211035"
FT   DOMAIN          2..54
FT                   /note="UBA"
FT   DOMAIN          285..304
FT                   /note="UIM"
FT   DOMAIN          408..485
FT                   /note="UBX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT   REGION          56..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        339..368
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         280
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         288
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17693683,
FT                   ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         306
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        84
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        99
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        134
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   MUTAGEN         288
FT                   /note="S->A,D: No effect on interactions with CUL2 and
FT                   HIF1A."
FT                   /evidence="ECO:0000269|PubMed:22537386"
FT   MUTAGEN         297
FT                   /note="S->A,H: Severely reduces interaction with neddylated
FT                   CUL2."
FT                   /evidence="ECO:0000269|PubMed:22537386"
FT   MUTAGEN         459
FT                   /note="P->G: Abolishes interaction with VCP/p97."
FT                   /evidence="ECO:0000269|PubMed:22537386"
FT   HELIX           11..23
FT                   /evidence="ECO:0007829|PDB:2DAL"
FT   HELIX           28..36
FT                   /evidence="ECO:0007829|PDB:2DAL"
FT   TURN            37..39
FT                   /evidence="ECO:0007829|PDB:2DAL"
FT   HELIX           42..51
FT                   /evidence="ECO:0007829|PDB:2DAL"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   HELIX           154..164
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   STRAND          167..173
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   TURN            177..179
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   HELIX           180..186
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   TURN            187..189
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   HELIX           191..199
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   STRAND          201..210
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   HELIX           211..220
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   STRAND          224..231
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   TURN            233..235
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   STRAND          240..244
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   HELIX           247..260
FT                   /evidence="ECO:0007829|PDB:2DLX"
FT   STRAND          412..418
FT                   /evidence="ECO:0007829|PDB:5X3P"
FT   STRAND          424..430
FT                   /evidence="ECO:0007829|PDB:5X3P"
FT   HELIX           435..444
FT                   /evidence="ECO:0007829|PDB:5X3P"
FT   TURN            449..451
FT                   /evidence="ECO:0007829|PDB:5X3P"
FT   STRAND          452..456
FT                   /evidence="ECO:0007829|PDB:5X3P"
FT   TURN            457..460
FT                   /evidence="ECO:0007829|PDB:5X3P"
FT   HELIX           463..465
FT                   /evidence="ECO:0007829|PDB:5X3P"
FT   STRAND          468..470
FT                   /evidence="ECO:0007829|PDB:1WJ4"
FT   HELIX           472..475
FT                   /evidence="ECO:0007829|PDB:5X3P"
FT   STRAND          479..487
FT                   /evidence="ECO:0007829|PDB:5X3P"
SQ   SEQUENCE   489 AA;  54862 MW;  3C894533B1A2C41A CRC64;
     MAAHGGSAAS SALKGLIQQF TTITGASESV GKHMLEACNN NLEMAVTMFL DGGGIAEEPS
     TSSASVSTVR PHTEEEVRAP IPQKQEILVE PEPLFGAPKR RRPARSIFDG FRDFQTETIR
     QEQELRNGGA IDKKLTTLAD LFRPPIDLMH KGSFETAKEC GQMQNKWLMI NIQNVQDFAC
     QCLNRDVWSN EAVKNIIREH FIFWQVYHDS EEGQRYIQFY KLGDFPYVSI LDPRTGQKLV
     EWHQLDVSSF LDQVTGFLGE HGQLDGLSSS PPKKCARSES LIDASEDSQL EAAIRASLQE
     THFDSTQTKQ DSRSDEESES ELFSGSEEFI SVCGSDEEEE VENLAKSRKS PHKDLGHRKE
     ENRRPLTEPP VRTDPGTATN HQGLPAVDSE ILEMPPEKAD GVVEGIDVNG PKAQLMLRYP
     DGKREQITLP EQAKLLALVK HVQSKGYPNE RFELLTNFPR RKLSHLDYDI TLQEAGLCPQ
     ETVFVQERN
//