UBXN7_HUMAN
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 03-AUG-2022, entry version 175.
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; 170.
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; O94888; -.
DR PeptideAtlas; O94888; -.
DR PRIDE; O94888; -.
DR ProteomicsDB; 50526; -.
DR Antibodypedia; 66084; 32 antibodies from 11 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 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; ICAFPRK; -.
DR OrthoDB; 1130151at2759; -.
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; 14 hits in 1082 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 203 other tissues.
DR ExpressionAtlas; O94888; baseline and differential.
DR Genevisible; O94888; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
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 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 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
