MVP_HUMAN
ID MVP_HUMAN Reviewed; 893 AA.
AC Q14764; Q96BG4; Q9BPW6; Q9BQT1; Q9UBD1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Major vault protein;
DE Short=MVP;
DE AltName: Full=Lung resistance-related protein;
GN Name=MVP; Synonyms=LRP;
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 [MRNA].
RX PubMed=7585126; DOI=10.1038/nm0695-578;
RA Scheffer G.L., Wijngaard P.L.J., Flens M.J., Izquierdo M.A., Slovak M.L.,
RA Pinedo H.M., Meijer C.J.L.M., Clevers H.C., Scheper R.J.;
RT "The drug resistance-related protein LRP is the human major vault
RT protein.";
RL Nat. Med. 1:578-582(1995).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Scheffer G.L.;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-169.
RX PubMed=11071864; DOI=10.1006/bbrc.2000.3782;
RA Lange C., Walther W., Schwabe H., Stein U.;
RT "Cloning and initial analysis of the human multidrug resistance-related
RT MVP/LRP gene promoter.";
RL Biochem. Biophys. Res. Commun. 278:125-133(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-65.
RC TISSUE=Lung cancer;
RX PubMed=11297743; DOI=10.1016/s0014-5793(01)02318-3;
RA Holzmann K., Ambrosch I., Elbling L., Micksche M., Berger W.;
RT "A small upstream open reading frame causes inhibition of human major vault
RT protein expression from a ubiquitous mRNA splice variant.";
RL FEBS Lett. 494:99-104(2001).
RN [6]
RP PROTEIN SEQUENCE OF 2-9; 68-82 AND 462-474, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Melanoma;
RA Quadroni M., Potts A., Barblan J., Bienvenut W.V.;
RL Submitted (JAN-2005) to UniProtKB.
RN [7]
RP ASSOCIATION WITH TEP1.
RX PubMed=10551828; DOI=10.1074/jbc.274.46.32712;
RA Kickhoefer V.A., Stephen A.G., Harrington L., Robinson M.O., Rome L.H.;
RT "Vaults and telomerase share a common subunit, TEP1.";
RL J. Biol. Chem. 274:32712-32717(1999).
RN [8]
RP INTERACTION WITH PTEN.
RX PubMed=12177006; DOI=10.1074/jbc.m207608200;
RA Yu Z., Fotouhi-Ardakani N., Wu L., Maoui M., Wang S., Banville D.,
RA Shen S.-H.;
RT "PTEN associates with the vault particles in HeLa cells.";
RL J. Biol. Chem. 277:40247-40252(2002).
RN [9]
RP PHOSPHORYLATION AT TYROSINE RESIDUES, IDENTIFICATION BY MASS SPECTROMETRY,
RP INTERACTION WITH PTPN11, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15133037; DOI=10.1074/jbc.m313955200;
RA Kolli S., Zito C.I., Mossink M.H., Wiemer E.A.C., Bennett A.M.;
RT "The major vault protein is a novel substrate for the tyrosine phosphatase
RT SHP-2 and scaffold protein in epidermal growth factor signaling.";
RL J. Biol. Chem. 279:29374-29385(2004).
RN [10]
RP INTERACTION WITH ZNF540.
RX PubMed=16815308; DOI=10.1016/j.bbrc.2006.06.076;
RA Xiang Z., Yuan W., Luo N., Wang Y., Tan K., Deng Y., Zhou X., Zhu C.,
RA Li Y., Liu M., Wu X., Li Y.;
RT "A novel human zinc finger protein ZNF540 interacts with MVP and inhibits
RT transcriptional activities of the ERK signal pathway.";
RL Biochem. Biophys. Res. Commun. 347:288-296(2006).
RN [11]
RP FUNCTION, INTERACTION WITH SRC, TYROSINE PHOSPHORYLATION, SUBCELLULAR
RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16441665; DOI=10.1111/j.1742-4658.2006.05112.x;
RA Kim E., Lee S., Mian M.F., Yun S.U., Song M., Yi K.-S., Ryu S.H.,
RA Suh P.-G.;
RT "Crosstalk between Src and major vault protein in epidermal growth factor-
RT dependent cell signalling.";
RL FEBS J. 273:793-804(2006).
RN [12]
RP INDUCTION, AND FUNCTION.
RX PubMed=16418217; DOI=10.1242/jcs.02773;
RA Steiner E., Holzmann K., Pirker C., Elbling L., Micksche M.,
RA Sutterluety H., Berger W.;
RT "The major vault protein is responsive to and interferes with interferon-
RT gamma-mediated STAT1 signals.";
RL J. Cell Sci. 119:459-469(2006).
RN [13]
RP INTERACTION WITH APEX1.
RX PubMed=18809583; DOI=10.1128/mcb.00244-08;
RA Chattopadhyay R., Das S., Maiti A.K., Boldogh I., Xie J., Hazra T.K.,
RA Kohno K., Mitra S., Bhakat K.K.;
RT "Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-mediated
RT activation of the multidrug resistance gene MDR1.";
RL Mol. Cell. Biol. 28:7066-7080(2008).
RN [14]
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 [15]
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 [16]
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=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
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=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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-444, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-444 AND LYS-704, 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 [21]
RP STRUCTURE BY NMR OF 113-221, AND INTERACTION WITH PARP4.
RX PubMed=16373071; DOI=10.1016/j.jmb.2005.11.064;
RA Kozlov G., Vavelyuk O., Minailiuc O., Banville D., Gehring K., Ekiel I.;
RT "Solution structure of a two-repeat fragment of major vault protein.";
RL J. Mol. Biol. 356:444-452(2006).
RN [22]
RP VARIANT GLU-87.
RX PubMed=28895081; DOI=10.1007/s12311-017-0883-4;
RA Kurihara M., Ishiura H., Sasaki T., Otsuka J., Hayashi T., Terao Y.,
RA Matsukawa T., Mitsui J., Kaneko J., Nishiyama K., Doi K., Yoshimura J.,
RA Morishita S., Shimizu J., Tsuji S.;
RT "Novel de novo KCND3 mutation in a Japanese patient with intellectual
RT disability, cerebellar ataxia, myoclonus, and dystonia.";
RL Cerebellum 17:237-242(2018).
CC -!- FUNCTION: Required for normal vault structure. Vaults are multi-subunit
CC structures that may act as scaffolds for proteins involved in signal
CC transduction. Vaults may also play a role in nucleo-cytoplasmic
CC transport. Down-regulates IFNG-mediated STAT1 signaling and subsequent
CC activation of JAK. Down-regulates SRC activity and signaling through
CC MAP kinases. {ECO:0000269|PubMed:15133037, ECO:0000269|PubMed:16418217,
CC ECO:0000269|PubMed:16441665}.
CC -!- SUBUNIT: The vault ribonucleoprotein particle is a huge (400 A x 670 A)
CC cage structure of 12.9 MDa. It consists of a dimer of half-vaults, with
CC each half-vault comprising 39 identical major vault protein (MVP)
CC chains, PARP4 and one or more vault RNAs (vRNAs). Interacts with TEP1.
CC Interacts with PTEN and activated MAPK1. The phosphorylated protein
CC interacts with the SH2 domains of PTPN11 and SRC. Interacts with APEX1.
CC May interact with ZNF540. {ECO:0000269|PubMed:12177006,
CC ECO:0000269|PubMed:15133037, ECO:0000269|PubMed:16373071,
CC ECO:0000269|PubMed:16441665, ECO:0000269|PubMed:16815308,
CC ECO:0000269|PubMed:18809583}.
CC -!- INTERACTION:
CC Q14764; Q86UW9: DTX2; NbExp=3; IntAct=EBI-2816254, EBI-740376;
CC Q14764; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-2816254, EBI-10242151;
CC Q14764; Q14764: MVP; NbExp=7; IntAct=EBI-2816254, EBI-2816254;
CC Q14764; Q16656-4: NRF1; NbExp=3; IntAct=EBI-2816254, EBI-11742836;
CC Q14764; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2816254, EBI-741158;
CC Q14764; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-2816254, EBI-74615;
CC Q14764; Q8WUN7: UBTD2; NbExp=3; IntAct=EBI-2816254, EBI-12867288;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15133037,
CC ECO:0000269|PubMed:16441665}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:16441665}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:16441665}. Note=5% found in the nuclear pore
CC complex (PubMed:15133037). Translocates from the nucleus to the
CC cytoplasm upon EGF treatment (PubMed:16441665).
CC -!- TISSUE SPECIFICITY: Present in most normal tissues. Higher expression
CC observed in epithelial cells with secretory and excretory functions, as
CC well as in cells chronically exposed to xenobiotics, such as bronchial
CC cells and cells lining the intestine. Overexpressed in many multidrug-
CC resistant cancer cells.
CC -!- INDUCTION: Up-regulated by IFNG/IFN-gamma.
CC {ECO:0000269|PubMed:16418217}.
CC -!- DOMAIN: MVP 3 mediates interaction with PTEN.
CC -!- DOMAIN: MVP 4 mediates interaction with PARP4.
CC -!- PTM: Phosphorylated on Tyr residues after EGF stimulation.
CC {ECO:0000269|PubMed:15133037}.
CC -!- PTM: Dephosphorylated by PTPN11.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LRPID120.html";
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DR EMBL; X79882; CAA56256.2; -; mRNA.
DR EMBL; BC015623; AAH15623.1; -; mRNA.
DR EMBL; AJ238512; CAB55354.1; -; Genomic_DNA.
DR EMBL; AJ238514; CAB55354.1; JOINED; Genomic_DNA.
DR EMBL; AJ238516; CAB55354.1; JOINED; Genomic_DNA.
DR EMBL; AJ238518; CAB55354.1; JOINED; Genomic_DNA.
DR EMBL; AJ238519; CAB55355.1; -; Genomic_DNA.
DR EMBL; AJ238514; CAB55355.1; JOINED; Genomic_DNA.
DR EMBL; AJ238516; CAB55355.1; JOINED; Genomic_DNA.
DR EMBL; AJ238518; CAB55355.1; JOINED; Genomic_DNA.
DR EMBL; AJ291365; CAC35313.1; -; Genomic_DNA.
DR EMBL; AJ291366; CAC35314.1; -; mRNA.
DR EMBL; AJ291367; CAC35316.1; -; mRNA.
DR CCDS; CCDS10656.1; -.
DR PIR; S57723; S57723.
DR RefSeq; NP_001280133.1; NM_001293204.1.
DR RefSeq; NP_001280134.1; NM_001293205.1.
DR RefSeq; NP_005106.2; NM_005115.4.
DR RefSeq; NP_059447.2; NM_017458.3.
DR PDB; 1Y7X; NMR; -; A=113-221.
DR PDBsum; 1Y7X; -.
DR AlphaFoldDB; Q14764; -.
DR SMR; Q14764; -.
DR BioGRID; 115286; 150.
DR IntAct; Q14764; 73.
DR MINT; Q14764; -.
DR STRING; 9606.ENSP00000378760; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; Q14764; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14764; -.
DR MetOSite; Q14764; -.
DR PhosphoSitePlus; Q14764; -.
DR SwissPalm; Q14764; -.
DR BioMuta; MVP; -.
DR DMDM; 21542417; -.
DR OGP; Q14764; -.
DR REPRODUCTION-2DPAGE; IPI00000105; -.
DR CPTAC; CPTAC-95; -.
DR CPTAC; CPTAC-96; -.
DR EPD; Q14764; -.
DR jPOST; Q14764; -.
DR MassIVE; Q14764; -.
DR PaxDb; Q14764; -.
DR PeptideAtlas; Q14764; -.
DR PRIDE; Q14764; -.
DR ProteomicsDB; 60157; -.
DR Antibodypedia; 1032; 742 antibodies from 41 providers.
DR DNASU; 9961; -.
DR Ensembl; ENST00000357402.10; ENSP00000349977.5; ENSG00000013364.19.
DR Ensembl; ENST00000395353.5; ENSP00000378760.1; ENSG00000013364.19.
DR GeneID; 9961; -.
DR KEGG; hsa:9961; -.
DR MANE-Select; ENST00000357402.10; ENSP00000349977.5; NM_005115.5; NP_005106.2.
DR CTD; 9961; -.
DR DisGeNET; 9961; -.
DR GeneCards; MVP; -.
DR HGNC; HGNC:7531; MVP.
DR HPA; ENSG00000013364; Low tissue specificity.
DR MIM; 605088; gene.
DR neXtProt; NX_Q14764; -.
DR OpenTargets; ENSG00000013364; -.
DR PharmGKB; PA31332; -.
DR VEuPathDB; HostDB:ENSG00000013364; -.
DR eggNOG; ENOG502QPP0; Eukaryota.
DR GeneTree; ENSGT00390000008969; -.
DR HOGENOM; CLU_016171_0_0_1; -.
DR InParanoid; Q14764; -.
DR OMA; VIRIKRY; -.
DR OrthoDB; 256008at2759; -.
DR PhylomeDB; Q14764; -.
DR TreeFam; TF329353; -.
DR PathwayCommons; Q14764; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q14764; -.
DR BioGRID-ORCS; 9961; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; MVP; human.
DR EvolutionaryTrace; Q14764; -.
DR GeneWiki; Major_vault_protein; -.
DR GenomeRNAi; 9961; -.
DR Pharos; Q14764; Tbio.
DR PRO; PR:Q14764; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q14764; protein.
DR Bgee; ENSG00000013364; Expressed in mucosa of transverse colon and 182 other tissues.
DR ExpressionAtlas; Q14764; baseline and differential.
DR Genevisible; Q14764; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IDA:UniProtKB.
DR GO; GO:0038127; P:ERBB signaling pathway; IDA:UniProtKB.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd08825; MVP_shoulder; 1.
DR Gene3D; 2.30.30.550; -; 4.
DR Gene3D; 2.30.30.560; -; 2.
DR Gene3D; 3.30.479.30; -; 1.
DR InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR InterPro; IPR039059; MVP.
DR InterPro; IPR041139; MVP_rep_dom.
DR InterPro; IPR043023; MVP_rep_sf.
DR InterPro; IPR021870; MVP_shoulder.
DR InterPro; IPR041134; Vault_2.
DR InterPro; IPR043179; Vault_2_sf.
DR InterPro; IPR040989; Vault_3.
DR InterPro; IPR041136; Vault_4.
DR InterPro; IPR002499; Vault_N.
DR PANTHER; PTHR14165; PTHR14165; 1.
DR Pfam; PF11978; MVP_shoulder; 1.
DR Pfam; PF01505; Vault; 4.
DR Pfam; PF17794; Vault_2; 2.
DR Pfam; PF17795; Vault_3; 1.
DR Pfam; PF17796; Vault_4; 1.
DR PROSITE; PS51224; MVP; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Ribonucleoprotein; Translocation; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..893
FT /note="Major vault protein"
FT /id="PRO_0000158980"
FT REPEAT 2..56
FT /note="MVP 1"
FT REPEAT 57..111
FT /note="MVP 2"
FT REPEAT 112..164
FT /note="MVP 3"
FT REPEAT 165..217
FT /note="MVP 4"
FT REPEAT 218..272
FT /note="MVP 5"
FT REPEAT 273..323
FT /note="MVP 6"
FT REPEAT 324..379
FT /note="MVP 7"
FT REPEAT 380..457
FT /note="MVP 8"
FT REPEAT 458..520
FT /note="MVP 9"
FT REGION 856..893
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 704
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 87
FT /note="D -> E"
FT /evidence="ECO:0000269|PubMed:28895081"
FT /id="VAR_079710"
FT VARIANT 635
FT /note="V -> I (in dbSNP:rs35916172)"
FT /id="VAR_050179"
FT VARIANT 651
FT /note="R -> Q (in dbSNP:rs3764944)"
FT /id="VAR_050180"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:1Y7X"
FT STRAND 137..139
FT /evidence="ECO:0007829|PDB:1Y7X"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:1Y7X"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1Y7X"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:1Y7X"
FT STRAND 170..181
FT /evidence="ECO:0007829|PDB:1Y7X"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1Y7X"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1Y7X"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:1Y7X"
SQ SEQUENCE 893 AA; 99327 MW; 6FEE5545B0A3FE65 CRC64;
MATEEFIIRI PPYHYIHVLD QNSNVSRVEV GPKTYIRQDN ERVLFAPMRM VTVPPRHYCT
VANPVSRDAQ GLVLFDVTGQ VRLRHADLEI RLAQDPFPLY PGEVLEKDIT PLQVVLPNTA
LHLKALLDFE DKDGDKVVAG DEWLFEGPGT YIPRKEVEVV EIIQATIIRQ NQALRLRARK
ECWDRDGKER VTGEEWLVTT VGAYLPAVFE EVLDLVDAVI LTEKTALHLR ARRNFRDFRG
VSRRTGEEWL VTVQDTEAHV PDVHEEVLGV VPITTLGPHN YCVILDPVGP DGKNQLGQKR
VVKGEKSFFL QPGEQLEQGI QDVYVLSEQQ GLLLRALQPL EEGEDEEKVS HQAGDHWLIR
GPLEYVPSAK VEVVEERQAI PLDENEGIYV QDVKTGKVRA VIGSTYMLTQ DEVLWEKELP
PGVEELLNKG QDPLADRGEK DTAKSLQPLA PRNKTRVVSY RVPHNAAVQV YDYREKRARV
VFGPELVSLG PEEQFTVLSL SAGRPKRPHA RRALCLLLGP DFFTDVITIE TADHARLQLQ
LAYNWHFEVN DRKDPQETAK LFSVPDFVGD ACKAIASRVR GAVASVTFDD FHKNSARIIR
TAVFGFETSE AKGPDGMALP RPRDQAVFPQ NGLVVSSVDV QSVEPVDQRT RDALQRSVQL
AIEITTNSQE AAAKHEAQRL EQEARGRLER QKILDQSEAE KARKELLELE ALSMAVESTG
TAKAEAESRA EAARIEGEGS VLQAKLKAQA LAIETEAELQ RVQKVRELEL VYARAQLELE
VSKAQQLAEV EVKKFKQMTE AIGPSTIRDL AVAGPEMQVK LLQSLGLKST LITDGSTPIN
LFNTAFGLLG MGPEGQPLGR RVASGPSPGE GISPQSAQAP QAPGDNHVVP VLR
