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 27-MAR-2024, entry version 204. 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="https://atlasgeneticsoncology.org/gene/120/LRP"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 173. 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; 9606-ENSP00000378760; -. DR PeptideAtlas; Q14764; -. DR ProteomicsDB; 60157; -. DR Pumba; Q14764; -. DR Antibodypedia; 1032; 834 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 AGR; HGNC:7531; -. 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; 4582at2759; -. 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 1155 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 184 other cell types or tissues. DR ExpressionAtlas; Q14764; baseline and differential. 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:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. 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; 2.30.30.560; -; 2. DR Gene3D; 2.30.30.570; -; 2. DR Gene3D; 2.30.30.620; -; 1. DR Gene3D; 6.10.250.720; -; 1. DR Gene3D; 6.20.380.10; -; 1. DR Gene3D; 3.30.479.30; Band 7 domain; 1. DR Gene3D; 2.30.30.550; Major Vault Protein repeat; 4. 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; MAJOR VAULT PROTEIN; 1. DR PANTHER; PTHR14165:SF3; MAJOR VAULT PROTEIN; 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. DR Genevisible; Q14764; HS. 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 //