IF5_HUMAN
ID IF5_HUMAN Reviewed; 431 AA.
AC P55010; Q53XB3; Q9H5N2; Q9UG48;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Eukaryotic translation initiation factor 5;
DE Short=eIF-5;
GN Name=EIF5;
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=8663286; DOI=10.1074/jbc.271.28.16934;
RA Si K., Das K., Maitra U.;
RT "Characterization of multiple mRNAs that encode mammalian translation
RT initiation factor 5 (eIF-5).";
RL J. Biol. Chem. 271:16934-16938(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Uterus;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-229; SER-389; SER-390
RP AND SER-419, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-390, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-389; SER-390 AND
RP SER-419, AND IDENTIFICATION BY 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 [12]
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 [13]
RP INTERACTION WITH EIF2S2.
RX PubMed=21745818; DOI=10.1093/nar/gkr339;
RA Singh C.R., Watanabe R., Zhou D., Jennings M.D., Fukao A., Lee B.,
RA Ikeda Y., Chiorini J.A., Campbell S.G., Ashe M.P., Fujiwara T., Wek R.C.,
RA Pavitt G.D., Asano K.;
RT "Mechanisms of translational regulation by a human eIF5-mimic protein.";
RL Nucleic Acids Res. 39:8314-8328(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-390, AND
RP IDENTIFICATION BY 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-227; SER-229;
RP SER-389; SER-390; SER-410 AND SER-419, AND IDENTIFICATION BY MASS
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, 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 [17]
RP INTERACTION WITH FMR1.
RX PubMed=24658146; DOI=10.1371/journal.pone.0091465;
RA Taha M.S., Nouri K., Milroy L.G., Moll J.M., Herrmann C., Brunsveld L.,
RA Piekorz R.P., Ahmadian M.R.;
RT "Subcellular fractionation and localization studies reveal a direct
RT interaction of the fragile X mental retardation protein (FMRP) with
RT nucleolin.";
RL PLoS ONE 9:E91465-E91465(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-413 AND LYS-418, 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 [19]
RP STRUCTURE BY NMR OF 1-150.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the EIF-5_EIF-2B domain from human eukaryotic
RT translation initiation factor 5.";
RL Submitted (JAN-2008) to the PDB data bank.
RN [20]
RP VARIANT [LARGE SCALE ANALYSIS] MET-418.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Catalyzes the hydrolysis of GTP bound to the 40S ribosomal
CC initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent
CC joining of a 60S ribosomal subunit resulting in the release of eIF-2
CC and the guanine nucleotide. The subsequent joining of a 60S ribosomal
CC subunit results in the formation of a functional 80S initiation complex
CC (80S.mRNA.Met-tRNA[F]).
CC -!- SUBUNIT: Interacts with FMR1 isoform 6; this interaction occurs in a
CC RNA-dependent manner (PubMed:24658146). Interacts with EIF2S2
CC (PubMed:21745818). {ECO:0000269|PubMed:21745818,
CC ECO:0000269|PubMed:24658146}.
CC -!- INTERACTION:
CC P55010; Q9UNI6: DUSP12; NbExp=6; IntAct=EBI-286450, EBI-715161;
CC P55010; P42858: HTT; NbExp=3; IntAct=EBI-286450, EBI-466029;
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}.
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DR EMBL; U49436; AAC50572.1; -; mRNA.
DR EMBL; AL080102; CAB45711.1; -; mRNA.
DR EMBL; AK026933; BAB15593.1; -; mRNA.
DR EMBL; BX537367; CAD97610.1; -; mRNA.
DR EMBL; CH471061; EAW81809.1; -; Genomic_DNA.
DR EMBL; BC007728; AAH07728.1; -; mRNA.
DR EMBL; BC032866; AAH32866.1; -; mRNA.
DR CCDS; CCDS9980.1; -.
DR PIR; T12450; T12450.
DR RefSeq; NP_001960.2; NM_001969.4.
DR RefSeq; NP_892116.2; NM_183004.4.
DR PDB; 2E9H; NMR; -; A=1-150.
DR PDB; 2G2K; NMR; -; A=2-170.
DR PDB; 2IU1; X-ray; 1.80 A; A=232-431.
DR PDBsum; 2E9H; -.
DR PDBsum; 2G2K; -.
DR PDBsum; 2IU1; -.
DR AlphaFoldDB; P55010; -.
DR BMRB; P55010; -.
DR SMR; P55010; -.
DR BioGRID; 108298; 89.
DR IntAct; P55010; 22.
DR MINT; P55010; -.
DR STRING; 9606.ENSP00000216554; -.
DR GlyGen; P55010; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55010; -.
DR MetOSite; P55010; -.
DR PhosphoSitePlus; P55010; -.
DR SwissPalm; P55010; -.
DR BioMuta; EIF5; -.
DR DMDM; 27735202; -.
DR CPTAC; CPTAC-357; -.
DR CPTAC; CPTAC-358; -.
DR EPD; P55010; -.
DR jPOST; P55010; -.
DR MassIVE; P55010; -.
DR MaxQB; P55010; -.
DR PaxDb; P55010; -.
DR PeptideAtlas; P55010; -.
DR PRIDE; P55010; -.
DR ProteomicsDB; 56756; -.
DR TopDownProteomics; P55010; -.
DR Antibodypedia; 47; 268 antibodies from 33 providers.
DR DNASU; 1983; -.
DR Ensembl; ENST00000216554.8; ENSP00000216554.3; ENSG00000100664.11.
DR Ensembl; ENST00000392715.6; ENSP00000376477.2; ENSG00000100664.11.
DR Ensembl; ENST00000558506.1; ENSP00000453743.1; ENSG00000100664.11.
DR GeneID; 1983; -.
DR KEGG; hsa:1983; -.
DR MANE-Select; ENST00000216554.8; ENSP00000216554.3; NM_001969.5; NP_001960.2.
DR UCSC; uc001ymq.5; human.
DR CTD; 1983; -.
DR DisGeNET; 1983; -.
DR GeneCards; EIF5; -.
DR HGNC; HGNC:3299; EIF5.
DR HPA; ENSG00000100664; Low tissue specificity.
DR MIM; 601710; gene.
DR neXtProt; NX_P55010; -.
DR OpenTargets; ENSG00000100664; -.
DR PharmGKB; PA27725; -.
DR VEuPathDB; HostDB:ENSG00000100664; -.
DR eggNOG; KOG2767; Eukaryota.
DR GeneTree; ENSGT00390000016478; -.
DR HOGENOM; CLU_026663_1_0_1; -.
DR InParanoid; P55010; -.
DR OMA; YRYKMEK; -.
DR OrthoDB; 979826at2759; -.
DR PhylomeDB; P55010; -.
DR TreeFam; TF101533; -.
DR PathwayCommons; P55010; -.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; P55010; -.
DR SIGNOR; P55010; -.
DR BioGRID-ORCS; 1983; 751 hits in 1047 CRISPR screens.
DR ChiTaRS; EIF5; human.
DR EvolutionaryTrace; P55010; -.
DR GeneWiki; EIF5; -.
DR GenomeRNAi; 1983; -.
DR Pharos; P55010; Tbio.
DR PRO; PR:P55010; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P55010; protein.
DR Bgee; ENSG00000100664; Expressed in postcentral gyrus and 218 other tissues.
DR ExpressionAtlas; P55010; baseline and differential.
DR Genevisible; P55010; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0071074; F:eukaryotic initiation factor eIF2 binding; IBA:GO_Central.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0001732; P:formation of cytoplasmic translation initiation complex; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0006446; P:regulation of translational initiation; IDA:CACAO.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR InterPro; IPR003307; W2_domain.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR Pfam; PF02020; W2; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SMART; SM00515; eIF5C; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
DR PROSITE; PS51363; W2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; GTP-binding; Initiation factor; Isopeptide bond;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..431
FT /note="Eukaryotic translation initiation factor 5"
FT /id="PRO_0000212516"
FT DOMAIN 233..392
FT /note="W2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT REGION 143..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..191
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 227
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="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 390
FT /note="Phosphoserine"
FT /evidence="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 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 418
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 418
FT /note="K -> M (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036467"
FT CONFLICT 60
FT /note="E -> G (in Ref. 2; CAB45711)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="W -> S (in Ref. 1; AAC50572)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="K -> E (in Ref. 2; CAB45711)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="Q -> K (in Ref. 6; AAH32866)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2E9H"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2E9H"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:2E9H"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:2E9H"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:2E9H"
FT HELIX 39..45
FT /evidence="ECO:0007829|PDB:2E9H"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:2E9H"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2E9H"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:2E9H"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2E9H"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:2E9H"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:2E9H"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:2G2K"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:2E9H"
FT TURN 113..116
FT /evidence="ECO:0007829|PDB:2E9H"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:2E9H"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2E9H"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2E9H"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:2G2K"
FT HELIX 137..143
FT /evidence="ECO:0007829|PDB:2E9H"
FT HELIX 236..252
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 276..284
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 289..295
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 308..324
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 333..342
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 348..356
FT /evidence="ECO:0007829|PDB:2IU1"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 365..383
FT /evidence="ECO:0007829|PDB:2IU1"
FT HELIX 400..408
FT /evidence="ECO:0007829|PDB:2IU1"
SQ SEQUENCE 431 AA; 49223 MW; C6CCC3A255F9B9BC CRC64;
MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP TYPTKYFGCE
LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP ECENPETDLH VNPKKQTIGN
SCKACGYRGM LDTHHKLCTF ILKNPPENSD SGTGKKEKEK KNRKGKDKEN GSVSSSETPP
PPPPPNEINP PPHTMEEEED DDWGEDTTEE AQRRRMDEIS DHAKVLTLSD DLERTIEERV
NILFDFVKKK KEEGVIDSSD KEIVAEAERL DVKAMGPLVL TEVLFNEKIR EQIKKYRRHF
LRFCHNNKKA QRYLLHGLEC VVAMHQAQLI SKIPHILKEM YDADLLEEEV IISWSEKASK
KYVSKELAKE IRVKAEPFIK WLKEAEEESS GGEEEDEDEN IEVVYSKAAS VPKVETVKSD
NKDDDIDIDA I
