RPN1_HUMAN
ID RPN1_HUMAN Reviewed; 607 AA.
AC P04843; B2R5Z0; D3DNB6; Q68DT1;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1 {ECO:0000305};
DE AltName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 67 kDa subunit;
DE AltName: Full=Ribophorin I;
DE Short=RPN-I;
DE AltName: Full=Ribophorin-1;
DE Flags: Precursor;
GN Name=RPN1 {ECO:0000312|HGNC:HGNC:10381};
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=3034581; DOI=10.1002/j.1460-2075.1987.tb04721.x;
RA Crimaudo C., Hortsch M., Gausepohl H., Meyer D.I.;
RT "Human ribophorins I and II: the primary structure and membrane topology of
RT two highly conserved rough endoplasmic reticulum-specific glycoproteins.";
RL EMBO J. 6:75-82(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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 MRNA].
RC TISSUE=Uterine endothelium;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix;
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 [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12887896; DOI=10.1016/s1097-2765(03)00243-0;
RA Kelleher D.J., Karaoglu D., Mandon E.C., Gilmore R.;
RT "Oligosaccharyltransferase isoforms that contain different catalytic STT3
RT subunits have distinct enzymatic properties.";
RL Mol. Cell 12:101-111(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-187, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
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 [12]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX PubMed=25135935; DOI=10.1083/jcb.201404083;
RA Cherepanova N.A., Shrimal S., Gilmore R.;
RT "Oxidoreductase activity is necessary for N-glycosylation of cysteine-
RT proximal acceptor sites in glycoproteins.";
RL J. Cell Biol. 206:525-539(2014).
RN [13]
RP IDENTIFICATION IN THE OLIGOSACCHARYLTRANSFERASE COMPLEX.
RX PubMed=23606741; DOI=10.1242/jcs.115410;
RA Dumax-Vorzet A., Roboti P., High S.;
RT "OST4 is a subunit of the mammalian oligosaccharyltransferase required for
RT efficient N-glycosylation.";
RL J. Cell Sci. 126:2595-2606(2013).
RN [14]
RP IDENTIFICATION BY 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-538, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP UFMYLATION.
RX PubMed=32160526; DOI=10.1016/j.cell.2020.02.017;
RA Liang J.R., Lingeman E., Luong T., Ahmed S., Muhar M., Nguyen T.,
RA Olzmann J.A., Corn J.E.;
RT "A genome-wide ER-phagy screen highlights key roles of mitochondrial
RT metabolism and ER-Resident UFMylation.";
RL Cell 180:1160-1177(2020).
RN [18] {ECO:0007744|PDB:6S7O, ECO:0007744|PDB:6S7T}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), IDENTIFICATION OF THE
RP OLIGOSACCHARYLTRANSFERASE (OST) COMPLEX, FUNCTION, AND PATHWAY.
RX PubMed=31831667; DOI=10.1126/science.aaz3505;
RA Ramirez A.S., Kowal J., Locher K.P.;
RT "Cryo-electron microscopy structures of human oligosaccharyltransferase
RT complexes OST-A and OST-B.";
RL Science 366:1372-1375(2019).
CC -!- FUNCTION: Subunit of the oligosaccharyl transferase (OST) complex that
CC catalyzes the initial transfer of a defined glycan
CC (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-
CC pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr
CC consensus motif in nascent polypeptide chains, the first step in
CC protein N-glycosylation (PubMed:31831667). N-glycosylation occurs
CC cotranslationally and the complex associates with the Sec61 complex at
CC the channel-forming translocon complex that mediates protein
CC translocation across the endoplasmic reticulum (ER). All subunits are
CC required for a maximal enzyme activity. {ECO:0000250|UniProtKB:E2RQ08,
CC ECO:0000269|PubMed:31831667}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:31831667}.
CC -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex
CC (PubMed:31831667). OST exists in two different complex forms which
CC contain common core subunits RPN1, RPN2, OST48, OST4, DAD1 and TMEM258,
CC either STT3A or STT3B as catalytic subunits, and form-specific
CC accessory subunits (PubMed:23606741, PubMed:25135935, PubMed:31831667).
CC STT3A complex assembly occurs through the formation of 3 subcomplexes.
CC Subcomplex 1 contains RPN1 and TMEM258, subcomplex 2 contains the
CC STT3A-specific subunits STT3A, DC2/OSTC, and KCP2 as well as the core
CC subunit OST4, and subcomplex 3 contains RPN2, DAD1, and OST48. The
CC STT3A complex can form stable complexes with the Sec61 complex or with
CC both the Sec61 and TRAP complexes (By similarity). Interacts with
CC TMEM35A/NACHO (By similarity). {ECO:0000250|UniProtKB:E2RQ08,
CC ECO:0000250|UniProtKB:Q91YQ5, ECO:0000269|PubMed:23606741,
CC ECO:0000269|PubMed:25135935, ECO:0000269|PubMed:31831667}.
CC -!- INTERACTION:
CC P04843; P49069: CAMLG; NbExp=3; IntAct=EBI-355963, EBI-1748958;
CC P04843; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-355963, EBI-11749135;
CC P04843; Q14165: MLEC; NbExp=2; IntAct=EBI-355963, EBI-1046466;
CC P04843; Q9H5K3: POMK; NbExp=2; IntAct=EBI-355963, EBI-11337900;
CC P04843; O43765: SGTA; NbExp=7; IntAct=EBI-355963, EBI-347996;
CC P04843; Q8TCJ2: STT3B; NbExp=2; IntAct=EBI-355963, EBI-2256290;
CC P04843; Q9UMX0: UBQLN1; NbExp=4; IntAct=EBI-355963, EBI-741480;
CC P04843; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-355963, EBI-10173939;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:E2RQ08, ECO:0000250|UniProtKB:Q9GMB0}.
CC Endoplasmic reticulum membrane; Single-pass type I membrane protein
CC {ECO:0000305}. Melanosome. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV.
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested.
CC {ECO:0000269|PubMed:12887896}.
CC -!- PTM: Ufmylated by UFL1 in response to endoplasmic reticulum stress,
CC promoting reticulophagy of endoplasmic reticulum sheets.
CC {ECO:0000269|PubMed:32160526}.
CC -!- SIMILARITY: Belongs to the OST1 family. {ECO:0000305}.
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DR EMBL; Y00281; CAA68392.1; -; mRNA.
DR EMBL; AK312369; BAG35287.1; -; mRNA.
DR EMBL; CR749284; CAH18139.1; -; mRNA.
DR EMBL; CH471052; EAW79306.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79307.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW79308.1; -; Genomic_DNA.
DR EMBL; BC010839; AAH10839.1; -; mRNA.
DR CCDS; CCDS3051.1; -.
DR PIR; A26168; A26168.
DR RefSeq; NP_002941.1; NM_002950.3.
DR PDB; 6S7O; EM; 3.50 A; E=1-607.
DR PDB; 6S7T; EM; 3.50 A; E=1-607.
DR PDBsum; 6S7O; -.
DR PDBsum; 6S7T; -.
DR AlphaFoldDB; P04843; -.
DR SMR; P04843; -.
DR BioGRID; 112099; 711.
DR ComplexPortal; CPX-5621; Oligosaccharyltransferase complex A.
DR ComplexPortal; CPX-5622; Oligosaccharyltransferase complex B.
DR CORUM; P04843; -.
DR DIP; DIP-38152N; -.
DR IntAct; P04843; 120.
DR MINT; P04843; -.
DR STRING; 9606.ENSP00000296255; -.
DR ChEMBL; CHEMBL4295697; -.
DR TCDB; 9.B.142.3.17; the integral membrane glycosyltransferase family 39 (gt39) family.
DR GlyConnect; 1186; 5 N-Linked glycans (1 site).
DR GlyGen; P04843; 2 sites, 5 N-linked glycans (1 site), 2 O-linked glycans (1 site).
DR iPTMnet; P04843; -.
DR PhosphoSitePlus; P04843; -.
DR SwissPalm; P04843; -.
DR BioMuta; RPN1; -.
DR DMDM; 132559; -.
DR CPTAC; CPTAC-125; -.
DR CPTAC; CPTAC-126; -.
DR EPD; P04843; -.
DR jPOST; P04843; -.
DR MassIVE; P04843; -.
DR MaxQB; P04843; -.
DR PaxDb; P04843; -.
DR PeptideAtlas; P04843; -.
DR PRIDE; P04843; -.
DR ProteomicsDB; 51749; -.
DR TopDownProteomics; P04843; -.
DR Antibodypedia; 4058; 572 antibodies from 30 providers.
DR DNASU; 6184; -.
DR Ensembl; ENST00000296255.8; ENSP00000296255.3; ENSG00000163902.12.
DR GeneID; 6184; -.
DR KEGG; hsa:6184; -.
DR MANE-Select; ENST00000296255.8; ENSP00000296255.3; NM_002950.4; NP_002941.1.
DR UCSC; uc003ekr.2; human.
DR CTD; 6184; -.
DR DisGeNET; 6184; -.
DR GeneCards; RPN1; -.
DR HGNC; HGNC:10381; RPN1.
DR HPA; ENSG00000163902; Low tissue specificity.
DR MalaCards; RPN1; -.
DR MIM; 180470; gene.
DR neXtProt; NX_P04843; -.
DR OpenTargets; ENSG00000163902; -.
DR Orphanet; 402020; Acute myeloid leukemia with inv(3)(q21q26.2) or t(3;3)(q21;q26.2).
DR PharmGKB; PA34777; -.
DR VEuPathDB; HostDB:ENSG00000163902; -.
DR eggNOG; KOG2291; Eukaryota.
DR GeneTree; ENSGT00390000009630; -.
DR InParanoid; P04843; -.
DR OMA; KTYMDTL; -.
DR OrthoDB; 1294725at2759; -.
DR PhylomeDB; P04843; -.
DR TreeFam; TF312988; -.
DR BRENDA; 2.4.99.18; 2681.
DR PathwayCommons; P04843; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-446203; Asparagine N-linked glycosylation.
DR Reactome; R-HSA-9694548; Maturation of spike protein.
DR SignaLink; P04843; -.
DR SIGNOR; P04843; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 6184; 612 hits in 1081 CRISPR screens.
DR ChiTaRS; RPN1; human.
DR GeneWiki; RPN1; -.
DR GenomeRNAi; 6184; -.
DR Pharos; P04843; Tbio.
DR PRO; PR:P04843; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P04843; protein.
DR Bgee; ENSG00000163902; Expressed in stromal cell of endometrium and 204 other tissues.
DR ExpressionAtlas; P04843; baseline and differential.
DR Genevisible; P04843; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0008250; C:oligosaccharyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB.
DR InterPro; IPR007676; Ribophorin_I.
DR PANTHER; PTHR21049; PTHR21049; 1.
DR Pfam; PF04597; Ribophorin_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Endoplasmic reticulum; Glycoprotein;
KW Isopeptide bond; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..23
FT CHAIN 24..607
FT /note="Dolichyl-diphosphooligosaccharide--protein
FT glycosyltransferase subunit 1"
FT /id="PRO_0000022241"
FT TOPO_DOM 24..438
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 187
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 538
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91YQ5"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CROSSLNK 538
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 43..57
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 126..137
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 214..219
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 242..251
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:6S7T"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 312..316
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 328..336
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 348..356
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 368..373
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 406..413
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 423..429
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 437..456
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 467..500
FT /evidence="ECO:0007829|PDB:6S7O"
FT TURN 506..508
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 509..533
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 541..564
FT /evidence="ECO:0007829|PDB:6S7O"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:6S7O"
FT HELIX 573..592
FT /evidence="ECO:0007829|PDB:6S7O"
SQ SEQUENCE 607 AA; 68569 MW; A2351A9CFABAEB6C CRC64;
MEAPAAGLFL LLLLGTWAPA PGSASSEAPP LINEDVKRTV DLSSHLAKVT AEVVLAHLGG
GSTSRATSFL LALEPELEAR LAHLGVQVKG EDEEENNLEV RETKIKGKSG RFFTVKLPVA
LDPGAKISVI VETVYTHVLH PYPTQITQSE KQFVVFEGNH YFYSPYPTKT QTMRVKLASR
NVESYTKLGN PTRSEDLLDY GPFRDVPAYS QDTFKVHYEN NSPFLTITSM TRVIEVSHWG
NIAVEENVDL KHTGAVLKGP FSRYDYQRQP DSGISSIRSF KTILPAAAQD VYYRDEIGNV
STSHLLILDD SVEMEIRPRF PLFGGWKTHY IVGYNLPSYE YLYNLGDQYA LKMRFVDHVF
DEQVIDSLTV KIILPEGAKN IEIDSPYEIS RAPDELHYTY LDTFGRPVIV AYKKNLVEQH
IQDIVVHYTF NKVLMLQEPL LVVAAFYILF FTVIIYVRLD FSITKDPAAE ARMKVACITE
QVLTLVNKRI GLYRHFDETV NRYKQSRDIS TLNSGKKSLE TEHKALTSEI ALLQSRLKTE
GSDLCDRVSE MQKLDAQVKE LVLKSAVEAE RLVAGKLKKD TYIENEKLIS GKRQELVTKI
DHILDAL
