RRBP1_HUMAN
ID RRBP1_HUMAN Reviewed; 1410 AA.
AC Q9P2E9; A0A0A0MRV0; A2A2S6; A6NCN6; O75300; O75301; Q5W165; Q96SB2; Q9BWP1;
AC Q9H476;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 5.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Ribosome-binding protein 1;
DE AltName: Full=180 kDa ribosome receptor homolog;
DE Short=RRp;
DE AltName: Full=ES/130-related protein;
DE AltName: Full=Ribosome receptor protein;
GN Name=RRBP1; Synonyms=KIAA1398;
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] (ISOFORM 2).
RX PubMed=9628588; DOI=10.1089/dna.1998.17.449;
RA Langley R., Leung E., Morris C., Berg R., McDonald M., Weaver A., Parry D.,
RA Ni J., Su J., Gentz R., Spurr N., Krissansen G.W.;
RT "Identification of multiple forms of 180-kDa ribosome receptor in human
RT cells.";
RL DNA Cell Biol. 17:449-460(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 413-1211 (ISOFORM 1).
RC TISSUE=Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 756-1410.
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-225; THR-245; THR-255;
RP SER-583 AND SER-615, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615; SER-1276 AND SER-1277,
RP AND 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-225; THR-235; THR-245;
RP THR-255; SER-533 AND SER-615, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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-583; SER-615 AND SER-978, 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-615 AND SER-959, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573; SER-615; SER-900;
RP SER-959 AND SER-1277, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-620, 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 [18]
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 [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: Acts as a ribosome receptor and mediates interaction between
CC the ribosome and the endoplasmic reticulum membrane. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass type III membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist. Additional isoforms may
CC derive from alternative splicing in the repeat region.
CC {ECO:0000269|PubMed:9628588};
CC Name=1;
CC IsoId=Q9P2E9-1; Sequence=Displayed;
CC Name=2; Synonyms=ES130;
CC IsoId=Q9P2E9-3; Sequence=VSP_003949, VSP_003950;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92636.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF006751; AAC25977.1; -; mRNA.
DR EMBL; AF007575; AAC25978.1; -; mRNA.
DR EMBL; AB037819; BAA92636.2; ALT_INIT; mRNA.
DR EMBL; AL132765; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF456852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL833822; CAD38684.1; -; mRNA.
DR EMBL; BC000099; AAH00099.4; -; mRNA.
DR CCDS; CCDS13128.1; -. [Q9P2E9-3]
DR RefSeq; NP_001036041.1; NM_001042576.1. [Q9P2E9-3]
DR RefSeq; NP_004578.2; NM_004587.2. [Q9P2E9-3]
DR AlphaFoldDB; Q9P2E9; -.
DR SMR; Q9P2E9; -.
DR BioGRID; 112152; 215.
DR IntAct; Q9P2E9; 86.
DR MINT; Q9P2E9; -.
DR DrugBank; DB12339; Radezolid.
DR GlyGen; Q9P2E9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P2E9; -.
DR MetOSite; Q9P2E9; -.
DR PhosphoSitePlus; Q9P2E9; -.
DR SwissPalm; Q9P2E9; -.
DR BioMuta; RRBP1; -.
DR DMDM; 23822112; -.
DR EPD; Q9P2E9; -.
DR jPOST; Q9P2E9; -.
DR MassIVE; Q9P2E9; -.
DR MaxQB; Q9P2E9; -.
DR PaxDb; Q9P2E9; -.
DR PeptideAtlas; Q9P2E9; -.
DR PRIDE; Q9P2E9; -.
DR ProteomicsDB; 83798; -. [Q9P2E9-1]
DR ProteomicsDB; 83800; -. [Q9P2E9-3]
DR Antibodypedia; 2409; 255 antibodies from 30 providers.
DR DNASU; 6238; -.
DR Ensembl; ENST00000246043.8; ENSP00000246043.4; ENSG00000125844.17. [Q9P2E9-1]
DR Ensembl; ENST00000360807.8; ENSP00000354045.4; ENSG00000125844.17. [Q9P2E9-3]
DR Ensembl; ENST00000377807.6; ENSP00000367038.2; ENSG00000125844.17. [Q9P2E9-3]
DR Ensembl; ENST00000377813.6; ENSP00000367044.1; ENSG00000125844.17. [Q9P2E9-1]
DR GeneID; 6238; -.
DR KEGG; hsa:6238; -.
DR MANE-Select; ENST00000377813.6; ENSP00000367044.1; NM_001365613.2; NP_001352542.1.
DR UCSC; uc002wpu.4; human.
DR UCSC; uc002wpv.1; human. [Q9P2E9-1]
DR CTD; 6238; -.
DR DisGeNET; 6238; -.
DR GeneCards; RRBP1; -.
DR HGNC; HGNC:10448; RRBP1.
DR HPA; ENSG00000125844; Tissue enhanced (pancreas).
DR MIM; 601418; gene.
DR neXtProt; NX_Q9P2E9; -.
DR OpenTargets; ENSG00000125844; -.
DR PharmGKB; PA34863; -.
DR VEuPathDB; HostDB:ENSG00000125844; -.
DR eggNOG; ENOG502QV05; Eukaryota.
DR GeneTree; ENSGT00940000158015; -.
DR HOGENOM; CLU_005662_1_0_1; -.
DR InParanoid; Q9P2E9; -.
DR OMA; REQNGPA; -.
DR OrthoDB; 327650at2759; -.
DR PhylomeDB; Q9P2E9; -.
DR TreeFam; TF333579; -.
DR PathwayCommons; Q9P2E9; -.
DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants.
DR SignaLink; Q9P2E9; -.
DR BioGRID-ORCS; 6238; 15 hits in 1083 CRISPR screens.
DR ChiTaRS; RRBP1; human.
DR GeneWiki; RRBP1; -.
DR GenomeRNAi; 6238; -.
DR Pharos; Q9P2E9; Tbio.
DR PRO; PR:Q9P2E9; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9P2E9; protein.
DR Bgee; ENSG00000125844; Expressed in body of pancreas and 209 other tissues.
DR ExpressionAtlas; Q9P2E9; baseline and differential.
DR Genevisible; Q9P2E9; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005840; C:ribosome; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR InterPro; IPR007794; Rib_rcpt_KP.
DR InterPro; IPR040248; RRBP1.
DR PANTHER; PTHR18939; PTHR18939; 2.
DR Pfam; PF05104; Rib_recp_KP_reg; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Endoplasmic reticulum; Isopeptide bond;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..1410
FT /note="Ribosome-binding protein 1"
FT /id="PRO_0000097441"
FT TOPO_DOM 1..7
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..1410
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 197..206
FT /note="1"
FT REPEAT 207..216
FT /note="2"
FT REPEAT 217..226
FT /note="3"
FT REPEAT 227..236
FT /note="4"
FT REPEAT 237..246
FT /note="5"
FT REPEAT 247..256
FT /note="6"
FT REPEAT 257..266
FT /note="7"
FT REPEAT 267..276
FT /note="8"
FT REPEAT 277..286
FT /note="9"
FT REPEAT 287..296
FT /note="10"
FT REPEAT 297..306
FT /note="11"
FT REPEAT 307..316
FT /note="12"
FT REPEAT 317..326
FT /note="13"
FT REPEAT 327..336
FT /note="14"
FT REPEAT 337..346
FT /note="15"
FT REPEAT 347..356
FT /note="16"
FT REPEAT 357..366
FT /note="17"
FT REPEAT 367..376
FT /note="18"
FT REPEAT 377..386
FT /note="19"
FT REPEAT 387..396
FT /note="20"
FT REPEAT 397..406
FT /note="21"
FT REPEAT 407..416
FT /note="22"
FT REPEAT 417..426
FT /note="23"
FT REPEAT 427..436
FT /note="24"
FT REPEAT 437..446
FT /note="25"
FT REPEAT 447..456
FT /note="26"
FT REPEAT 457..466
FT /note="27"
FT REPEAT 467..476
FT /note="28"
FT REPEAT 477..486
FT /note="29"
FT REPEAT 487..496
FT /note="30"
FT REPEAT 497..506
FT /note="31"
FT REPEAT 507..516
FT /note="32"
FT REPEAT 517..526
FT /note="33"
FT REPEAT 527..534
FT /note="34; approximate"
FT REPEAT 535..544
FT /note="35"
FT REPEAT 545..554
FT /note="36; approximate"
FT REPEAT 555..564
FT /note="37"
FT REPEAT 565..574
FT /note="38"
FT REPEAT 575..584
FT /note="39; approximate"
FT REPEAT 585..594
FT /note="40"
FT REPEAT 595..604
FT /note="41"
FT REGION 44..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..604
FT /note="41 X 10 AA approximate tandem repeats of [TN]-Q-
FT [GSA]-[KRQT]-K-[ATGSV]-[ED]-[GTAS]-[ATIS]-[PQTAS]"
FT REGION 895..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1330..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..616
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..921
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1378..1403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PL5"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99PL5"
FT MOD_RES 225
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 245
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 255
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 932
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99PL5"
FT MOD_RES 959
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 620
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 177..606
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9628588"
FT /id="VSP_003949"
FT VAR_SEQ 635..637
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9628588"
FT /id="VSP_003950"
FT VARIANT 1324
FT /note="R -> L (in dbSNP:rs1132274)"
FT /id="VAR_056982"
FT CONFLICT 350
FT /note="K -> KKTEEAQKQGKKAEGAQIQGKKNEGAQTQGKKAEGAQNQGKKNEGAQ
FT TQGKKAEGAQTQGKKADGAQNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQGKKADGA
FT QNQGKKAEGAQNQGKKAEGAQNQGT (in Ref. 1; AAC25978)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="Q -> QNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQGKKAEGAQNQDKKA
FT EGAQNQGRKAEGAQNQGRKAEGAQNQGKKAEGAPNQGKKAEGAPNQGKKAEGTPNQGKK
FT AEGTPNQGKKAEGTPNQGKKAEGAQNQGKKAEGAQNQGKKAEGTP (in Ref. 2;
FT BAA92636)"
FT /evidence="ECO:0000305"
FT CONFLICT 1043
FT /note="L -> H (in Ref. 1; AAC25977, 2; BAA92636, 5;
FT CAD38684 and 6; AAH00099)"
FT /evidence="ECO:0000305"
FT CONFLICT 1057
FT /note="C -> R (in Ref. 5; CAD38684)"
FT /evidence="ECO:0000305"
FT CONFLICT 1073
FT /note="E -> K (in Ref. 5; CAD38684)"
FT /evidence="ECO:0000305"
FT CONFLICT 1199
FT /note="S -> L (in Ref. 2; BAA92636, 5; CAD38684 and 6;
FT AAH00099)"
FT /evidence="ECO:0000305"
FT CONFLICT 1312
FT /note="T -> M (in Ref. 1; AAC25977)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1410 AA; 152456 MW; 76E5D15D01D4B66B CRC64;
MDIYDTQTLG VVVFGGFMVV SAIGIFLVST FSMKETSYEE ALANQRKEMA KTHHQKVEKK
KKEKTVEKKG KTKKKEEKPN GKIPDHDPAP NVTVLLREPV RAPAVAVAPT PVQPPIIVAP
VATVPAMPQE KLASSPKDKK KKEKKVAKVE PAVSSVVNSI QVLTSKAAIL ETAPKEVPMV
VVPPVGAKGN TPATGTTQGK KAEGTQNQSK KAEGAPNQGR KAEGTPNQGK KTEGTPNQGK
KAEGTPNQGK KAEGTPNQGK KAEGAQNQGK KVDTTPNQGK KVEGAPTQGR KAEGAQNQAK
KVEGAQNQGK KAEGAQNQGK KGEGAQNQGK KAEGAQNQGK KAEGAQNQGK KAEGAQNQGK
KAEGAQNQGK KAEGAQNQGK KAEGAQNQGK KVEGAQNQGK KAEGAQNQGK KAEGAQNQGK
KAEGAQNQGK KAEGAQNQGK KAEGAQNQGK KAEGAQNQGK KAEGAQNQGK KVEGAQNQGK
KAEGAQNQGK KAEGAQNQGK KAEGAQNQGQ KGEGAQNQGK KTEGAQGKKA ERSPNQGKKG
EGAPIQGKKA DSVANQGTKV EGITNQGKKA EGSPSEGKKA EGSPNQGKKA DAAANQGKKT
ESASVQGRNT DVAQSPEAPK QEAPAKKKSG SKKKGEPGPP DADGPLYLPY KTLVSTVGSM
VFNEGEAQRL IEILSEKAGI IQDTWHKATQ KGDPVAILKR QLEEKEKLLA TEQEDAAVAK
SKLRELNKEM AAEKAKAAAG EAKVKKQLVA REQEITAVQA RMQASYREHV KEVQQLQGKI
RTLQEQLENG PNTQLARLQQ ENSILRDALN QATSQVESKQ NAELAKLRQE LSKVSKELVE
KSEAVRQDEQ QRKALEAKAA AFEKQVLQLQ ASHRESEEAL QKRLDEVSRE LCHTQSSHAS
LRADAEKAQE QQQQMAELHS KLQSSEAEVR SKCEELSGLH GQLQEARAEN SQLTERIRSI
EALLEAGQAR DAQDVQASQA EADQQQTRLK ELESQVSGLE KEAIELREAV EQQKVKNNDL
REKNWKAMEA LATAEQACKE KLLSLTQAKE ESEKQLCLIE AQTMEALLAL LPELSVLAQQ
NYTEWLQDLK EKGPTLLKHP PAPAEPSSDL ASKLREAEET QSTLQAECDQ YRSILAETEG
MLRDLQKSVE EEEQVWRAKV GAAEEELQKS RVTVKHLEEI VEKLKGELES SDQVREHTSH
LEAELEKHMA AASAECQNYA KEVAGLRQLL LESQSQLDAA KSEAQKQSDE LALVRQQLSE
MKSHVEDGDI AGAPASSPEA PPAEQDPVQL KTQLEWTEAI LEDEQTQRQK LTAEFEEAQT
SACRLQEELE KLRTAGPLES SETEEASQLK ERLEKEKKLT SDLGRAATRL QELLKTTQEQ
LAREKDTVKK LQEQLEKAED GSSSKEGTSV
