RBM19_HUMAN
ID RBM19_HUMAN Reviewed; 960 AA.
AC Q9Y4C8; A8K5X9; Q9BPY6; Q9UFN5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Probable RNA-binding protein 19;
DE AltName: Full=RNA-binding motif protein 19;
GN Name=RBM19; Synonyms=KIAA0682;
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 [LARGE SCALE MRNA], AND VARIANTS GLU-602; ARG-609;
RP THR-623 AND ALA-665.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Ohara O., Suyama M., Nagase T., Ishikawa K.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-602 AND GLN-921.
RC TISSUE=Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLU-602.
RC TISSUE=Brain, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-602; ARG-609;
RP THR-623 AND ALA-665.
RC TISSUE=Lymph;
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16027046; DOI=10.1016/j.modgep.2005.05.001;
RA Lorenzen J.A., Bonacci B.B., Palmer R.E., Wells C., Zhang J., Haber D.A.,
RA Goldstein A.M., Mayer A.N.;
RT "Rbm19 is a nucleolar protein expressed in crypt/progenitor cells of the
RT intestinal epithelium.";
RL Gene Expr. Patterns 6:45-56(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-176 AND SER-180, AND
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-949 AND SER-951, AND
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-176; SER-180;
RP SER-936; SER-949 AND SER-951, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-481, 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).
RN [14]
RP STRUCTURE BY NMR OF 291-373.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second RNA recognition motif in RNA-binding
RT protein 19.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Plays a role in embryo pre-implantation development.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849,
CC ECO:0000269|PubMed:16027046}. Nucleus, nucleoplasm {ECO:0000250}.
CC Cytoplasm {ECO:0000250}. Chromosome {ECO:0000250}. Note=In discrete
CC foci distributed throughout the cytoplasm and nucleoplasm during the 4
CC to 8 cell stages and the morula stage, but not in the periphery of the
CC nucleolar precursor body (NPB). During blastocyst development, becomes
CC increasingly localized to the nucleolus and less to the cytoplasm. At
CC the late blastocyst stage, localized predominantly in the nucleolus.
CC Localized in the nucleolus during interphase and to the perichromosomal
CC sheath during mitosis. Does not colocalize in the cytoplasm with GW182
CC in P-bodies. May translocate to the nucleolus upon early embryonic
CC development (By similarity). Colocalizes with NPM1 during interphase.
CC By late prophase, metaphase, anaphase and telophase, associates with
CC the chromosome periphery. By telophase localizes to NPB. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the crypts of Lieberkuhn of the
CC intestine and in intestinal neoplasia (at protein level).
CC {ECO:0000269|PubMed:16027046}.
CC -!- SIMILARITY: Belongs to the RRM MRD1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31657.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014582; BAA31657.2; ALT_INIT; mRNA.
DR EMBL; AL117547; CAB55987.1; -; mRNA.
DR EMBL; AK291444; BAF84133.1; -; mRNA.
DR EMBL; AK314606; BAG37176.1; -; mRNA.
DR EMBL; AC009731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004289; AAH04289.1; -; mRNA.
DR EMBL; BC006137; AAH06137.1; -; mRNA.
DR CCDS; CCDS9172.1; -.
DR PIR; T17297; T17297.
DR RefSeq; NP_001140170.1; NM_001146698.1.
DR RefSeq; NP_001140171.1; NM_001146699.1.
DR RefSeq; NP_057280.2; NM_016196.3.
DR PDB; 2DGW; NMR; -; A=291-368.
DR PDBsum; 2DGW; -.
DR AlphaFoldDB; Q9Y4C8; -.
DR SMR; Q9Y4C8; -.
DR BioGRID; 115233; 219.
DR IntAct; Q9Y4C8; 35.
DR MINT; Q9Y4C8; -.
DR STRING; 9606.ENSP00000442053; -.
DR GlyGen; Q9Y4C8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y4C8; -.
DR PhosphoSitePlus; Q9Y4C8; -.
DR BioMuta; RBM19; -.
DR DMDM; 308153566; -.
DR SWISS-2DPAGE; Q9Y4C8; -.
DR EPD; Q9Y4C8; -.
DR jPOST; Q9Y4C8; -.
DR MassIVE; Q9Y4C8; -.
DR MaxQB; Q9Y4C8; -.
DR PaxDb; Q9Y4C8; -.
DR PeptideAtlas; Q9Y4C8; -.
DR PRIDE; Q9Y4C8; -.
DR ProteomicsDB; 86163; -.
DR Antibodypedia; 31281; 55 antibodies from 16 providers.
DR DNASU; 9904; -.
DR Ensembl; ENST00000261741.10; ENSP00000261741.5; ENSG00000122965.11.
DR Ensembl; ENST00000392561.7; ENSP00000376344.3; ENSG00000122965.11.
DR Ensembl; ENST00000545145.6; ENSP00000442053.2; ENSG00000122965.11.
DR GeneID; 9904; -.
DR KEGG; hsa:9904; -.
DR MANE-Select; ENST00000261741.10; ENSP00000261741.5; NM_016196.4; NP_057280.2.
DR UCSC; uc001tvm.4; human.
DR CTD; 9904; -.
DR DisGeNET; 9904; -.
DR GeneCards; RBM19; -.
DR HGNC; HGNC:29098; RBM19.
DR HPA; ENSG00000122965; Low tissue specificity.
DR MIM; 616444; gene.
DR neXtProt; NX_Q9Y4C8; -.
DR OpenTargets; ENSG00000122965; -.
DR PharmGKB; PA134886784; -.
DR VEuPathDB; HostDB:ENSG00000122965; -.
DR eggNOG; KOG0110; Eukaryota.
DR GeneTree; ENSGT00840000129953; -.
DR HOGENOM; CLU_008479_1_0_1; -.
DR InParanoid; Q9Y4C8; -.
DR OMA; TALIEYC; -.
DR OrthoDB; 1428854at2759; -.
DR PhylomeDB; Q9Y4C8; -.
DR TreeFam; TF105725; -.
DR PathwayCommons; Q9Y4C8; -.
DR SignaLink; Q9Y4C8; -.
DR BioGRID-ORCS; 9904; 625 hits in 1090 CRISPR screens.
DR ChiTaRS; RBM19; human.
DR EvolutionaryTrace; Q9Y4C8; -.
DR GeneWiki; RBM19; -.
DR GenomeRNAi; 9904; -.
DR Pharos; Q9Y4C8; Tbio.
DR PRO; PR:Q9Y4C8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9Y4C8; protein.
DR Bgee; ENSG00000122965; Expressed in sural nerve and 109 other tissues.
DR ExpressionAtlas; Q9Y4C8; baseline and differential.
DR Genevisible; Q9Y4C8; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0040019; P:positive regulation of embryonic development; ISS:UniProtKB.
DR CDD; cd12564; RRM1_RBM19; 1.
DR CDD; cd12502; RRM2_RMB19; 1.
DR CDD; cd12567; RRM3_RBM19; 1.
DR CDD; cd12569; RRM4_RBM19; 1.
DR CDD; cd12318; RRM5_RBM19_like; 1.
DR CDD; cd12571; RRM6_RBM19; 1.
DR Gene3D; 3.30.70.330; -; 6.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR034419; RBM19_RRM3.
DR InterPro; IPR034420; RBM19_RRM4.
DR InterPro; IPR034423; RBM19_RRM5.
DR InterPro; IPR034421; RBM19_RRM6.
DR InterPro; IPR034418; RMB19_RRM1.
DR InterPro; IPR034417; RMB19_RRM2.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 6.
DR SMART; SM00360; RRM; 6.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 5.
DR PROSITE; PS50102; RRM; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Cytoplasm; Developmental protein;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Ubl conjugation.
FT CHAIN 1..960
FT /note="Probable RNA-binding protein 19"
FT /id="PRO_0000081781"
FT DOMAIN 2..79
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 294..369
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 402..480
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 587..659
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 730..811
FT /note="RRM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 832..912
FT /note="RRM 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 85..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..190
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..245
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..727
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 951
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 481
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 602
FT /note="Q -> E (in dbSNP:rs7299217)"
FT /evidence="ECO:0000269|PubMed:11230166,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9734811"
FT /id="VAR_059822"
FT VARIANT 609
FT /note="H -> R (in dbSNP:rs2290789)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9734811"
FT /id="VAR_023114"
FT VARIANT 623
FT /note="I -> T (in dbSNP:rs2290788)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9734811"
FT /id="VAR_023115"
FT VARIANT 665
FT /note="T -> A (in dbSNP:rs2290787)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9734811"
FT /id="VAR_023116"
FT VARIANT 821
FT /note="R -> G (in dbSNP:rs16943379)"
FT /id="VAR_057246"
FT VARIANT 921
FT /note="R -> Q (in dbSNP:rs2075387)"
FT /evidence="ECO:0000269|PubMed:11230166"
FT /id="VAR_023117"
FT CONFLICT 141
FT /note="Q -> R (in Ref. 1; BAA31657)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="K -> R (in Ref. 1; BAA31657 and 6; AAH06137/
FT AAH04289)"
FT /evidence="ECO:0000305"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:2DGW"
FT HELIX 307..314
FT /evidence="ECO:0007829|PDB:2DGW"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:2DGW"
FT STRAND 332..339
FT /evidence="ECO:0007829|PDB:2DGW"
FT HELIX 343..351
FT /evidence="ECO:0007829|PDB:2DGW"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:2DGW"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:2DGW"
SQ SEQUENCE 960 AA; 107332 MW; 28B6F37B18D7B9B1 CRC64;
MSRLIVKNLP NGMKEERFRQ LFAAFGTLTD CSLKFTKDGK FRKFGFIGFK SEEEAQKAQK
HFNKSFIDTS RITVEFCKSF GDPAKPRAWS KHAQKPSQPK QPPKDSTTPE IKKDEKKKKV
AGQLEKLKED TEFQEFLSVH QRRAQAATWA NDGLDAEPSK GKSKPASDYL NFDSDSGQES
EEEGAGEDLE EEASLEPKAA VQKELSDMDY LKSKMVKAGS SSSSEEEESE DEAVHCDEGS
EAEEEDSSAT PVLQERDSKG AGQEQGMPAG KKRPPEARAE TEKPANQKEP TTCHTVKLRG
APFNVTEKNV MEFLAPLKPV AIRIVRNAHG NKTGYIFVDF SNEEEVKQAL KCNREYMGGR
YIEVFREKNV PTTKGAPKNT TKSWQGRILG ENEEEEDLAE SGRLFVRNLP YTSTEEDLEK
LFSKYGPLSE LHYPIDSLTK KPKGFAFITF MFPEHAVKAY SEVDGQVFQG RMLHVLPSTI
KKEASEDASA LGSSSYKKKK EAQDKANSAS SHNWNTLFMG PNAVADAIAQ KYNATKSQVF
DHETKGSVAV RVALGETQLV QEVRRFLIDN GVSLDSFSQA AAERSKTVIL VKNLPAGTLA
AQLQETFGHF GSLGRVLLPE GGITAIVEFL EPLEARKAFR HLAYSKFHHV PLYLEWAPVG
VFSSTAPQKK KLQDTPSEPM EKDPAEPETV PDGETPEDEN PTEEGADNSS AKMEEEEEEE
EEEEESLPGC TLFIKNLNFD TTEEKLKEVF SKVGTVKSCS ISKKKNKAGV LLSMGFGFVE
YRKPEQAQKA LKQLQGHVVD GHKLEVRISE RATKPAVTLA RKKQVPRKQT TSKILVRNIP
FQAHSREIRE LFSTFGELKT VRLPKKMTGT GTHRGFGFVD FLTKQDAKRA FNALCHSTHL
YGRRLVLEWA DSEVTLQALR RKTAAHFHEP PKKKRSVVLD EILEQLEGSD SDSEEQTLQL
