ID RBM28_HUMAN Reviewed; 759 AA. AC Q9NW13; A4D100; B4DU52; E9PDD9; Q53H65; Q96CV3; DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 185. DE RecName: Full=RNA-binding protein 28; DE AltName: Full=RNA-binding motif protein 28; GN Name=RBM28; 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] (ISOFORMS 1 AND 2). RC TISSUE=Prostate, and Teratocarcinoma; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Colon; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). 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] (ISOFORM 1). RC TISSUE=Skin; 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 PROTEIN SEQUENCE OF 2-10; 155-162; 183-192; 197-208; 454-465; 506-515; RP 559-571 AND 730-738, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP ALA-2, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V.; RL Submitted (OCT-2004) to UniProtKB. RN [8] RP PROTEIN SEQUENCE OF 17-31; 326-335; 477-486 AND 601-610, FUNCTION, RP SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH SPLICEOSOMAL RP SNRNAS U1; U2; U4; U5 AND U6. RX PubMed=17081119; DOI=10.1515/bc.2006.182; RA Damianov A., Kann M., Lane W.S., Bindereif A.; RT "Human RBM28 protein is a specific nucleolar component of the spliceosomal RT snRNPs."; RL Biol. Chem. 387:1455-1460(2006). RN [9] 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY RP 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 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 BY MASS SPECTROMETRY [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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-653, 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 [15] RP VARIANT ANES PRO-351, AND TISSUE SPECIFICITY. RX PubMed=18439547; DOI=10.1016/j.ajhg.2008.03.014; RA Nousbeck J., Spiegel R., Ishida-Yamamoto A., Indelman M., Shani-Adir A., RA Adir N., Lipkin E., Bercovici S., Geiger D., van Steensel M.A., RA Steijlen P.M., Bergman R., Bindereif A., Choder M., Shalev S., Sprecher E.; RT "Alopecia, neurological defects, and endocrinopathy syndrome caused by RT decreased expression of RBM28, a nucleolar protein associated with ribosome RT biogenesis."; RL Am. J. Hum. Genet. 82:1114-1121(2008). CC -!- FUNCTION: Nucleolar component of the spliceosomal ribonucleoprotein CC complexes. {ECO:0000269|PubMed:17081119}. CC -!- SUBUNIT: Interacts with U1, U2, U4, U5, and U6 spliceosomal small CC nuclear RNAs (snRNAs). {ECO:0000269|PubMed:17081119}. CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, CC ECO:0000269|PubMed:17081119, ECO:0000269|Ref.7}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NW13-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NW13-2; Sequence=VSP_046111; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:18439547}. CC -!- DISEASE: Alopecia, neurologic defects, and endocrinopathy syndrome CC (ANES) [MIM:612079]: Affected individuals have hair loss of variable CC severity, ranging from complete alopecia to near-normal scalp hair with CC absence of body hair. All have moderate to severe intellectual CC disability, progressive motor deterioration and central CC hypogonadotropic hypogonadism with delayed or absent puberty and CC central adrenal insufficiency. Additional features included short CC stature, microcephaly, gynecomastia, pigmentary anomalies, hypodontia, CC kyphoscoliosis, ulnar deviation of the hands, and loss of subcutaneous CC fat. {ECO:0000269|PubMed:18439547}. Note=The disease is caused by CC variants affecting the gene represented in this entry. 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; AK001239; BAA91575.1; -; mRNA. DR EMBL; AK300500; BAG62214.1; -; mRNA. DR EMBL; AK222716; BAD96436.1; -; mRNA. DR EMBL; AC010655; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC018635; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236947; EAL24314.1; -; Genomic_DNA. DR EMBL; CH471070; EAW83643.1; -; Genomic_DNA. DR EMBL; BC013889; AAH13889.1; -; mRNA. DR CCDS; CCDS55159.1; -. [Q9NW13-2] DR CCDS; CCDS5801.1; -. [Q9NW13-1] DR RefSeq; NP_001159607.1; NM_001166135.1. [Q9NW13-2] DR RefSeq; NP_060547.2; NM_018077.2. [Q9NW13-1] DR AlphaFoldDB; Q9NW13; -. DR BioGRID; 120437; 343. DR CORUM; Q9NW13; -. DR IntAct; Q9NW13; 129. DR MINT; Q9NW13; -. DR STRING; 9606.ENSP00000223073; -. DR GlyGen; Q9NW13; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NW13; -. DR PhosphoSitePlus; Q9NW13; -. DR SwissPalm; Q9NW13; -. DR BioMuta; RBM28; -. DR DMDM; 55976611; -. DR EPD; Q9NW13; -. DR jPOST; Q9NW13; -. DR MassIVE; Q9NW13; -. DR MaxQB; Q9NW13; -. DR PaxDb; 9606-ENSP00000223073; -. DR PeptideAtlas; Q9NW13; -. DR ProteomicsDB; 19642; -. DR ProteomicsDB; 82886; -. [Q9NW13-1] DR Pumba; Q9NW13; -. DR Antibodypedia; 17763; 168 antibodies from 25 providers. DR DNASU; 55131; -. DR Ensembl; ENST00000223073.6; ENSP00000223073.1; ENSG00000106344.8. [Q9NW13-1] DR Ensembl; ENST00000415472.6; ENSP00000390517.2; ENSG00000106344.8. [Q9NW13-2] DR GeneID; 55131; -. DR KEGG; hsa:55131; -. DR MANE-Select; ENST00000223073.6; ENSP00000223073.1; NM_018077.3; NP_060547.2. DR UCSC; uc011koj.2; human. [Q9NW13-1] DR AGR; HGNC:21863; -. DR CTD; 55131; -. DR DisGeNET; 55131; -. DR GeneCards; RBM28; -. DR HGNC; HGNC:21863; RBM28. DR HPA; ENSG00000106344; Low tissue specificity. DR MalaCards; RBM28; -. DR MIM; 612074; gene. DR MIM; 612079; phenotype. DR neXtProt; NX_Q9NW13; -. DR OpenTargets; ENSG00000106344; -. DR Orphanet; 157954; ANE syndrome. DR PharmGKB; PA134867266; -. DR VEuPathDB; HostDB:ENSG00000106344; -. DR eggNOG; KOG0127; Eukaryota. DR GeneTree; ENSGT00550000074976; -. DR HOGENOM; CLU_011608_2_0_1; -. DR InParanoid; Q9NW13; -. DR OMA; FTHRHAL; -. DR OrthoDB; 2918334at2759; -. DR PhylomeDB; Q9NW13; -. DR TreeFam; TF312798; -. DR PathwayCommons; Q9NW13; -. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR SignaLink; Q9NW13; -. DR BioGRID-ORCS; 55131; 495 hits in 1170 CRISPR screens. DR ChiTaRS; RBM28; human. DR GeneWiki; RBM28; -. DR GenomeRNAi; 55131; -. DR Pharos; Q9NW13; Tbio. DR PRO; PR:Q9NW13; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q9NW13; Protein. DR Bgee; ENSG00000106344; Expressed in sural nerve and 197 other cell types or tissues. DR ExpressionAtlas; Q9NW13; baseline and differential. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR CDD; cd12413; RRM1_RBM28_like; 1. DR CDD; cd12414; RRM2_RBM28_like; 1. DR CDD; cd12415; RRM3_RBM28_like; 1. DR CDD; cd12416; RRM4_RBM28_like; 1. DR Gene3D; 3.30.70.330; -; 4. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR48039; RNA-BINDING MOTIF PROTEIN 14B; 1. DR PANTHER; PTHR48039:SF5; RNA-BINDING PROTEIN 28; 1. DR Pfam; PF00076; RRM_1; 3. DR SMART; SM00360; RRM; 4. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 4. DR PROSITE; PS50102; RRM; 4. DR SWISS-2DPAGE; Q9NW13; -. DR Genevisible; Q9NW13; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Direct protein sequencing; KW Disease variant; Hypotrichosis; Intellectual disability; Isopeptide bond; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; RNA-binding; Spliceosome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.7" FT CHAIN 2..759 FT /note="RNA-binding protein 28" FT /id="PRO_0000081785" FT DOMAIN 4..80 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 114..191 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 335..419 FT /note="RRM 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 487..597 FT /note="RRM 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 84..105 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 201..330 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 594..759 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 87..105 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 201..226 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 227..256 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 287..307 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 308..330 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 620..637 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 638..653 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 670..695 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 712..726 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.7" FT MOD_RES 122 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 397 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 653 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 39..179 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046111" FT VARIANT 253 FT /note="E -> Q (in dbSNP:rs11554671)" FT /id="VAR_045654" FT VARIANT 351 FT /note="L -> P (in ANES; dbSNP:rs118204055)" FT /evidence="ECO:0000269|PubMed:18439547" FT /id="VAR_045655" FT CONFLICT 21 FT /note="E -> G (in Ref. 2; BAD96436)" FT /evidence="ECO:0000305" FT CONFLICT 361 FT /note="L -> P (in Ref. 1; BAG62214)" FT /evidence="ECO:0000305" FT CONFLICT 668 FT /note="R -> K (in Ref. 1; BAG62214)" FT /evidence="ECO:0000305" FT CONFLICT 739 FT /note="Q -> R (in Ref. 1; BAA91575)" FT /evidence="ECO:0000305" SQ SEQUENCE 759 AA; 85738 MW; B477EDB9561D6771 CRC64; MAGLTLFVGR LPPSARSEQL EELFSQVGPV KQCFVVTEKG SKACRGFGYV TFSMLEDVQR ALKEITTFEG CKINVTVAKK KLRNKTKEKG KNENSECPKK EPKAKKAKVA DKKARLIIRN LSFKCSEDDL KTVFAQFGAV LEVNIPRKPD GKMRGFGFVQ FKNLLEAGKA LKGMNMKEIK GRTVAVDWAV AKDKYKDTQS VSAIGEEKSH ESKHQESVKK KGREEEDMEE EENDDDDDDD DEEDGVFDDE DEEEENIESK VTKPVQIQKR AVKRPAPAKS SDHSEEDSDL EESDSIDDGE ELAQSDTSTE EQEDKAVQVS NKKKRKLPSD VNEGKTVFIR NLSFDSEEEE LGELLQQFGE LKYVRIVLHP DTEHSKGCAF AQFMTQEAAQ KCLLAASPEN EAGGLKLDGR QLKVDLAVTR DEAAKLQTTK VKKPTGTRNL YLAREGLIRA GTKAAEGVSA ADMAKRERFE LLKHQKLKDQ NIFVSRTRLC LHNLPKAVDD KQLRKLLLSA TSGEKGVRIK ECRVMRDLKG VHGNMKGQSL GYAFAEFQEH EHALKALRLI NNNPEIFGPL KRPIVEFSLE DRRKLKMKEL RIQRSLQKMR SKPATGEPQK GQPEPAKDQQ QKAAQHHTEE QSKVPPEQKR KAGSTSWTGF QTKAEVEQVE LPDGKKRRKV LALPSHRGPK IRLRDKGKVK PVHPKKPKPQ INQWKQEKQQ LSSEQVSRKK AKGNKTETRF NQLVEQYKQK LLGPSKGAPL AKRSKWFDS //