RBM28_HUMAN
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 03-AUG-2022, entry version 176.
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; 289.
DR CORUM; Q9NW13; -.
DR IntAct; Q9NW13; 113.
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 SWISS-2DPAGE; Q9NW13; -.
DR EPD; Q9NW13; -.
DR jPOST; Q9NW13; -.
DR MassIVE; Q9NW13; -.
DR MaxQB; Q9NW13; -.
DR PaxDb; Q9NW13; -.
DR PeptideAtlas; Q9NW13; -.
DR PRIDE; Q9NW13; -.
DR ProteomicsDB; 19642; -.
DR ProteomicsDB; 82886; -. [Q9NW13-1]
DR Antibodypedia; 17763; 149 antibodies from 26 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 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; RNLPWSV; -.
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; 487 hits in 1089 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 195 other tissues.
DR ExpressionAtlas; Q9NW13; baseline and differential.
DR Genevisible; Q9NW13; HS.
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 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 Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 4.
DR SUPFAM; SSF54928; SSF54928; 4.
DR PROSITE; PS50102; RRM; 4.
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
