ID   BMS1_HUMAN              Reviewed;        1282 AA.
AC   Q14692; Q5QPT5; Q86XJ9;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Ribosome biogenesis protein BMS1 homolog;
DE   AltName: Full=Ribosome assembly protein BMS1 homolog;
GN   Name=BMS1 {ECO:0000312|HGNC:HGNC:23505}; Synonyms=BMS1L, KIAA0187;
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].
RC   TISSUE=Bone marrow;
RX   PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA   Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. V. The
RT   coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT   cDNA clones from human cell line KG-1.";
RL   DNA Res. 3:17-24(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-1141.
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   [5]
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552; SER-625 AND THR-708, 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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND THR-708, 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   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639, AND IDENTIFICATION BY
RP   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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-552, 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   [12]
RP   INVOLVEMENT IN ACC, AND VARIANT ACC HIS-930.
RX   PubMed=23785305; DOI=10.1371/journal.pgen.1003573;
RA   Marneros A.G.;
RT   "BMS1 is mutated in aplasia cutis congenita.";
RL   PLoS Genet. 9:E1003573-E1003573(2013).
RN   [13]
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   [14]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-415 AND LYS-810, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [15]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-810, 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   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-810, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [17]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43; LYS-399; LYS-415; LYS-646;
RP   LYS-810 AND LYS-1206, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [18] {ECO:0007744|PDB:7MQ9, ECO:0007744|PDB:7MQA}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION, SUBCELLULAR
RP   LOCATION, AND SUBUNIT.
RX   PubMed=34516797; DOI=10.1126/science.abj5338;
RA   Singh S., Vanden Broeck A., Miller L., Chaker-Margot M., Klinge S.;
RT   "Nucleolar maturation of the human small subunit processome.";
RL   Science 373:eabj5338-eabj5338(2021).
CC   -!- FUNCTION: Part of the small subunit (SSU) processome, first precursor
CC       of the small eukaryotic ribosomal subunit. During the assembly of the
CC       SSU processome in the nucleolus, many ribosome biogenesis factors, an
CC       RNA chaperone and ribosomal proteins associate with the nascent pre-
CC       rRNA and work in concert to generate RNA folding, modifications,
CC       rearrangements and cleavage as well as targeted degradation of pre-
CC       ribosomal RNA by the RNA exosome. {ECO:0000269|PubMed:34516797}.
CC   -!- SUBUNIT: Part of the small subunit (SSU) processome, composed of more
CC       than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3.
CC       {ECO:0000269|PubMed:34516797}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:34516797}.
CC   -!- DISEASE: Aplasia cutis congenita, non-syndromic (ACC) [MIM:107600]: A
CC       disorder characterized by congenital absence of a portion of skin in a
CC       localized or widespread area of the body. The lesions are most commonly
CC       localized on the scalp, however aplasia cutis congenita can affect any
CC       part of the body. {ECO:0000269|PubMed:23785305}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Bms1-like GTPase family. BMS1 subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA11504.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; D80009; BAA11504.2; ALT_INIT; mRNA.
DR   EMBL; AL022344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471160; EAW86571.1; -; Genomic_DNA.
DR   EMBL; BC043345; AAH43345.1; -; mRNA.
DR   EMBL; BC150252; AAI50253.1; -; mRNA.
DR   CCDS; CCDS7199.1; -.
DR   RefSeq; NP_055568.3; NM_014753.3.
DR   RefSeq; XP_005271903.1; XM_005271846.3.
DR   RefSeq; XP_011538704.1; XM_011540402.2.
DR   PDB; 7MQ9; EM; 3.87 A; SI=1-1282.
DR   PDB; 7MQA; EM; 2.70 A; SI=1-1282.
DR   PDBsum; 7MQ9; -.
DR   PDBsum; 7MQA; -.
DR   AlphaFoldDB; Q14692; -.
DR   EMDB; EMD-23937; -.
DR   EMDB; EMD-23938; -.
DR   SMR; Q14692; -.
DR   BioGRID; 115134; 238.
DR   ComplexPortal; CPX-2511; Small ribosomal subunit processome.
DR   IntAct; Q14692; 46.
DR   MINT; Q14692; -.
DR   STRING; 9606.ENSP00000363642; -.
DR   GlyGen; Q14692; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q14692; -.
DR   PhosphoSitePlus; Q14692; -.
DR   SwissPalm; Q14692; -.
DR   BioMuta; BMS1; -.
DR   DMDM; 27151474; -.
DR   EPD; Q14692; -.
DR   jPOST; Q14692; -.
DR   MassIVE; Q14692; -.
DR   MaxQB; Q14692; -.
DR   PaxDb; 9606-ENSP00000363642; -.
DR   PeptideAtlas; Q14692; -.
DR   ProteomicsDB; 60130; -.
DR   Pumba; Q14692; -.
DR   Antibodypedia; 13377; 95 antibodies from 23 providers.
DR   DNASU; 9790; -.
DR   Ensembl; ENST00000374518.6; ENSP00000363642.4; ENSG00000165733.8.
DR   GeneID; 9790; -.
DR   KEGG; hsa:9790; -.
DR   MANE-Select; ENST00000374518.6; ENSP00000363642.4; NM_014753.4; NP_055568.3.
DR   UCSC; uc001jaj.4; human.
DR   AGR; HGNC:23505; -.
DR   CTD; 9790; -.
DR   DisGeNET; 9790; -.
DR   GeneCards; BMS1; -.
DR   HGNC; HGNC:23505; BMS1.
DR   HPA; ENSG00000165733; Low tissue specificity.
DR   MalaCards; BMS1; -.
DR   MIM; 107600; phenotype.
DR   MIM; 611448; gene.
DR   neXtProt; NX_Q14692; -.
DR   OpenTargets; ENSG00000165733; -.
DR   Orphanet; 1114; Aplasia cutis congenita.
DR   PharmGKB; PA162377556; -.
DR   VEuPathDB; HostDB:ENSG00000165733; -.
DR   eggNOG; KOG1951; Eukaryota.
DR   GeneTree; ENSGT00940000153195; -.
DR   HOGENOM; CLU_002486_0_1_1; -.
DR   InParanoid; Q14692; -.
DR   OMA; KLHVPMV; -.
DR   OrthoDB; 5478101at2759; -.
DR   PhylomeDB; Q14692; -.
DR   TreeFam; TF105751; -.
DR   PathwayCommons; Q14692; -.
DR   Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
DR   Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   SignaLink; Q14692; -.
DR   BioGRID-ORCS; 9790; 746 hits in 1165 CRISPR screens.
DR   ChiTaRS; BMS1; human.
DR   GenomeRNAi; 9790; -.
DR   Pharos; Q14692; Tbio.
DR   PRO; PR:Q14692; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q14692; Protein.
DR   Bgee; ENSG00000165733; Expressed in tendon of biceps brachii and 215 other cell types or tissues.
DR   GO; GO:0030686; C:90S preribosome; IBA:GO_Central.
DR   GO; GO:0005694; C:chromosome; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0032040; C:small-subunit processome; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0034511; F:U3 snoRNA binding; IBA:GO_Central.
DR   GO; GO:0000479; P:endonucleolytic cleavage of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:UniProtKB.
DR   CDD; cd01882; BMS1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR012948; AARP2CN.
DR   InterPro; IPR039761; Bms1/Tsr1.
DR   InterPro; IPR037875; Bms1_N.
DR   InterPro; IPR007034; BMS1_TSR1_C.
DR   InterPro; IPR030387; G_Bms1/Tsr1_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR12858; RIBOSOME BIOGENESIS PROTEIN; 1.
DR   PANTHER; PTHR12858:SF2; RIBOSOME BIOGENESIS PROTEIN BMS1 HOMOLOG; 1.
DR   Pfam; PF08142; AARP2CN; 1.
DR   Pfam; PF04950; RIBIOP_C; 1.
DR   SMART; SM00785; AARP2CN; 1.
DR   SMART; SM01362; DUF663; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51714; G_BMS1; 1.
DR   Genevisible; Q14692; HS.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Disease variant; Ectodermal dysplasia;
KW   GTP-binding; Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Ribosome biogenesis; Ubl conjugation.
FT   CHAIN           1..1282
FT                   /note="Ribosome biogenesis protein BMS1 homolog"
FT                   /id="PRO_0000195004"
FT   DOMAIN          80..245
FT                   /note="Bms1-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          89..96
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT   REGION          117..121
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT   REGION          132..135
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT   REGION          184..187
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT   REGION          219..228
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01051"
FT   REGION          397..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          787..822
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1178..1202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1219..1282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        410..436
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..473
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..529
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..607
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        618..639
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..667
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        787..808
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1185..1202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1232..1273
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         89..96
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         552
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         625
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         639
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         708
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231"
FT   CROSSLNK        43
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        399
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        415
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        646
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        810
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        810
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211,
FT                   ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        1206
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         237
FT                   /note="R -> H (in dbSNP:rs2272881)"
FT                   /id="VAR_057503"
FT   VARIANT         552
FT                   /note="S -> P (in dbSNP:rs3814621)"
FT                   /id="VAR_057504"
FT   VARIANT         652
FT                   /note="K -> R (in dbSNP:rs787795)"
FT                   /id="VAR_057505"
FT   VARIANT         884
FT                   /note="M -> V (in dbSNP:rs2419109)"
FT                   /id="VAR_057506"
FT   VARIANT         930
FT                   /note="R -> H (in ACC; fibroblasts show CDKN1A-mediated
FT                   G1/S phase transition defect with a significantly reduced
FT                   cell proliferation rate compared to controls; in vitro
FT                   scratch assay reveal an increased cell migration rate;
FT                   dbSNP:rs587777706)"
FT                   /evidence="ECO:0000269|PubMed:23785305"
FT                   /id="VAR_072539"
FT   VARIANT         1141
FT                   /note="V -> I (in dbSNP:rs12764004)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_057507"
SQ   SEQUENCE   1282 AA;  145807 MW;  54A736ED250A5138 CRC64;
     MEAKDQKKHR KKNSGPKAAK KKKRLLQDLQ LGDEEDARKR NPKAFAVQSA VRMARSFHRT
     QDLKTKKHHI PVVDRTPLEP PPIVVVVMGP PKVGKSTLIQ CLIRNFTRQK LTEIRGPVTI
     VSGKKRRLTI IECGCDINMM IDLAKVADLV LMLIDASFGF EMETFEFLNI CQVHGFPKIM
     GVLTHLDSFK HNKQLKKTKK RLKHRFWTEV YPGAKLFYLS GMVHGEYQNQ EIHNLGRFIT
     VMKFRPLTWQ TSHPYILADR MEDLTNPEDI RTNIKCDRKV SLYGYLRGAH LKNKSQIHMP
     GVGDFAVSDI SFLPDPCALP EQQKKRCLNE KEKLVYAPLS GVGGVLYDKD AVYVDLGGSH
     VFQDEVGPTH ELVQSLISTH STIDAKMASS RVTLFSDSKP LGSEDIDNQG LMMPKEEKQM
     DLNTGRMRRK AIFGDEDESG DSDDEEDDEM SEDDGLENGS SDEEAEEEEN AEMTDQYMAV
     KGIKRRKLEL EEDSEMDLPA FADSDDDLER SSAEEGEAEE ADESSEEEDC TAGEKGISGS
     KAAGEGSKAG LSPANCQSDR VNLEKSLLMK KAALPTFDSG HCTAEEVFAS EDESEESSSL
     SAEEEDSENE EAIRKKLSKP SQVSSGQKLG PQNFIDETSD IENLLKEEED YKEENNDSKE
     TSGALKWKED LSRKAAEAFL RQQQAAPNLR KLIYGTVTED NEEEDDDTLE ELGGLFRVNQ
     PDRECKHKAD SLDCSRFLVE APHDWDLEEV MNSIRDCFVT GKWEDDKDAA KVLAEDEELY
     GDFEDLETGD VHKGKSGPNT QNEDIEKEVK EEIDPDEEES AKKKHLDKKR KLKEMFDAEY
     DEGESTYFDD LKGEMQKQAQ LNRAEFEDQD DEARVQYEGF RPGMYVRIEI ENVPCEFVQN
     FDPHYPIILG GLGNSEGNVG YVQMRLKKHR WYKKILKSRD PIIFSVGWRR FQTIPLYYIE
     DHNGRQRLLK YTPQHMHCGA AFWGPITPQG TGFLAIQSVS GIMPDFRIAA TGVVLDLDKS
     IKIVKKLKLT GFPYKIFKNT SFIKGMFNSA LEVAKFEGAV IRTVSGIRGQ IKKALRAPEG
     AFRASFEDKL LMSDIVFMRT WYPVSIPAFY NPVTSLLKPV GEKDTWSGMR TTGQLRLAHG
     VRLKANKDSL YKPILRQKKH FNSLHIPKAL QKALPFKNKP KTQAKAGKVP KDRRRPAVIR
     EPHERKILAL LDALSTVHSQ KMKKAKEQRH LHNKEHFRAK QKEEEEKLKR QKDLRKKLFR
     IQGQKERRNQ KSSLKGAEGQ LQ
//