BMS1_HUMAN
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 03-AUG-2022, entry version 181.
DE RecName: Full=Ribosome biogenesis protein BMS1 homolog;
DE AltName: Full=Ribosome assembly protein BMS1 homolog;
GN Name=BMS1; 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).
CC -!- FUNCTION: May act as a molecular switch during maturation of the 40S
CC ribosomal subunit in the nucleolus. {ECO:0000250|UniProtKB:Q08965}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250}.
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 SMR; Q14692; -.
DR BioGRID; 115134; 214.
DR IntAct; Q14692; 43.
DR MINT; Q14692; -.
DR STRING; 9606.ENSP00000363642; -.
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; Q14692; -.
DR PeptideAtlas; Q14692; -.
DR PRIDE; Q14692; -.
DR ProteomicsDB; 60130; -.
DR Antibodypedia; 13377; 80 antibodies from 22 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 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; QMEQQEF; -.
DR OrthoDB; 463678at2759; -.
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; 727 hits in 1087 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 213 other tissues.
DR Genevisible; Q14692; HS.
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: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 CDD; cd01882; BMS1; 1.
DR Gene3D; 3.40.50.300; -; 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; PTHR12858; 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; SSF52540; 1.
DR PROSITE; PS51714; G_BMS1; 1.
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 G1/
FT S phase transition defect with a significantly reduced cell
FT proliferation rate compared to controls; in vitro scratch
FT 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
