NOLC1_MOUSE
ID NOLC1_MOUSE Reviewed; 702 AA.
AC E9Q5C9; Q3TKZ9; Q3U6W2; Q3UBB6; Q3UI16; Q6ZQK6; Q8CE21;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Nucleolar and coiled-body phosphoprotein 1 {ECO:0000305};
DE AltName: Full=140 kDa nucleolar phosphoprotein {ECO:0000303|PubMed:11424213};
DE Short=Nopp140 {ECO:0000303|PubMed:11424213};
GN Name=Nolc1 {ECO:0000312|MGI:MGI:1918019};
GN Synonyms=Kiaa0035 {ECO:0000303|PubMed:14621295};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Amnion, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-702 (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP FUNCTION.
RX PubMed=11424213; DOI=10.1002/mrd.1032;
RA Baran V., Brochard V., Renard J.P., Flechon J.E.;
RT "Nopp 140 involvement in nucleologenesis of mouse preimplantation
RT embryos.";
RL Mol. Reprod. Dev. 59:277-284(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563; SER-646 AND SER-701, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563 AND SER-701, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563; THR-594; THR-610;
RP SER-646; SER-689 AND SER-701, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33 AND LYS-666, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP PYROPHOSPHORYLATION, AND MUTAGENESIS OF 77-LYS--LYS-98; 84-SER--SER-89 AND
RP 87-ASP--ASP-97.
RX PubMed=15604408; DOI=10.1126/science.1103344;
RA Saiardi A., Bhandari R., Resnick A.C., Snowman A.M., Snyder S.H.;
RT "Phosphorylation of proteins by inositol pyrophosphates.";
RL Science 306:2101-2105(2004).
RN [10]
RP PYROPHOSPHORYLATION AT SER-89 AND SER-92, PHOSPHORYLATION AT SER-89 AND
RP SER-92, AND MUTAGENESIS OF THR-83.
RX PubMed=17873058; DOI=10.1073/pnas.0707338104;
RA Bhandari R., Saiardi A., Ahmadibeni Y., Snowman A.M., Resnick A.C.,
RA Kristiansen T.Z., Molina H., Pandey A., Werner J.K. Jr., Juluri K.R.,
RA Xu Y., Prestwich G.D., Parang K., Snyder S.H.;
RT "Protein pyrophosphorylation by inositol pyrophosphates is a
RT posttranslational event.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15305-15310(2007).
CC -!- FUNCTION: Nucleolar protein that acts as a regulator of RNA polymerase
CC I by connecting RNA polymerase I with enzymes responsible for ribosomal
CC processing and modification (By similarity). Required for neural crest
CC specification: following monoubiquitination by the BCR(KBTBD8) complex,
CC associates with TCOF1 and acts as a platform to connect RNA polymerase
CC I with enzymes responsible for ribosomal processing and modification,
CC leading to remodel the translational program of differentiating cells
CC in favor of neural crest specification (By similarity). Involved in
CC nucleologenesis, possibly by playing a role in the maintenance of the
CC fundamental structure of the fibrillar center and dense fibrillar
CC component in the nucleolus (PubMed:11424213). It has intrinsic GTPase
CC and ATPase activities (By similarity). {ECO:0000250|UniProtKB:Q14978,
CC ECO:0000269|PubMed:11424213}.
CC -!- SUBUNIT: Interacts with RNA polymerase I 194 kDa subunit (RPA194) and
CC with casein kinase-II (By similarity). Interacts with DKC1/NAP57, NOP58
CC and fibrillarin (By similarity). {ECO:0000250|UniProtKB:P41777,
CC ECO:0000250|UniProtKB:Q14978}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q14978}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q14978}. Note=Shuttles between the nucleolus and
CC the cytoplasm. At telophase it begins to assemble into granular-like
CC pre-nucleolar bodies which are subsequently relocated to nucleoli at
CC the early G1-phase. {ECO:0000250|UniProtKB:Q14978}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E9Q5C9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9Q5C9-2; Sequence=VSP_058892, VSP_058893;
CC -!- PTM: Undergoes rapid and massive phosphorylation/dephosphorylation
CC cycles on CK2 and PKC sites. NOLC1 is one of the mostly phosphorylated
CC proteins in the cell. {ECO:0000250|UniProtKB:Q14978}.
CC -!- PTM: Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-
CC IP7) (PubMed:15604408). Serine pyrophosphorylation is achieved by
CC Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate
CC from a inositol pyrophosphate to a pre-phosphorylated serine residue
CC (PubMed:15604408, PubMed:17873058). {ECO:0000269|PubMed:15604408,
CC ECO:0000269|PubMed:17873058}.
CC -!- PTM: Ubiquitinated. Monoubiquitination by the BCR(KBTBD8) complex
CC promotes the formation of a NOLC1-TCOF1 complex that acts as a platform
CC to connect RNA polymerase I with enzymes responsible for ribosomal
CC processing and modification, leading to remodel the translational
CC program of differentiating cells in favor of neural crest
CC specification. {ECO:0000250|UniProtKB:Q14978}.
CC -!- SIMILARITY: Belongs to the NOLC1 family. {ECO:0000305}.
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DR EMBL; AK029150; BAC26327.1; -; mRNA.
DR EMBL; AK147118; BAE27690.1; -; mRNA.
DR EMBL; AK150332; BAE29474.1; -; mRNA.
DR EMBL; AK151031; BAE30048.1; -; mRNA.
DR EMBL; AK152941; BAE31612.1; -; mRNA.
DR EMBL; AK166753; BAE38994.1; -; mRNA.
DR EMBL; AC140233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK129040; BAC97850.1; -; mRNA.
DR CCDS; CCDS38006.1; -. [E9Q5C9-1]
DR RefSeq; NP_001034440.1; NM_001039351.2.
DR RefSeq; NP_001034441.1; NM_001039352.2. [E9Q5C9-1]
DR RefSeq; NP_001034442.1; NM_001039353.2.
DR RefSeq; NP_444316.2; NM_053086.3.
DR AlphaFoldDB; E9Q5C9; -.
DR IntAct; E9Q5C9; 1.
DR STRING; 10090.ENSMUSP00000128331; -.
DR iPTMnet; E9Q5C9; -.
DR PhosphoSitePlus; E9Q5C9; -.
DR jPOST; E9Q5C9; -.
DR MaxQB; E9Q5C9; -.
DR PaxDb; E9Q5C9; -.
DR PeptideAtlas; E9Q5C9; -.
DR PRIDE; E9Q5C9; -.
DR ProteomicsDB; 293698; -. [E9Q5C9-1]
DR ProteomicsDB; 293699; -. [E9Q5C9-2]
DR Antibodypedia; 31392; 292 antibodies from 33 providers.
DR DNASU; 70769; -.
DR Ensembl; ENSMUST00000165017; ENSMUSP00000128331; ENSMUSG00000015176. [E9Q5C9-1]
DR Ensembl; ENSMUST00000235620; ENSMUSP00000157687; ENSMUSG00000015176. [E9Q5C9-1]
DR GeneID; 70769; -.
DR KEGG; mmu:70769; -.
DR UCSC; uc008hsh.3; mouse. [E9Q5C9-1]
DR CTD; 9221; -.
DR MGI; MGI:1918019; Nolc1.
DR VEuPathDB; HostDB:ENSMUSG00000015176; -.
DR eggNOG; KOG2992; Eukaryota.
DR GeneTree; ENSGT00730000111092; -.
DR HOGENOM; CLU_014527_0_0_1; -.
DR InParanoid; E9Q5C9; -.
DR OMA; RESGCQG; -.
DR OrthoDB; 1610147at2759; -.
DR TreeFam; TF341730; -.
DR BioGRID-ORCS; 70769; 13 hits in 72 CRISPR screens.
DR ChiTaRS; Nolc1; mouse.
DR PRO; PR:E9Q5C9; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; E9Q5C9; protein.
DR Bgee; ENSMUSG00000015176; Expressed in ectoplacental cone and 260 other tissues.
DR ExpressionAtlas; E9Q5C9; baseline and differential.
DR Genevisible; E9Q5C9; MM.
DR GO; GO:0031428; C:box C/D RNP complex; ISO:MGI.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; ISO:MGI.
DR GO; GO:0015030; C:Cajal body; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR GO; GO:0030532; C:small nuclear ribonucleoprotein complex; TAS:MGI.
DR GO; GO:0034512; F:box C/D RNA binding; ISO:MGI.
DR GO; GO:0062064; F:box C/D snoRNP complex binding; ISO:MGI.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; ISO:MGI.
DR GO; GO:0062065; F:box H/ACA snoRNP complex binding; ISO:MGI.
DR GO; GO:0008139; F:nuclear localization sequence binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; ISO:MGI.
DR GO; GO:0033979; P:box H/ACA RNA metabolic process; ISO:MGI.
DR GO; GO:0014032; P:neural crest cell development; ISS:UniProtKB.
DR GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR GO; GO:0007000; P:nucleolus organization; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0042306; P:regulation of protein import into nucleus; ISO:MGI.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0006970; P:response to osmotic stress; IEA:Ensembl.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR007718; Srp40_C.
DR Pfam; PF05022; SRP40_C; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..702
FT /note="Nucleolar and coiled-body phosphoprotein 1"
FT /id="PRO_0000439641"
FT DOMAIN 10..42
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REPEAT 85..96
FT /note="Acidic serine cluster 1"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT REPEAT 130..141
FT /note="Acidic serine cluster 2"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT REPEAT 176..187
FT /note="Acidic serine cluster 3"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT REPEAT 232..241
FT /note="Acidic serine cluster 4"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT REPEAT 273..284
FT /note="Acidic serine cluster 5"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT REPEAT 334..345
FT /note="Acidic serine cluster 6"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT REPEAT 372..383
FT /note="Acidic serine cluster 7"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT REPEAT 431..442
FT /note="Acidic serine cluster 8"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT REPEAT 474..484
FT /note="Acidic serine cluster 9"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT REPEAT 521..531
FT /note="Acidic serine cluster 10"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT REPEAT 555..566
FT /note="Acidic serine cluster 11"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT REGION 65..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..566
FT /note="11 X 12 AA approximate repeats of an acidic serine
FT cluster"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT REGION 215..390
FT /note="Interaction with RPA194"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOTIF 69..83
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 392..590
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 604..620
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 80..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 89
FT /note="Diphosphoserine"
FT /evidence="ECO:0000269|PubMed:17873058"
FT MOD_RES 89
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:17873058"
FT MOD_RES 92
FT /note="Diphosphoserine"
FT /evidence="ECO:0000269|PubMed:17873058"
FT MOD_RES 92
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:17873058"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 421
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 563
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 594
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 610
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 613
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 646
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 666
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 686
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 77
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 351
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 356
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 402
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 407
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 421
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 421
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 447
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 459
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 575
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 582
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 607
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 616
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 650
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 666
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT CROSSLNK 698
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q14978"
FT VAR_SEQ 657..664
FT /note="WGERANQV -> GGSEPIRF (in isoform 2)"
FT /id="VSP_058892"
FT VAR_SEQ 665..702
FT /note="Missing (in isoform 2)"
FT /id="VSP_058893"
FT MUTAGEN 77..98
FT /note="KKAKKETSSSDSSEDSSEDEDK->AAAAAETSSSDSSEDSSEDEDA:
FT Strongly reduced pyrophosphorylation."
FT /evidence="ECO:0000269|PubMed:15604408"
FT MUTAGEN 83
FT /note="T->A: Does not affect pyrophosphorylation."
FT /evidence="ECO:0000269|PubMed:17873058"
FT MUTAGEN 84..89
FT /note="SSSDSS->AAADAA: Abolished pyrophosphorylation."
FT /evidence="ECO:0000269|PubMed:15604408"
FT MUTAGEN 87..97
FT /note="DSSEDSSEDED->NSSQNSSQQQN: Strongly reduced
FT pyrophosphorylation."
FT /evidence="ECO:0000269|PubMed:15604408"
FT CONFLICT 59..60
FT /note="NR -> K (in Ref. 1; BAC26327/BAE27690/BAE31612/
FT BAE29474/BAE30048)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="Missing (in Ref. 1; BAE38994/BAC26327/BAE31612/
FT BAE29474/BAE30048)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="A -> ASSS (in Ref. 3; BAC97850)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="P -> T (in Ref. 1; BAE31612/BAE29474/BAE30048)"
FT /evidence="ECO:0000305"
FT CONFLICT 514..515
FT /note="KS -> E (in Ref. 3; BAC97850)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="W -> R (in Ref. 1; BAE31612)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 702 AA; 73698 MW; 08DF638A34B50ABD CRC64;
MADTGLRRVV PSDLYPLVLR FLRDSQLSEV ASKFAKATGA TQQDANASSL LDIYSFWLNR
STKAPKVKLQ SNGPVTKKAK KETSSSDSSE DSSEDEDKKA QGLPTQKAAA QVKRASVPQH
AGKAAAKASE SSSSEESSEE EEEDKKKKPV QQKAAKPQAK AVRPPAKKAE SSESDSDSDS
DSSSEEETPQ TQKPKAAVAA KAQTKAEAKP GTPAKAQPKV ANGKAAASSS SSSSSDDSEE
EKKAAAPPKK TVPKKQVVAK APVKVAAAPT QKSSSSEDSS SEEEEGQRQP MKKKAGPYSS
VPPPSVPLPK KSPGTQAPKK AAAQTQPADS SDDSSDDSDS SSEEEKKPPA KTVVSKTPAK
AAPVKKKAES SSDSSDSDSS EDEAPAKPVS TTKSPKPAVT PKPSAAKAVT TPKQPAGSNQ
KPQSRKADSS SSEEESSSSE EEEASKKSAT TPKAKVTAKA APAKQAPQAA GDSSSDSDSS
SSEEEEKTPK PPAKKKAAGG AVSTPAPGKK AEAKSSSSSS SSSSEDSSEE EKKKKPKATT
PKIQASKANG TPASLNGKAA KESEEEEEEE ETEEKKKAAG TKPGSGKKRK QNETADEATT
PQAKKVKLET PNTFPKRKKG ERRASSPFRR VREEEIEVDS RVADNSFDAK RGAAGDWGER
ANQVLKFTKG KSFRHEKTKK KRGSYRGGSI SVQVNSVKFD SE
