NASP_MOUSE
ID NASP_MOUSE Reviewed; 773 AA.
AC Q99MD9; O35499; O88993; Q3V150; Q99KE9;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Nuclear autoantigenic sperm protein;
DE Short=NASP;
GN Name=Nasp {ECO:0000312|MGI:MGI:1355328};
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] {ECO:0000305, ECO:0000312|EMBL:AAB87567.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH HISTONES,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAB87567.2};
RC TISSUE=Ovary {ECO:0000312|EMBL:AAC64195.1},
RC Spleen {ECO:0000269|PubMed:10893414}, and
RC Testis {ECO:0000269|PubMed:10893414};
RX PubMed=10893414; DOI=10.1074/jbc.m003781200;
RA Richardson R.T., Batova I.N., Widgren E.E., Zheng L.-X., Whitfield M.,
RA Marzluff W.F., O'Rand M.G.;
RT "Characterization of the histone H1-binding protein, NASP, as a cell cycle-
RT regulated somatic protein.";
RL J. Biol. Chem. 275:30378-30386(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK31171.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=129/SvJ {ECO:0000312|EMBL:AAK31171.1};
RX PubMed=16728391; DOI=10.1074/jbc.m603816200;
RA Richardson R.T., Alekseev O.M., Grossman G., Widgren E.E., Thresher R.,
RA Wagner E.J., Sullivan K.D., Marzluff W.F., O'Rand M.G.;
RT "Nuclear autoantigenic sperm protein (NASP), a linker histone chaperone
RT that is required for cell proliferation.";
RL J. Biol. Chem. 281:21526-21534(2006).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAE21303.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-453 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE21303.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAE21303.1}, and
RC Thymus {ECO:0000312|EMBL:BAC38871.1};
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 [4] {ECO:0000312|EMBL:AAH04693.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH04693.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH04693.1};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HISTONES.
RX PubMed=12509435; DOI=10.1074/jbc.m210352200;
RA Alekseev O.M., Bencic D.C., Richardson R.T., Widgren E.E., O'Rand M.G.;
RT "Overexpression of the linker histone-binding protein tNASP affects
RT progression through the cell cycle.";
RL J. Biol. Chem. 278:8846-8852(2003).
RN [6] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH H1-6 AND HSP90.
RX PubMed=15533935; DOI=10.1074/jbc.m410397200;
RA Alekseev O.M., Widgren E.E., Richardson R.T., O'Rand M.G.;
RT "Association of NASP with HSP90 in mouse spermatogenic cells: stimulation
RT of ATPase activity and transport of linker histones into nuclei.";
RL J. Biol. Chem. 280:2904-2911(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463 AND SER-466, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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-241; LYS-251 AND LYS-284, 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).
CC -!- FUNCTION: Required for DNA replication, normal cell cycle progression
CC and cell proliferation. Forms a cytoplasmic complex with HSP90 and
CC linker H1 histones and stimulates HSP90 ATPase activity. NASP and H1
CC histone are subsequently released from the complex and translocate to
CC the nucleus where the histone is released for binding to DNA.
CC {ECO:0000269|PubMed:12509435, ECO:0000269|PubMed:15533935,
CC ECO:0000269|PubMed:16728391}.
CC -!- SUBUNIT: Binds to linker H1 histones but not to core histones
CC (PubMed:10893414, PubMed:12509435). Interacts with histones H2A, H2B,
CC H3 and H4 (By similarity). Interacts with histone H3.3 (By similarity).
CC Also binds to HSP90 in the cytoplasm (PubMed:15533935). This
CC interaction stimulates binding of NASP to H1-6/H1T (PubMed:15533935).
CC {ECO:0000250|UniProtKB:P49321, ECO:0000269|PubMed:10893414,
CC ECO:0000269|PubMed:12509435, ECO:0000269|PubMed:15533935}.
CC -!- INTERACTION:
CC Q99MD9; P15864: H1-2; NbExp=3; IntAct=EBI-913410, EBI-913436;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10893414,
CC ECO:0000269|PubMed:12509435, ECO:0000269|PubMed:16728391}. Nucleus
CC {ECO:0000269|PubMed:10893414, ECO:0000269|PubMed:12509435,
CC ECO:0000269|PubMed:16728391}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:10893414, ECO:0000269|PubMed:16728391};
CC Synonyms=Testicular NASP {ECO:0000269|PubMed:10893414}, tNASP
CC {ECO:0000269|PubMed:10893414};
CC IsoId=Q99MD9-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10893414, ECO:0000269|PubMed:16728391};
CC Synonyms=Somatic NASP {ECO:0000269|PubMed:10893414}, sNASP
CC {ECO:0000269|PubMed:10893414};
CC IsoId=Q99MD9-2; Sequence=VSP_052237, VSP_052238;
CC -!- TISSUE SPECIFICITY: Isoform 1 is found in gametes, embryonic cells and
CC transformed cells. Isoform 2 is found in dividing somatic cells (at
CC protein level). {ECO:0000269|PubMed:10893414}.
CC -!- DEVELOPMENTAL STAGE: During the cell cycle, levels increase during S-
CC phase. {ECO:0000269|PubMed:10893414}.
CC -!- DISRUPTION PHENOTYPE: Mice develop to blastocyst stage, probably as a
CC result of maternally-derived Nasp, and then die.
CC {ECO:0000269|PubMed:16728391}.
CC -!- SIMILARITY: Belongs to the NASP family. {ECO:0000305}.
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DR EMBL; AF034610; AAB87567.2; -; mRNA.
DR EMBL; AF095722; AAC64195.1; -; mRNA.
DR EMBL; AF349432; AAK31170.1; -; Genomic_DNA.
DR EMBL; AF349432; AAK31171.1; -; Genomic_DNA.
DR EMBL; AK083333; BAC38871.1; -; mRNA.
DR EMBL; AK132690; BAE21303.1; -; mRNA.
DR EMBL; BC004693; AAH04693.1; -; mRNA.
DR CCDS; CCDS18513.1; -. [Q99MD9-1]
DR CCDS; CCDS71451.1; -. [Q99MD9-2]
DR RefSeq; NP_001074944.1; NM_001081475.1.
DR RefSeq; NP_001271158.1; NM_001284229.1. [Q99MD9-2]
DR AlphaFoldDB; Q99MD9; -.
DR SMR; Q99MD9; -.
DR BioGRID; 206159; 12.
DR CORUM; Q99MD9; -.
DR IntAct; Q99MD9; 8.
DR STRING; 10090.ENSMUSP00000030456; -.
DR iPTMnet; Q99MD9; -.
DR PhosphoSitePlus; Q99MD9; -.
DR SwissPalm; Q99MD9; -.
DR REPRODUCTION-2DPAGE; Q99MD9; -.
DR EPD; Q99MD9; -.
DR jPOST; Q99MD9; -.
DR MaxQB; Q99MD9; -.
DR PaxDb; Q99MD9; -.
DR PeptideAtlas; Q99MD9; -.
DR PRIDE; Q99MD9; -.
DR ProteomicsDB; 286149; -. [Q99MD9-1]
DR ProteomicsDB; 286150; -. [Q99MD9-2]
DR Antibodypedia; 32662; 196 antibodies from 29 providers.
DR DNASU; 50927; -.
DR Ensembl; ENSMUST00000081182; ENSMUSP00000079946; ENSMUSG00000028693. [Q99MD9-2]
DR GeneID; 50927; -.
DR KEGG; mmu:50927; -.
DR UCSC; uc008ugw.1; mouse. [Q99MD9-2]
DR CTD; 4678; -.
DR MGI; MGI:1355328; Nasp.
DR VEuPathDB; HostDB:ENSMUSG00000028693; -.
DR eggNOG; KOG4563; Eukaryota.
DR GeneTree; ENSGT00390000016650; -.
DR InParanoid; Q99MD9; -.
DR PhylomeDB; Q99MD9; -.
DR BioGRID-ORCS; 50927; 11 hits in 72 CRISPR screens.
DR ChiTaRS; Nasp; mouse.
DR PRO; PR:Q99MD9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q99MD9; protein.
DR Bgee; ENSMUSG00000028693; Expressed in embryonic post-anal tail and 246 other tissues.
DR ExpressionAtlas; Q99MD9; baseline and differential.
DR Genevisible; Q99MD9; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0001824; P:blastocyst development; IMP:UniProtKB.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006335; P:DNA replication-dependent chromatin assembly; IDA:UniProtKB.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:MGI.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0043486; P:histone exchange; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR019544; Tetratricopeptide_SHNi-TPR_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF10516; SHNi-TPR; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Coiled coil; Cytoplasm;
KW DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; TPR repeat; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT CHAIN 2..773
FT /note="Nuclear autoantigenic sperm protein"
FT /id="PRO_0000261597"
FT REPEAT 43..76
FT /note="TPR 1"
FT /evidence="ECO:0000255"
FT REPEAT 237..270
FT /note="TPR 2"
FT /evidence="ECO:0000255"
FT REPEAT 528..561
FT /note="TPR 3"
FT /evidence="ECO:0000255"
FT REPEAT 570..603
FT /note="TPR 4"
FT /evidence="ECO:0000255"
FT REGION 115..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..127
FT /note="Histone-binding"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT REGION 210..242
FT /note="Histone-binding"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT REGION 258..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..498
FT /note="Histone-binding"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT REGION 683..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 126..160
FT /evidence="ECO:0000255"
FT COILED 595..648
FT /evidence="ECO:0000255"
FT MOTIF 702..708
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 127..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..475
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..726
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 33
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 123
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 169
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 241
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 284
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HD3"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 377
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66HD3"
FT MOD_RES 450
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 669
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 712
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT CROSSLNK 722
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:P49321"
FT VAR_SEQ 74..100
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10893414,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_052237"
FT VAR_SEQ 138..462
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10893414,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_052238"
FT CONFLICT 432
FT /note="K -> R (in Ref. 3; BAE21303)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="P -> Q (in Ref. 3; BAE21303)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="Missing (in Ref. 2; AAK31170)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 773 AA; 83954 MW; 63C5CCA025972390 CRC64;
MATESTAAAA IAAELVSADK IEDAPAPSTS ADKMESLDVD SEAKKLLGLG QKHLVMGDIP
AAVNAFQEAA SLLGKKYGET ANECGEAFFF YGKSLLELAR MENGVLGNAL EGVHVEEEEG
EKTEDESLVE NNDNVDEEAR EELREQVYDA MGEKEAKKAE GKSLTKPETD KEQESEVEKG
GREDMDISEP EEKLQETVEP TSKQLTESSE EAKEAAIPGL NEDEVASGKT EQESLCTEKG
KSISGAYVQN KEFRETVEEG EEIISLEKKP KETSEDQPIR AAEKQGTLMK VVEIEAEIDP
QVKSADVGGE EPKDQVATSE SELGKAVLME LSGQDVEASP VVAAEAGAEV SEKPGQEITV
IPNNGPVVGQ STVGDQTPSE PQTSAERLTE TKDGSSVEEV KAELVPEQEE AMLPVEESEA
AGDGVETKVA QKATEKAPED KFKIAANEET PERDEQMKEG EETEGSEEED RENDKAEETP
NESVLEKKSL QENEEEEIGN LELAWDMLDL AKIIFKRQET KEAQLYAAQA HLKLGEVSVE
SENYIQAVEE FQACLSLQEQ YLEAHDRLLA ETHYQLGLAY GYNSQYDEAV AQFGKSIDVI
EKRMAVLHEQ MKEAEGSFTE YEKEIEELKE LLPEIREKIE DAKESQRSGN VAELALKATL
VESSTSGFTP SGAGASVSMI ASRKPTDGAS SSNCVTDISH LVRKKRKPEE ESPRKDDAKK
AKQEPEVNGG SGDAVSSGKE VSENMEAEAE NQAESQTAEG TVESAATIKS TAC
