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Proliferation marker protein Ki-67 (Antigen identified by monoclonal antibody Ki-67 homolog) (Antigen KI-67 homolog) (Antigen Ki67 homolog)

 KI67_MOUSE              Reviewed;        3177 AA.
E9PVX6; Q61769; Q7TSF6;
05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
05-APR-2011, sequence version 1.
22-NOV-2017, entry version 55.
RecName: Full=Proliferation marker protein Ki-67 {ECO:0000305};
AltName: Full=Antigen identified by monoclonal antibody Ki-67 homolog {ECO:0000305};
Short=Antigen KI-67 homolog {ECO:0000305};
Short=Antigen Ki67 homolog {ECO:0000305};
Name=Mki67 {ECO:0000312|MGI:MGI:106035};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=CBA/J; TISSUE=Testis;
PubMed=8834799;
Starborg M., Gell K., Brundell E., Hoog C.;
"The murine Ki-67 cell proliferation antigen accumulates in the
nucleolar and heterochromatic regions of interphase cells and at the
periphery of the mitotic chromosomes in a process essential for cell
cycle progression.";
J. Cell Sci. 109:143-153(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2379-3177.
TISSUE=Limb;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
SUBCELLULAR LOCATION.
PubMed=12355204; DOI=10.1007/s00412-002-0202-8;
Traut W., Endl E., Scholzen T., Gerdes J., Winking H.;
"The temporal and spatial distribution of the proliferation associated
Ki-67 protein during female and male meiosis.";
Chromosoma 111:156-164(2002).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337; SER-373; SER-1587;
SER-2545 AND THR-3021, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-276; SER-277;
SER-286; SER-287; SER-503; SER-588; THR-1150; SER-1152; THR-1159;
THR-1175; THR-1363; SER-1366; THR-1400; THR-1416; SER-1469; SER-1734;
SER-1825; THR-1868; THR-1884; THR-1989; THR-2005; THR-2073; SER-2076;
SER-2103; THR-2106; THR-2122; THR-2218; SER-2220; THR-2227; THR-2243;
SER-2390; SER-2392; SER-2423; SER-2425; SER-2545; SER-2780 AND
THR-3021, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2928, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=26949251; DOI=10.7554/eLife.13722;
Sobecki M., Mrouj K., Camasses A., Parisis N., Nicolas E., Lleres D.,
Gerbe F., Prieto S., Krasinska L., David A., Eguren M., Birling M.C.,
Urbach S., Hem S., Dejardin J., Malumbres M., Jay P., Dulic V.,
Lafontaine D.L.J., Feil R., Fisher D.;
"The cell proliferation antigen Ki-67 organises heterochromatin.";
Elife 5:0-0(2016).
[9]
FUNCTION.
PubMed=27362226; DOI=10.1038/nature18610;
Cuylen S., Blaukopf C., Politi A.Z., Mueller-Reichert T., Neumann B.,
Poser I., Ellenberg J., Hyman A.A., Gerlich D.W.;
"Ki-67 acts as a biological surfactant to disperse mitotic
chromosomes.";
Nature 535:308-312(2016).
-!- FUNCTION: Required to maintain individual mitotic chromosomes
dispersed in the cytoplasm following nuclear envelope disassembly
(PubMed:27362226). Associates with the surface of the mitotic
chromosome, the perichromosomal layer, and covers a substantial
fraction of the chromosome surface (PubMed:27362226). Prevents
chromosomes from collapsing into a single chromatin mass by
forming a steric and electrostatic charge barrier: the protein has
a high net electrical charge and acts as a surfactant, dispersing
chromosomes and enabling independent chromosome motility
(PubMed:27362226). Binds DNA, with a preference for supercoiled
DNA and AT-rich DNA (By similarity). Does not contribute to the
internal structure of mitotic chromosomes (PubMed:26949251). May
play a role in chromatin organization (PubMed:26949251). It is
however unclear whether it plays a direct role in chromatin
organization or whether it is an indirect consequence of its
function in maintaining mitotic chromosomes dispersed.
{ECO:0000250|UniProtKB:P46013, ECO:0000269|PubMed:26949251,
ECO:0000269|PubMed:27362226, ECO:0000305}.
-!- SUBUNIT: Interacts with KIF15. Interacts (via the FHA domain) with
NIFK. Interacts with PPP1CC. Part of a complex composed at least
of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A,
WDR5 and ZNF335; this complex may have a histone H3-specific
methyltransferase activity. {ECO:0000250|UniProtKB:P46013}.
-!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:12355204,
ECO:0000269|PubMed:8834799}. Nucleus {ECO:0000269|PubMed:12355204,
ECO:0000269|PubMed:8834799}. Nucleus, nucleolus
{ECO:0000269|PubMed:12355204, ECO:0000269|PubMed:8834799}.
Note=Associates with the surface of the mitotic chromosome, the
perichromosomal layer, and covers a substantial fraction of the
mitotic chromosome surface (PubMed:8834799, PubMed:12355204).
Associates with satellite DNA in G1 phase (By similarity). Binds
tightly to chromatin in interphase, chromatin-binding decreases in
mitosis when it associates with the surface of the condensed
chromosomes (By similarity). Predominantly localized in the G1
phase in the perinucleolar region, in the later phases it is also
detected throughout the nuclear interior, being predominantly
localized in the nuclear matrix (By similarity).
{ECO:0000250|UniProtKB:P46013, ECO:0000269|PubMed:12355204,
ECO:0000269|PubMed:8834799}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=E9PVX6-1; Sequence=Displayed;
Name=2;
IsoId=E9PVX6-2; Sequence=VSP_058551;
-!- TISSUE SPECIFICITY: Mainly present in proliferating cells (at
protein level). {ECO:0000269|PubMed:8834799}.
-!- DEVELOPMENTAL STAGE: Accumulates during the late G1 stage in the
nucleus and maximum expression is found during G2 phase and
mitosis (PubMed:8834799). During male meiosis, present in nuclei
of all stages from the spermatogonium through spermatocytes I and
II up to the earliest spermatid stage (early round spermatids) and
then fades out (PubMed:12355204). Not detected in later spermatid
stages or sperm (PubMed:12355204). During female meiosis, present
in prophase I oocytes of fetal ovaries, while it is absent in
resting oocytes. Reappears in oocytes of growing follicles and is
continuously present up to metaphase II (at protein level)
(PubMed:12355204). {ECO:0000269|PubMed:12355204,
ECO:0000269|PubMed:8834799}.
-!- PTM: Phosphorylated. Hyperphosphorylated in mitosis.
Hyperphosphorylated form does not bind DNA.
{ECO:0000250|UniProtKB:P46013}.
-!- DISRUPTION PHENOTYPE: No visible phenotype. Mice were born at the
expected Mendelian ratio and show no overt phenotype
(PubMed:26949251). Cells do not show proliferation defects, but
chromatin organization is impaired, with defects in
heterochromatin compaction and long-range genomic interactions
(PubMed:26949251). {ECO:0000269|PubMed:26949251}.
-!- CAUTION: Was thought to play a key role in cell proliferation, and
is commonly used as a marker of cell proliferation. However, its
primary function is uncoupled from cell proliferation
(PubMed:26949251). Required to maintain mitotic chromosomes
dispersed by forming a steric and electrostatic charge barrier
(PubMed:27362226). {ECO:0000269|PubMed:26949251,
ECO:0000269|PubMed:27362226}.
-!- SEQUENCE CAUTION:
Sequence=AAH53453.1; Type=Frameshift; Positions=2463; Evidence={ECO:0000305};
Sequence=CAA58026.1; Type=Frameshift; Positions=46, 54, 194, 213, 2853, 2860; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The contours of
heredity - Issue 186 of December 2016;
URL="https://web.expasy.org/spotlight/back_issues/186/";
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EMBL; X82786; CAA58026.1; ALT_FRAME; mRNA.
EMBL; AC123047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC053453; AAH53453.1; ALT_FRAME; mRNA.
CCDS; CCDS52421.1; -. [E9PVX6-1]
PIR; T30249; T30249.
RefSeq; NP_001074586.2; NM_001081117.2. [E9PVX6-1]
UniGene; Mm.4078; -.
ProteinModelPortal; E9PVX6; -.
SMR; E9PVX6; -.
IntAct; E9PVX6; 19.
MINT; MINT-4109797; -.
STRING; 10090.ENSMUSP00000033310; -.
iPTMnet; E9PVX6; -.
PhosphoSitePlus; E9PVX6; -.
MaxQB; E9PVX6; -.
PaxDb; E9PVX6; -.
PeptideAtlas; E9PVX6; -.
PRIDE; E9PVX6; -.
Ensembl; ENSMUST00000033310; ENSMUSP00000033310; ENSMUSG00000031004. [E9PVX6-1]
GeneID; 17345; -.
KEGG; mmu:17345; -.
UCSC; uc009kem.2; mouse. [E9PVX6-1]
CTD; 4288; -.
MGI; MGI:106035; Mki67.
eggNOG; ENOG410JR7C; Eukaryota.
eggNOG; ENOG410ZXYW; LUCA.
GeneTree; ENSGT00530000064425; -.
HOGENOM; HOG000113223; -.
HOVERGEN; HBG006213; -.
InParanoid; E9PVX6; -.
KO; K17582; -.
OMA; QTPKEKA; -.
OrthoDB; EOG091G005S; -.
TreeFam; TF336000; -.
ChiTaRS; Mki67; mouse.
PRO; PR:E9PVX6; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000031004; -.
ExpressionAtlas; E9PVX6; baseline and differential.
Genevisible; E9PVX6; MM.
GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
GO; GO:0000793; C:condensed chromosome; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IDA:MGI.
GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
GO; GO:1990705; P:cholangiocyte proliferation; IDA:MGI.
GO; GO:0006259; P:DNA metabolic process; IEA:Ensembl.
GO; GO:0072574; P:hepatocyte proliferation; IDA:MGI.
GO; GO:0030212; P:hyaluronan metabolic process; IEA:Ensembl.
GO; GO:0051321; P:meiotic cell cycle; IDA:MGI.
GO; GO:1902275; P:regulation of chromatin organization; IMP:UniProtKB.
GO; GO:0051983; P:regulation of chromosome segregation; ISS:UniProtKB.
GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
CDD; cd00060; FHA; 1.
InterPro; IPR000253; FHA_dom.
InterPro; IPR012568; K167R.
InterPro; IPR029334; PP1-bd.
InterPro; IPR008984; SMAD_FHA_dom_sf.
Pfam; PF00498; FHA; 1.
Pfam; PF08065; K167R; 17.
Pfam; PF15276; PP1_bind; 1.
SMART; SM00240; FHA; 1.
SMART; SM01295; K167R; 16.
SUPFAM; SSF49879; SSF49879; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Cell cycle;
Chromosome; Complete proteome; DNA-binding; Isopeptide bond;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Repeat; Ubl conjugation.
CHAIN 1 3177 Proliferation marker protein Ki-67.
/FTId=PRO_0000437535.
DOMAIN 27 76 FHA. {ECO:0000255|PROSITE-
ProRule:PRU00086}.
DOMAIN 462 509 PP1-binding. {ECO:0000255}.
REPEAT 994 1101 K167R 1. {ECO:0000255}.
REPEAT 1108 1216 K167R 2. {ECO:0000255}.
REPEAT 1228 1336 K167R 3. {ECO:0000255}.
REPEAT 1348 1450 K167R 4. {ECO:0000255}.
REPEAT 1461 1569 K167R 5. {ECO:0000255}.
REPEAT 1582 1684 K167R 6. {ECO:0000255}.
REPEAT 1696 1806 K167R 7. {ECO:0000255}.
REPEAT 1817 1925 K167R 8. {ECO:0000255}.
REPEAT 1937 2046 K167R 9. {ECO:0000255}.
REPEAT 2059 2163 K167R 10. {ECO:0000255}.
REPEAT 2175 2284 K167R 11. {ECO:0000255}.
REPEAT 2296 2405 K167R 12. {ECO:0000255}.
REPEAT 2419 2526 K167R 13. {ECO:0000255}.
REPEAT 2643 2748 K167R 15. {ECO:0000255}.
REPEAT 2762 2870 K167R 16. {ECO:0000255}.
NP_BIND 2973 2980 ATP. {ECO:0000255}.
MOD_RES 125 125 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 128 128 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 250 250 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 277 277 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 286 286 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 307 307 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 316 316 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 503 503 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 588 588 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 701 701 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1062 1062 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1114 1114 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1122 1122 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1125 1125 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1150 1150 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1152 1152 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1159 1159 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1175 1175 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1189 1189 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1215 1215 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1235 1235 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1243 1243 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1279 1279 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1295 1295 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1307 1307 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1315 1315 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1335 1335 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1356 1356 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1363 1363 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1366 1366 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1400 1400 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1416 1416 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1469 1469 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1477 1477 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1480 1480 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1513 1513 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1542 1542 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1587 1587 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 1609 1609 N6-acetyllysine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1684 1684 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1712 1712 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1734 1734 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1766 1766 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1779 1779 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1805 1805 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1825 1825 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1859 1859 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1868 1868 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1884 1884 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1924 1924 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1944 1944 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1966 1966 N6-acetyllysine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 1989 1989 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2005 2005 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2025 2025 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2045 2045 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2065 2065 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2073 2073 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2076 2076 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2095 2095 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2103 2103 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2106 2106 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2122 2122 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2162 2162 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2182 2182 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2190 2190 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2198 2198 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2218 2218 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2220 2220 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2227 2227 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2243 2243 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2283 2283 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2303 2303 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2311 2311 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2348 2348 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2390 2390 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2392 2392 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2405 2405 Phosphothreonine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2423 2423 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2425 2425 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2464 2464 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2487 2487 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2545 2545 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 2592 2592 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2649 2649 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2768 2768 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 2780 2780 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2928 2928 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 2980 2980 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
MOD_RES 3021 3021 Phosphothreonine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 3061 3061 Phosphoserine.
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 236 236 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 1013 1013 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 1026 1026 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 1082 1082 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 1082 1082 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 1317 1317 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 1668 1668 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 2027 2027 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 2027 2027 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 2451 2451 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 2675 2675 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 2675 2675 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P46013}.
CROSSLNK 2909 2909 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P46013}.
VAR_SEQ 1150 1390 Missing (in isoform 2).
/FTId=VSP_058551.
CONFLICT 344 344 E -> G (in Ref. 1; CAA58026).
{ECO:0000305}.
CONFLICT 364 365 AA -> TP (in Ref. 1; CAA58026).
{ECO:0000305}.
CONFLICT 372 372 A -> G (in Ref. 1; CAA58026).
{ECO:0000305}.
CONFLICT 384 385 KK -> PQ (in Ref. 1; CAA58026).
{ECO:0000305}.
CONFLICT 401 401 K -> N (in Ref. 1; CAA58026).
{ECO:0000305}.
CONFLICT 546 546 K -> N (in Ref. 1; CAA58026).
{ECO:0000305}.
CONFLICT 622 622 Q -> P (in Ref. 1; CAA58026).
{ECO:0000305}.
CONFLICT 1079 1079 E -> G (in Ref. 1; CAA58026).
{ECO:0000305}.
CONFLICT 2911 2911 D -> V (in Ref. 1; CAA58026).
{ECO:0000305}.
CONFLICT 2978 2978 H -> Y (in Ref. 1; CAA58026).
{ECO:0000305}.
SEQUENCE 3177 AA; 350864 MW; 969A3BE300D755B0 CRC64;
MASSAHLVTI KRSGDDGAHF PLSLSSCLFG RSIECDIRIQ LPVVSKRHCK IEVKEQEAIL
YNFSSTNPTQ VNGVTIDEPV RLRHGDIITI IDRSFRYEDG NHEDGSKPTE FPGKSLGKEP
SRRASRDSFC ADPDGEGQDT KASKMTASRR SFVYAKGLSA DSPASDGSKN SVSQDSSGHV
EQHTGRNIVE PTSGDLFKKS RSTGSSYREP KSSPTQSLSN SNEKESPFEK LYQSMKEELD
VKSQKSCRKS EPQPDRAAEE SRETQLLVSG RARAKSSGST PVTAASSPKV GKIWTERWRG
GMVPVQTSTE TAKMKTPVRH SQQLKDEDSR VTGRRHSVNL DEGESAQAVH KTVTPGKLAT
RNQAAVEAGD VASPADTPEH SSSKKRSIPA KVEAPSAETQ KRLSLTQRLV PGEKKTPKGS
FSKPEKLATA AEQTCSGLPG LSSVDISNFG DSINKSEGMP MKRRRVSFGG HLRPELFDEN
LPPNTPLKRG ETPTKRKSLG THSPAVLKTI IKERPQSPGK QESPGITPPR TNDQRRRSGR
TSSGSKFLCE TDIPKKAGRK SGNLPAKRAS ISRSQHGILQ MICSKRRSGA SEANLIVAKS
WADVVKLGVK QTQTKVAKHV PQKQTSKRQR RPSTPKKPTS NLHNQFTTGH ANSPCTIVVG
RAQIEKVSVP ARPYKMLNNL MLNRKVDFSE DLSGLTEMFK TPVKEKQQQM SDTGSVLSNS
ANLSERQLQV TNSGDIPEPI TTEILGEKVL SSTRNAAKQQ SDRYSASPTL RRRSIKHENT
VQTPKNVHNI TDLEKKTPVS ETEPLKTASS VSKLRRSREL RHTLVETMNE KTEAVLAENT
TARHLRGTFR EQKVDQQVQD NENAPQRCKE SGELSEGSEK TSARRSSARK QKPTKDLLGS
QMVTQTADYA EELLSQGQGT IQNLEESMHM QNTSISEDQG ITEKKVNIIV YATKEKHSPK
TPGKKAQPLE GPAGLKEHFE TPNPKDKPIT EDRTRVLCKS PQVTTENITT NTKPQTSTSG
KKVDMKEESS ALTKRIHMPG ESRHNPKILK LECEDIKALK QSENEMLTST VNGSKRTLEK
SKKKAQPLED LTCFQELFIS PVPTNIIKKI PSKSPHTQPV RTPASTKRLS KTGLSKVDVR
QEPSTLGKRT KSPGRAPGTP APVQEENDST AFMETPKQKL DFAGNSSGSK RRSRTSKNRS
QPLEDLDGFQ ELFQTPAGAS DSVTVEESAK ISLESSQAEP VKTPASTKRR SKMSLMKVDM
KELSILEKQT QSRGRDAGTP APMQEGNGTT AIMETPKQKL DFTGNSTGHK RRPRTPKIRA
QPLEDLDGFQ ELFQTPAGAN DSVTVEESAK MSLESSQAEP VKTPASTKRL SKTDLSKVDV
REDPSILGKK TKSPGRAPGT PAPVQEENDC TAYMETPKQK LESIENLTGL RKQSRTPKDI
TGFQDSFQIP DHANGPLVVV KTKKMFFNSP QPESAITRKS RERQSRASIS KIDVKEELLE
SEEHLQLGEG VDTFQVSTNK VIRSSRKPAK RKLDSTAGMP NSKRMRCSSK DNTPCLEDLN
GFQELFQMPG YANDSLTTGI STMLARSPQL GPVRTQINKK SLPKIILRKM DVTEEISGLW
KQSLGRVHTT QEQEDNAIKA IMEIPKETLQ TAADGTRLTR QPQTPKEKVQ PLEDHSVFQE
LFQTSRYCSD PLIGNKQTRM SLRSPQPGFV RTPRTSKRLA KTSVGNIAVR EKISPVSLPQ
CATGEVVHIP IGPEDDTENK GVKESTPQTL DSSASRTVSK RQQGAHEERP QFSGDLFHPQ
ELFQTPASGK DPVTVDETTK IALQSPQPGH IINPASMKRQ SNMSLRKDMR EFSILEKQTQ
SRGRDAGTPA PMQEENGTTA IMETPKQKLD FIGNSTGHKR RPRTPKNRAQ PLEDLDGFQE
LFQTPAGASD PVSVEESAKI SLASSQAEPV RTPASTKRRS KTGLSKVDVR QEPSTLGKRM
KSLGRAPGTP APVQEENDST AFMETPKQKL DFTGNSSGHK RRPQTPKIRA QPLEDLDGFQ
ELFQTPAGAN DSVTVEESVK MSLESSQAEP VKTPASTKRL SKTGLSKVDV REDPSILEKK
TKSPGTPAPV QEENDCTAFM ETPKQKLDFT GNSSGHKRRP RTPKIRAQPL EDLDGFQELF
QTPAGASDSV TVEESAKMSL ESSQAKPVKT PASTKRLSKT GLSKVDVRED PSTLGKKTKS
PGRAPGTPAP VQEENDSTAF METPKQKLDF AENSSGSKRR SRTSKNRSQP LEDLDGFQEL
FQTPAGASNP VSVEESAKIS LESSQAEPVR TRASTKRLSK TGLNKMDVRE GHSPLSKSSC
ASQKVMQTLT LGEDHGRETK DGKVLLAQKL EPAIYVTRGK RQQRSCKKRS QSPEDLSGVQ
EVFQTSGHNK DSVTVDNLAK LPSSSPPLEP TDTSVTSRRQ ARTGLRKVHV KNELSGGIMH
PQISGEIVDL PREPEGEGKV IKTRKQSVKR KLDTEVNVPR SKRQRITRAE KTLEDLPGFQ
ELCQAPSLVM DSVIVEKTPK MPDKSPEPVD TTSETQARRR LRRLVVTEEP IPQRKTTRVV
RQTRNTQKEP ISDNQGMEEF KESSVQKQDP SVSLTGRRNQ PRTVKEKTQP LEELTSFQEE
TAKRISSKSP QPEEKETLAG LKRQLRIQLI NDGVKEEPTA QRKQPSRETR NTLKEPVGDS
INVEEVKKST KQKIDPVASV PVSKRPRRVP KEKAQALELA GLKGPIQTLG HTDESASDKG
PTQMPCNSLQ PEQVDSFQSS PRRPRTRRGK VEADEEPSAV RKTVSTSRQT MRSRKVPEIG
NNGTQVSKAS IKQTLDTVAK VTGSRRQLRT HKDGVQPLEV LGDSKEITQI SDHSEKLAHD
TSILKSTQQQ KPDSVKPLRT CRRVLRASKE DPKEVLVDTR DHATLQSKSN PLLSPKRKSA
RDGSIVRTRA LRSLAPKQEA TDEKPVPEKK RAASSKRHVS PEPVKMKHLK IVSNKLESVE
EQVSTVMKTE EMEAKRENPV TPDQNSRYRK KTNVKQPRPK FDASAENVGI KKNEKTMKTA
SQETELQNPD DGAKKSTSRG QVSGKRTCLR SRGTTEMPQP CEAEEKTSKP AAEILIKPQE
EKGVSGESDV RCLRSRKTRV ALDSEPKPRV TRGTKKDAKT LKEDEDIVCT KKLRTRS


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