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Nucleolar protein 8 (Nucleolar protein Nop132)

 NOL8_HUMAN              Reviewed;        1167 AA.
Q76FK4; Q5TCC7; Q5TCC8; Q5TCD3; Q5TCD5; Q5TCD6; Q5TCD7; Q76D35;
Q7L3E2; Q9H586; Q9H795; Q9H7W7; Q9H9J6; Q9NWA4; Q9NWM4;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
27-SEP-2017, entry version 126.
RecName: Full=Nucleolar protein 8;
AltName: Full=Nucleolar protein Nop132;
Name=NOL8 {ECO:0000312|HGNC:HGNC:23387}; Synonyms=C9orf34, NOP132;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:BAD12268.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, INDUCTION, AND PHOSPHORYLATION.
PubMed=15132771; DOI=10.1111/j.1349-7006.2004.tb03227.x;
Jinawath N., Furukawa Y., Nakamura Y.;
"Identification of NOL8, a nucleolar protein containing an RNA
recognition motif (RRM), which was overexpressed in diffuse-type
gastric cancer.";
Cancer Sci. 95:430-435(2004).
[2] {ECO:0000305, ECO:0000312|EMBL:BAC99315.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 946-964,
FUNCTION, AND INTERACTION WITH NIP7; RRAGA; RRAGC AND RRAGD.
PubMed=14660641; DOI=10.1074/jbc.M305935200;
Sekiguchi T., Todaka Y., Wang Y., Hirose E., Nakashima N.,
Nishimoto T.;
"A novel human nucleolar protein, Nop132, binds to the G proteins,
RRAG A/C/D.";
J. Biol. Chem. 279:8343-8350(2004).
[3] {ECO:0000305, ECO:0000312|EMBL:BAB14857.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Embryonic head {ECO:0000312|EMBL:BAA91479.1},
Hepatoma {ECO:0000312|EMBL:BAA91356.1},
Smooth muscle {ECO:0000312|EMBL:BAB15003.1}, and
Teratocarcinoma {ECO:0000312|EMBL:BAB14857.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[5] {ECO:0000305, ECO:0000312|EMBL:AAH13788.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 473-1167 (ISOFORMS 1/2).
TISSUE=Colon {ECO:0000312|EMBL:AAH13788.2};
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; THR-888 AND
SER-890, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[7]
FUNCTION, INTERACTION WITH DDX18 AND DDX47, AND SUBCELLULAR LOCATION.
PubMed=16963496; DOI=10.1093/nar/gkl603;
Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T.;
"NOP132 is required for proper nucleolus localization of DEAD-box RNA
helicase DDX47.";
Nucleic Acids Res. 34:4593-4608(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-378; THR-381;
SER-837; SER-838; SER-843; SER-845; SER-1036; SER-1082; SER-1083;
SER-1084 AND SER-1099, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; THR-302; SER-304;
SER-378; THR-381; SER-837; THR-888; SER-1082; SER-1083 AND SER-1084,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; THR-888 AND
SER-890, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; THR-302; SER-304;
SER-365; TYR-376; SER-378; THR-381; THR-888; SER-890; SER-1082;
SER-1083; SER-1084 AND SER-1099, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; SER-331; SER-365;
SER-378; THR-381; SER-432; SER-723; THR-888; SER-890 AND SER-1099, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-837; SER-838; SER-843
AND SER-845, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1057, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-225; LYS-314 AND LYS-1057,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Plays an essential role in the survival of diffuse-type
gastric cancer cells. Acts as a nucleolar anchoring protein for
DDX47. May be involved in regulation of gene expression at the
post-transcriptional level or in ribosome biogenesis in cancer
cells. {ECO:0000269|PubMed:14660641, ECO:0000269|PubMed:15132771,
ECO:0000269|PubMed:16963496}.
-!- SUBUNIT: Interacts with the GTP form of RRAGA, RRAGC and RRAGD.
Interacts with NIP7. Interacts with DDX18; the interaction is RNA-
dependent. Interacts with DDX47; the interaction is RNA-dependent.
{ECO:0000269|PubMed:14660641, ECO:0000269|PubMed:16963496}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:15132771, ECO:0000269|PubMed:16963496}.
Note=Localizes in the nucleolar-organizing region during ribosome
biogenesis.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1 {ECO:0000269|PubMed:14660641, ECO:0000269|PubMed:15132771};
IsoId=Q76FK4-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:15164053};
IsoId=Q76FK4-2; Sequence=VSP_052055;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
Name=4 {ECO:0000269|PubMed:15164053};
IsoId=Q76FK4-4; Sequence=VSP_052056;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- TISSUE SPECIFICITY: Expressed in various diffuse-type gastric
cancers. Detected at lower levels in skeletal muscle.
{ECO:0000269|PubMed:15132771}.
-!- INDUCTION: Up-regulated in diffuse-type gastric cancers.
{ECO:0000269|PubMed:15132771}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:15132771}.
-!- SEQUENCE CAUTION:
Sequence=BAA91356.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA91356.1; Type=Frameshift; Positions=1136; Evidence={ECO:0000305};
Sequence=BAB14229.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB15003.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB105104; BAD12268.1; -; mRNA.
EMBL; AB109030; BAC99315.1; -; mRNA.
EMBL; AK000743; BAA91356.1; ALT_SEQ; mRNA.
EMBL; AK001049; BAA91479.1; -; mRNA.
EMBL; AK022755; BAB14229.1; ALT_INIT; mRNA.
EMBL; AK024245; BAB14857.1; -; mRNA.
EMBL; AK024786; BAB15003.1; ALT_INIT; mRNA.
EMBL; AL136097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC013788; AAH13788.2; -; mRNA.
CCDS; CCDS47993.1; -. [Q76FK4-1]
CCDS; CCDS59135.1; -. [Q76FK4-2]
CCDS; CCDS83384.1; -. [Q76FK4-4]
RefSeq; NP_001243323.1; NM_001256394.1. [Q76FK4-2]
RefSeq; NP_001317651.1; NM_001330722.1. [Q76FK4-4]
RefSeq; NP_060418.4; NM_017948.5. [Q76FK4-1]
RefSeq; XP_006717229.1; XM_006717166.3. [Q76FK4-1]
RefSeq; XP_006717230.1; XM_006717167.3. [Q76FK4-1]
RefSeq; XP_006717232.1; XM_006717169.3. [Q76FK4-2]
RefSeq; XP_006717233.1; XM_006717170.3. [Q76FK4-2]
RefSeq; XP_011517126.1; XM_011518824.2. [Q76FK4-2]
RefSeq; XP_016870365.1; XM_017014876.1. [Q76FK4-4]
UniGene; Hs.442199; -.
ProteinModelPortal; Q76FK4; -.
SMR; Q76FK4; -.
BioGrid; 120364; 31.
IntAct; Q76FK4; 11.
MINT; MINT-4539421; -.
STRING; 9606.ENSP00000401177; -.
iPTMnet; Q76FK4; -.
PhosphoSitePlus; Q76FK4; -.
BioMuta; NOL8; -.
DMDM; 74758950; -.
EPD; Q76FK4; -.
MaxQB; Q76FK4; -.
PaxDb; Q76FK4; -.
PeptideAtlas; Q76FK4; -.
PRIDE; Q76FK4; -.
Ensembl; ENST00000358855; ENSP00000351723; ENSG00000198000. [Q76FK4-2]
Ensembl; ENST00000442668; ENSP00000401177; ENSG00000198000. [Q76FK4-1]
Ensembl; ENST00000535387; ENSP00000441300; ENSG00000198000. [Q76FK4-4]
Ensembl; ENST00000542053; ENSP00000440709; ENSG00000198000. [Q76FK4-2]
Ensembl; ENST00000545558; ENSP00000441140; ENSG00000198000. [Q76FK4-1]
GeneID; 55035; -.
KEGG; hsa:55035; -.
UCSC; uc064uhl.1; human. [Q76FK4-1]
CTD; 55035; -.
DisGeNET; 55035; -.
EuPathDB; HostDB:ENSG00000198000.11; -.
GeneCards; NOL8; -.
HGNC; HGNC:23387; NOL8.
HPA; HPA044440; -.
HPA; HPA062922; -.
MIM; 611534; gene.
neXtProt; NX_Q76FK4; -.
OpenTargets; ENSG00000198000; -.
PharmGKB; PA134918056; -.
eggNOG; KOG4365; Eukaryota.
eggNOG; ENOG410Y5CN; LUCA.
GeneTree; ENSGT00390000004860; -.
HOVERGEN; HBG057565; -.
InParanoid; Q76FK4; -.
OMA; KHKDARR; -.
OrthoDB; EOG091G03DU; -.
PhylomeDB; Q76FK4; -.
TreeFam; TF323283; -.
ChiTaRS; NOL8; human.
GeneWiki; NOL8; -.
GenomeRNAi; 55035; -.
PRO; PR:Q76FK4; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000198000; -.
ExpressionAtlas; Q76FK4; baseline and differential.
Genevisible; Q76FK4; HS.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:1902570; P:protein localization to nucleolus; IMP:BHF-UCL.
GO; GO:0006364; P:rRNA processing; IMP:UniProtKB.
CDD; cd12226; RRM_NOL8; 1.
InterPro; IPR034138; NOP8_RRM.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome;
Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; RNA-binding; rRNA processing;
Ubl conjugation.
CHAIN 1 1167 Nucleolar protein 8.
/FTId=PRO_0000239443.
DOMAIN 8 89 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COILED 753 779 {ECO:0000255}.
COILED 886 924 {ECO:0000255}.
COMPBIAS 1113 1116 Poly-Phe. {ECO:0000255}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 302 302 Phosphothreonine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 331 331 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 376 376 Phosphotyrosine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 381 381 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 723 723 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 795 795 Phosphothreonine.
{ECO:0000250|UniProtKB:Q3UHX0}.
MOD_RES 801 801 Phosphoserine.
{ECO:0000250|UniProtKB:Q3UHX0}.
MOD_RES 837 837 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 838 838 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 843 843 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 845 845 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 888 888 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1036 1036 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1082 1082 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 1083 1083 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 1084 1084 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 1099 1099 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 225 225 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 314 314 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1057 1057 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 68 Missing (in isoform 2).
{ECO:0000303|PubMed:15164053}.
/FTId=VSP_052055.
VAR_SEQ 787 824 Missing (in isoform 4).
{ECO:0000303|PubMed:15164053}.
/FTId=VSP_052056.
VARIANT 470 470 G -> E (in dbSNP:rs58545014).
/FTId=VAR_061830.
VARIANT 748 748 V -> L (in dbSNP:rs2236344).
/FTId=VAR_052211.
VARIANT 841 841 D -> E (in dbSNP:rs15717).
/FTId=VAR_052212.
VARIANT 988 988 E -> D (in dbSNP:rs34224798).
/FTId=VAR_052213.
VARIANT 1021 1021 G -> S (in dbSNP:rs921122).
/FTId=VAR_052214.
CONFLICT 69 69 M -> I (in Ref. 2; BAC99315 and 3;
BAA91479). {ECO:0000305}.
CONFLICT 454 454 S -> G (in Ref. 3; BAB14857).
{ECO:0000305}.
CONFLICT 479 479 K -> E (in Ref. 3; BAB14857).
{ECO:0000305}.
CONFLICT 630 630 C -> W (in Ref. 2; BAC99315 and 3;
BAA91356). {ECO:0000305}.
CONFLICT 733 733 E -> G (in Ref. 3; BAB14857).
{ECO:0000305}.
CONFLICT 749 749 S -> G (in Ref. 3; BAB14857).
{ECO:0000305}.
CONFLICT 945 945 I -> L (in Ref. 2; BAC99315 and 3;
BAA91356). {ECO:0000305}.
CONFLICT 966 966 K -> R (in Ref. 2; BAC99315 and 3;
BAA91356). {ECO:0000305}.
SEQUENCE 1167 AA; 131616 MW; 6E64780D6F0E7415 CRC64;
MKVNRETKRL YVGGLSQDIS EADLQNQFSR FGEVSDVEII TRKDDQGNPQ KVFAYINISV
AEADLKKCMS VLNKTKWKGG TLQIQLAKES FLHRLAQERE AAKAKKEEST TGNANLLEKT
GGVDFHMKAV PGTEVPGHKN WVVSKFGRVL PVLHLKNQHK RKIIKYDPSK YCHNLKKIGE
DFSNTIPISS LTWELEGGND PMSKKRRGEF SDFHGPPKKI IKVQKDESST GSLAMSTRPR
RVIERPPLTQ QQAAQKRTCD SITPSKSSPV PVSDTQKLKN LPFKTSGLET AKKRNSISDD
DTDSEDELRM MIAKEENLQR TTQPSINESE SDPFEVVRDD FKSGVHKLHS LIGLGIKNRV
SCHDSDDDIM RNDREYDSGD TDEIIAMKKN VAKVKNSTEF SQMEKSTKKT SFKNRENCEL
SDHCIKLQKR KSNVESALSH GLKSLNRKSP SHSSSSEDAD SASELADSEG GEEYNAMMKN
CLRVNLTLAD LEQLAGSDLK VPNEDTKSDG PETTTQCKFD RGSKSPKTPT GLRRGRQCIR
PAEIVASLLE GEENTCGKQK PKENNLKPKF QAFKGVGCLY EKESMKKSLK DSVASNNKDQ
NSMKHEDPSI ISMEDGSPYV NGSLGEVTPC QHAKKANGPN YIQPQKRQTT FESQDRKAVS
PSSSEKRSKN PISRPLEGKK SLSLSAKTHN IGFDKDSCHS TTKTEASQEE RSDSSGLTSL
KKSPKVSSKD TREIKTDFSL SISNSSDVSA KDKHAEDNEK RLAALEARQK AKEVQKKLVH
NALANLDGHP EDKPTHIIFG SDSECETEET STQEQSHPGE EWVKESMGKT SGKLFDSSDD
DESDSEDDSN RFKIKPQFEG RAGQKLMDLQ SHFGTDDRFR MDSRFLETDS EEEQEEVNEK
KTAEEEELAE EKKKALNVVQ SVLQINLSNS TNRGSVAAKK FKDIIHYDPT KQDHATYERK
RDDKPKESKA KRKKKREEAE KLPEVSKEMY YNIAMDLKEI FQTTKYTSEK EEGTPWNEDC
GKEKPEEIQD PAALTSDAEQ PSGFTFSFFD SDTKDIKEET YRVETVKPGK IVWQEDPRLQ
DSSSEEEDVT EETDHRNSSP GEASLLEKET TRFFFFSKND ERLQGSDLFW RGVGSNMSRN
SWEARTTNLR MDCRKKHKDA KRKMKPK


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