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RNA-binding protein 6 (Lung cancer antigen NY-LU-12) (Protein G16) (RNA-binding motif protein 6) (RNA-binding protein DEF-3)

 RBM6_HUMAN              Reviewed;        1123 AA.
P78332; B4E0G6; O60549; O75524; Q86SS3;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 5.
18-JUL-2018, entry version 169.
RecName: Full=RNA-binding protein 6;
AltName: Full=Lung cancer antigen NY-LU-12;
AltName: Full=Protein G16;
AltName: Full=RNA-binding motif protein 6;
AltName: Full=RNA-binding protein DEF-3;
Name=RBM6; Synonyms=DEF3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lung;
PubMed=9500467;
Gure A.O., Altorki N.K., Stockert E., Scanlan M.J., Old L.J.,
Chen Y.-T.;
"Human lung cancer antigens recognized by autologous antibodies:
definition of a novel cDNA derived from the tumor suppressor gene
locus on chromosome 3p21.3.";
Cancer Res. 58:1034-1041(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10352938; DOI=10.1038/sj.ejhg.5200334;
Timmer T., Terpstra P., van den Berg A., Veldhuis P.M., Ter Elst A.,
Voutsinas G., Hulsbeek M.M.F., Draaijers T.G., Looman M.W.G., Kok K.,
Naylor S.L., Buys C.H.C.M.;
"A comparison of genomic structures and expression patterns of two
closely related flanking genes in a critical lung cancer region at
3p21.3.";
Eur. J. Hum. Genet. 7:478-486(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10353602; DOI=10.1038/sj.onc.1202601;
Drabkin H.A., West J.D., Hotfilder M., Heng Y.M., Erickson P.,
Calvo R., Dalmau J., Gemmill R.M., Sablitzky F.;
"DEF-3(g16/NY-LU-12), an RNA binding protein from the 3p21.3
homozygous deletion region in SCLC.";
Oncogene 18:2589-2597(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Latif F., Duh F.-M., Wei M.H., Sekido Y., Forgacs E., Minna J.D.,
Lerman M.I.;
"A highly conserved and universally expressed gene is interrupted by a
homozygous deletion in a small cell lung cancer cell line NCI-H740.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Thymus;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
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).
[8]
DISCUSSION OF SEQUENCE, AND VARIANT PHE-353.
PubMed=11085536;
The international lung cancer chromosome 3p21.3 tumor suppressor gene consortium;
Lerman M.I., Minna J.D.;
"The 630-kb lung cancer homozygous deletion region on human chromosome
3p21.3: identification and evaluation of the resident candidate tumor
suppressor genes.";
Cancer Res. 60:6116-6133(2000).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1025, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 AND SER-362, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1025, AND 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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-362 AND
SER-1025, 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).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 AND SER-362, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-891 AND SER-1025, 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).
[16]
INTERACTION WITH FAM168B.
PubMed=20716133; DOI=10.1111/j.1582-4934.2010.01134.x;
Mishra M., Akatsu H., Heese K.;
"The novel protein MANI modulates neurogenesis and neurite-cone
growth.";
J. Cell. Mol. Med. 15:1713-1725(2011).
[17]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-240; THR-344;
SER-360; SER-362; SER-1022 AND SER-1025, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-362; SER-891
AND SER-1025, 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).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-386; LYS-453; LYS-569 AND
LYS-1046, 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).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-453 AND LYS-569, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-453 AND LYS-569, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-331; LYS-386;
LYS-453; LYS-469; LYS-569; LYS-871; LYS-879; LYS-887; LYS-935;
LYS-948; LYS-991; LYS-1019; LYS-1042; LYS-1046 AND LYS-1066, 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: Specifically binds poly(G) RNA homopolymers in vitro.
-!- SUBUNIT: May interact with FAM168B.
-!- INTERACTION:
P26641-2:EEF1G; NbExp=3; IntAct=EBI-2692323, EBI-10177695;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P78332-1; Sequence=Displayed;
Name=2;
IsoId=P78332-2; Sequence=VSP_045202;
Note=No experimental confirmation available.;
Name=3;
IsoId=P78332-3; Sequence=VSP_057401, VSP_057402;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous in adults.
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EMBL; AF042857; AAC05826.1; -; mRNA.
EMBL; AF069517; AAC21578.1; -; mRNA.
EMBL; AF091264; AAD04160.1; -; mRNA.
EMBL; U50839; AAC35207.1; -; mRNA.
EMBL; AK303371; BAG64428.1; -; mRNA.
EMBL; AC104450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC046643; AAH46643.1; -; mRNA.
CCDS; CCDS2809.1; -. [P78332-1]
CCDS; CCDS54586.1; -. [P78332-2]
RefSeq; NP_001161054.1; NM_001167582.1. [P78332-2]
RefSeq; NP_005768.1; NM_005777.2. [P78332-1]
RefSeq; XP_005264843.1; XM_005264786.1.
RefSeq; XP_005264844.1; XM_005264787.2.
RefSeq; XP_016860988.1; XM_017005499.1.
RefSeq; XP_016860989.1; XM_017005500.1. [P78332-2]
RefSeq; XP_016860990.1; XM_017005501.1. [P78332-2]
RefSeq; XP_016860991.1; XM_017005502.1. [P78332-2]
UniGene; Hs.696735; -.
ProteinModelPortal; P78332; -.
BioGrid; 115479; 33.
IntAct; P78332; 21.
STRING; 9606.ENSP00000266022; -.
iPTMnet; P78332; -.
PhosphoSitePlus; P78332; -.
BioMuta; RBM6; -.
DMDM; 116242749; -.
EPD; P78332; -.
MaxQB; P78332; -.
PaxDb; P78332; -.
PeptideAtlas; P78332; -.
PRIDE; P78332; -.
ProteomicsDB; 57570; -.
DNASU; 10180; -.
Ensembl; ENST00000266022; ENSP00000266022; ENSG00000004534. [P78332-1]
Ensembl; ENST00000422955; ENSP00000392939; ENSG00000004534. [P78332-2]
Ensembl; ENST00000425608; ENSP00000408665; ENSG00000004534. [P78332-3]
Ensembl; ENST00000442092; ENSP00000393530; ENSG00000004534. [P78332-2]
GeneID; 10180; -.
KEGG; hsa:10180; -.
UCSC; uc003cyc.4; human. [P78332-1]
UCSC; uc062jzu.1; human.
CTD; 10180; -.
DisGeNET; 10180; -.
EuPathDB; HostDB:ENSG00000004534.14; -.
GeneCards; RBM6; -.
HGNC; HGNC:9903; RBM6.
HPA; HPA026272; -.
HPA; HPA027164; -.
MIM; 606886; gene.
neXtProt; NX_P78332; -.
OpenTargets; ENSG00000004534; -.
PharmGKB; PA34268; -.
eggNOG; ENOG410IQDR; Eukaryota.
eggNOG; ENOG4111TS3; LUCA.
GeneTree; ENSGT00510000046476; -.
HOGENOM; HOG000133022; -.
HOVERGEN; HBG007537; -.
InParanoid; P78332; -.
OMA; YDLDFRG; -.
OrthoDB; EOG091G00Y8; -.
PhylomeDB; P78332; -.
TreeFam; TF315789; -.
ChiTaRS; RBM6; human.
GeneWiki; RBM6; -.
GenomeRNAi; 10180; -.
PRO; PR:P78332; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000004534; -.
CleanEx; HS_RBM6; -.
ExpressionAtlas; P78332; baseline and differential.
Genevisible; P78332; HS.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0006396; P:RNA processing; TAS:ProtInc.
CDD; cd16163; OCRE_RBM6; 1.
CDD; cd12314; RRM1_RBM6; 1.
CDD; cd12563; RRM2_RBM6; 1.
Gene3D; 3.30.70.330; -; 2.
InterPro; IPR000467; G_patch_dom.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR028806; RBM6.
InterPro; IPR035617; RBM6_OCRE.
InterPro; IPR034123; RBM6_RRM1.
InterPro; IPR034125; RBM6_RRM2.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR13948:SF22; PTHR13948:SF22; 1.
Pfam; PF01585; G-patch; 1.
SMART; SM00443; G_patch; 1.
SMART; SM00360; RRM; 2.
SUPFAM; SSF54928; SSF54928; 2.
PROSITE; PS50174; G_PATCH; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; RNA-binding;
Ubl conjugation.
CHAIN 1 1123 RNA-binding protein 6.
/FTId=PRO_0000081760.
DOMAIN 456 536 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 1051 1097 G-patch. {ECO:0000255|PROSITE-
ProRule:PRU00092}.
COMPBIAS 826 829 Poly-Glu.
COMPBIAS 892 895 Poly-Pro.
COMPBIAS 915 921 Poly-Glu.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 344 344 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 360 360 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 891 891 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 1022 1022 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1025 1025 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CROSSLNK 36 36 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 331 331 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 386 386 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 453 453 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 469 469 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 569 569 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 871 871 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 879 879 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 887 887 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 935 935 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 948 948 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 991 991 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1019 1019 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1042 1042 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1046 1046 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 1066 1066 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 522 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045202.
VAR_SEQ 496 520 YDYGYVCVEFSLLEDAIGCMEANQG -> NSNDPGQRSYPG
VCIKPGFLVLQTM (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057401.
VAR_SEQ 521 1123 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057402.
VARIANT 353 353 S -> F (in a non-small cell lung cancer
cell line; dbSNP:rs61731329).
{ECO:0000269|PubMed:11085536}.
/FTId=VAR_014226.
VARIANT 721 721 N -> T (in dbSNP:rs34707170).
/FTId=VAR_052216.
CONFLICT 642 642 R -> K (in Ref. 2; AAC21578).
{ECO:0000305}.
CONFLICT 710 710 A -> V (in Ref. 1; AAC05826).
{ECO:0000305}.
CONFLICT 796 796 T -> S (in Ref. 1; AAC05826).
{ECO:0000305}.
SEQUENCE 1123 AA; 128644 MW; 2952ED1BAA839DE4 CRC64;
MWGDSRPANR TGPFRGSQEE RFAPGWNRDY PPPPLKSHAQ ERHSGNFPGR DSLPFDFQGH
SGPPFANVEE HSFSYGARDG PHGDYRGGEG PGHDFRGGDF SSSDFQSRDS SQLDFRGRDI
HSGDFRDREG PPMDYRGGDG TSMDYRGREA PHMNYRDRDA HAVDFRGRDA PPSDFRGRGT
YDLDFRGRDG SHADFRGRDL SDLDFRAREQ SRSDFRNRDV SDLDFRDKDG TQVDFRGRGS
GTTDLDFRDR DTPHSDFRGR HRSRTDQDFR GREMGSCMEF KDREMPPVDP NILDYIQPST
QDREHSGMNV NRREESTHDH TIERPAFGIQ KGEFEHSETR EGETQGVAFE HESPADFQNS
QSPVQDQDKS QLSGREEQSS DAGLFKEEGG LDFLGRQDTD YRSMEYRDVD HRLPGSQMFG
YGQSKSFPEG KTARDAQRDL QDQDYRTGPS EEKPSRLIRL SGVPEDATKE EILNAFRTPD
GMPVKNLQLK EYNTGYDYGY VCVEFSLLED AIGCMEANQG TLMIQDKEVT LEYVSSLDFW
YCKRCKANIG GHRSSCSFCK NPREVTEAKQ ELITYPQPQK TSIPAPLEKQ PNQPLRPADK
EPEPRKREEG QESRLGHQKR EAERYLPPSR REGPTFRRDR ERESWSGETR QDGESKTIML
KRIYRSTPPE VIVEVLEPYV RLTTANVRII KNRTGPMGHT YGFIDLDSHA EALRVVKILQ
NLDPPFSIDG KMVAVNLATG KRRNDSGDHS DHMHYYQGKK YFRDRRGGGR NSDWSSDTNR
QGQQSSSDCY IYDSATGYYY DPLAGTYYDP NTQQEVYVPQ DPGLPEEEEI KEKKPTSQGK
SSSKKEMSKR DGKEKKDRGV TRFQENASEG KAPAEDVFKK PLPPTVKKEE SPPPPKVVNP
LIGLLGEYGG DSDYEEEEEE EQTPPPQPRT AQPQKREEQT KKENEEDKLT DWNKLACLLC
RRQFPNKEVL IKHQQLSDLH KQNLEIHRKI KQSEQELAYL ERREREGKFK GRGNDRREKL
QSFDSPERKR IKYSRETDSD RKLVDKEDID TSSKGGCVQQ ATGWRKGTGL GYGHPGLASS
EEAEGRMRGP SVGASGRTSK RQSNETYRDA VRRVMFARYK ELD


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