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Retinoblastoma-like protein 2 (130 kDa retinoblastoma-associated protein) (p130) (Retinoblastoma-related protein 2) (RBR-2) (pRb2)

 RBL2_HUMAN              Reviewed;        1139 AA.
Q08999; B7Z913; Q15073; Q16084; Q8NE70; Q92812;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 3.
25-OCT-2017, entry version 172.
RecName: Full=Retinoblastoma-like protein 2;
AltName: Full=130 kDa retinoblastoma-associated protein;
Short=p130;
AltName: Full=Retinoblastoma-related protein 2;
Short=RBR-2;
AltName: Full=pRb2;
Name=RBL2; Synonyms=RB2;
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=Placenta, and Spleen;
PubMed=8253383; DOI=10.1101/gad.7.12a.2366;
Li Y., Graham C., Lacy S., Duncan A.M.V., Whyte P.;
"The adenovirus E1A-associated 130-kD protein is encoded by a member
of the retinoblastoma gene family and physically interacts with
cyclins A and E.";
Genes Dev. 7:2366-2377(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8253384; DOI=10.1101/gad.7.12a.2378;
Hannon G.J., Demetrick D., Beach D.;
"Isolation of the Rb-related p130 through its interaction with CDK2
and cyclins.";
Genes Dev. 7:2378-2391(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Trachea;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 58-1139 (ISOFORM 1).
PubMed=8361765;
Mayol X., Grana X., Baldi A., Sang N., Hu Q., Giordano A.;
"Cloning of a new member of the retinoblastoma gene family (pRb2)
which binds to the E1A transforming domain.";
Oncogene 8:2561-2566(1993).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
TISSUE=Placenta;
PubMed=8643454; DOI=10.1073/pnas.93.10.4629;
Baldi A., Boccia V., Claudio P.P., de Luca A., Giordano A.;
"Genomic structure of the human retinoblastoma-related Rb2/p130
gene.";
Proc. Natl. Acad. Sci. U.S.A. 93:4629-4632(1996).
[8]
PHOSPHORYLATION AT SER-639; SER-952; SER-966; SER-971; SER-972;
SER-973; THR-974; SER-981; SER-982 AND THR-986, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=11042701; DOI=10.1038/sj.onc.1203893;
Canhoto A.J., Chestukhin A., Litovchick L., DeCaprio J.A.;
"Phosphorylation of the retinoblastoma-related protein p130 in growth-
arrested cells.";
Oncogene 19:5116-5122(2000).
[9]
INTERACTION WITH AATF.
PubMed=12450794; DOI=10.1016/S1535-6108(02)00182-4;
Bruno T., De Angelis R., De Nicola F., Barbato C., Di Padova M.,
Corbi N., Libri V., Benassi B., Mattei E., Chersi A., Soddu S.,
Floridi A., Passananti C., Fanciulli M.;
"Che-1 affects cell growth by interfering with the recruitment of
HDAC1 by Rb.";
Cancer Cell 2:387-399(2002).
[10]
PHOSPHORYLATION AT SER-672.
PubMed=12435635; DOI=10.1101/gad.1011202;
Tedesco D., Lukas J., Reed S.I.;
"The pRb-related protein p130 is regulated by phosphorylation-
dependent proteolysis via the protein-ubiquitin ligase SCF(Skp2).";
Genes Dev. 16:2946-2957(2002).
[11]
INTERACTION WITH RINT1.
PubMed=16600870; DOI=10.1016/j.molcel.2006.02.016;
Kong L.-J., Meloni A.R., Nevins J.R.;
"The Rb-related p130 protein controls telomere lengthening through an
interaction with a Rad50-interacting protein, RINT-1.";
Mol. Cell 22:63-71(2006).
[12]
IDENTIFICATION IN THE DREAM COMPLEX.
PubMed=17671431; DOI=10.4161/cc.6.15.4512;
Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C.,
von Eyss B., Gagrica S., Haenel F., Brehm A., Gaubatz S.;
"LINC, a human complex that is related to pRB-containing complexes in
invertebrates regulates the expression of G2/M genes.";
Cell Cycle 6:1903-1913(2007).
[13]
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).
[14]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662; SER-672 AND
SER-1035, 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).
[16]
INTERACTION WITH PML.
PubMed=22002537; DOI=10.1038/emboj.2011.370;
Martin N., Benhamed M., Nacerddine K., Demarque M.D., van Lohuizen M.,
Dejean A., Bischof O.;
"Physical and functional interaction between PML and TBX2 in the
establishment of cellular senescence.";
EMBO J. 31:95-109(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413; SER-662; SER-688;
SER-1068; SER-1080 AND SER-1112, 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).
[18]
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).
[19]
VARIANT PHE-99.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
-!- FUNCTION: Key regulator of entry into cell division. Directly
involved in heterochromatin formation by maintaining overall
chromatin structure and, in particular, that of constitutive
heterochromatin by stabilizing histone methylation. Recruits and
targets histone methyltransferases KMT5B and KMT5C, leading to
epigenetic transcriptional repression. Controls histone H4 'Lys-
20' trimethylation. Probably acts as a transcription repressor by
recruiting chromatin-modifying enzymes to promoters. Potent
inhibitor of E2F-mediated trans-activation, associates
preferentially with E2F5. Binds to cyclins A and E. Binds to and
may be involved in the transforming capacity of the adenovirus E1A
protein. May act as a tumor suppressor.
-!- SUBUNIT: Interacts with AATF. Interacts with KMT5B, KMT5C and USP4
(By similarity). Component of the DREAM complex (also named LINC
complex) at least composed of E2F4, E2F5, LIN9, LIN37, LIN52,
LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The
complex exists in quiescent cells where it represses cell cycle-
dependent genes. It dissociates in S phase when LIN9, LIN37, LIN52
and LIN54 form a subcomplex that binds to MYBL2. Interacts with
RINT1. Interacts with PML (isoform PML-1, isoform PML-2, isoform
PML-3, isoform PML-4 and isoform PML-5). {ECO:0000250,
ECO:0000269|PubMed:12450794, ECO:0000269|PubMed:16600870,
ECO:0000269|PubMed:17671431, ECO:0000269|PubMed:22002537}.
-!- INTERACTION:
P03255:- (xeno); NbExp=2; IntAct=EBI-971439, EBI-2603114;
Q13574-2:DGKZ; NbExp=2; IntAct=EBI-971439, EBI-715527;
Q16254:E2F4; NbExp=7; IntAct=EBI-971439, EBI-448943;
Q6MZP7:LIN54; NbExp=10; IntAct=EBI-971439, EBI-1389411;
P24610:Pax3 (xeno); NbExp=3; IntAct=EBI-971439, EBI-1208116;
P67775:PPP2CA; NbExp=2; IntAct=EBI-971439, EBI-712311;
I6L8A6:RBBP8; NbExp=3; IntAct=EBI-971439, EBI-11525639;
Q923E4:Sirt1 (xeno); NbExp=2; IntAct=EBI-971439, EBI-1802585;
Q61412:Vsx2 (xeno); NbExp=4; IntAct=EBI-971439, EBI-1208174;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q08999-1; Sequence=Displayed;
Name=2;
IsoId=Q08999-2; Sequence=VSP_054328, VSP_054329;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: G0-restricted expression.
-!- PTM: During G0 and early G1 phase of the cell cycle,
phosphorylated on Ser-639 and on 5 sites within the domain B.
Phosphorylation on Ser-672 in G1 leads to its ubiquitin-dependent
proteolysis. {ECO:0000269|PubMed:11042701,
ECO:0000269|PubMed:12435635}.
-!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RBL2ID443.html";
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EMBL; X76061; CAA53661.1; -; mRNA.
EMBL; S67171; AAB29227.1; -; mRNA.
EMBL; AK304283; BAH14149.1; -; mRNA.
EMBL; AC007342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC034490; AAH34490.1; -; mRNA.
EMBL; X74594; CAA52671.1; -; mRNA.
EMBL; U53220; AAC50479.1; -; Genomic_DNA.
CCDS; CCDS10748.1; -. [Q08999-1]
PIR; A49370; A49370.
RefSeq; NP_001310537.1; NM_001323608.1. [Q08999-1]
RefSeq; NP_005602.3; NM_005611.3. [Q08999-1]
UniGene; Hs.513609; -.
PDB; 4XI9; X-ray; 3.10 A; E/F/G/H=416-422.
PDB; 5C1D; X-ray; 2.05 A; C=416-422.
PDBsum; 4XI9; -.
PDBsum; 5C1D; -.
ProteinModelPortal; Q08999; -.
SMR; Q08999; -.
BioGrid; 111869; 63.
CORUM; Q08999; -.
DIP; DIP-425N; -.
ELM; Q08999; -.
IntAct; Q08999; 41.
MINT; MINT-102310; -.
STRING; 9606.ENSP00000262133; -.
iPTMnet; Q08999; -.
PhosphoSitePlus; Q08999; -.
BioMuta; RBL2; -.
DMDM; 116242746; -.
EPD; Q08999; -.
MaxQB; Q08999; -.
PaxDb; Q08999; -.
PeptideAtlas; Q08999; -.
PRIDE; Q08999; -.
DNASU; 5934; -.
Ensembl; ENST00000262133; ENSP00000262133; ENSG00000103479. [Q08999-1]
GeneID; 5934; -.
KEGG; hsa:5934; -.
UCSC; uc002ehi.5; human. [Q08999-1]
CTD; 5934; -.
DisGeNET; 5934; -.
EuPathDB; HostDB:ENSG00000103479.14; -.
GeneCards; RBL2; -.
HGNC; HGNC:9894; RBL2.
HPA; CAB016547; -.
HPA; HPA019703; -.
MIM; 180203; gene.
neXtProt; NX_Q08999; -.
OpenTargets; ENSG00000103479; -.
PharmGKB; PA34258; -.
eggNOG; KOG1010; Eukaryota.
eggNOG; ENOG410XQF7; LUCA.
GeneTree; ENSGT00530000063235; -.
HOGENOM; HOG000273892; -.
HOVERGEN; HBG017710; -.
InParanoid; Q08999; -.
KO; K16332; -.
OMA; FSYKPPG; -.
OrthoDB; EOG091G0398; -.
PhylomeDB; Q08999; -.
TreeFam; TF105568; -.
Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
Reactome; R-HSA-1538133; G0 and Early G1.
Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest.
Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
SIGNOR; Q08999; -.
ChiTaRS; RBL2; human.
GeneWiki; Retinoblastoma-like_protein_2; -.
GenomeRNAi; 5934; -.
PRO; PR:Q08999; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103479; -.
CleanEx; HS_RBL2; -.
ExpressionAtlas; Q08999; baseline and differential.
Genevisible; Q08999; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0005667; C:transcription factor complex; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
GO; GO:0043550; P:regulation of lipid kinase activity; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00043; CYCLIN; 1.
Gene3D; 1.10.472.10; -; 3.
InterPro; IPR013763; Cyclin-like.
InterPro; IPR036915; Cyclin-like_sf.
InterPro; IPR028308; RB2.
InterPro; IPR002720; RB_A.
InterPro; IPR002719; RB_B.
InterPro; IPR015030; RB_C.
InterPro; IPR028309; RB_fam.
InterPro; IPR024599; RB_N.
PANTHER; PTHR13742; PTHR13742; 1.
PANTHER; PTHR13742:SF8; PTHR13742:SF8; 1.
Pfam; PF11934; DUF3452; 1.
Pfam; PF01858; RB_A; 1.
Pfam; PF01857; RB_B; 1.
SMART; SM00385; CYCLIN; 2.
SMART; SM01367; DUF3452; 1.
SMART; SM01368; RB_A; 1.
SMART; SM01369; Rb_C; 1.
SUPFAM; SSF47954; SSF47954; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Chromatin regulator;
Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; Transcription;
Transcription regulation; Tumor suppressor.
CHAIN 1 1139 Retinoblastoma-like protein 2.
/FTId=PRO_0000167841.
REGION 417 1024 Pocket; binds E1A.
REGION 417 616 Domain A.
REGION 617 827 Spacer.
REGION 828 1024 Domain B.
COMPBIAS 9 16 Poly-Pro.
COMPBIAS 17 20 Poly-Ala.
COMPBIAS 23 26 Poly-Glu.
COMPBIAS 998 1001 Poly-Glu.
MOD_RES 413 413 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 417 417 Phosphothreonine.
{ECO:0000250|UniProtKB:Q64700}.
MOD_RES 639 639 Phosphoserine.
{ECO:0000269|PubMed:11042701}.
MOD_RES 642 642 Phosphothreonine.
{ECO:0000250|UniProtKB:Q64700}.
MOD_RES 662 662 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 672 672 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:12435635}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 948 948 Phosphoserine.
{ECO:0000250|UniProtKB:Q64700}.
MOD_RES 952 952 Phosphoserine.
{ECO:0000269|PubMed:11042701}.
MOD_RES 966 966 Phosphoserine.
{ECO:0000269|PubMed:11042701}.
MOD_RES 971 971 Phosphoserine.
{ECO:0000305|PubMed:11042701}.
MOD_RES 972 972 Phosphoserine.
{ECO:0000305|PubMed:11042701}.
MOD_RES 973 973 Phosphoserine.
{ECO:0000305|PubMed:11042701}.
MOD_RES 974 974 Phosphothreonine.
{ECO:0000305|PubMed:11042701}.
MOD_RES 981 981 Phosphoserine.
{ECO:0000305|PubMed:11042701}.
MOD_RES 982 982 Phosphoserine.
{ECO:0000269|PubMed:11042701}.
MOD_RES 986 986 Phosphothreonine.
{ECO:0000269|PubMed:11042701}.
MOD_RES 1035 1035 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1068 1068 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1080 1080 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1112 1112 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 216 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054328.
VAR_SEQ 638 1042 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054329.
VARIANT 99 99 V -> F. {ECO:0000269|PubMed:23033978}.
/FTId=VAR_069377.
VARIANT 210 210 Y -> C (in dbSNP:rs17800727).
/FTId=VAR_028437.
CONFLICT 37 37 P -> S (in Ref. 1; CAA53661 and 7;
AAC50479). {ECO:0000305}.
CONFLICT 64 64 A -> P (in Ref. 1 and 7). {ECO:0000305}.
CONFLICT 206 206 V -> M (in Ref. 6; CAA52671).
{ECO:0000305}.
CONFLICT 1093 1093 R -> H (in Ref. 5; AAH34490).
{ECO:0000305}.
SEQUENCE 1139 AA; 128367 MW; D129032FB1F383D4 CRC64;
MPSGGDQSPP PPPPPPAAAA SDEEEEDDGE AEDAAPPAES PTPQIQQRFD ELCSRLNMDE
AARAEAWDSY RSMSESYTLE GNDLHWLACA LYVACRKSVP TVSKGTVEGN YVSLTRILKC
SEQSLIEFFN KMKKWEDMAN LPPHFRERTE RLERNFTVSA VIFKKYEPIF QDIFKYPQEE
QPRQQRGRKQ RRQPCTVSEI FHFCWVLFIY AKGNFPMISD DLVNSYHLLL CALDLVYGNA
LQCSNRKELV NPNFKGLSED FHAKDSKPSS DPPCIIEKLC SLHDGLVLEA KGIKEHFWKP
YIRKLYEKKL LKGKEENLTG FLEPGNFGES FKAINKAYEE YVLSVGNLDE RIFLGEDAEE
EIGTLSRCLN AGSGTETAER VQMKNILQQH FDKSKALRIS TPLTGVRYIK ENSPCVTPVS
TATHSLSRLH TMLTGLRNAP SEKLEQILRT CSRDPTQAIA NRLKEMFEIY SQHFQPDEDF
SNCAKEIASK HFRFAEMLYY KVLESVIEQE QKRLGDMDLS GILEQDAFHR SLLACCLEVV
TFSYKPPGNF PFITEIFDVP LYHFYKVIEV FIRAEDGLCR EVVKHLNQIE EQILDHLAWK
PESPLWEKIR DNENRVPTCE EVMPPQNLER ADEICIAGSP LTPRRVTEVR ADTGGLGRSI
TSPTTLYDRY SSPPASTTRR RLFVENDSPS DGGTPGRMPP QPLVNAVPVQ NVSGETVSVT
PVPGQTLVTM ATATVTANNG QTVTIPVQGI ANENGGITFF PVQVNVGGQA QAVTGSIQPL
SAQALAGSLS SQQVTGTTLQ VPGQVAIQQI SPGGQQQKQG QSVTSSSNRP RKTSSLSLFF
RKVYHLAAVR LRDLCAKLDI SDELRKKIWT CFEFSIIQCP ELMMDRHLDQ LLMCAIYVMA
KVTKEDKSFQ NIMRCYRTQP QARSQVYRSV LIKGKRKRRN SGSSDSRSHQ NSPTELNKDR
TSRDSSPVMR SSSTLPVPQP SSAPPTPTRL TGANSDMEEE ERGDLIQFYN NIYIKQIKTF
AMKYSQANMD APPLSPYPFV RTGSPRRIQL SQNHPVYISP HKNETMLSPR EKIFYYFSNS
PSKRLREINS MIRTGETPTK KRGILLEDGS ESPAKRICPE NHSALLRRLQ DVANDRGSH


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