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E3 ubiquitin-protein ligase RBBP6 (EC 2.3.2.27) (Proliferation potential-related protein) (Protein P2P-R) (RING-type E3 ubiquitin transferase RBBP6) (Retinoblastoma-binding protein 6) (p53-associated cellular protein of testis)

 RBBP6_MOUSE             Reviewed;        1790 AA.
P97868; P70287; Q3TTR9; Q3TUM7; Q3UMP7; Q4U217; Q7TT06; Q8BNY8;
Q8R399;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 5.
25-OCT-2017, entry version 145.
RecName: Full=E3 ubiquitin-protein ligase RBBP6;
EC=2.3.2.27;
AltName: Full=Proliferation potential-related protein;
AltName: Full=Protein P2P-R;
AltName: Full=RING-type E3 ubiquitin transferase RBBP6 {ECO:0000305};
AltName: Full=Retinoblastoma-binding protein 6;
AltName: Full=p53-associated cellular protein of testis;
Name=Rbbp6; Synonyms=P2pr, Pact;
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 [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 546-1148 (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1356-1790 (ISOFORMS 1/2).
STRAIN=C57BL/6J;
TISSUE=Corpora quadrigemina, Corpus striatum, Embryo, Head, and Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[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] (ISOFORM 3).
STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 154-1790 (ISOFORM 2), INTERACTION WITH
RB1, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=BALB/cJ;
PubMed=9037032; DOI=10.1073/pnas.94.4.1212;
Witte M.M., Scott R.E.;
"The proliferation potential protein-related (P2P-R) gene with domains
encoding heterogeneous nuclear ribonucleoprotein association and Rb1
binding shows repressed expression during terminal differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 94:1212-1217(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 204-1790 (ISOFORM 1), INTERACTION WITH
TP53 AND RB1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Testis;
PubMed=9010216; DOI=10.1038/sj.onc.1200825;
Simons A., Melamed-Bessudo C., Wolkowicz R., Sperling J., Sperling R.,
Eisenbach L., Rotter V.;
"PACT: cloning and characterization of a cellular p53 binding protein
that interacts with Rb.";
Oncogene 14:145-155(1997).
[6]
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=12064457; DOI=10.1002/jcp.10084;
Gao S., Witte M.M., Scott R.E.;
"P2P-R protein localizes to the nucleolus of interphase cells and the
periphery of chromosomes in mitotic cells which show maximum P2P-R
immunoreactivity.";
J. Cell. Physiol. 191:145-154(2002).
[7]
ERRATUM.
Gao S., Witte M.M., Scott R.E.;
J. Cell. Physiol. 192:359-360(2002).
[8]
SUBCELLULAR LOCATION.
PubMed=12384997; DOI=10.1002/jcp.10163;
Gao S., Scott R.E.;
"P2P-R protein overexpression restricts mitotic progression at
prometaphase and promotes mitotic apoptosis.";
J. Cell. Physiol. 193:199-207(2002).
[9]
INTERACTION WITH TP53.
PubMed=14566974; DOI=10.1002/jcp.10381;
Gao S., Scott R.E.;
"Stable overexpression of specific segments of the P2P-R protein in
human MCF-7 cells promotes camptothecin-induced apoptosis.";
J. Cell. Physiol. 197:445-452(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-985; SER-1179; THR-1272
AND SER-1329, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[11]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=17470788; DOI=10.1073/pnas.0701916104;
Li L., Deng B., Xing G., Teng Y., Tian C., Cheng X., Yin X., Yang J.,
Gao X., Zhu Y., Sun Q., Zhang L., Yang X., He F.;
"PACT is a negative regulator of p53 and essential for cell growth and
embryonic development.";
Proc. Natl. Acad. Sci. U.S.A. 104:7951-7956(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179 AND SER-1329, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361; THR-985; SER-1179;
SER-1278; SER-1329; SER-1648 AND SER-1651, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
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).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130, 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).
[15]
FUNCTION.
PubMed=24726359; DOI=10.1016/j.celrep.2014.03.030;
Miotto B., Chibi M., Xie P., Koundrioukoff S., Moolman-Smook H.,
Pugh D., Debatisse M., He F., Zhang L., Defossez P.A.;
"The RBBP6/ZBTB38/MCM10 axis regulates DNA replication and common
fragile site stability.";
Cell Rep. 7:575-587(2014).
-!- FUNCTION: E3 ubiquitin-protein ligase which promotes
ubiquitination of YBX1, leading to its degradation by the
proteasome (By similarity). May play a role as a scaffold protein
to promote the assembly of the p53/TP53-MDM2 complex, resulting in
increase of MDM2-mediated ubiquitination and degradation of
p53/TP53; may function as negative regulator of p53/TP53, leading
to both apoptosis and cell growth retardation (PubMed:17470788).
Regulates DNA-replication and common fragile sites (CFS) stability
in a ZBTB38- and MCM10-dependent manner. Controls ZBTB38 protein
stability and abundance via ubiquitination and proteasomal
degradation, and ZBTB38 in turn negatively regulates the
expression of MCM10 which plays an important role in DNA-
replication (PubMed:24726359). {ECO:0000250|UniProtKB:Q7Z6E9,
ECO:0000269|PubMed:17470788, ECO:0000269|PubMed:24726359}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with MDM2 and YBX1 (By similarity). Interacts
also with p53/TP53 and RB1. Interacts with NEK6 (By similarity).
Interacts with ZBTB38 (By similarity).
{ECO:0000250|UniProtKB:Q7Z6E9, ECO:0000269|PubMed:14566974,
ECO:0000269|PubMed:9010216, ECO:0000269|PubMed:9037032}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome
{ECO:0000250}. Note=Colocalizes with mitotic chromosomes. Co-
localizes with NEK6 in the centrosome (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P97868-1; Sequence=Displayed;
Name=2;
IsoId=P97868-2; Sequence=VSP_018287;
Name=3;
IsoId=P97868-3; Sequence=VSP_018285, VSP_018286;
-!- TISSUE SPECIFICITY: Highly expressed in testis. Expressed at lower
levels in brain, heart, kidney, liver, lung, skeletal muscle,
spleen, thymus and tongue. {ECO:0000269|PubMed:9010216,
ECO:0000269|PubMed:9037032}.
-!- DEVELOPMENTAL STAGE: Expression is reduced during terminal
differentiation. Expression is induced in the G2/M phase of the
cell cycle (at protein level). {ECO:0000269|PubMed:12064457,
ECO:0000269|PubMed:9037032}.
-!- PTM: Phosphorylated by NEK6. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Early embryonic lethality before E7.5,
accompanied by accumulation of p53 and widespread apoptosis.
{ECO:0000269|PubMed:17470788}.
-!- SEQUENCE CAUTION:
Sequence=AAC72432.1; Type=Frameshift; Positions=176; Evidence={ECO:0000305};
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EMBL; AK045635; BAC32441.1; -; mRNA.
EMBL; AK079129; BAC37553.1; -; mRNA.
EMBL; AK081261; BAC38179.1; -; mRNA.
EMBL; AK144758; BAE26051.1; -; mRNA.
EMBL; AK160656; BAE35944.1; -; mRNA.
EMBL; AK161231; BAE36255.1; -; mRNA.
EMBL; AC125221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC025874; AAH25874.1; -; mRNA.
EMBL; U83913; AAC72432.1; ALT_FRAME; mRNA.
EMBL; U28789; AAB49620.1; -; mRNA.
CCDS; CCDS52387.1; -. [P97868-1]
PIR; T42727; T42727.
RefSeq; NP_035377.2; NM_011247.2. [P97868-1]
RefSeq; NP_778188.1; NM_175023.3.
RefSeq; XP_006507533.1; XM_006507470.3. [P97868-2]
UniGene; Mm.4480; -.
ProteinModelPortal; P97868; -.
SMR; P97868; -.
BioGrid; 202817; 1.
IntAct; P97868; 1.
MINT; MINT-4106375; -.
STRING; 10090.ENSMUSP00000049528; -.
iPTMnet; P97868; -.
PhosphoSitePlus; P97868; -.
MaxQB; P97868; -.
PaxDb; P97868; -.
PeptideAtlas; P97868; -.
PRIDE; P97868; -.
Ensembl; ENSMUST00000052135; ENSMUSP00000049528; ENSMUSG00000030779. [P97868-1]
Ensembl; ENSMUST00000071590; ENSMUSP00000071519; ENSMUSG00000030779. [P97868-2]
GeneID; 19647; -.
KEGG; mmu:19647; -.
UCSC; uc009jow.2; mouse. [P97868-3]
UCSC; uc009joy.2; mouse. [P97868-1]
CTD; 5930; -.
MGI; MGI:894835; Rbbp6.
eggNOG; KOG0314; Eukaryota.
eggNOG; COG5222; LUCA.
GeneTree; ENSGT00610000086096; -.
HOVERGEN; HBG093889; -.
InParanoid; P97868; -.
KO; K10624; -.
OMA; KERYREW; -.
OrthoDB; EOG091G09Q6; -.
PhylomeDB; P97868; -.
TreeFam; TF350543; -.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; Rbbp6; mouse.
PRO; PR:P97868; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000030779; -.
CleanEx; MM_RBBP6; -.
ExpressionAtlas; P97868; baseline and differential.
Genevisible; P97868; MM.
GO; GO:0005813; C:centrosome; IEA:Ensembl.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0048568; P:embryonic organ development; IGI:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0006397; P:mRNA processing; IEA:InterPro.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
GO; GO:0061053; P:somite development; IMP:MGI.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 4.10.60.10; -; 1.
InterPro; IPR014891; DWNN_domain.
InterPro; IPR033489; RBBP6.
InterPro; IPR003613; Ubox_domain.
InterPro; IPR025829; Zn_knuckle_CX2CX3GHX4C.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
PANTHER; PTHR15439:SF3; PTHR15439:SF3; 1.
Pfam; PF08783; DWNN; 1.
Pfam; PF04564; U-box; 1.
Pfam; PF13696; zf-CCHC_2; 1.
SMART; SM01180; DWNN; 1.
SMART; SM00184; RING; 1.
SMART; SM00343; ZnF_C2HC; 1.
SUPFAM; SSF57756; SSF57756; 1.
PROSITE; PS51282; DWNN; 1.
PROSITE; PS50158; ZF_CCHC; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Chromosome; Complete proteome;
Cytoplasm; Cytoskeleton; DNA damage; DNA replication; Isopeptide bond;
Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
CHAIN 1 1790 E3 ubiquitin-protein ligase RBBP6.
/FTId=PRO_0000234355.
DOMAIN 4 76 DWNN. {ECO:0000255|PROSITE-
ProRule:PRU00612}.
ZN_FING 160 177 CCHC-type. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 260 301 RING-type; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
REGION 983 1139 Interaction with RB1.
REGION 1434 1544 Interaction with p53.
MOD_RES 130 130 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 248 248 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 361 361 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 517 517 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 769 769 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 771 771 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 773 773 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 816 816 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 862 862 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 874 874 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 958 958 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 985 985 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1179 1179 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1272 1272 Phosphothreonine.
{ECO:0000244|PubMed:17242355}.
MOD_RES 1278 1278 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1329 1329 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1342 1342 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 1348 1348 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 1469 1469 Phosphothreonine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 1646 1646 Phosphoserine.
{ECO:0000250|UniProtKB:Q7Z6E9}.
MOD_RES 1648 1648 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1651 1651 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 1107 1107 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q7Z6E9}.
CROSSLNK 1169 1169 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q7Z6E9}.
VAR_SEQ 102 123 IDDASASISLAQLTKTANLAEA -> VCKNTITLFLHNCFY
LYNVSVT (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_018285.
VAR_SEQ 124 1756 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_018286.
VAR_SEQ 653 686 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:9037032}.
/FTId=VSP_018287.
CONFLICT 254 254 I -> F (in Ref. 5; AAB49620).
{ECO:0000305}.
CONFLICT 317 318 RQ -> GR (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 341 341 P -> H (in Ref. 5; AAB49620).
{ECO:0000305}.
CONFLICT 418 418 S -> F (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 421 421 V -> S (in Ref. 5; AAB49620).
{ECO:0000305}.
CONFLICT 580 580 P -> L (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 595 595 P -> T (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 615 622 PWVSSGVQ -> ACFSPGVP (in Ref. 4;
AAC72432). {ECO:0000305}.
CONFLICT 629 629 I -> M (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 636 636 P -> L (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 647 647 R -> K (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 689 689 S -> F (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 703 703 Y -> D (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 789 789 Q -> R (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 940 940 R -> Q (in Ref. 1; BAE36255).
{ECO:0000305}.
CONFLICT 941 941 R -> RNEE (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 956 958 ETS -> GKF (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 963 963 E -> G (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 978 978 L -> F (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 982 982 D -> E (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 1012 1012 K -> N (in Ref. 5; AAB49620).
{ECO:0000305}.
CONFLICT 1290 1290 K -> T (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 1316 1316 Q -> H (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 1564 1564 N -> I (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 1581 1581 E -> D (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 1591 1591 P -> L (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 1596 1596 P -> L (in Ref. 4; AAC72432).
{ECO:0000305}.
CONFLICT 1604 1604 A -> V (in Ref. 4; AAC72432).
{ECO:0000305}.
SEQUENCE 1790 AA; 199587 MW; 3909C30EB9DD2CE3 CRC64;
MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADSDLQITN AQTKEEYTDD
NALIPKNSSV IVRRIPIGGV KSTSKTYVIS RTEPVMGTTK AIDDASASIS LAQLTKTANL
AEANASEEDK IKAMMSQSGH EYDPINYMKK TLVGPPPPSY TCFRCGKPGH YIKNCPTNGD
KNFESGPRIK KSTGIPRSFM MEVKDPNMKG AMLTNTGKYA IPTIDAEAYA IGKKEKPPFL
PEEPSSSSEE DDPIPDELLC LICKDIMTDA VVIPCCGNSY CDECIRTALL ESDEHTCPTC
HQNDVSPDAL IANKFLRQAV NNFKNETGYT KRLRKQLPPP PPPVPPPRPL MQRNLQPLMR
SPISRQQDPL MIPVTSSSAH SAPSISSLTS NPSALAPSVS GNPSSAPAPV PDITATVSIS
VHSEKSDGPF RDSDNKLLPA AALTSEHSKG ASSIAITALM EEKGYQVPVL GTPSLLGQSL
LHGQLIPTTG PVRINAARPG GGRPGWEHSN KLGYLVSPPQ QIRRGERSCY RSINRGRHHS
ERSQRTQGPS LPATPVFVPV PPPPLYPPPP HTLPLPPGVP PPQFSPQFPP GQPPPAGYSV
PPPGFPPAPA NISTPWVSSG VQTAHSNTIP TTQAPPLSRE EFYREQRRLK EEEKKKSKLD
EFTNDFAKEL MEYKKIQKER RRSFSRSKSP YSGSSYSRSS YTYSKSRSGS TRSRSYSRSF
SRSHSRSYSR SPPYPRRGRG KSRNYRSRSR SHGYHRSRSR SPPYRRYHSR SRSPQAFRGQ
SPTKRNVPQG ETEREYFNRY REVPPPYDIK AYYGRSVDFR DPFEKERYRE WERKYREWYE
KYYKGYAVGA QPRPSANRED FSPERLLPLN IRNSPFTRGR REDYAAGQSH RNRNLGGNYP
EKLSTRDSHN AKDNPKSKEK ESENVPGDGK GNKHKKHRKR RKGEESESFL NPELLETSRK
CRESSGIDET KTDTLFVLPS RDDATPVRDE PMDAESITFK SVSDKDKREK DKPKVKSDKT
KRKSDGSATA KKDNVLKPSK GPQEKVDGDR EKSPRSEPPL KKAKEEATKI DSVKPSSSSQ
KDEKVTGTPR KAHSKSAKEH QEAKPAKDEK VKKDCSKDIK SEKPASKDEK AKKPEKNKLL
DSKGEKRKRK TEEKSVDKDF ESSSMKISKV EGTEIVKPSP KRKMEGDVEK LERTPEKDKI
ASSTTPAKKI KLNRETGKKI GNAENASTTK EPSEKLESTS SKIKQEKVKG KAKRKVAGSE
GSSSTLVDYT STSSTGGSPV RKSEEKTDTK RTVIKTMEEY NNDNTAPAED VIIMIQVPQS
KWDKDDFESE EEDVKTTQPI QSVGKPSSII KNVTTKPSAT AKYTEKESEQ PEKLQKLPKE
ASHELMQHEL RSSKGSASSE KGRAKDREHS GSEKDNPDKR KSGAQPDKES TVDRLSEQGH
FKTLSQSSKE TRTSEKHESV RGSSNKDFTP GRDKKVDYDS RDYSSSKRRD ERGELARRKD
SPPRGKESLS GQKSKLREER DLPKKGAESK KSNSSPPRDK KPHDHKAPYE TKRPCEETKP
VDKNSGKERE KHAAEARNGK ESSGGKLPCI PNPPDPPMEK ELAAGQVEKS AVKPKPQLSH
SSRLSSDLTR ETDEAAFEPD YNESDSESNV SVKEEEAVAS ISKDLKEKTT EKAKESLTVA
TASQPGADRS QSQSSPSVSP SRSHSPSGSQ TRSHSSSASS AGSQDSKKKK KKKEKKKHKK
HKKHKKHKKH AGADGDVEKS QKHKHKKKKA KKNKDKEKEK DDQKVRSVTV


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