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Myc proto-oncogene protein (Proto-oncogene c-Myc) (Transcription factor p64)

 MYC_MOUSE               Reviewed;         439 AA.
P01108; P70247; Q3UM70; Q61422;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 186.
RecName: Full=Myc proto-oncogene protein;
AltName: Full=Proto-oncogene c-Myc;
AltName: Full=Transcription factor p64;
Name=Myc;
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 [GENOMIC DNA].
STRAIN=BALB/cJ; TISSUE=Spleen;
PubMed=6321164;
Bernard O., Cory S., Gerondakis S., Webb E., Adams J.M.;
"Sequence of the murine and human cellular myc oncogenes and two modes
of myc transcription resulting from chromosome translocation in B
lymphoid tumours.";
EMBO J. 2:2375-2383(1983).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6462227; DOI=10.1038/310423a0;
Stanton L.W., Fahrlander P.D., Tesser P.M., Marcu K.B.;
"Nucleotide sequence comparison of normal and translocated murine c-
myc genes.";
Nature 310:423-425(1984).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Mammary gland, and Thymus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
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).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-252.
PubMed=6412145; DOI=10.1038/305240a0;
Neuberger M.S., Calabi F.;
"Reciprocal chromosome translocation between c-myc and immunoglobulin
gamma 2b genes.";
Nature 305:240-243(1983).
[6]
DEVELOPMENTAL STAGE.
PubMed=8521822;
Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
Copeland N.G., Jenkins N.A., Eisenman R.N.;
"Mad3 and Mad4: novel Max-interacting transcriptional repressors that
suppress c-myc dependent transformation and are expressed during
neural and epidermal differentiation.";
EMBO J. 14:5646-5659(1995).
[7]
ERRATUM.
PubMed=8617250;
Hurlin P.J., Queva C., Koskinen P.J., Steingrimsson E., Ayer D.E.,
Copeland N.G., Jenkins N.A., Eisenman R.N.;
EMBO J. 15:2030-2030(1996).
[8]
INTERACTION WITH SPAG9.
PubMed=12391307; DOI=10.1073/pnas.232310199;
Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
"JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules
and transcription factors.";
Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
[9]
BIOTECHNOLOGY.
PubMed=16904174; DOI=10.1016/j.cell.2006.07.024;
Takahashi K., Yamanaka S.;
"Induction of pluripotent stem cells from mouse embryonic and adult
fibroblast cultures by defined factors.";
Cell 126:663-676(2006).
[10]
PHOSPHORYLATION AT SER-329, MUTAGENESIS OF SER-329, AND INTERACTION
WITH PIM2.
PubMed=18438430; DOI=10.1038/onc.2008.123;
Zhang Y., Wang Z., Li X., Magnuson N.S.;
"Pim kinase-dependent inhibition of c-Myc degradation.";
Oncogene 27:4809-4819(2008).
[11]
MUTAGENESIS OF THR-58 AND SER-62, INTERACTION WITH TRIM6, AND
UBIQUITINATION.
PubMed=22328504; DOI=10.1242/jcs.095273;
Sato T., Okumura F., Ariga T., Hatakeyama S.;
"TRIM6 interacts with Myc and maintains the pluripotency of mouse
embryonic stem cells.";
J. Cell Sci. 125:1544-1555(2012).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-149, 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).
-!- FUNCTION: Transcription factor that binds DNA in a non-specific
manner, yet also specifically recognizes the core sequence 5'-
CAC[GA]TG-3'. Activates the transcription of growth-related genes.
Binds to the VEGFA promoter, promoting VEGFA production and
subsequent sprouting angiogenesis. {ECO:0000250|UniProtKB:P01106}.
-!- SUBUNIT: Efficient DNA binding requires dimerization with another
bHLH protein. Binds DNA as a heterodimer with MAX (By similarity).
Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts
with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-58 and
Ser-62) with FBXW7. Interacts with PIM2 (PubMed:18438430).
Interacts with RIOX1. The heterodimer MYC:MAX interacts with ABI1;
the interaction may enhance MYC:MAX transcriptional activity (By
similarity). Interacts with TRIM6 (PubMed:22328504). Interacts
with NPM1; the binary complex is recruited to the promoter of MYC
target genes and enhances their transcription (By similarity).
{ECO:0000250|UniProtKB:P01106, ECO:0000269|PubMed:12391307,
ECO:0000269|PubMed:18438430, ECO:0000269|PubMed:22328504}.
-!- INTERACTION:
P28574:Max; NbExp=6; IntAct=EBI-1183114, EBI-1183003;
Q8CH72:Trim32; NbExp=2; IntAct=EBI-1183114, EBI-773837;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000250|UniProtKB:P01106}. Nucleus, nucleolus
{ECO:0000250|UniProtKB:P01106}.
-!- DEVELOPMENTAL STAGE: Expressed in the proliferating cells of the
developing CNS and the epidermis. In the spinal cord at embryonic
days 10.5, 11.5 and 12.5 dpc, expressed within a subset of cells
in the proliferative ventricular zone, as well as in the
differentiating cells at the ventral portion of the intermediate
zone. Also detected in the roof plate and in the neural crest. At
14.5 dpc, found in regions containing differentiating postmitotic
neurons. In the developing epidermis at 14.5 dpc, found in the
dorsal lateral epidermis. At 17 dpc, expression is confined
primarily to the proliferative malphigian layer of the epidermis
and to the dermal papilla and primary germ cells in the dermis.
{ECO:0000269|PubMed:8521822}.
-!- PTM: Phosphorylated by PRKDC. Phosphorylated at Ser-62 by DYRK2;
this primes the protein for subsequent phosphorylation by GSK3B at
Thr-58. Phosphorylation at Thr-58 and Ser-62 by GSK3 is required
for ubiquitination and degradation by the proteasome.
Phosphorylation at Ser-62 by CDK2 prevents Ras-induced senescence
(By similarity). Phosphorylation at Ser-329 by PIM2 leads to the
stabilization of MYC. {ECO:0000250, ECO:0000269|PubMed:18438430}.
-!- PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated
at Thr-58 and Ser-62, leading to its degradation by the
proteasome. In the nucleoplasm, ubiquitination is counteracted by
USP28, which interacts with of FBXW7 (FBW7alpha), leading to its
deubiquitination and preventing degradation. Also
polyubiquitinated by the DCX(TRUSS) complex (By similarity).
Ubiquitinated by TRIM6 in a phosphorylation-independent manner
(PubMed:22328504). {ECO:0000250|UniProtKB:P01106,
ECO:0000269|PubMed:22328504}.
-!- BIOTECHNOLOGY: POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four
Yamanaka factors. When combined, these factors are sufficient to
reprogram differentiated cells to an embryonic-like state
designated iPS (induced pluripotent stem) cells. iPS cells exhibit
the morphology and growth properties of ES cells and express ES
cell marker genes. {ECO:0000269|PubMed:16904174}.
-!- SEQUENCE CAUTION:
Sequence=AAH06728.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; L00039; AAB59728.1; -; Genomic_DNA.
EMBL; L00038; AAB59728.1; JOINED; Genomic_DNA.
EMBL; X01023; CAA25508.1; -; mRNA.
EMBL; AK087961; BAC40060.1; -; mRNA.
EMBL; AK133952; BAE21948.1; -; mRNA.
EMBL; AK145084; BAE26228.1; -; mRNA.
EMBL; BC006728; AAH06728.2; ALT_INIT; mRNA.
EMBL; K00683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS49615.1; -.
PIR; A93337; TVMS.
RefSeq; NP_001170823.1; NM_001177352.1.
RefSeq; NP_001170824.1; NM_001177353.1.
RefSeq; NP_001170825.1; NM_001177354.1.
UniGene; Mm.2444; -.
ProteinModelPortal; P01108; -.
SMR; P01108; -.
BioGrid; 201635; 15.
CORUM; P01108; -.
DIP; DIP-1064N; -.
IntAct; P01108; 17.
STRING; 10090.ENSMUSP00000022971; -.
iPTMnet; P01108; -.
PhosphoSitePlus; P01108; -.
EPD; P01108; -.
MaxQB; P01108; -.
PaxDb; P01108; -.
PeptideAtlas; P01108; -.
PRIDE; P01108; -.
Ensembl; ENSMUST00000159327; ENSMUSP00000124758; ENSMUSG00000022346.
Ensembl; ENSMUST00000160009; ENSMUSP00000123852; ENSMUSG00000022346.
Ensembl; ENSMUST00000161976; ENSMUSP00000123821; ENSMUSG00000022346.
GeneID; 17869; -.
KEGG; mmu:17869; -.
UCSC; uc007vyh.2; mouse.
CTD; 4609; -.
MGI; MGI:97250; Myc.
eggNOG; ENOG410IFSM; Eukaryota.
eggNOG; ENOG41124Q3; LUCA.
GeneTree; ENSGT00510000046414; -.
HOVERGEN; HBG000472; -.
InParanoid; P01108; -.
KO; K04377; -.
PhylomeDB; P01108; -.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
ChiTaRS; Myc; mouse.
PRO; PR:P01108; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022346; -.
CleanEx; MM_MYC; -.
ExpressionAtlas; P01108; baseline and differential.
Genevisible; P01108; MM.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:0016604; C:nuclear body; IDA:MGI.
GO; GO:0005719; C:nuclear euchromatin; IDA:BHF-UCL.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0005819; C:spindle; IDA:MGI.
GO; GO:0033613; F:activating transcription factor binding; ISO:MGI.
GO; GO:0000987; F:core promoter proximal region sequence-specific DNA binding; IDA:MGI.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
GO; GO:0032403; F:protein complex binding; ISS:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0070491; F:repressing transcription factor binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; ISO:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0001783; P:B cell apoptotic process; IMP:MGI.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:UniProtKB.
GO; GO:0060070; P:canonical Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0044336; P:canonical Wnt signaling pathway involved in negative regulation of apoptotic process; IGI:MGI.
GO; GO:0044337; P:canonical Wnt signaling pathway involved in positive regulation of apoptotic process; IGI:MGI.
GO; GO:0007050; P:cell cycle arrest; ISO:MGI.
GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:0035690; P:cellular response to drug; IDA:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
GO; GO:0035457; P:cellular response to interferon-alpha; IDA:MGI.
GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
GO; GO:0051276; P:chromosome organization; ISS:UniProtKB.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI.
GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IDA:MGI.
GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
GO; GO:0042474; P:middle ear morphogenesis; IMP:MGI.
GO; GO:0051782; P:negative regulation of cell division; ISS:UniProtKB.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISO:MGI.
GO; GO:0045656; P:negative regulation of monocyte differentiation; ISS:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0043473; P:pigmentation; IMP:MGI.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:MGI.
GO; GO:0002904; P:positive regulation of B cell apoptotic process; IGI:MGI.
GO; GO:0043085; P:positive regulation of catalytic activity; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; ISS:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:UniProtKB.
GO; GO:0090096; P:positive regulation of metanephric cap mesenchymal cell proliferation; IMP:UniProtKB.
GO; GO:2001022; P:positive regulation of response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0051973; P:positive regulation of telomerase activity; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0016485; P:protein processing; IMP:MGI.
GO; GO:0032986; P:protein-DNA complex disassembly; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IDA:MGI.
GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
GO; GO:0032204; P:regulation of telomere maintenance; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IGI:MGI.
GO; GO:0043279; P:response to alkaloid; IMP:MGI.
GO; GO:0010332; P:response to gamma radiation; ISS:UniProtKB.
GO; GO:0009314; P:response to radiation; IDA:MGI.
GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR003327; Myc-LZ.
InterPro; IPR002418; Tscrpt_reg_Myc.
InterPro; IPR012682; Tscrpt_reg_Myc_N.
Pfam; PF00010; HLH; 1.
Pfam; PF02344; Myc-LZ; 1.
Pfam; PF01056; Myc_N; 1.
PIRSF; PIRSF001705; Myc_protein; 1.
PRINTS; PR00044; LEUZIPPRMYC.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
Acetylation; Activator; Complete proteome; DNA-binding; Glycoprotein;
Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 439 Myc proto-oncogene protein.
/FTId=PRO_0000127296.
DOMAIN 354 406 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 413 434 Leucine-zipper.
COMPBIAS 34 37 Poly-Gln.
COMPBIAS 89 92 Poly-Gly.
MOD_RES 8 8 Phosphothreonine.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 58 58 Phosphothreonine; by GSK3; alternate.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 62 62 Phosphoserine; by DYRK2, GSK3 and CDK2.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 144 144 N6-acetyllysine; by PCAF; alternate.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 149 149 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
MOD_RES 158 158 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 275 275 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 293 293 Phosphoserine.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 317 317 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 323 323 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
MOD_RES 329 329 Phosphoserine; by PIM2; in vitro.
{ECO:0000269|PubMed:18438430}.
MOD_RES 371 371 N6-acetyllysine; by PCAF.
{ECO:0000250|UniProtKB:P01106}.
CARBOHYD 58 58 O-linked (GlcNAc) threonine; alternate.
{ECO:0000250}.
CROSSLNK 52 52 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P01106}.
CROSSLNK 144 144 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P01106}.
CROSSLNK 149 149 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P01106}.
CROSSLNK 298 298 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P01106}.
MUTAGEN 58 58 T->A: Does not affect interaction with
TRIM6. {ECO:0000269|PubMed:22328504}.
MUTAGEN 62 62 S->A: Does not affect interaction with
TRIM6. {ECO:0000269|PubMed:22328504}.
MUTAGEN 329 329 S->A: Reduces phosphorylation by PIM2 by
60%, and decreases the transcriptional
activity of MYC.
{ECO:0000269|PubMed:18438430}.
CONFLICT 39 39 E -> D (in Ref. 5; K00683).
{ECO:0000305}.
CONFLICT 101 101 E -> Q (in Ref. 1; AAB59728).
{ECO:0000305}.
CONFLICT 284 284 S -> F (in Ref. 1; AAB59728).
{ECO:0000305}.
SEQUENCE 439 AA; 48971 MW; 3FCA39BFFD6FC59E CRC64;
MPLNVNFTNR NYDLDYDSVQ PYFICDEEEN FYHQQQQSEL QPPAPSEDIW KKFELLPTPP
LSPSRRSGLC SPSYVAVATS FSPREDDDGG GGNFSTADQL EMMTELLGGD MVNQSFICDP
DDETFIKNII IQDCMWSGFS AAAKLVSEKL ASYQAARKDS TSLSPARGHS VCSTSSLYLQ
DLTAAASECI DPSVVFPYPL NDSSSPKSCT SSDSTAFSPS SDSLLSSESS PRASPEPLVL
HEETPPTTSS DSEEEQEDEE EIDVVSVEKR QTPAKRSESG SSPSRGHSKP PHSPLVLKRC
HVSTHQHNYA APPSTRKDYP AAKRAKLDSG RVLKQISNNR KCSSPRSSDT EENDKRRTHN
VLERQRRNEL KRSFFALRDQ IPELENNEKA PKVVILKKAT AYILSIQADE HKLTSEKDLL
RKRREQLKHK LEQLRNSGA


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