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Transcription initiation factor TFIID subunit 1 (EC 2.3.1.48) (EC 2.7.11.1) (Cell cycle gene 1 protein) (TBP-associated factor 250 kDa) (p250) (Transcription initiation factor TFIID 250 kDa subunit) (TAF(II)250) (TAFII-250) (TAFII250)

 TAF1_MOUSE              Reviewed;        1891 AA.
Q80UV9; A2AM32; A2AM33; O35361; Q3UPF3; Q3V223; Q505F9; Q8BQH8;
Q8BQQ7; Q8BR59; Q8C7N8; Q9WTW9; Q9WTX0; Q9WTX1;
06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 2.
25-OCT-2017, entry version 110.
RecName: Full=Transcription initiation factor TFIID subunit 1;
EC=2.3.1.48 {ECO:0000250|UniProtKB:P21675};
EC=2.7.11.1;
AltName: Full=Cell cycle gene 1 protein;
AltName: Full=TBP-associated factor 250 kDa;
Short=p250;
AltName: Full=Transcription initiation factor TFIID 250 kDa subunit;
Short=TAF(II)250;
Short=TAFII-250;
Short=TAFII250;
Name=Taf1; Synonyms=Ccg1;
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 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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 601-1891.
STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and 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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-280 (ISOFORM 3),
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 849-1237 (ISOFORM 1), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-401 AND 1143-1891.
STRAIN=C57BL/6J;
TISSUE=Adipose tissue, Corpora quadrigemina, Head, Hippocampus, and
Spleen;
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 [MRNA] OF 217-370; 841-876 AND 1199-1488.
STRAIN=CD-1; TISSUE=Heart;
PubMed=10070062;
Saadane N., Alpert L., Chalifour L.E.;
"TAFII250, Egr-1, and D-type cyclin expression in mice and neonatal
rat cardiomyocytes treated with doxorubicin.";
Am. J. Physiol. 276:H803-H814(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 867-1306.
TISSUE=Spleen;
PubMed=9751712; DOI=10.1073/pnas.95.20.11601;
Weissman J.D., Brown J.A., Howcroft T.K., Hwang J., Chawla A.,
Roche P.A., Schiltz L., Nakatani Y., Singer D.S.;
"HIV-1 tat binds TAFII250 and represses TAFII250-dependent
transcription of major histocompatibility class I genes.";
Proc. Natl. Acad. Sci. U.S.A. 95:11601-11606(1998).
[6]
FUNCTION, AND SUBUNIT.
PubMed=10438527; DOI=10.1074/jbc.274.33.23480;
Wu S.Y., Thomas M.C., Hou S.Y., Likhite V., Chiang C.M.;
"Isolation of mouse TFIID and functional characterization of TBP and
TFIID in mediating estrogen receptor and chromatin transcription.";
J. Biol. Chem. 274:23480-23490(1999).
[7]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1690; SER-1693;
SER-1799; SER-1802 AND SER-1820, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, 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).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-565, 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: Largest component and core scaffold of the TFIID basal
transcription factor complex (PubMed:10438527). Contains novel
N- and C-terminal Ser/Thr kinase domains which can
autophosphorylate or transphosphorylate other transcription
factors. Phosphorylates TP53 on 'Thr-55' which leads to MDM2-
mediated degradation of TP53. Phosphorylates GTF2A1 and GTF2F1 on
Ser residues. Possesses DNA-binding activity. Essential for
progression of the G1 phase of the cell cycle. Exhibits histone
acetyltransferase activity towards histones H3 and H4.
{ECO:0000250|UniProtKB:P21675, ECO:0000250|UniProtKB:Q60544,
ECO:0000269|PubMed:10438527}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000250|UniProtKB:P21675}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Autophosphorylates on Ser residues. Inhibited
by retinoblastoma tumor suppressor protein, RB1. Binding to TAF1
or CIITA inhibits the histone acetyltransferase activity.
{ECO:0000250|UniProtKB:P21675}.
-!- SUBUNIT: TAF1 is the largest component of transcription factor
TFIID that is composed of TBP and a variety of TBP-associated
factors (PubMed:10438527). TAF1, when part of the TFIID complex,
interacts with C-terminus of TP53. Part of a TFIID-containing RNA
polymerase II pre-initiation complex that is composed of TBP and
at least GTF2A1, GTF2A2, GTF2E1, GTF2E2, GTF2F1, GTF2H2, GTF2H3,
GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2, ERCC3, TAF1, TAF2, TAF3,
TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13.
Interacts with TAF7; the interaction is direct. Component of some
MLL1/MLL complex, at least composed of the core components
KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the
facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2,
RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9
and TEX10. RB1 interacts with the N-terminal domain of TAF1.
Interacts with ASF1A and ASF1B. Interacts (via bromo domains) with
acetylated lysine residues on the N-terminus of histone H1.4, H2A,
H2B, H3 and H4 (in vitro) (By similarity).
{ECO:0000250|UniProtKB:P21675}.
-!- INTERACTION:
Q15545:TAF7 (xeno); NbExp=2; IntAct=EBI-15563115, EBI-1560194;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P21675}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q80UV9-1; Sequence=Displayed;
Name=2;
IsoId=Q80UV9-2; Sequence=VSP_023320;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q80UV9-3; Sequence=VSP_023321;
Note=No experimental confirmation available.;
-!- DOMAIN: The Bromo domain mediates interaction with histones that
have acetylated lysine residues at specific positions. The second
domain also recognizes and binds histones that are butyrylated and
crotonylated. {ECO:0000250|UniProtKB:P21675}.
-!- PTM: Phosphorylated by casein kinase II in vitro.
{ECO:0000250|UniProtKB:P21675}.
-!- SIMILARITY: Belongs to the TAF1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC34383.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AL831722; CAM20496.1; -; Genomic_DNA.
EMBL; AL806534; CAM20496.1; JOINED; Genomic_DNA.
EMBL; AL831722; CAM20497.1; -; Genomic_DNA.
EMBL; AL806534; CAM20497.1; JOINED; Genomic_DNA.
EMBL; AL806534; CAM21283.1; -; Genomic_DNA.
EMBL; AL831722; CAM21283.1; JOINED; Genomic_DNA.
EMBL; AL806534; CAM21284.1; -; Genomic_DNA.
EMBL; AL831722; CAM21284.1; JOINED; Genomic_DNA.
EMBL; BC047418; AAH47418.1; -; mRNA.
EMBL; BC094568; AAH94568.1; -; mRNA.
EMBL; AK045586; BAC32425.1; -; mRNA.
EMBL; AK046668; BAC32828.1; -; mRNA.
EMBL; AK049826; BAC33938.1; -; mRNA.
EMBL; AK050691; BAC34383.1; ALT_INIT; mRNA.
EMBL; AK132088; BAE20976.1; -; mRNA.
EMBL; AK143571; BAE25442.1; -; mRNA.
EMBL; AF081115; AAD23349.1; -; mRNA.
EMBL; AF081116; AAD23348.1; -; mRNA.
EMBL; AF081117; AAD23350.1; -; mRNA.
EMBL; AF022178; AAC62118.1; -; mRNA.
RefSeq; NP_001277658.1; NM_001290729.1.
RefSeq; XP_006528113.1; XM_006528050.3. [Q80UV9-1]
RefSeq; XP_006528115.1; XM_006528052.3. [Q80UV9-3]
UniGene; Mm.261750; -.
ProteinModelPortal; Q80UV9; -.
SMR; Q80UV9; -.
BioGrid; 234808; 2.
CORUM; Q80UV9; -.
DIP; DIP-61093N; -.
IntAct; Q80UV9; 1.
STRING; 10090.ENSMUSP00000098895; -.
iPTMnet; Q80UV9; -.
PhosphoSitePlus; Q80UV9; -.
PaxDb; Q80UV9; -.
PeptideAtlas; Q80UV9; -.
PRIDE; Q80UV9; -.
Ensembl; ENSMUST00000118878; ENSMUSP00000112772; ENSMUSG00000031314. [Q80UV9-3]
GeneID; 270627; -.
KEGG; mmu:270627; -.
UCSC; uc009txy.1; mouse. [Q80UV9-2]
CTD; 6872; -.
MGI; MGI:1336878; Taf1.
eggNOG; KOG0008; Eukaryota.
eggNOG; COG5076; LUCA.
eggNOG; COG5179; LUCA.
GeneTree; ENSGT00390000012659; -.
HOVERGEN; HBG050223; -.
InParanoid; Q80UV9; -.
KO; K03125; -.
Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape.
Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
ChiTaRS; Taf1; mouse.
PRO; PR:Q80UV9; -.
Proteomes; UP000000589; Chromosome X.
Bgee; ENSMUSG00000031314; -.
ExpressionAtlas; Q80UV9; baseline and differential.
Genevisible; Q80UV9; MM.
GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0045120; C:pronucleus; IDA:MGI.
GO; GO:0005667; C:transcription factor complex; ISO:MGI.
GO; GO:0005669; C:transcription factor TFIID complex; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; ISO:MGI.
GO; GO:0070577; F:lysine-acetylated histone binding; ISO:MGI.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
GO; GO:0001129; F:RNA polymerase II transcription factor activity, TBP-class protein binding, involved in preinitiation complex assembly; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0017025; F:TBP-class protein binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; ISO:MGI.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0071318; P:cellular response to ATP; ISO:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
GO; GO:0034644; P:cellular response to UV; ISO:MGI.
GO; GO:0016573; P:histone acetylation; IDA:UniProtKB.
GO; GO:0030901; P:midbrain development; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:1905524; P:negative regulation of protein autoubiquitination; ISO:MGI.
GO; GO:2000059; P:negative regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:1903026; P:negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI.
GO; GO:2000825; P:positive regulation of androgen receptor activity; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
GO; GO:0045943; P:positive regulation of transcription from RNA polymerase I promoter; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISO:MGI.
GO; GO:0010767; P:regulation of transcription from RNA polymerase II promoter in response to UV-induced DNA damage; ISO:MGI.
GO; GO:0036369; P:transcription factor catabolic process; ISO:MGI.
Gene3D; 1.10.1100.10; -; 1.
Gene3D; 1.20.920.10; -; 2.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR011177; TAF1_animal.
InterPro; IPR009067; TAF_II_230-bd.
InterPro; IPR036741; TAFII-230_TBP-bd_sf.
InterPro; IPR022591; TFIID_sub1_DUF3591.
Pfam; PF00439; Bromodomain; 2.
Pfam; PF12157; DUF3591; 1.
Pfam; PF09247; TBP-binding; 1.
PIRSF; PIRSF003047; TAF1_animal; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 2.
SUPFAM; SSF47055; SSF47055; 1.
SUPFAM; SSF47370; SSF47370; 2.
PROSITE; PS00633; BROMODOMAIN_1; 2.
PROSITE; PS50014; BROMODOMAIN_2; 2.
1: Evidence at protein level;
Acetylation; Acyltransferase; Alternative splicing; ATP-binding;
Bromodomain; Cell cycle; Complete proteome; DNA-binding;
Isopeptide bond; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transcription; Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1 1891 Transcription initiation factor TFIID
subunit 1.
/FTId=PRO_0000278524.
DOMAIN 1 435 Protein kinase 1.
DOMAIN 1418 1488 Bromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DOMAIN 1446 1891 Protein kinase 2.
DOMAIN 1541 1611 Bromo 2. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
DNA_BIND 1216 1294 HMG box. {ECO:0000250}.
REGION 538 997 Histone acetyltransferase (HAT).
{ECO:0000250}.
REGION 1363 1650 Interaction with ASF1A and ASF1B.
{ECO:0000250}.
MOTIF 1372 1379 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 157 165 Poly-Pro.
COMPBIAS 204 211 Poly-Ser.
COMPBIAS 1848 1855 Poly-Glu.
MOD_RES 328 328 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:P21675}.
MOD_RES 565 565 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 1690 1690 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1693 1693 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1799 1799 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1802 1802 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1820 1820 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1847 1847 Phosphoserine.
{ECO:0000250|UniProtKB:P21675}.
CROSSLNK 570 570 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P21675}.
CROSSLNK 583 583 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P21675}.
VAR_SEQ 1 962 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_023320.
VAR_SEQ 178 198 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_023321.
CONFLICT 217 217 D -> E (in Ref. 4; AAD23348).
{ECO:0000305}.
CONFLICT 221 221 S -> A (in Ref. 4; AAD23348).
{ECO:0000305}.
CONFLICT 261 261 R -> H (in Ref. 4; AAD23348).
{ECO:0000305}.
CONFLICT 289 289 E -> K (in Ref. 4; AAD23348).
{ECO:0000305}.
CONFLICT 867 868 LK -> EG (in Ref. 5; AAC62118).
{ECO:0000305}.
CONFLICT 876 876 T -> Q (in Ref. 4; AAD23349).
{ECO:0000305}.
CONFLICT 1302 1306 LYYQT -> AFVAS (in Ref. 5; AAC62118).
{ECO:0000305}.
CONFLICT 1358 1358 R -> P (in Ref. 4; AAD23350).
{ECO:0000305}.
CONFLICT 1388 1388 L -> F (in Ref. 4; AAD23350).
{ECO:0000305}.
CONFLICT 1450 1450 T -> E (in Ref. 4; AAD23350).
{ECO:0000305}.
CONFLICT 1469 1470 HL -> QM (in Ref. 4; AAD23350).
{ECO:0000305}.
CONFLICT 1736 1736 D -> N (in Ref. 2; AAH94568).
{ECO:0000305}.
SEQUENCE 1891 AA; 214419 MW; 9A4EA0475BB3E885 CRC64;
MGPGWAGLLQ DKGGGSPSVV MSDTDSDEES AGGGPFSLTG FLFGNINGAG QLEGESVLDD
ECKKHLAGLG ALGLGSLITE LTANEELSGS DGALVNDEGW IRSREDAVDY SDINEVAEDE
SRRYQQTMGS LQPLCHTDYD EDDYDADCED IDCKLMPPPP PPPGPLKKEK DQDDITGVSE
DGEGIILPSI IAPSSLASEK VDFSSSSDSE SEMGPQDAAQ SESKDGQLTL PLAGIMQHDA
TKLLPSVTEL FPEFRPGKVL RFLRLFGPGK NVPSVWRSAR RKRKKKHREL IQEGQVQEEE
CSVELEVNQK SLWNYDYAPP PLPDQCLSDD EITMMAPVES KFSQSTGDTD KVMDTKPRVA
EWRYGPARLW YDMLGVPEDG SGFDYGFKMK KTEHESTIKC NIMKKLRKLE ENSGVDLLAD
ENFLMVTQLH WEDDIIWDGE DVKHKGTKPQ RASLAGWLPS SMTRNAMAYN VQQGFTATLD
DDKPWYSIFP IDNEDLVYGR WEDNIIWDAQ NMPRILEPPV LTLDPNDENL ILEIPDEKEE
ATSNSPSKEN KKESSLKKSR ILLGKTGVIK EEPQQNMSQP EVKDPWNLSN DEYYYPKQQG
LRGTFGGNII QHSIPAVELR QPFFPTHMGP IKLRQFHRPP LKKYSFGALS QPGPHSVQPL
LKHIKKKAKM REQERQASGG GEMFFMRTPQ DLTGKDGDLI LAEYSEENGP LMMQVGMATK
IKNYYKRKPG KDPGAPDCKY GETVYCHTSP FLGSLHPGQL LQAFENNLFR APIYLHKMPE
SDFLIIRTRQ GYFIRELVDI FVVGQQCPLF EVPGPNSKRA NTHIRDFLQV FIYRLFWKSK
DRPRRIRMED IKKAFPSHSE SSIRKRLKLC ADFKRTGMDS NWWVLKSDFR LPTEEEIRAM
VSPEQCCAYY SMIAAEQRLK DAGYGEKSFF APEEENEEDF QMKIDDEVRT APWNTTRAFI
AAMKGKCLLE VTGVADPTGC GEGFSYVKIP NKPTQQKDDK EPQPVKKTVT GTDADLRRLS
LKNAKQLLRK FGVPEEEIKK LSRWEVIDVV RTMSTEQARS GEGPMSKFAR GSRFSVAEHQ
ERYKEECQRI FDLQNKVLSS TEVLSTDTDS SSAEDSDFEE MGKNIENMLQ NKKTSSQLSR
EREEQERKEL QRMLLAAGSA AAGNNHRDDD TASVTSLNSS ATGRCLKIYR TFRDEEGKEY
VRCETVRKAT VIDAYVRIRT TKDEEFIRKF ALFDEQHREE MRKERRRIQE QLRRLKRNQE
KEKLKGPPEK KPKKMKERPD LKLKCGACGA IGHMRTNKFC PLYYQTNAPP SNPVAMTEEQ
EEELEKTVIH NDNEELIKVE GTKIVLGKQL IESADEVRRK SLVLKFPKQQ LPPKKKRRVG
TTVHCDYLNR PHKSIHRRRT DPMVTLSSIL ESIINDMRDL PNTYPFHTPV NAKVVKDYYK
IITRPMDLQT LRENVRKRLY PSREEFREHL ELIVKNSATY NGPKHSLTQI SQSMLDLCDE
KLKEKEDKLA RLEKAINPLL DDDDQVAFSF ILDNIVTQKM MAVPDSWPFH HPVNKKFVPD
YYKVIVSPMD LETIRKNISK HKYQSRESFL DDVNLILANS VKYNGPESQY TKTAQEIVNV
CHQTLTEYDE HLTQLEKDIC TAKEAALEEA ELESLDPMTP GPYTPQPPDL YDNNTSLSVS
RDASVYQDES NLSVLDIPSA TSEKQLTQEG GDGDGDLADE EEGTVQQPQA SVLYEDLLMS
EGEDDEEDAG SDEEGDNPFF AIQLSESGSD SDVESGSLRP KQPRVLQENT RMGMENEESM
MSYEGDGGDA SRGLEDSNIS YGSYEEPDPK SNTQDTSFSS IGGYEVSEEE EDEEEQRSGP
SVLSQVHLSE DEEDSEDFHS IAGDTDLDSD E


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