AFF1_HUMAN
ID AFF1_HUMAN Reviewed; 1210 AA.
AC P51825; B4DTU1; E9PBM3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=AF4/FMR2 family member 1;
DE AltName: Full=ALL1-fused gene from chromosome 4 protein;
DE Short=Protein AF-4;
DE AltName: Full=Protein FEL;
DE AltName: Full=Proto-oncogene AF4;
GN Name=AFF1; Synonyms=AF4, FEL, MLLT2, PBM1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8506309; DOI=10.1073/pnas.90.10.4631;
RA Nakamura T., Alder H., Gu Y., Prasad R., Canaani O., Kamada N., Gale R.P.,
RA Lange B., Crist W.M., Nowell P.C., Croce C.M., Canaani E.;
RT "Genes on chromosomes 4, 9, and 19 involved in 11q23 abnormalities in acute
RT leukemia share sequence homology and/or common motifs.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:4631-4635(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND CHROMOSOMAL TRANSLOCATION WITH
RP KMT2A.
RX PubMed=8443374;
RA Morrissey J., Tkachuk D.C., Milatovich A., Francke U., Link M.,
RA Cleary M.L.;
RT "A serine/proline-rich protein is fused to HRX in t(4;11) acute
RT leukemias.";
RL Blood 81:1124-1131(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP CHROMOSOMAL TRANSLOCATION WITH KMT2A.
RX PubMed=1423625; DOI=10.1016/0092-8674(92)90603-a;
RA Gu Y., Nakamura T., Alder H., Prasad R., Canaani O., Cimino G., Croce C.M.,
RA Canaani E.;
RT "The t(4;11) chromosome translocation of human acute leukemias fuses the
RT ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene.";
RL Cell 71:701-708(1992).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212 AND THR-697, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; THR-220;
RP SER-750 AND THR-755, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; SER-588 AND
RP SER-750, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-750, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-681, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION IN THE SEC COMPLEX.
RX PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
RA Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
RA Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P.,
RA Eissenberg J.C., Shilatifard A.;
RT "The little elongation complex regulates small nuclear RNA transcription.";
RL Mol. Cell 44:954-965(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-697, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP REVIEW ON THE SUPER ELONGATION COMPLEX.
RX PubMed=22895430; DOI=10.1038/nrm3417;
RA Luo Z., Lin C., Shilatifard A.;
RT "The super elongation complex (SEC) family in transcriptional control.";
RL Nat. Rev. Mol. Cell Biol. 13:543-547(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND SER-750, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP STRUCTURE BY NMR OF 738-779 IN COMPLEX WITH MLLT3.
RX PubMed=23260655; DOI=10.1016/j.str.2012.11.011;
RA Leach B.I., Kuntimaddi A., Schmidt C.R., Cierpicki T., Johnson S.A.,
RA Bushweller J.H.;
RT "Leukemia fusion target AF9 is an intrinsically disordered transcriptional
RT regulator that recruits multiple partners via coupled folding and
RT binding.";
RL Structure 21:176-183(2013).
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-1204.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- SUBUNIT: Component of the super elongation complex (SEC), at least
CC composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb
CC complex and ELL (ELL, ELL2 or ELL3). {ECO:0000269|PubMed:22195968,
CC ECO:0000269|PubMed:23260655}.
CC -!- INTERACTION:
CC P51825; P46108: CRK; NbExp=2; IntAct=EBI-2610180, EBI-886;
CC P51825; P42568: MLLT3; NbExp=7; IntAct=EBI-2610180, EBI-716132;
CC P51825; P04608: tat; Xeno; NbExp=3; IntAct=EBI-2610180, EBI-6164389;
CC P51825-3; P53367: ARFIP1; NbExp=3; IntAct=EBI-24213872, EBI-2808808;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P51825-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51825-2; Sequence=VSP_046095, VSP_046096;
CC Name=3;
CC IsoId=P51825-3; Sequence=VSP_046096;
CC -!- DISEASE: Note=A chromosomal aberration involving AFF1 is associated
CC with acute leukemias. Translocation t(4;11)(q21;q23) with KMT2A/MLL1.
CC The result is a rogue activator protein.
CC -!- SIMILARITY: Belongs to the AF4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36642.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/AF4ID3.html";
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DR EMBL; L13773; AAA58360.1; -; mRNA.
DR EMBL; L25050; AAA36642.1; ALT_FRAME; mRNA.
DR EMBL; AK300364; BAG62103.1; -; mRNA.
DR EMBL; AC092658; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS3616.1; -. [P51825-1]
DR CCDS; CCDS54775.1; -. [P51825-2]
DR PIR; A58198; A58198.
DR PIR; I39410; I39410.
DR RefSeq; NP_001160165.1; NM_001166693.2. [P51825-2]
DR RefSeq; NP_001300888.1; NM_001313959.1. [P51825-3]
DR RefSeq; NP_001300889.1; NM_001313960.1.
DR RefSeq; NP_005926.1; NM_005935.3. [P51825-1]
DR RefSeq; XP_005263064.1; XM_005263007.3. [P51825-2]
DR RefSeq; XP_011530275.1; XM_011531973.2. [P51825-2]
DR PDB; 2LM0; NMR; -; A=738-779.
DR PDBsum; 2LM0; -.
DR AlphaFoldDB; P51825; -.
DR SMR; P51825; -.
DR BioGRID; 110445; 55.
DR CORUM; P51825; -.
DR DIP; DIP-56407N; -.
DR IntAct; P51825; 30.
DR MINT; P51825; -.
DR STRING; 9606.ENSP00000378578; -.
DR iPTMnet; P51825; -.
DR PhosphoSitePlus; P51825; -.
DR BioMuta; AFF1; -.
DR DMDM; 1703194; -.
DR EPD; P51825; -.
DR jPOST; P51825; -.
DR MassIVE; P51825; -.
DR MaxQB; P51825; -.
DR PaxDb; P51825; -.
DR PeptideAtlas; P51825; -.
DR PRIDE; P51825; -.
DR ProteomicsDB; 19254; -.
DR ProteomicsDB; 56427; -. [P51825-1]
DR Antibodypedia; 25387; 269 antibodies from 31 providers.
DR DNASU; 4299; -.
DR Ensembl; ENST00000307808.10; ENSP00000305689.6; ENSG00000172493.23. [P51825-1]
DR Ensembl; ENST00000395146.9; ENSP00000378578.4; ENSG00000172493.23. [P51825-2]
DR Ensembl; ENST00000544085.6; ENSP00000440843.3; ENSG00000172493.23. [P51825-3]
DR GeneID; 4299; -.
DR KEGG; hsa:4299; -.
DR MANE-Select; ENST00000395146.9; ENSP00000378578.4; NM_001166693.3; NP_001160165.1. [P51825-2]
DR UCSC; uc003hqj.5; human. [P51825-1]
DR CTD; 4299; -.
DR DisGeNET; 4299; -.
DR GeneCards; AFF1; -.
DR HGNC; HGNC:7135; AFF1.
DR HPA; ENSG00000172493; Low tissue specificity.
DR MalaCards; AFF1; -.
DR MIM; 159557; gene.
DR neXtProt; NX_P51825; -.
DR OpenTargets; ENSG00000172493; -.
DR Orphanet; 585877; B-lymphoblastic leukemia/lymphoma with recurrent genetic abnormality.
DR PharmGKB; PA30851; -.
DR VEuPathDB; HostDB:ENSG00000172493; -.
DR eggNOG; ENOG502QVDA; Eukaryota.
DR GeneTree; ENSGT00950000182974; -.
DR HOGENOM; CLU_006484_0_0_1; -.
DR InParanoid; P51825; -.
DR OMA; ECELTAQ; -.
DR PhylomeDB; P51825; -.
DR TreeFam; TF326216; -.
DR PathwayCommons; P51825; -.
DR SignaLink; P51825; -.
DR SIGNOR; P51825; -.
DR BioGRID-ORCS; 4299; 20 hits in 1087 CRISPR screens.
DR ChiTaRS; AFF1; human.
DR GeneWiki; AFF1; -.
DR GenomeRNAi; 4299; -.
DR Pharos; P51825; Tbio.
DR PRO; PR:P51825; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P51825; protein.
DR Bgee; ENSG00000172493; Expressed in choroid plexus epithelium and 213 other tissues.
DR ExpressionAtlas; P51825; baseline and differential.
DR Genevisible; P51825; HS.
DR GO; GO:0032783; C:super elongation complex; IBA:GO_Central.
DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR IDEAL; IID00554; -.
DR InterPro; IPR007797; AF4/FMR2.
DR InterPro; IPR043640; AF4/FMR2_CHD.
DR InterPro; IPR043639; AF4_int.
DR PANTHER; PTHR10528; PTHR10528; 1.
DR Pfam; PF18876; AF-4_C; 1.
DR Pfam; PF18875; AF4_int; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosomal rearrangement;
KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome.
FT CHAIN 1..1210
FT /note="AF4/FMR2 family member 1"
FT /id="PRO_0000215910"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 366..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..879
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 929..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88573"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 681
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 697
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 755
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..5
FT /note="MAAQS -> MAFTERVNSSGN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046095"
FT VAR_SEQ 1096
FT /note="A -> AR (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8443374"
FT /id="VSP_046096"
FT VARIANT 209
FT /note="P -> A (in dbSNP:rs3733378)"
FT /id="VAR_020370"
FT VARIANT 1204
FT /note="Q -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036130"
FT CONFLICT 46
FT /note="K -> R (in Ref. 2; AAA36642)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="E -> G (in Ref. 2; AAA36642)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="M -> V (in Ref. 3; BAG62103)"
FT /evidence="ECO:0000305"
FT CONFLICT 820
FT /note="R -> G (in Ref. 3; BAG62103)"
FT /evidence="ECO:0000305"
FT CONFLICT 899..905
FT /note="SASSTKS -> VPAVPRV (in Ref. 2; AAA36642)"
FT /evidence="ECO:0000305"
FT CONFLICT 928..929
FT /note="EH -> AD (in Ref. 2; AAA36642)"
FT /evidence="ECO:0000305"
FT CONFLICT 999
FT /note="I -> N (in Ref. 2; AAA36642)"
FT /evidence="ECO:0000305"
FT CONFLICT 1140
FT /note="N -> I (in Ref. 2; AAA36642)"
FT /evidence="ECO:0000305"
FT TURN 768..770
FT /evidence="ECO:0007829|PDB:2LM0"
SQ SEQUENCE 1210 AA; 131422 MW; F0E334DF8FC2FF04 CRC64;
MAAQSSLYND DRNLLRIREK ERRNQEAHQE KEAFPEKIPL FGEPYKTAKG DELSSRIQNM
LGNYEEVKEF LSTKSHTHRL DASENRLGKP KYPLIPDKGS SIPSSSFHTS VHHQSIHTPA
SGPLSVGNIS HNPKMAQPRT EPMPSLHAKS CGPPDSQHLT QDRLGQEGFG SSHHKKGDRR
ADGDHCASVT DSAPERELSP LISLPSPVPP LSPIHSNQQT LPRTQGSSKV HGSSNNSKGY
CPAKSPKDLA VKVHDKETPQ DSLVAPAQPP SQTFPPPSLP SKSVAMQQKP TAYVRPMDGQ
DQAPSESPEL KPLPEDYRQQ TFEKTDLKVP AKAKLTKLKM PSQSVEQTYS NEVHCVEEIL
KEMTHSWPPP LTAIHTPSTA EPSKFPFPTK DSQHVSSVTQ NQKQYDTSSK THSNSQQGTS
SMLEDDLQLS DSEDSDSEQT PEKPPSSSAP PSAPQSLPEP VASAHSSSAE SESTSDSDSS
SDSESESSSS DSEENEPLET PAPEPEPPTT NKWQLDNWLT KVSQPAAPPE GPRSTEPPRR
HPESKGSSDS ATSQEHSESK DPPPKSSSKA PRAPPEAPHP GKRSCQKSPA QQEPPQRQTV
GTKQPKKPVK ASARAGSRTS LQGEREPGLL PYGSRDQTSK DKPKVKTKGR PRAAASNEPK
PAVPPSSEKK KHKSSLPAPS KALSGPEPAK DNVEDRTPEH FALVPLTESQ GPPHSGSGSR
TSGCRQAVVV QEDSRKDRLP LPLRDTKLLS PLRDTPPPQS LMVKITLDLL SRIPQPPGKG
SRQRKAEDKQ PPAGKKHSSE KRSSDSSSKL AKKRKGEAER DCDNKKIRLE KEIKSQSSSS
SSSHKESSKT KPSRPSSQSS KKEMLPPPPV SSSSQKPAKP ALKRSRREAD TCGQDPPKSA
SSTKSNHKDS SIPKQRRVEG KGSRSSSEHK GSSGDTANPF PVPSLPNGNS KPGKPQVKFD
KQQADLHMRE AKKMKQKAEL MTDRVGKAFK YLEAVLSFIE CGIATESESQ SSKSAYSVYS
ETVDLIKFIM SLKSFSDATA PTQEKIFAVL CMRCQSILNM AMFRCKKDIA IKYSRTLNKH
FESSSKVAQA PSPCIASTGT PSPLSPMPSP ASSVGSQSSA GSVGSSGVAA TISTPVTIQN
MTSSYVTITS HVLTAFDLWE QAEALTRKNK EFFARLSTNV CTLALNSSLV DLVHYTRQGF
QQLQELTKTP
