RFX7_HUMAN
ID RFX7_HUMAN Reviewed; 1363 AA.
AC Q2KHR2; Q6ZRR1; Q6ZTY6; Q8N3J0; Q9H7A9; Q9H956;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=DNA-binding protein RFX7 {ECO:0000305};
DE AltName: Full=Regulatory factor X 7;
DE AltName: Full=Regulatory factor X domain-containing protein 2;
GN Name=RFX7 {ECO:0000312|HGNC:HGNC:25777}; Synonyms=RFXDC2;
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 [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 187-1363 (ISOFORM 1).
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 968-1363 (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP IDENTIFICATION.
RX PubMed=18673564; DOI=10.1186/1471-2148-8-226;
RA Aftab S., Semenec L., Chu J.S.-C., Chen N.;
RT "Identification and characterization of novel human tissue-specific RFX
RT transcription factors.";
RL BMC Evol. Biol. 8:226-226(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282; SER-358; THR-891;
RP SER-1081 AND SER-1232, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-607, 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-1081, 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 BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-282; SER-321;
RP SER-358; THR-467; SER-565; THR-891 AND SER-1081, AND IDENTIFICATION BY MASS
RP 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 85-101 IN COMPLEX WITH RFXANK,
RP AND MOTIF.
RA Tempel W., Xu C., Dong A., Li Y., Bountra C., Arrowsmith C.H.,
RA Edwards A.M., Min J.;
RT "Crystal structure of RFXANK ankyrin repeats in complex with RFX7.";
RL Submitted (JUN-2014) to the PDB data bank.
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 85-101 IN COMPLEX WITH ANKRA2,
RP INTERACTION WITH ANKRA2 AND RFXANK, AND MOTIF.
RX PubMed=25752541; DOI=10.1016/j.str.2015.02.001;
RA Nie J., Xu C., Jin J., Aka J.A., Tempel W., Nguyen V., You L., Weist R.,
RA Min J., Pawson T., Yang X.J.;
RT "Ankyrin repeats of ANKRA2 recognize a PxLPxL motif on the 3M syndrome
RT protein CCDC8.";
RL Structure 23:700-712(2015).
CC -!- SUBUNIT: Interacts (via PxLPxI/L motif) with RFXANK (via ankyrin
CC repeats) (PubMed:25752541). Interacts (via PxLPxI/L motif) with ANKRA2
CC (via ankyrin repeats) (PubMed:25752541). {ECO:0000269|PubMed:25752541,
CC ECO:0000312|PDB:6MEW}.
CC -!- INTERACTION:
CC Q2KHR2; Q9H9E1: ANKRA2; NbExp=2; IntAct=EBI-1222187, EBI-10215533;
CC Q2KHR2; O14593: RFXANK; NbExp=2; IntAct=EBI-1222187, EBI-1057665;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00858}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q2KHR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q2KHR2-2; Sequence=VSP_034394;
CC Name=4;
CC IsoId=Q2KHR2-3; Sequence=VSP_061441;
CC -!- DOMAIN: The PxLPxI/L motif mediates interaction with ankyrin repeats of
CC ANKRA2 and RFXANK. {ECO:0000269|PubMed:25752541, ECO:0000312|PDB:6MEW}.
CC -!- SIMILARITY: Belongs to the RFX family. {ECO:0000255|PROSITE-
CC ProRule:PRU00858}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14381.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14988.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC86441.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK023056; BAB14381.1; ALT_INIT; mRNA.
DR EMBL; AK024757; BAB14988.1; ALT_INIT; mRNA.
DR EMBL; AK126103; BAC86441.1; ALT_INIT; mRNA.
DR EMBL; AK128045; BAC87248.1; -; mRNA.
DR EMBL; AC068726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC247040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC112936; AAI12937.1; -; mRNA.
DR EMBL; AL834302; CAD38972.1; -; mRNA.
DR RefSeq; NP_073752.5; NM_022841.5.
DR RefSeq; XP_011520227.1; XM_011521925.2.
DR RefSeq; XP_016877996.1; XM_017022507.1.
DR RefSeq; XP_016877997.1; XM_017022508.1. [Q2KHR2-1]
DR PDB; 4QQI; X-ray; 2.03 A; X=85-101.
DR PDB; 6MEW; X-ray; 1.78 A; B/D=85-101.
DR PDBsum; 4QQI; -.
DR PDBsum; 6MEW; -.
DR AlphaFoldDB; Q2KHR2; -.
DR SMR; Q2KHR2; -.
DR BioGRID; 122335; 16.
DR ELM; Q2KHR2; -.
DR IntAct; Q2KHR2; 15.
DR STRING; 9606.ENSP00000453281; -.
DR GlyGen; Q2KHR2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q2KHR2; -.
DR PhosphoSitePlus; Q2KHR2; -.
DR BioMuta; RFX7; -.
DR DMDM; 121946796; -.
DR EPD; Q2KHR2; -.
DR jPOST; Q2KHR2; -.
DR MassIVE; Q2KHR2; -.
DR MaxQB; Q2KHR2; -.
DR PaxDb; Q2KHR2; -.
DR PeptideAtlas; Q2KHR2; -.
DR PRIDE; Q2KHR2; -.
DR ProteomicsDB; 61305; -. [Q2KHR2-1]
DR ProteomicsDB; 61306; -. [Q2KHR2-2]
DR Antibodypedia; 25133; 54 antibodies from 10 providers.
DR DNASU; 64864; -.
DR Ensembl; ENST00000559447.8; ENSP00000453281.3; ENSG00000181827.16. [Q2KHR2-3]
DR Ensembl; ENST00000673948.1; ENSP00000501249.1; ENSG00000181827.16. [Q2KHR2-2]
DR Ensembl; ENST00000673997.1; ENSP00000501278.1; ENSG00000181827.16. [Q2KHR2-1]
DR Ensembl; ENST00000674082.1; ENSP00000501248.1; ENSG00000181827.16. [Q2KHR2-1]
DR GeneID; 64864; -.
DR KEGG; hsa:64864; -.
DR MANE-Select; ENST00000559447.8; ENSP00000453281.3; NM_022841.7; NP_073752.6. [Q2KHR2-3]
DR UCSC; uc059jng.1; human. [Q2KHR2-1]
DR CTD; 64864; -.
DR DisGeNET; 64864; -.
DR GeneCards; RFX7; -.
DR HGNC; HGNC:25777; RFX7.
DR HPA; ENSG00000181827; Low tissue specificity.
DR MIM; 612660; gene.
DR neXtProt; NX_Q2KHR2; -.
DR OpenTargets; ENSG00000181827; -.
DR PharmGKB; PA162401255; -.
DR VEuPathDB; HostDB:ENSG00000181827; -.
DR eggNOG; KOG3712; Eukaryota.
DR GeneTree; ENSGT01050000244970; -.
DR HOGENOM; CLU_252972_0_0_1; -.
DR InParanoid; Q2KHR2; -.
DR OrthoDB; 67697at2759; -.
DR PhylomeDB; Q2KHR2; -.
DR TreeFam; TF321340; -.
DR PathwayCommons; Q2KHR2; -.
DR SignaLink; Q2KHR2; -.
DR BioGRID-ORCS; 64864; 21 hits in 311 CRISPR screens.
DR ChiTaRS; RFX7; human.
DR GenomeRNAi; 64864; -.
DR Pharos; Q2KHR2; Tdark.
DR PRO; PR:Q2KHR2; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q2KHR2; protein.
DR Bgee; ENSG00000181827; Expressed in skeletal muscle tissue of rectus abdominis and 182 other tissues.
DR ExpressionAtlas; Q2KHR2; baseline and differential.
DR Genevisible; Q2KHR2; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR003150; DNA-bd_RFX.
DR InterPro; IPR039779; RFX-like.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12619; PTHR12619; 1.
DR Pfam; PF02257; RFX_DNA_binding; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51526; RFX_DBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1363
FT /note="DNA-binding protein RFX7"
FT /id="PRO_0000342186"
FT DNA_BIND 11..86
FT /note="RFX-type winged-helix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00858"
FT REGION 211..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 91..96
FT /note="PxLPxI/L motif; mediates interaction with ANKRA2 and
FT RFXANK"
FT /evidence="ECO:0000269|PubMed:25752541,
FT ECO:0000312|PDB:6MEW"
FT COMPBIAS 234..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..866
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 467
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 607
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 891
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1081
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1232
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1
FT /note="M -> MAEEQQQPPPQQPDAHQQLPPSAPNSGVALPALVPGLPGTEASALQH
FT KIKNSICKTVQSKVDCILQEVEKFTDLEKLYLYLQLPSGLSNGEKSDQNAM (in
FT isoform 4)"
FT /id="VSP_061441"
FT VAR_SEQ 1269..1363
FT /note="VGQGASDLTNTASDFSSDIRLSSELSGSINDLNTLDPNLLFDPGRQQGQDDE
FT ATLEELKNDPLFQQICSESMNSMTSSGFEWIESKDHPTVEMLG -> CSCPSSLLAGMQ
FT M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_034394"
FT VARIANT 434
FT /note="G -> V (in dbSNP:rs16976751)"
FT /id="VAR_044135"
FT VARIANT 677
FT /note="V -> L (in dbSNP:rs3803460)"
FT /id="VAR_044136"
FT VARIANT 1256
FT /note="L -> P (in dbSNP:rs33984059)"
FT /id="VAR_044137"
FT CONFLICT 511
FT /note="E -> K (in Ref. 1; BAC86441)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="H -> R (in Ref. 1; BAC87248)"
FT /evidence="ECO:0000305"
FT CONFLICT 1093
FT /note="R -> Q (in Ref. 1; BAC87248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1363 AA; 146896 MW; 6037DB7455278EAE CRC64;
MSSSRAQQMH AFSWIRNTLE EHPETSLPKQ EVYDEYKSYC DNLGYHPLSA ADFGKIMKNV
FPNMKARRLG TRGKSKYCYS GLRKKAFVHM PTLPNLDFHK TGDGLEGAEP SGQLQNIDEE
VISSACRLVC EWAQKVLSQP FDTVLELARF LVKSHYIGTK SMAALTVMAA APAGMKGITQ
PSAFIPTAES NSFQPQVKTL PSPIDAKQQL QRKIQKKQQE QKLQSPLPGE SAAKKSESAT
SNGVTNLPNG NPSILSPQPI GIVVAAVPSP IPVQRTRQLV TSPSPMSSSD GKVLPLNVQV
VTQHMQSVKQ APKTPQNVPA SPGGDRSARH RYPQILPKPA NTSALTIRSP TTVLFTSSPI
KTAVVPASHM SSLNVVKMTT ISLTPSNSNT PLKHSASVSS ATGTTEESRS VPQIKNGSVV
SLQSPGSRSS SAGGTSAVEV KVEPETSSDE HPVQCQENSD EAKAPQTPSA LLGQKSNTDG
ALQKPSNEGV IEIKATKVCD QRTKCKSRCN EMLPGTSTGN NQSTITLSVA SQNLTFTSSS
SPPNGDSINK DPKLCTKSPR KRLSSTLQET QVPPVKKPIV EQLSAATIEG QKQGSVKKDQ
KVPHSGKTEG STAGAQIPSK VSVNVSSHIG ANQPLNSSAL VISDSALEQQ TTPSSSPDIK
VKLEGSVFLL DSDSKSVGSF NPNGWQQITK DSEFISASCE QQQDISVMTI PEHSDINDLE
KSVWELEGMP QDTYSQQLHS QIQESSLNQI QAHSSDQLPL QSELKEFEPS VSQTNESYFP
FDDELTQDSI VEELVLMEQQ MSMNNSHSYG NCLGMTLQSQ SVTPGAPMSS HTSSTHFYHP
IHSNGTPIHT PTPTPTPTPT PTPTPTPTSE MIAGSQSLSR ESPCSRLAQT TPVDSALGSS
RHTPIGTPHS NCSSSVPPSP VECRNPFAFT PISSSMAYHD ASIVSSSPVK PMQRPMATHP
DKTKLEWMNN GYSGVGNSSV SGHGILPSYQ ELVEDRFRKP HAFAVPGQSY QSQSRHHDTH
FGRLTPVSPV QHQGATVNNT NKQEGFAVPA PLDNKGTNSS ASSNFRCRSV SPAVHRQRNL
SGSTLYPVSN IPRSNVTPFG SPVTPEVHVF TNVHTDACAN NIAQRSQSVP LTVMMQTAFP
NALQKQANSK KITNVLLSKL DSDNDDAVRG LGMNNLPSNY TARMNLTQIL EPSTVFPSAN
PQNMIDSSTS VYEFQTPSYL TKSNSTGQIN FSPGDNQAQS EIGEQQLDFN STVKDLLSGD
SLQTNQQLVG QGASDLTNTA SDFSSDIRLS SELSGSINDL NTLDPNLLFD PGRQQGQDDE
ATLEELKNDP LFQQICSESM NSMTSSGFEW IESKDHPTVE MLG
