ID ERF_HUMAN Reviewed; 548 AA. AC P50548; B2RAP1; B7Z4R0; Q59G38; Q9UPI7; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 2. DT 27-SEP-2017, entry version 159. DE RecName: Full=ETS domain-containing transcription factor ERF; DE AltName: Full=Ets2 repressor factor; DE AltName: Full=PE-2; GN Name=ERF; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION AT THR-526, RP AND MUTAGENESIS OF THR-526. RX PubMed=7588608; RA Sgouras D.N., Athanasiou M.A., Beal G.J. Jr., Fisher R.J., Blair D.G., RA Mavrothalassitis G.J.; RT "ERF: an ETS domain protein with strong transcriptional repressor RT activity, can suppress ets-associated tumorigenesis and is regulated RT by phosphorylation during cell cycle and mitogenic stimulation."; RL EMBO J. 14:4781-4793(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Heart; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Duodenum; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 102-110; 206-218; 313-347; 377-386; 402-426 AND RP 515-528, PHOSPHORYLATION AT SER-327, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Lempens A., Norman J.C.; RL Submitted (OCT-2009) to UniProtKB. RN [8] RP TISSUE SPECIFICITY. RX PubMed=9192842; DOI=10.1006/geno.1997.4730; RA de Castro C.M., Rabe S.M., Langdon S.D., Fleenor D.E., RA Slentz-Kesler K., Ahmed M.N., Qumsiyeh M.B., Kaufman R.E.; RT "Genomic structure and chromosomal localization of the novel ETS RT factor, PE-2 (ERF)."; RL Genomics 42:227-235(1997). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; THR-7; SER-20; RP SER-185; SER-327; SER-431; SER-435; THR-441; SER-444; SER-531 AND RP SER-548, 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-444 AND RP THR-526, 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24; SER-185; SER-327; RP THR-526; SER-531 AND SER-532, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526, AND IDENTIFICATION RP 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-465 AND LYS-512, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-465; LYS-481 AND LYS-512, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co- RT modification with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [17] RP VARIANTS CRS4 GLN-65 AND CYS-86. RX PubMed=23354439; DOI=10.1038/ng.2539; RA Twigg S.R., Vorgia E., McGowan S.J., Peraki I., Fenwick A.L., RA Sharma V.P., Allegra M., Zaragkoulias A., Sadighi Akha E., RA Knight S.J., Lord H., Lester T., Izatt L., Lampe A.K., Mohammed S.N., RA Stewart F.J., Verloes A., Wilson L.C., Healy C., Sharpe P.T., RA Hammond P., Hughes J., Taylor S., Johnson D., Wall S.A., RA Mavrothalassitis G., Wilkie A.O.; RT "Reduced dosage of ERF causes complex craniosynostosis in humans and RT mice and links ERK1/2 signaling to regulation of osteogenesis."; RL Nat. Genet. 45:308-313(2013). RN [18] RP INVOLVEMENT IN CHYTS, AND VARIANT CHYTS CYS-89. RX PubMed=27738187; DOI=10.1136/jmedgenet-2016-104143; RG DDD Study; RA Balasubramanian M., Lord H., Levesque S., Guturu H., Thuriot F., RA Sillon G., Wenger A.M., Sureka D.L., Lester T., Johnson D.S., RA Bowen J., Calhoun A.R., Viskochil D.H., Bejerano G., Bernstein J.A., RA Chitayat D.; RT "Chitayat syndrome: hyperphalangism, characteristic facies, hallux RT valgus and bronchomalacia results from a recurrent c.266A>G RT p.(Tyr89Cys) variant in the ERF gene."; RL J. Med. Genet. 54:157-165(2017). CC -!- FUNCTION: Potent transcriptional repressor that binds to the H1 CC element of the Ets2 promoter. May regulate other genes involved in CC cellular proliferation. Required for extraembryonic ectoderm CC differentiation, ectoplacental cone cavity closure, and CC chorioallantoic attachment (By similarity). May be important for CC regulating trophoblast stem cell differentiation (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P50548-1; Sequence=Displayed; CC Name=2; CC IsoId=P50548-2; Sequence=VSP_055487; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Highest levels in testis, ovary, pancreas, and CC heart. {ECO:0000269|PubMed:9192842}. CC -!- PTM: Phosphorylated by multiple kinases including MAPK1/ERK2 at CC THR-526. Phosphorylation regulates the activity of ERF. CC {ECO:0000269|PubMed:7588608, ECO:0000269|Ref.7}. CC -!- DISEASE: Craniosynostosis 4 (CRS4) [MIM:600775]: A primary CC abnormality of skull growth involving premature fusion of one or CC more cranial sutures. The growth velocity of the skull often CC cannot match that of the developing brain resulting in an abnormal CC head shape and, in some cases, increased intracranial pressure, CC which must be treated promptly to avoid permanent CC neurodevelopmental disability. {ECO:0000269|PubMed:23354439}. CC Note=The disease is caused by mutations affecting the gene CC represented in this entry. CC -!- DISEASE: Chitayat syndrome (CHYTS) [MIM:617180]: An autosomal CC dominant syndrome characterized by hyperphalangism, partial CC syndactyly, bilateral accessory phalanx resulting in shortened CC index fingers, hallux valgus, brachydactyly, facial anomalies, CC diffuse bronchomalacia, and respiratory distress at birth and in CC infancy. {ECO:0000269|PubMed:27738187}. Note=The disease is caused CC by mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92508.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U15655; AAA86686.1; -; mRNA. DR EMBL; AK297666; BAH12646.1; -; mRNA. DR EMBL; AK314278; BAG36938.1; -; mRNA. DR EMBL; AB209271; BAD92508.1; ALT_SEQ; Transcribed_RNA. DR EMBL; AC006486; AAD11987.1; -; Genomic_DNA. DR EMBL; CH471126; EAW57116.1; -; Genomic_DNA. DR EMBL; CH471126; EAW57118.1; -; Genomic_DNA. DR EMBL; BC022231; AAH22231.1; -; mRNA. DR CCDS; CCDS12600.1; -. [P50548-1] DR CCDS; CCDS77308.1; -. [P50548-2] DR PIR; S59133; S59133. DR RefSeq; NP_001287964.1; NM_001301035.1. [P50548-2] DR RefSeq; NP_001295331.1; NM_001308402.1. [P50548-2] DR RefSeq; NP_001299585.1; NM_001312656.1. [P50548-2] DR RefSeq; NP_006485.2; NM_006494.3. [P50548-1] DR RefSeq; XP_016881957.1; XM_017026468.1. [P50548-2] DR RefSeq; XP_016881958.1; XM_017026469.1. [P50548-2] DR UniGene; Hs.655969; -. DR ProteinModelPortal; P50548; -. DR SMR; P50548; -. DR BioGrid; 108388; 34. DR IntAct; P50548; 14. DR MINT; MINT-240265; -. DR STRING; 9606.ENSP00000222329; -. DR iPTMnet; P50548; -. DR PhosphoSitePlus; P50548; -. DR BioMuta; ERF; -. DR DMDM; 50403684; -. DR EPD; P50548; -. DR MaxQB; P50548; -. DR PaxDb; P50548; -. DR PeptideAtlas; P50548; -. DR PRIDE; P50548; -. DR DNASU; 2077; -. DR Ensembl; ENST00000222329; ENSP00000222329; ENSG00000105722. [P50548-1] DR Ensembl; ENST00000440177; ENSP00000388173; ENSG00000105722. [P50548-2] DR GeneID; 2077; -. DR KEGG; hsa:2077; -. DR UCSC; uc002ote.5; human. [P50548-1] DR CTD; 2077; -. DR DisGeNET; 2077; -. DR EuPathDB; HostDB:ENSG00000105722.9; -. DR GeneCards; ERF; -. DR HGNC; HGNC:3444; ERF. DR HPA; HPA058532; -. DR HPA; HPA067952; -. DR MalaCards; ERF; -. DR MIM; 600775; phenotype. DR MIM; 611888; gene. DR MIM; 617180; phenotype. DR neXtProt; NX_P50548; -. DR OpenTargets; ENSG00000105722; -. DR Orphanet; 207; Crouzon disease. DR Orphanet; 3267; Familial lambdoid synostosis. DR Orphanet; 2343; Isolated cloverleaf skull syndrome. DR Orphanet; 35093; Isolated scaphocephaly. DR PharmGKB; PA27857; -. DR eggNOG; KOG3806; Eukaryota. DR eggNOG; ENOG410Z0ZF; LUCA. DR GeneTree; ENSGT00760000118907; -. DR HOGENOM; HOG000070246; -. DR HOVERGEN; HBG005183; -. DR InParanoid; P50548; -. DR KO; K09434; -. DR OMA; GASQCMP; -. DR OrthoDB; EOG091G05C7; -. DR PhylomeDB; P50548; -. DR TreeFam; TF351065; -. DR Reactome; R-HSA-2559585; Oncogene Induced Senescence. DR SIGNOR; P50548; -. DR ChiTaRS; ERF; human. DR GeneWiki; ERF_(gene); -. DR GenomeRNAi; 2077; -. DR PRO; PR:P50548; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000105722; -. DR CleanEx; HS_ERF; -. DR ExpressionAtlas; P50548; baseline and differential. DR Genevisible; P50548; HS. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB. DR GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IC:NTNU_SB. DR GO; GO:0007049; P:cell cycle; NAS:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR032925; ERF. DR InterPro; IPR000418; Ets_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR PANTHER; PTHR11849:SF246; PTHR11849:SF246; 1. DR Pfam; PF00178; Ets; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Craniosynostosis; KW Direct protein sequencing; Disease mutation; DNA-binding; KW Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1 548 ETS domain-containing transcription FT factor ERF. FT /FTId=PRO_0000204101. FT DNA_BIND 27 107 ETS. {ECO:0000255|PROSITE- FT ProRule:PRU00237}. FT COMPBIAS 166 171 Poly-Ser. FT COMPBIAS 290 293 Poly-Gly. FT COMPBIAS 362 373 Poly-Ser. FT COMPBIAS 418 423 Poly-Pro. FT COMPBIAS 496 499 Poly-Gly. FT MOD_RES 3 3 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 7 7 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 20 20 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 24 24 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 185 185 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 190 190 Phosphoserine. FT {ECO:0000244|PubMed:17081983}. FT MOD_RES 327 327 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163, FT ECO:0000269|Ref.7}. FT MOD_RES 431 431 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332}. FT MOD_RES 435 435 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 441 441 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 444 444 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332}. FT MOD_RES 526 526 Phosphothreonine; by MAPK1. FT {ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569, FT ECO:0000269|PubMed:7588608}. FT MOD_RES 531 531 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 532 532 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 548 548 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT CROSSLNK 465 465 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:28112733}. FT CROSSLNK 481 481 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:28112733}. FT CROSSLNK 512 512 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:28112733}. FT VAR_SEQ 1 75 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_055487. FT VARIANT 65 65 R -> Q (in CRS4; dbSNP:rs587777009). FT {ECO:0000269|PubMed:23354439}. FT /FTId=VAR_070098. FT VARIANT 86 86 R -> C (in CRS4; dbSNP:rs587777008). FT {ECO:0000269|PubMed:23354439}. FT /FTId=VAR_070099. FT VARIANT 89 89 Y -> C (in CHYTS). FT {ECO:0000269|PubMed:27738187}. FT /FTId=VAR_078043. FT VARIANT 205 205 R -> H (in dbSNP:rs1053655). FT /FTId=VAR_048947. FT MUTAGEN 526 526 T->A: Loss of a phosphorylation site. FT {ECO:0000269|PubMed:7588608}. FT CONFLICT 381 381 P -> R (in Ref. 1; AAA86686). FT {ECO:0000305}. FT CONFLICT 398 398 G -> A (in Ref. 1; AAA86686). FT {ECO:0000305}. SQ SEQUENCE 548 AA; 58703 MW; 01242339B8D328ED CRC64; MKTPADTGFA FPDWAYKPES SPGSRQIQLW HFILELLRKE EYQGVIAWQG DYGEFVIKDP DEVARLWGVR KCKPQMNYDK LSRALRYYYN KRILHKTKGK RFTYKFNFNK LVLVNYPFID VGLAGGAVPQ SAPPVPSGGS HFRFPPSTPS EVLSPTEDPR SPPACSSSSS SLFSAVVARR LGRGSVSDCS DGTSELEEPL GEDPRARPPG PPDLGAFRGP PLARLPHDPG VFRVYPRPRG GPEPLSPFPV SPLAGPGSLL PPQLSPALPM TPTHLAYTPS PTLSPMYPSG GGGPSGSGGG SHFSFSPEDM KRYLQAHTQS VYNYHLSPRA FLHYPGLVVP QPQRPDKCPL PPMAPETPPV PSSASSSSSS SSSPFKFKLQ PPPLGRRQRA AGEKAVAGAD KSGGSAGGLA EGAGALAPPP PPPQIKVEPI SEGESEEVEV TDISDEDEED GEVFKTPRAP PAPPKPEPGE APGASQCMPL KLRFKRRWSE DCRLEGGGGP AGGFEDEGED KKVRGEGPGE AGGPLTPRRV SSDLQHATAQ LSLEHRDS //