ID ESCO2_HUMAN Reviewed; 601 AA. AC Q56NI9; B3KW59; Q49AP4; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 150. DE RecName: Full=N-acetyltransferase ESCO2 {ECO:0000305}; DE EC=2.3.1.- {ECO:0000269|PubMed:15958495}; DE AltName: Full=Establishment factor-like protein 2; DE Short=EFO2 {ECO:0000303|PubMed:15958495}; DE Short=EFO2p; DE Short=hEFO2; DE AltName: Full=Establishment of cohesion 1 homolog 2; DE Short=ECO1 homolog 2; GN Name=ESCO2 {ECO:0000312|HGNC:HGNC:27230}; 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), FUNCTION, TISSUE SPECIFICITY, AND RP VARIANT RBS GLY-539. RX PubMed=15821733; DOI=10.1038/ng1548; RA Vega H., Waisfisz Q., Gordillo M., Sakai N., Yanagihara I., Yamada M., RA van Gosliga D., Kayserili H., Xu C., Ozono K., Wang Jabs E., Inui K., RA Joenje H.; RT "Roberts syndrome is caused by mutations in ESCO2, a human homolog of yeast RT ECO1 that is essential for the establishment of sister chromatid RT cohesion."; RL Nat. Genet. 37:468-470(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Thymus; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [5] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL RP STAGE. RX PubMed=15958495; DOI=10.1091/mbc.e04-12-1063; RA Hou F., Zou H.; RT "Two human orthologues of Eco1/Ctf7 acetyltransferases are both required RT for proper sister-chromatid cohesion."; RL Mol. Biol. Cell 16:3908-3918(2005). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY RP 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., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [7] 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-244, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [9] 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 [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=19907496; DOI=10.1038/nature08550; RA Terret M.E., Sherwood R., Rahman S., Qin J., Jallepalli P.V.; RT "Cohesin acetylation speeds the replication fork."; RL Nature 462:231-234(2009). RN [11] RP FUNCTION. RX PubMed=21111234; DOI=10.1016/j.cell.2010.10.031; RA Nishiyama T., Ladurner R., Schmitz J., Kreidl E., Schleiffer A., RA Bhaskara V., Bando M., Shirahige K., Hyman A.A., Mechtler K., Peters J.M.; RT "Sororin mediates sister chromatid cohesion by antagonizing wapl."; RL Cell 143:737-749(2010). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-244, AND RP IDENTIFICATION BY 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-75; SER-223; SER-244; RP SER-312 AND SER-512, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 INVOLVEMENT IN RBS. RX PubMed=16380922; DOI=10.1086/498695; RA Schuele B., Oviedo A., Johnston K., Pai S., Francke U.; RT "Inactivating mutations in ESCO2 cause SC phocomelia and Roberts syndrome: RT no phenotype-genotype correlation."; RL Am. J. Hum. Genet. 77:1117-1128(2005). RN [15] RP VARIANT JHS 552-ARG--SER-601 DEL, AND CHARACTERIZATION OF VARIANT JHS RP 552-ARG--SER-601 DEL. RX PubMed=32977150; DOI=10.1016/j.archoralbio.2020.104918; RA Kantaputra P.N., Dejkhamron P., Tongsima S., Ngamphiw C., Intachai W., RA Ngiwsara L., Sawangareetrakul P., Svasti J., Olsen B., Cairns J.R.K., RA Bumroongkit K.; RT "Juberg-Hayward syndrome and Roberts syndrome are allelic, caused by RT mutations in ESCO2."; RL Arch. Oral Biol. 119:104918-104918(2020). RN [16] RP VARIANT JHS 552-ARG--SER-601 DEL. RX PubMed=32255174; DOI=10.1093/ejo/cjaa023; RA Kantaputra P.N., Dejkhamron P., Intachai W., Ngamphiw C., Kawasaki K., RA Ohazama A., Krisanaprakornkit S., Olsen B., Tongsima S., RA Ketudat Cairns J.R.; RT "Juberg-Hayward syndrome is a cohesinopathy, caused by mutation in ESCO2."; RL Eur. J. Orthod. 43:45-50(2021). CC -!- FUNCTION: Acetyltransferase required for the establishment of sister CC chromatid cohesion (PubMed:15821733, PubMed:15958495). Couples the CC processes of cohesion and DNA replication to ensure that only sister CC chromatids become paired together. In contrast to the structural CC cohesins, the deposition and establishment factors are required only CC during the S phase. Acetylates the cohesin component SMC3 CC (PubMed:21111234). {ECO:0000269|PubMed:15821733, CC ECO:0000269|PubMed:15958495, ECO:0000269|PubMed:19907496, CC ECO:0000269|PubMed:21111234}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L- CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; CC Evidence={ECO:0000269|PubMed:15958495}; CC -!- INTERACTION: CC Q56NI9; P51114-2: FXR1; NbExp=3; IntAct=EBI-3951849, EBI-11022345; CC Q56NI9; Q08379: GOLGA2; NbExp=3; IntAct=EBI-3951849, EBI-618309; CC Q56NI9; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-3951849, EBI-79165; CC Q56NI9; Q15276: RABEP1; NbExp=3; IntAct=EBI-3951849, EBI-447043; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15958495, CC ECO:0000269|PubMed:19907496}. Chromosome {ECO:0000269|PubMed:15958495, CC ECO:0000269|PubMed:19907496}. Note=Nuclear in interphase cells, CC excluded from chromosomes during metaphase but reassociates with CC chromosomes in telophase. {ECO:0000269|PubMed:15958495}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q56NI9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q56NI9-2; Sequence=VSP_055773, VSP_055774; CC -!- TISSUE SPECIFICITY: Widely expressed in fetal tissues. In adult, it is CC expressed in thymus, placenta and small intestine. CC {ECO:0000269|PubMed:15821733}. CC -!- DEVELOPMENTAL STAGE: Cell-cycle regulated. Down-regulated when cells CC enter M phase. Expression increases again when cells enter S phase of CC the next cell cycle. {ECO:0000269|PubMed:15958495}. CC -!- DOMAIN: The N-terminal region seems to be responsible for association CC with chromosomes, thus excluding any involvement of the Zn finger in CC this process. {ECO:0000269|PubMed:15958495}. CC -!- DISEASE: Roberts-SC phocomelia syndrome (RBS) [MIM:268300]: An CC autosomal recessive disorder characterized by pre- and postnatal growth CC retardation, intellectual disability, microcephaly, bilateral cleft lip CC and cleft palate, and mesomelic symmetric limb reduction. Severely CC affected infants may be stillborn or die shortly after birth. Patient CC chromosomes have a lack of cohesion involving heterochromatic C-banding CC regions around centromeres and the heterochromatin regions on the 1, 9, CC 16, and Y chromosomes. These findings are referred to as premature CC centromere separation (PCS) and heterochromatin repulsion (HR), and CC they are important for the diagnosis of the syndrome. CC {ECO:0000269|PubMed:15821733, ECO:0000269|PubMed:16380922}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Juberg-Hayward syndrome (JHS) [MIM:216100]: An autosomal CC recessive syndrome characterized by cleft lip/palate, microcephaly, CC ptosis, hypoplasia or aplasia of thumbs, short stature, dislocation of CC radial head, and fusion of humerus and radius leading to elbow CC restriction. {ECO:0000269|PubMed:32255174, CC ECO:0000269|PubMed:32977150}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the acetyltransferase family. ECO subfamily. CC {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; AY882862; AAX68677.1; -; mRNA. DR EMBL; AK124215; BAG54021.1; -; mRNA. DR EMBL; AC104997; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC034641; AAH34641.1; -; mRNA. DR CCDS; CCDS34872.1; -. [Q56NI9-1] DR RefSeq; NP_001017420.1; NM_001017420.2. [Q56NI9-1] DR RefSeq; XP_011542723.1; XM_011544421.2. [Q56NI9-1] DR AlphaFoldDB; Q56NI9; -. DR SMR; Q56NI9; -. DR BioGRID; 127605; 72. DR IntAct; Q56NI9; 18. DR MINT; Q56NI9; -. DR STRING; 9606.ENSP00000306999; -. DR iPTMnet; Q56NI9; -. DR PhosphoSitePlus; Q56NI9; -. DR BioMuta; ESCO2; -. DR DMDM; 67460434; -. DR EPD; Q56NI9; -. DR jPOST; Q56NI9; -. DR MassIVE; Q56NI9; -. DR MaxQB; Q56NI9; -. DR PaxDb; 9606-ENSP00000306999; -. DR PeptideAtlas; Q56NI9; -. DR ProteomicsDB; 62062; -. DR ProteomicsDB; 62581; -. [Q56NI9-1] DR Pumba; Q56NI9; -. DR Antibodypedia; 23057; 101 antibodies from 17 providers. DR DNASU; 157570; -. DR Ensembl; ENST00000305188.13; ENSP00000306999.8; ENSG00000171320.15. [Q56NI9-1] DR Ensembl; ENST00000397418.4; ENSP00000380563.2; ENSG00000171320.15. [Q56NI9-2] DR GeneID; 157570; -. DR KEGG; hsa:157570; -. DR MANE-Select; ENST00000305188.13; ENSP00000306999.8; NM_001017420.3; NP_001017420.1. DR UCSC; uc003xgg.4; human. [Q56NI9-1] DR AGR; HGNC:27230; -. DR CTD; 157570; -. DR DisGeNET; 157570; -. DR GeneCards; ESCO2; -. DR GeneReviews; ESCO2; -. DR HGNC; HGNC:27230; ESCO2. DR HPA; ENSG00000171320; Tissue enhanced (bone marrow, intestine, lymphoid tissue). DR MalaCards; ESCO2; -. DR MIM; 216100; phenotype. DR MIM; 268300; phenotype. DR MIM; 609353; gene. DR neXtProt; NX_Q56NI9; -. DR OpenTargets; ENSG00000171320; -. DR Orphanet; 2319; Juberg-Hayward syndrome. DR Orphanet; 3103; Roberts syndrome. DR PharmGKB; PA134891970; -. DR VEuPathDB; HostDB:ENSG00000171320; -. DR eggNOG; KOG3014; Eukaryota. DR GeneTree; ENSGT00940000158598; -. DR HOGENOM; CLU_031546_1_0_1; -. DR InParanoid; Q56NI9; -. DR OMA; HIQYHHR; -. DR OrthoDB; 22809at2759; -. DR PhylomeDB; Q56NI9; -. DR TreeFam; TF314027; -. DR PathwayCommons; Q56NI9; -. DR Reactome; R-HSA-2468052; Establishment of Sister Chromatid Cohesion. DR SignaLink; Q56NI9; -. DR BioGRID-ORCS; 157570; 163 hits in 1159 CRISPR screens. DR ChiTaRS; ESCO2; human. DR GeneWiki; ESCO2; -. DR GenomeRNAi; 157570; -. DR Pharos; Q56NI9; Tbio. DR PRO; PR:Q56NI9; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q56NI9; Protein. DR Bgee; ENSG00000171320; Expressed in oocyte and 106 other cell types or tissues. DR ExpressionAtlas; Q56NI9; baseline and differential. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0010369; C:chromocenter; IEA:Ensembl. DR GO; GO:0005694; C:chromosome; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl. DR GO; GO:0035861; C:site of double-strand break; IEA:Ensembl. DR GO; GO:0001741; C:XY body; IEA:Ensembl. DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0004468; F:lysine N-acetyltransferase activity, acting on acetyl phosphate as donor; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008080; F:N-acetyltransferase activity; TAS:Reactome. DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0007059; P:chromosome segregation; IEA:Ensembl. DR GO; GO:0006302; P:double-strand break repair; IEA:Ensembl. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl. DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central. DR GO; GO:0034421; P:post-translational protein acetylation; IMP:UniProtKB. DR GO; GO:0071168; P:protein localization to chromatin; IEA:Ensembl. DR GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB. DR GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome. DR InterPro; IPR028005; AcTrfase_ESCO_Znf_dom. DR InterPro; IPR028009; ESCO_Acetyltransf_dom. DR PANTHER; PTHR45884; N-ACETYLTRANSFERASE ECO; 1. DR PANTHER; PTHR45884:SF3; N-ACETYLTRANSFERASE ESCO2; 1. DR Pfam; PF13880; Acetyltransf_13; 1. DR Pfam; PF13878; zf-C2H2_3; 1. DR Genevisible; Q56NI9; HS. PE 1: Evidence at protein level; KW Acyltransferase; Alternative splicing; Cell cycle; Chromosome; KW Disease variant; Dwarfism; Intellectual disability; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Transferase; Zinc; Zinc-finger. FT CHAIN 1..601 FT /note="N-acetyltransferase ESCO2" FT /id="PRO_0000074542" FT ZN_FING 387..411 FT /note="CCHH-type" FT REGION 222..243 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 282..315 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 282..310 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 29 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:23186163" FT MOD_RES 75 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 223 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 244 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 312 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 512 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..352 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055773" FT VAR_SEQ 581..601 FT /note="GKLFATKYCNTPNFLVYNFNS -> DCRRLNRYQET (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055774" FT VARIANT 80 FT /note="A -> V (in dbSNP:rs4732748)" FT /id="VAR_033840" FT VARIANT 359 FT /note="Q -> P (in dbSNP:rs57479434)" FT /id="VAR_060994" FT VARIANT 539 FT /note="W -> G (in RBS; dbSNP:rs80359868)" FT /evidence="ECO:0000269|PubMed:15821733" FT /id="VAR_022649" FT VARIANT 552..601 FT /note="Missing (in JHS; strongly decreased protein levels)" FT /evidence="ECO:0000269|PubMed:32977150" FT /id="VAR_085392" SQ SEQUENCE 601 AA; 68307 MW; A3D10BFD486572AE CRC64; MAALTPRKRK QDSLKCDSLL HFTENLFPSP NKKHCFYQNS DKNEENLHCS QQEHFVLSAL KTTEINRLPS ANQGSPFKSA LSTVSFYNQN KWYLNPLERK LIKESRSTCL KTNDEDKSFP IVTEKMQGKP VCSKKNNKKP QKSLTAKYQP KYRHIKPVSR NSRNSKQNRV IYKPIVEKEN NCHSAENNSN APRVLSQKIK PQVTLQGGAA FFVRKKSSLR KSSLENEPSL GRTQKSKSEV IEDSDVETVS EKKTFATRQV PKCLVLEEKL KIGLLSASSK NKEKLIKDSS DDRVSSKEHK VDKNEAFSSE DSLGENKTIS PKSTVYPIFS ASSVNSKRSL GEEQFSVGSV NFMKQTNIQK NTNTRDTSKK TKDQLIIDAG QKHFGATVCK SCGMIYTASN PEDEMQHVQH HHRFLEGIKY VGWKKERVVA EFWDGKIVLV LPHDPSFAIK KVEDVQELVD NELGFQQVVP KCPNKIKTFL FISDEKRVVG CLIAEPIKQA FRVLSEPIGP ESPSSTECPR AWQCSDVPEP AVCGISRIWV FRLKRRKRIA RRLVDTLRNC FMFGCFLSTD EIAFSDPTPD GKLFATKYCN TPNFLVYNFN S //