ID TPD52_HUMAN Reviewed; 224 AA. AC P55327; B7Z414; C9J502; D0UFD1; D0UFD2; D0UFD3; D0UFD4; D0UFD5; E5RKB4; AC Q13056; Q53EK8; Q6FGP3; Q6FGS3; Q86YZ2; Q9UCX8; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 25-NOV-2008, sequence version 2. DT 02-SEP-2026, entry version 201. DE RecName: Full=Tumor protein D52; DE AltName: Full=Protein N8; GN Name=TPD52; 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 2). RC TISSUE=Mammary carcinoma; RX PubMed=7796418; RA Byrne J.A., Tomasetto C., Garnier J.-M., Rouyer N., Mattei M.-G., RA Bellocq J.-P., Rio M.C., Basset P.; RT "A screening method to identify genes commonly overexpressed in carcinomas RT and the identification of a novel complementary DNA sequence."; RL Cancer Res. 55:2896-2903(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING. RC TISSUE=Lung tumor; RX PubMed=8632896; RA Chen S.-L., Maroulakou I.G., Green J.E., Romano-Spica V., Modi W., RA Lautenberger J., Bhat N.K.; RT "Isolation and characterization of a novel gene expressed in multiple RT cancers."; RL Oncogene 12:741-751(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=14996714; DOI=10.1158/0008-5472.can-03-3331; RA Wang R., Xu J., Saramaki O., Visakorpi T., Sutherland W.M., Zhou J., RA Sen B., Lim S.D., Mabjeesh N., Amin M., Dong J.T., Petros J.A., RA Nelson P.S., Marshall F.F., Zhau H.E., Chung L.W.; RT "PrLZ, a novel prostate-specific and androgen-responsive gene of the TPD52 RT family, amplified in chromosome 8q21.1 and overexpressed in human prostate RT cancer."; RL Cancer Res. 64:1589-1594(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 5; 6; 7 AND 8), ALTERNATIVE RP SPLICING, AND INTERACTION WITH 14-3-3 PROTEINS. RX PubMed=19732746; DOI=10.1016/j.bbrc.2009.08.165; RA Wang R., He H., Sun X., Xu J., Marshall F.F., Zhau H., Chung L.W., Fu H., RA He D.; RT "Transcription variants of the prostate-specific PrLZ gene and their RT interaction with 14-3-3 proteins."; RL Biochem. Biophys. Res. Commun. 389:455-460(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). RC TISSUE=Colon, Hippocampus, and Tongue; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Rectum tumor; 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Spleen; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [10] 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 [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Skin; 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 [13] RP INTERACTION. RX PubMed=9484778; DOI=10.1038/sj.onc.1201604; RA Byrne J.A., Nourse C.R., Basset P., Gunning P.; RT "Identification of homo- and heteromeric interactions between members of RT the breast carcinoma-associated D52 protein family using the yeast two- RT hybrid system."; RL Oncogene 16:873-881(1998). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND IDENTIFICATION BY RP 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 [15] 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 [16] 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). CC -!- SUBUNIT: Forms a homodimer or heterodimer with other members of the CC family. All isoforms interact with several 14-3-3 proteins. CC -!- INTERACTION: CC P55327; Q16890: TPD52L1; NbExp=7; IntAct=EBI-782581, EBI-717470; CC P55327; Q96J77: TPD52L3; NbExp=3; IntAct=EBI-782581, EBI-932162; CC P55327; Q62393: Tpd52; Xeno; NbExp=2; IntAct=EBI-782581, EBI-782591; CC P55327-2; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-12124194, EBI-740987; CC P55327-2; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-12124194, EBI-2623095; CC P55327-2; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-12124194, EBI-742688; CC P55327-2; Q8WY91: THAP4; NbExp=3; IntAct=EBI-12124194, EBI-726691; CC P55327-2; Q16890-2: TPD52L1; NbExp=3; IntAct=EBI-12124194, EBI-18777952; CC P55327-2; P49638: TTPA; NbExp=3; IntAct=EBI-12124194, EBI-10210710; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=8; CC Name=1; CC IsoId=P55327-1; Sequence=Displayed; CC Name=2; CC IsoId=P55327-2; Sequence=VSP_035751; CC Name=3; Synonyms=N8L; CC IsoId=P55327-3; Sequence=VSP_037378; CC Name=4; CC IsoId=P55327-4; Sequence=VSP_035751, VSP_043510; CC Name=5; Synonyms=PrLZ-238; CC IsoId=P55327-5; Sequence=VSP_047719; CC Name=6; Synonyms=PrLZ-247; CC IsoId=P55327-6; Sequence=VSP_043510; CC Name=7; Synonyms=PrLZ-233; CC IsoId=P55327-7; Sequence=VSP_047720; CC Name=8; Synonyms=PrLZ-151; CC IsoId=P55327-8; Sequence=VSP_047718; CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in colon, breast, prostate, CC pancreas and kidney tumor cell lines. Isoform 2 is expressed at high CC levels in kidney, prostate, brain, small intestine and pancreas, at CC moderate levels in placenta and colon, at low levels in lung, liver and CC heart, and at very low levels in spleen, thymus, peripheral mononuclear CC blood cells, testis and ovary. {ECO:0000269|PubMed:8632896}. CC -!- DEVELOPMENTAL STAGE: Isoform 2 is expressed at lower levels in fetal CC brain and kidney than in adult brain and kidney. CC {ECO:0000269|PubMed:8632896}. CC -!- MISCELLANEOUS: [Isoform 8]: Interacts only with YWHAB and YWHAQ among CC 14-3-3 proteins. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TPD52 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD97351.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42676/TPD52"; 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; U18914; AAC50183.1; -; mRNA. DR EMBL; S82081; AAB36475.1; -; mRNA. DR EMBL; AF202897; AAO22156.1; -; mRNA. DR EMBL; GQ499324; ACY08776.1; -; mRNA. DR EMBL; GQ499325; ACY08777.1; -; mRNA. DR EMBL; GQ499326; ACY08778.1; -; mRNA. DR EMBL; GQ499327; ACY08779.1; -; mRNA. DR EMBL; GQ499328; ACY08780.1; -; mRNA. DR EMBL; AK295468; BAH12078.1; -; mRNA. DR EMBL; AK296615; BAH12400.1; -; mRNA. DR EMBL; AK313135; BAG35954.1; -; mRNA. DR EMBL; CR542034; CAG46831.1; -; mRNA. DR EMBL; CR542064; CAG46861.1; -; mRNA. DR EMBL; BT019444; AAV38251.1; -; mRNA. DR EMBL; BX640835; CAE45908.1; -; mRNA. DR EMBL; AK223631; BAD97351.1; ALT_INIT; mRNA. DR EMBL; AC009686; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC018952; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC036214; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104212; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471068; EAW87074.1; -; Genomic_DNA. DR EMBL; BC018117; AAH18117.1; -; mRNA. DR CCDS; CCDS34912.1; -. [P55327-1] DR CCDS; CCDS47879.1; -. [P55327-4] DR CCDS; CCDS55249.1; -. [P55327-2] DR CCDS; CCDS75757.1; -. [P55327-5] DR CCDS; CCDS75758.1; -. [P55327-7] DR CCDS; CCDS75759.1; -. [P55327-6] DR PIR; I38910; I38910. DR RefSeq; NP_001020423.1; NM_001025252.3. [P55327-1] DR RefSeq; NP_001020424.1; NM_001025253.3. [P55327-4] DR RefSeq; NP_001274069.1; NM_001287140.2. [P55327-6] DR RefSeq; NP_001274071.1; NM_001287142.2. [P55327-5] DR RefSeq; NP_001274072.1; NM_001287143.2. [P55327-7] DR RefSeq; NP_001274073.1; NM_001287144.2. DR RefSeq; NP_005070.1; NM_005079.4. [P55327-2] DR AlphaFoldDB; P55327; -. DR SMR; P55327; -. DR BioGRID; 113016; 131. DR FunCoup; P55327; 1974. DR IntAct; P55327; 55. DR MINT; P55327; -. DR STRING; 9606.ENSP00000429309; -. DR GlyCosmos; P55327; 1 site, 1 glycan. DR GlyGen; P55327; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P55327; -. DR PhosphoSitePlus; P55327; -. DR BioMuta; TPD52; -. DR DMDM; 215273966; -. DR jPOST; P55327; -. DR MassIVE; P55327; -. DR PaxDb; 9606-ENSP00000429309; -. DR PeptideAtlas; P55327; -. DR ProteomicsDB; 12721; -. DR ProteomicsDB; 12722; -. DR ProteomicsDB; 12723; -. DR ProteomicsDB; 56847; -. [P55327-1] DR ProteomicsDB; 56848; -. [P55327-2] DR ProteomicsDB; 56849; -. [P55327-3] DR ProteomicsDB; 56850; -. [P55327-4] DR ProteomicsDB; 8547; -. DR Pumba; P55327; -. DR TopDownProteomics; P55327-2; -. [P55327-2] DR TopDownProteomics; P55327-4; -. [P55327-4] DR Antibodypedia; 25297; 297 antibodies from 32 providers. DR DNASU; 7163; -. DR Ensembl; ENST00000379096.9; ENSP00000368390.4; ENSG00000076554.17. [P55327-2] DR Ensembl; ENST00000379097.7; ENSP00000368391.3; ENSG00000076554.17. [P55327-1] DR Ensembl; ENST00000448733.3; ENSP00000410222.2; ENSG00000076554.17. [P55327-5] DR Ensembl; ENST00000517427.5; ENSP00000429351.1; ENSG00000076554.17. [P55327-7] DR Ensembl; ENST00000517462.6; ENSP00000429708.1; ENSG00000076554.17. [P55327-8] DR Ensembl; ENST00000518937.6; ENSP00000429915.1; ENSG00000076554.17. [P55327-4] DR Ensembl; ENST00000520527.5; ENSP00000429309.1; ENSG00000076554.17. [P55327-6] DR GeneID; 7163; -. DR KEGG; hsa:7163; -. DR MANE-Select; ENST00000518937.6; ENSP00000429915.1; NM_001025253.3; NP_001020424.1. [P55327-4] DR UCSC; uc003ybr.3; human. [P55327-1] DR AGR; HGNC:12005; -. DR ClinPGx; PA36686; -. DR CTD; 7163; -. DR DisGeNET; 7163; -. DR GeneCards; TPD52; -. DR HGNC; HGNC:12005; TPD52. DR HPA; ENSG00000076554; Tissue enhanced (retina). DR MIM; 604068; gene. DR OpenTargets; ENSG00000076554; -. DR VEuPathDB; HostDB:ENSG00000076554; -. DR eggNOG; KOG4010; Eukaryota. DR GeneTree; ENSGT00940000155294; -. DR HOGENOM; CLU_080743_0_1_1; -. DR InParanoid; P55327; -. DR OMA; MDRREMD; -. DR OrthoDB; 10000687at2759; -. DR PAN-GO; P55327; 3 GO annotations based on evolutionary models. DR PhylomeDB; P55327; -. DR PathwayCommons; P55327; -. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. DR SignaLink; P55327; -. DR SIGNOR; P55327; -. DR Agora; ENSG00000076554; -. DR BioGRID-ORCS; 7163; 9 hits in 1144 CRISPR screens. DR ChiTaRS; TPD52; human. DR GeneWiki; TPD52; -. DR GenomeRNAi; 7163; -. DR Pharos; P55327; Tbio. DR PRO; PR:P55327; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P55327; protein. DR Bgee; ENSG00000076554; Expressed in jejunal mucosa and 207 other cell types or tissues. DR ExpressionAtlas; P55327; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc. DR GO; GO:0030183; P:B cell differentiation; IEP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central. DR GO; GO:0046903; P:secretion; TAS:UniProtKB. DR InterPro; IPR007327; TPD52. DR PANTHER; PTHR19307; TUMOR PROTEIN D52; 1. DR PANTHER; PTHR19307:SF12; TUMOR PROTEIN D52; 1. DR Pfam; PF04201; TPD52; 1. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Phosphoprotein; KW Proteomics identification; Reference proteome. FT CHAIN 1..224 FT /note="Tumor protein D52" FT /id="PRO_0000185738" FT REGION 187..224 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 62..114 FT /evidence="ECO:0000255" FT COMPBIAS 203..213 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62393" FT MOD_RES 40 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62393" FT MOD_RES 176 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62393" FT MOD_RES 223 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 1..46 FT /note="MDCREMDLYEDYQSPFDFDAGVNKSYLYLSPSGNSSPPGSPTLQKF -> MD FT RGEQ (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7796418, FT ECO:0000303|PubMed:8632896, ECO:0000303|Ref.6, FT ECO:0000303|Ref.7, ECO:0000303|Ref.9" FT /id="VSP_035751" FT VAR_SEQ 1..46 FT /note="MDCREMDLYEDYQSPFDFDAGVNKSYLYLSPSGNSSPPGSPTLQKF -> MT FT PRESAPGRGRAAPPRPTPLGVGTSRESPAEARRSSARRGGRSEPGRAAGGGAAEDTRRR FT AGDMDRGEQ (in isoform 3)" FT /evidence="ECO:0000303|PubMed:8632896" FT /id="VSP_037378" FT VAR_SEQ 136..224 FT /note="YKKTSETLSQAGQKASAAFSSVGSVITKKLEDVKNSPTFKSFEEKVENLKSK FT VGGTKPAGGDFGEVLNSAANASATTTEPLPEKTQESL -> RSKLLAAETELLCLLY FT (in isoform 8)" FT /evidence="ECO:0000303|PubMed:19732746" FT /id="VSP_047718" FT VAR_SEQ 168..169 FT /note="VK -> VNIRSIQHSISMPAMR (in isoform 5)" FT /evidence="ECO:0000303|PubMed:19732746" FT /id="VSP_047719" FT VAR_SEQ 169 FT /note="K -> KLQAFSHSFSIRSIQHSISMPAMR (in isoform 4 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:19732746" FT /id="VSP_043510" FT VAR_SEQ 169 FT /note="K -> KLQAFSHSFR (in isoform 7)" FT /evidence="ECO:0000303|PubMed:19732746" FT /id="VSP_047720" FT VARIANT 52 FT /note="D -> Y (in dbSNP:rs35099105)" FT /id="VAR_061860" FT CONFLICT 74 FT /note="E -> K (in Ref. 9; BAD97351)" FT /evidence="ECO:0000305" FT CONFLICT 165 FT /note="L -> P (in Ref. 6; CAG46831)" FT /evidence="ECO:0000305" SQ SEQUENCE 224 AA; 24327 MW; 4C8183C5914BB976 CRC64; MDCREMDLYE DYQSPFDFDA GVNKSYLYLS PSGNSSPPGS PTLQKFGLLR TDPVPEEGED VAATISATET LSEEEQEELR RELAKVEEEI QTLSQVLAAK EKHLAEIKRK LGINSLQELK QNIAKGWQDV TATSAYKKTS ETLSQAGQKA SAAFSSVGSV ITKKLEDVKN SPTFKSFEEK VENLKSKVGG TKPAGGDFGE VLNSAANASA TTTEPLPEKT QESL //