TPD52_HUMAN
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 03-AUG-2022, entry version 182.
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=3; IntAct=EBI-782581, EBI-717470;
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="http://atlasgeneticsoncology.org/Genes/TPD52ID42676ch8q21.html";
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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_001025252.2. [P55327-1]
DR RefSeq; NP_001020424.1; NM_001025253.2. [P55327-4]
DR RefSeq; NP_001274069.1; NM_001287140.1. [P55327-6]
DR RefSeq; NP_001274071.1; NM_001287142.1. [P55327-5]
DR RefSeq; NP_001274072.1; NM_001287143.1. [P55327-7]
DR RefSeq; NP_001274073.1; NM_001287144.1.
DR RefSeq; NP_005070.1; NM_005079.3. [P55327-2]
DR AlphaFoldDB; P55327; -.
DR SMR; P55327; -.
DR BioGRID; 113016; 83.
DR IntAct; P55327; 35.
DR MINT; P55327; -.
DR STRING; 9606.ENSP00000429309; -.
DR GlyGen; P55327; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55327; -.
DR PhosphoSitePlus; P55327; -.
DR BioMuta; TPD52; -.
DR DMDM; 215273966; -.
DR EPD; P55327; -.
DR jPOST; P55327; -.
DR MassIVE; P55327; -.
DR MaxQB; P55327; -.
DR PaxDb; P55327; -.
DR PeptideAtlas; P55327; -.
DR PRIDE; 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 TopDownProteomics; P55327-2; -. [P55327-2]
DR TopDownProteomics; P55327-4; -. [P55327-4]
DR Antibodypedia; 25297; 270 antibodies from 31 providers.
DR DNASU; 7163; -.
DR Ensembl; ENST00000379096.9; ENSP00000368390.4; ENSG00000076554.16. [P55327-2]
DR Ensembl; ENST00000379097.7; ENSP00000368391.3; ENSG00000076554.16. [P55327-1]
DR Ensembl; ENST00000448733.3; ENSP00000410222.2; ENSG00000076554.16. [P55327-5]
DR Ensembl; ENST00000517427.5; ENSP00000429351.1; ENSG00000076554.16. [P55327-7]
DR Ensembl; ENST00000517462.6; ENSP00000429708.1; ENSG00000076554.16. [P55327-8]
DR Ensembl; ENST00000518937.6; ENSP00000429915.1; ENSG00000076554.16. [P55327-4]
DR Ensembl; ENST00000520527.5; ENSP00000429309.1; ENSG00000076554.16. [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 CTD; 7163; -.
DR DisGeNET; 7163; -.
DR GeneCards; TPD52; -.
DR HGNC; HGNC:12005; TPD52.
DR HPA; ENSG00000076554; Tissue enhanced (retina).
DR MalaCards; TPD52; -.
DR MIM; 604068; gene.
DR neXtProt; NX_P55327; -.
DR OpenTargets; ENSG00000076554; -.
DR PharmGKB; PA36686; -.
DR VEuPathDB; HostDB:ENSG00000076554; -.
DR eggNOG; KOG4010; Eukaryota.
DR GeneTree; ENSGT00940000155294; -.
DR HOGENOM; CLU_080743_0_1_1; -.
DR InParanoid; P55327; -.
DR OMA; CREMEFY; -.
DR OrthoDB; 1225782at2759; -.
DR PhylomeDB; P55327; -.
DR TreeFam; TF317562; -.
DR PathwayCommons; P55327; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; P55327; -.
DR SIGNOR; P55327; -.
DR BioGRID-ORCS; 7163; 9 hits in 1066 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 205 other tissues.
DR ExpressionAtlas; P55327; baseline and differential.
DR Genevisible; P55327; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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:0046903; P:secretion; TAS:UniProtKB.
DR InterPro; IPR007327; TPD52.
DR PANTHER; PTHR19307; PTHR19307; 1.
DR Pfam; PF04201; TPD52; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Phosphoprotein; 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 204..224
FT /note="Polar residues"
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
