TPD54_HUMAN
ID TPD54_HUMAN Reviewed; 206 AA.
AC O43399; B4DPJ6; E1P5G7; O43398; Q5JWU5; Q5JWU6; Q5JWU8; Q5U0E0; Q9H3Z6;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Tumor protein D54;
DE Short=hD54;
DE AltName: Full=Tumor protein D52-like 2;
GN Name=TPD52L2;
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), AND ALTERNATIVE SPLICING.
RC TISSUE=Mammary gland;
RX PubMed=9838088; DOI=10.1016/s0167-4781(98)00211-5;
RA Nourse C.R., Mattei M.-G., Gunning P., Byrne J.A.;
RT "Cloning of a third member of the D52 gene family indicates alternative
RT coding sequence usage in D52-like transcripts.";
RL Biochim. Biophys. Acta 1443:155-168(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
RC TISSUE=Brain, and Kidney;
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 MRNA] (ISOFORM 5).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 7).
RC TISSUE=Placenta, and Retinoblastoma;
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 [7]
RP INTERACTION WITH MAL2.
RX PubMed=11549320; DOI=10.1006/geno.2001.6610;
RA Wilson S.H.D., Bailey A.M., Nourse C.R., Mattei M.-G., Byrne J.A.;
RT "Identification of MAL2, a novel member of the mal proteolipid family,
RT though interactions with TPD52-like proteins in the yeast two-hybrid
RT system.";
RL Genomics 76:81-88(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-166, AND
RP IDENTIFICATION 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., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-166, AND
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-12; SER-96 AND
RP SER-166, AND 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-149 AND SER-166, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-12; SER-19; SER-21; SER-96 AND SER-166, AND IDENTIFICATION
RP 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 [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 ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3; SER-12 AND SER-166, AND IDENTIFICATION BY MASS
RP 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-19; SER-21; SER-96;
RP SER-149; SER-161; THR-163; SER-166; THR-173 AND SER-195, AND IDENTIFICATION
RP BY MASS 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-166, AND
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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- SUBUNIT: Forms a homodimer or heterodimer with other members of the
CC family (By similarity). Interacts with MAL2. {ECO:0000250,
CC ECO:0000269|PubMed:11549320}.
CC -!- INTERACTION:
CC O43399; Q8WTS1: ABHD5; NbExp=3; IntAct=EBI-782604, EBI-2813554;
CC O43399; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-782604, EBI-745535;
CC O43399; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-782604, EBI-2623095;
CC O43399-2; Q62393: Tpd52; Xeno; NbExp=2; IntAct=EBI-782616, EBI-782591;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=HD54+ins2;
CC IsoId=O43399-1; Sequence=Displayed;
CC Name=2; Synonyms=HD54-ins2;
CC IsoId=O43399-2; Sequence=VSP_006547;
CC Name=3;
CC IsoId=O43399-3; Sequence=VSP_006547, VSP_036756;
CC Name=4;
CC IsoId=O43399-4; Sequence=VSP_006547, VSP_038361;
CC Name=5;
CC IsoId=O43399-5; Sequence=VSP_038361;
CC Name=6;
CC IsoId=O43399-6; Sequence=VSP_045154, VSP_006547;
CC Name=7;
CC IsoId=O43399-7; Sequence=VSP_047409;
CC -!- SIMILARITY: Belongs to the TPD52 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BU165202; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF004429; AAC98477.1; -; mRNA.
DR EMBL; AF004430; AAC98478.1; -; mRNA.
DR EMBL; AK055068; BAG51460.1; -; mRNA.
DR EMBL; AK298366; BAG60608.1; -; mRNA.
DR EMBL; BT019631; AAV38437.1; -; mRNA.
DR EMBL; AL118506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75195.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75197.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75198.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75199.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75201.1; -; Genomic_DNA.
DR EMBL; BC006804; AAH06804.1; -; mRNA.
DR EMBL; BU165202; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13540.1; -. [O43399-1]
DR CCDS; CCDS13541.1; -. [O43399-2]
DR CCDS; CCDS13542.1; -. [O43399-7]
DR CCDS; CCDS13543.1; -. [O43399-3]
DR CCDS; CCDS13544.1; -. [O43399-5]
DR CCDS; CCDS13545.1; -. [O43399-4]
DR CCDS; CCDS58785.1; -. [O43399-6]
DR RefSeq; NP_001230821.1; NM_001243892.1. [O43399-6]
DR RefSeq; NP_003279.2; NM_003288.3. [O43399-1]
DR RefSeq; NP_955392.1; NM_199360.2. [O43399-7]
DR RefSeq; NP_955393.1; NM_199361.2. [O43399-3]
DR RefSeq; NP_955394.1; NM_199362.2. [O43399-5]
DR RefSeq; NP_955395.1; NM_199363.2. [O43399-4]
DR AlphaFoldDB; O43399; -.
DR SMR; O43399; -.
DR BioGRID; 113018; 133.
DR IntAct; O43399; 32.
DR MINT; O43399; -.
DR STRING; 9606.ENSP00000217121; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GlyGen; O43399; 4 sites, 2 O-linked glycans (4 sites).
DR iPTMnet; O43399; -.
DR MetOSite; O43399; -.
DR PhosphoSitePlus; O43399; -.
DR SwissPalm; O43399; -.
DR BioMuta; TPD52L2; -.
DR OGP; O43399; -.
DR CPTAC; CPTAC-134; -.
DR CPTAC; CPTAC-135; -.
DR EPD; O43399; -.
DR jPOST; O43399; -.
DR MassIVE; O43399; -.
DR MaxQB; O43399; -.
DR PeptideAtlas; O43399; -.
DR PRIDE; O43399; -.
DR ProteomicsDB; 4791; -.
DR ProteomicsDB; 48923; -. [O43399-1]
DR ProteomicsDB; 48924; -. [O43399-2]
DR ProteomicsDB; 48925; -. [O43399-3]
DR ProteomicsDB; 48926; -. [O43399-4]
DR ProteomicsDB; 48927; -. [O43399-5]
DR ProteomicsDB; 63405; -.
DR TopDownProteomics; O43399-5; -. [O43399-5]
DR Antibodypedia; 29897; 244 antibodies from 34 providers.
DR DNASU; 7165; -.
DR Ensembl; ENST00000217121.9; ENSP00000217121.5; ENSG00000101150.18. [O43399-7]
DR Ensembl; ENST00000346249.9; ENSP00000343547.4; ENSG00000101150.18. [O43399-1]
DR Ensembl; ENST00000348257.9; ENSP00000343554.5; ENSG00000101150.18. [O43399-2]
DR Ensembl; ENST00000351424.8; ENSP00000340006.4; ENSG00000101150.18. [O43399-3]
DR Ensembl; ENST00000352482.8; ENSP00000344647.4; ENSG00000101150.18. [O43399-5]
DR Ensembl; ENST00000358548.4; ENSP00000351350.4; ENSG00000101150.18. [O43399-4]
DR Ensembl; ENST00000369927.8; ENSP00000358943.2; ENSG00000101150.18. [O43399-6]
DR GeneID; 7165; -.
DR KEGG; hsa:7165; -.
DR MANE-Select; ENST00000346249.9; ENSP00000343547.4; NM_003288.4; NP_003279.2.
DR UCSC; uc002ygy.4; human. [O43399-1]
DR CTD; 7165; -.
DR DisGeNET; 7165; -.
DR GeneCards; TPD52L2; -.
DR HGNC; HGNC:12007; TPD52L2.
DR HPA; ENSG00000101150; Low tissue specificity.
DR MIM; 603747; gene.
DR neXtProt; NX_O43399; -.
DR OpenTargets; ENSG00000101150; -.
DR PharmGKB; PA36688; -.
DR VEuPathDB; HostDB:ENSG00000101150; -.
DR GeneTree; ENSGT00940000155572; -.
DR HOGENOM; CLU_080743_1_1_1; -.
DR InParanoid; O43399; -.
DR OMA; KLGQWNE; -.
DR OrthoDB; 1225782at2759; -.
DR PhylomeDB; O43399; -.
DR TreeFam; TF317562; -.
DR PathwayCommons; O43399; -.
DR SignaLink; O43399; -.
DR BioGRID-ORCS; 7165; 12 hits in 1082 CRISPR screens.
DR ChiTaRS; TPD52L2; human.
DR GeneWiki; TPD52L2; -.
DR GenomeRNAi; 7165; -.
DR Pharos; O43399; Tbio.
DR PRO; PR:O43399; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O43399; protein.
DR Bgee; ENSG00000101150; Expressed in lower esophagus mucosa and 203 other tissues.
DR ExpressionAtlas; O43399; baseline and differential.
DR Genevisible; O43399; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0042127; P:regulation of cell population proliferation; TAS:UniProtKB.
DR Gene3D; 1.50.10.10; -; 1.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR007327; TPD52.
DR PANTHER; PTHR19307; PTHR19307; 1.
DR Pfam; PF04201; TPD52; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..206
FT /note="Tumor protein D54"
FT /id="PRO_0000185744"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 38..82
FT /evidence="ECO:0000255"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 163
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CYZ2"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 7..29
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045154"
FT VAR_SEQ 106..125
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_006547"
FT VAR_SEQ 157
FT /note="D -> DMSSYSIRHSISMPA (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_038361"
FT VAR_SEQ 157
FT /note="D -> DMRAHPFSHSFSSYSIRHSISMPA (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_047409"
FT VAR_SEQ 159
FT /note="R -> RAHPFSHSFSSYSIRHSISMPAMR (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_036756"
FT CONFLICT 72
FT /note="R -> K (in Ref. 1; AAC98478)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 206 AA; 22238 MW; 58F01BC67B1E3DE9 CRC64;
MDSAGQDINL NSPNKGLLSD SMTDVPVDTG VAARTPAVEG LTEAEEEELR AELTKVEEEI
VTLRQVLAAK ERHCGELKRR LGLSTLGELK QNLSRSWHDV QVSSAYVKTS EKLGEWNEKV
TQSDLYKKTQ ETLSQAGQKT SAALSTVGSA ISRKLGDMRN SATFKSFEDR VGTIKSKVVG
DRENGSDNLP SSAGSGDKPL SDPAPF
