Full text data of TPD52L2
TPD52L2
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Tumor protein D54; hD54 (Tumor protein D52-like 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Tumor protein D54; hD54 (Tumor protein D52-like 2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O43399
ID TPD54_HUMAN Reviewed; 206 AA.
AC O43399; B4DPJ6; E1P5G7; O43398; Q5JWU5; Q5JWU6; Q5JWU8; Q5U0E0;
read moreAC Q9H3Z6;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 22-JAN-2014, entry version 126.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT alternative 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.,
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 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
RT 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
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 (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
RT project: 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 MASS
RP SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND MASS
RP SPECTROMETRY.
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
RT sequential 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 MASS
RP SPECTROMETRY.
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
RT the 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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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,
RP AND MASS SPECTROMETRY.
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
RP SCALE ANALYSIS] AT SER-12; SER-19; SER-21; SER-96 AND SER-166, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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
RP SCALE ANALYSIS] AT SER-3; SER-12 AND SER-166, AND MASS SPECTROMETRY.
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 [17]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- SUBUNIT: Forms a homodimer or heterodimer with other members of
CC the family (By similarity). Interacts with MAL2.
CC -!- INTERACTION:
CC 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 Note=No experimental confirmation available;
CC Name=6;
CC IsoId=O43399-6; Sequence=VSP_045154, VSP_006547;
CC Name=7;
CC IsoId=O43399-7; Sequence=VSP_047409;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the TPD52 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BU165202; Type=Frameshift; Positions=155, 157, 173, 188;
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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; CAC15492.1; -; Genomic_DNA.
DR EMBL; AL118506; CAI21899.1; -; Genomic_DNA.
DR EMBL; AL118506; CAI21900.1; -; Genomic_DNA.
DR EMBL; AL118506; CAI21902.1; -; 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 RefSeq; NP_001230821.1; NM_001243892.1.
DR RefSeq; NP_003279.2; NM_003288.3.
DR RefSeq; NP_955392.1; NM_199360.2.
DR RefSeq; NP_955393.1; NM_199361.2.
DR RefSeq; NP_955394.1; NM_199362.2.
DR RefSeq; NP_955395.1; NM_199363.2.
DR UniGene; Hs.473296; -.
DR ProteinModelPortal; O43399; -.
DR IntAct; O43399; 8.
DR STRING; 9606.ENSP00000217121; -.
DR PhosphoSite; O43399; -.
DR OGP; O43399; -.
DR PaxDb; O43399; -.
DR PRIDE; O43399; -.
DR DNASU; 7165; -.
DR Ensembl; ENST00000217121; ENSP00000217121; ENSG00000101150.
DR Ensembl; ENST00000346249; ENSP00000343547; ENSG00000101150.
DR Ensembl; ENST00000348257; ENSP00000343554; ENSG00000101150.
DR Ensembl; ENST00000351424; ENSP00000340006; ENSG00000101150.
DR Ensembl; ENST00000352482; ENSP00000344647; ENSG00000101150.
DR Ensembl; ENST00000358548; ENSP00000351350; ENSG00000101150.
DR Ensembl; ENST00000369927; ENSP00000358943; ENSG00000101150.
DR GeneID; 7165; -.
DR KEGG; hsa:7165; -.
DR UCSC; uc011abl.2; human.
DR CTD; 7165; -.
DR GeneCards; GC20P062490; -.
DR HGNC; HGNC:12007; TPD52L2.
DR HPA; HPA047489; -.
DR MIM; 603747; gene.
DR neXtProt; NX_O43399; -.
DR PharmGKB; PA36688; -.
DR eggNOG; NOG329468; -.
DR HOGENOM; HOG000231968; -.
DR HOVERGEN; HBG058643; -.
DR OMA; RARPFSH; -.
DR OrthoDB; EOG744TBQ; -.
DR SignaLink; O43399; -.
DR ChiTaRS; TPD52L2; human.
DR GeneWiki; TPD52L2; -.
DR GenomeRNAi; 7165; -.
DR NextBio; 28048; -.
DR PRO; PR:O43399; -.
DR ArrayExpress; O43399; -.
DR Bgee; O43399; -.
DR CleanEx; HS_TPD52L2; -.
DR Genevestigator; O43399; -.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0042127; P:regulation of cell proliferation; TAS:UniProtKB.
DR InterPro; IPR007327; TPD52.
DR PANTHER; PTHR19307; PTHR19307; 1.
DR Pfam; PF04201; TPD52; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 206 Tumor protein D54.
FT /FTId=PRO_0000185744.
FT COILED 38 82 Potential.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 3 3 Phosphoserine.
FT MOD_RES 12 12 Phosphoserine.
FT MOD_RES 19 19 Phosphoserine.
FT MOD_RES 21 21 Phosphoserine.
FT MOD_RES 96 96 Phosphoserine.
FT MOD_RES 149 149 Phosphoserine.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 192 192 Phosphoserine (By similarity).
FT VAR_SEQ 7 29 Missing (in isoform 6).
FT /FTId=VSP_045154.
FT VAR_SEQ 106 125 Missing (in isoform 2, isoform 3, isoform
FT 4 and isoform 6).
FT /FTId=VSP_006547.
FT VAR_SEQ 157 157 D -> DMSSYSIRHSISMPA (in isoform 4 and
FT isoform 5).
FT /FTId=VSP_038361.
FT VAR_SEQ 157 157 D -> DMRAHPFSHSFSSYSIRHSISMPA (in isoform
FT 7).
FT /FTId=VSP_047409.
FT VAR_SEQ 159 159 R -> RAHPFSHSFSSYSIRHSISMPAMR (in isoform
FT 3).
FT /FTId=VSP_036756.
FT CONFLICT 72 72 R -> K (in Ref. 1; AAC98478).
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
//
ID TPD54_HUMAN Reviewed; 206 AA.
AC O43399; B4DPJ6; E1P5G7; O43398; Q5JWU5; Q5JWU6; Q5JWU8; Q5U0E0;
read moreAC Q9H3Z6;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 22-JAN-2014, entry version 126.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT alternative 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.,
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 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
RT 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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.,
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 (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
RT project: 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 MASS
RP SPECTROMETRY.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND MASS
RP SPECTROMETRY.
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
RT sequential 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 MASS
RP SPECTROMETRY.
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
RT the 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 MASS SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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,
RP AND MASS SPECTROMETRY.
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
RP SCALE ANALYSIS] AT SER-12; SER-19; SER-21; SER-96 AND SER-166, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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
RP SCALE ANALYSIS] AT SER-3; SER-12 AND SER-166, AND MASS SPECTROMETRY.
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 [17]
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- SUBUNIT: Forms a homodimer or heterodimer with other members of
CC the family (By similarity). Interacts with MAL2.
CC -!- INTERACTION:
CC 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 Note=No experimental confirmation available;
CC Name=6;
CC IsoId=O43399-6; Sequence=VSP_045154, VSP_006547;
CC Name=7;
CC IsoId=O43399-7; Sequence=VSP_047409;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the TPD52 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BU165202; Type=Frameshift; Positions=155, 157, 173, 188;
CC -----------------------------------------------------------------------
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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; CAC15492.1; -; Genomic_DNA.
DR EMBL; AL118506; CAI21899.1; -; Genomic_DNA.
DR EMBL; AL118506; CAI21900.1; -; Genomic_DNA.
DR EMBL; AL118506; CAI21902.1; -; 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 RefSeq; NP_001230821.1; NM_001243892.1.
DR RefSeq; NP_003279.2; NM_003288.3.
DR RefSeq; NP_955392.1; NM_199360.2.
DR RefSeq; NP_955393.1; NM_199361.2.
DR RefSeq; NP_955394.1; NM_199362.2.
DR RefSeq; NP_955395.1; NM_199363.2.
DR UniGene; Hs.473296; -.
DR ProteinModelPortal; O43399; -.
DR IntAct; O43399; 8.
DR STRING; 9606.ENSP00000217121; -.
DR PhosphoSite; O43399; -.
DR OGP; O43399; -.
DR PaxDb; O43399; -.
DR PRIDE; O43399; -.
DR DNASU; 7165; -.
DR Ensembl; ENST00000217121; ENSP00000217121; ENSG00000101150.
DR Ensembl; ENST00000346249; ENSP00000343547; ENSG00000101150.
DR Ensembl; ENST00000348257; ENSP00000343554; ENSG00000101150.
DR Ensembl; ENST00000351424; ENSP00000340006; ENSG00000101150.
DR Ensembl; ENST00000352482; ENSP00000344647; ENSG00000101150.
DR Ensembl; ENST00000358548; ENSP00000351350; ENSG00000101150.
DR Ensembl; ENST00000369927; ENSP00000358943; ENSG00000101150.
DR GeneID; 7165; -.
DR KEGG; hsa:7165; -.
DR UCSC; uc011abl.2; human.
DR CTD; 7165; -.
DR GeneCards; GC20P062490; -.
DR HGNC; HGNC:12007; TPD52L2.
DR HPA; HPA047489; -.
DR MIM; 603747; gene.
DR neXtProt; NX_O43399; -.
DR PharmGKB; PA36688; -.
DR eggNOG; NOG329468; -.
DR HOGENOM; HOG000231968; -.
DR HOVERGEN; HBG058643; -.
DR OMA; RARPFSH; -.
DR OrthoDB; EOG744TBQ; -.
DR SignaLink; O43399; -.
DR ChiTaRS; TPD52L2; human.
DR GeneWiki; TPD52L2; -.
DR GenomeRNAi; 7165; -.
DR NextBio; 28048; -.
DR PRO; PR:O43399; -.
DR ArrayExpress; O43399; -.
DR Bgee; O43399; -.
DR CleanEx; HS_TPD52L2; -.
DR Genevestigator; O43399; -.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0042127; P:regulation of cell proliferation; TAS:UniProtKB.
DR InterPro; IPR007327; TPD52.
DR PANTHER; PTHR19307; PTHR19307; 1.
DR Pfam; PF04201; TPD52; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1 206 Tumor protein D54.
FT /FTId=PRO_0000185744.
FT COILED 38 82 Potential.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 3 3 Phosphoserine.
FT MOD_RES 12 12 Phosphoserine.
FT MOD_RES 19 19 Phosphoserine.
FT MOD_RES 21 21 Phosphoserine.
FT MOD_RES 96 96 Phosphoserine.
FT MOD_RES 149 149 Phosphoserine.
FT MOD_RES 166 166 Phosphoserine.
FT MOD_RES 192 192 Phosphoserine (By similarity).
FT VAR_SEQ 7 29 Missing (in isoform 6).
FT /FTId=VSP_045154.
FT VAR_SEQ 106 125 Missing (in isoform 2, isoform 3, isoform
FT 4 and isoform 6).
FT /FTId=VSP_006547.
FT VAR_SEQ 157 157 D -> DMSSYSIRHSISMPA (in isoform 4 and
FT isoform 5).
FT /FTId=VSP_038361.
FT VAR_SEQ 157 157 D -> DMRAHPFSHSFSSYSIRHSISMPA (in isoform
FT 7).
FT /FTId=VSP_047409.
FT VAR_SEQ 159 159 R -> RAHPFSHSFSSYSIRHSISMPAMR (in isoform
FT 3).
FT /FTId=VSP_036756.
FT CONFLICT 72 72 R -> K (in Ref. 1; AAC98478).
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
//
MIM
603747
*RECORD*
*FIELD* NO
603747
*FIELD* TI
*603747 TUMOR PROTEIN D52-LIKE 2; TPD52L2
;;D54
*FIELD* TX
Nourse et al. (1998) identified EST sequences with similarity to tumor
read moreprotein D52. They cloned the corresponding cDNA, termed D54, from a
breast carcinoma library. The longest cDNA predicted a 206-amino acid
polypeptide with 56% and 51% identity to TPD52 and TPD52L1,
respectively. Nourse et al. (1998) reported that some of the D54 clones
that they isolated were alternatively spliced variants. Northern blot
analysis and RT-PCR of rat tissues revealed that some splice variants of
D54 were ubiquitously expressed, while others had a restricted
expression pattern.
Nourse et al. (1998) used isotopic in situ hybridization to map the
TPD52L2 gene to human chromosome 20q13.2-q13.3, a region that is
frequently amplified in breast and other cancers. This localization is
independent of the map locations of TPD52 and TPD52L1.
*FIELD* RF
1. Nourse, C. R.; Mattei, M.-G.; Gunning, P.; Byrne, J. A.: Cloning
of a third member of the D52 gene family indicates alternative coding
sequence usage in D52-like transcripts. Biochim. Biophys. Acta 1443:
155-168, 1998.
*FIELD* CD
Jennifer P. Macke: 4/19/1999
*FIELD* ED
alopez: 07/27/1999
alopez: 6/21/1999
alopez: 4/19/1999
*RECORD*
*FIELD* NO
603747
*FIELD* TI
*603747 TUMOR PROTEIN D52-LIKE 2; TPD52L2
;;D54
*FIELD* TX
Nourse et al. (1998) identified EST sequences with similarity to tumor
read moreprotein D52. They cloned the corresponding cDNA, termed D54, from a
breast carcinoma library. The longest cDNA predicted a 206-amino acid
polypeptide with 56% and 51% identity to TPD52 and TPD52L1,
respectively. Nourse et al. (1998) reported that some of the D54 clones
that they isolated were alternatively spliced variants. Northern blot
analysis and RT-PCR of rat tissues revealed that some splice variants of
D54 were ubiquitously expressed, while others had a restricted
expression pattern.
Nourse et al. (1998) used isotopic in situ hybridization to map the
TPD52L2 gene to human chromosome 20q13.2-q13.3, a region that is
frequently amplified in breast and other cancers. This localization is
independent of the map locations of TPD52 and TPD52L1.
*FIELD* RF
1. Nourse, C. R.; Mattei, M.-G.; Gunning, P.; Byrne, J. A.: Cloning
of a third member of the D52 gene family indicates alternative coding
sequence usage in D52-like transcripts. Biochim. Biophys. Acta 1443:
155-168, 1998.
*FIELD* CD
Jennifer P. Macke: 4/19/1999
*FIELD* ED
alopez: 07/27/1999
alopez: 6/21/1999
alopez: 4/19/1999