ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q16890


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name TPD53_HUMAN
Primary accession number Q16890
Secondary accession numbers A8K757 A8K772 A8MUD2 A8MUJ7 A8MW70 O43397 Q5TC99 Q9BUQ6 Q9C054
Integrated into Swiss-Prot on January 24, 2001
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    May 26, 2009 (Entry version 64)
Name and origin of the protein
Protein name Tumor protein D53
Synonyms hD53
Tumor protein D52-like 1
Gene name
Name: TPD52L1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mammary carcinoma;
DOI=10.1006/geno.1996.0393; PubMed=8812487 [NCBI, ExPASy, EBI, Israel, Japan]
Byrne J.A., Mattei M.-G., Basset P.;
"Definition of the tumor protein D52 (TPD52) gene family through cloning of D52 homologues in human (hD53) and mouse (mD52).";
Genomics 35:523-532(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), SELF-ASSOCIATION, AND INTERACTION WITH TPD52 AND TPD52L2.
DOI=10.1038/sj.onc.1201604; PubMed=9484778 [NCBI, ExPASy, EBI, Israel, Japan]
Byrne J.A., Nourse C.R., Basset P., Gunning P.;
"Identification of homo- and heteromeric interactions between members of the breast carcinoma-associated D52 protein family using the yeast two-hybrid system.";
Oncogene 16:873-881(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Cho S., Kim J., Ryu S.E.;
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Skeletal muscle;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U44427; AAB40894.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U44428; AAB40895.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF004427; AAC98475.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF208012; AAG49634.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291866; BAF84555.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291872; BAF84561.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291887; BAF84576.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121938; CAI19649.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136128; CAI19649.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136128; CAI23004.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121938; CAI23004.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121938; CAI19647.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136128; CAI19647.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121938; CAI19648.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136128; CAI19648.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136128; CAI23002.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121938; CAI23002.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136128; CAI23003.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121938; CAI23003.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471051; EAW48142.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002375; AAH02375.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00383670; -.
IPI00414728; -.
IPI00457045; -.
IPI00642078; -.
RefSeq NP_001003395.1; -.
NP_001003396.1; -.
NP_001003397.1; -.
NP_003278.1; -.
UniGene Hs.591347
3D structure databases
ModBase Q16890.
Protein-protein interaction databases
IntAct Q16890; 11.
PTM databases
PhosphoSite Q16890; -.
Organism-specific databases
GeneCards GC06P125516; -.
H-InvDB HIX0006195; -.
HGNC HGNC:12006; TPD52L1.
GenAtlas TPD52L1.
MIM 604069; gene. [NCBI / EBI]
PharmGKB PA36687; -.
Gene expression databases
ArrayExpress Q16890; -.
Bgee Q16890; -.
CleanEx HS_TPD52L1; -.
GermOnline ENSG00000111907; Homo sapiens.
Ontologies
GO
GO:0048471; Cellular component: perinuclear region of cytoplasm (inferred from direct assay from UniProtKB).
GO:0046982; Molecular function: protein heterodimerization activity (inferred from direct assay from UniProtKB).
GO:0042803; Molecular function: protein homodimerization activity (inferred from direct assay from UniProtKB).
GO:0000086; Biological process: G2/M transition of mitotic cell cycle (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR007327; TPD52.
Graphical view of domain structure.
PANTHER PTHR19307; TPD52; 1.
Pfam PF04201; TPD52; 1.
Pfam graphical view of domain structure.
Proteomic databases
PRIDE Q16890; -.
Genome annotation databases
Ensembl ENSG00000111907; Homo sapiens. [Contig view]
GeneID 7164; -.
KEGG hsa:7164; -.
Phylogenomic databases
HOGENOM Q16890; -.
HOVERGEN Q16890; -.
OMA Q16890; EEEELQC.
Other
NextBio 28038; -.
SOURCE TPD52L1; Homo sapiens.
ProtoNet Q16890.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Coiled coil; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   204  204     Tumor protein D53. PRO_0000185741
COILED   22    73  52     Potential. 
MOD_RES   149   149        Phosphoserine. 
VAR_SEQ   1    29        Missing (in isoform 4). VSP_036751
VAR_SEQ   129   131        SYS -> RRK (in isoform 3 and isoform 4). VSP_036752
VAR_SEQ   132   204        Missing (in isoform 3 and isoform 4). VSP_036753
VAR_SEQ   143   144        NS -> RK (in isoform 2). VSP_036754
VAR_SEQ   145   204        Missing (in isoform 2). VSP_036755
VARIANT   62    62  1     R -> K (in dbSNP:rs6905231 [NCBI]). VAR_034568 
CONFLICT   74    74        N -> T (in Ref. 4; BAF84576). 
CONFLICT   107   107        G -> E (in Ref. 4; BAF84561). 
Sequence information
Length: 204 AA [This is the length of the unprocessed precursor] Molecular weight: 22449 Da [This is the MW of the unprocessed precursor] CRC64: 6B3C336D5C0653C9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEAQAQGLLE TEPLQGTDED AVASADFSSM LSEEEKEELK AELVQLEDEI TTLRQVLSAK 

        70         80         90        100        110        120 
ERHLVEIKQK LGMNLMNELK QNFSKSWHDM QTTTAYKKTH ETLSHAGQKA TAAFSNVGTA 

       130        140        150        160        170        180 
ISKKFGDMSY SIRHSISMPA MRNSPTFKSF EERVETTVTS LKTKVGGTNP NGGSFEEVLS 

       190        200 
STAHASAQSL AGGSRRTKEE ELQC 

Q16890 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!