O43399 (TPD54_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 121.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Tumor protein D54 Short name=hD54 Alternative name(s): Tumor protein D52-like 2 | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Reference proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 206 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Subunit structure | Forms a homodimer or heterodimer with other members of the family By similarity. Interacts with MAL2. Ref.7 |
| Sequence similarities | Belongs to the TPD52 family. |
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Alternative splicing |
| Domain | Coiled coil |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | regulation of cell proliferation Traceable author statement PubMed 9484778PubMed 9484778. Source: UniProtKB |
| Cellular_component | perinuclear region of cytoplasm Inferred from direct assay PubMed 16112108PubMed 16112108. Source: UniProtKB |
| Molecular_function | protein homodimerization activity Inferred from direct assay PubMed 9484778. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Tpd52 | Q62393 | 2 | EBI-782616,EBI-782591 | From a different organism. |
Alternative products
| This entry describes 6 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 1 (identifier: O43399-1) Also known as: HD54+ins2; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 2 (identifier: O43399-2) Also known as: HD54-ins2; The sequence of this isoform differs from the canonical sequence as follows: 106-125: Missing. | ||||||
| Isoform 3 (identifier: O43399-3) The sequence of this isoform differs from the canonical sequence as follows: 106-125: Missing. 159-159: R → RAHPFSHSFSSYSIRHSISMPAMR | ||||||
| Isoform 4 (identifier: O43399-4) The sequence of this isoform differs from the canonical sequence as follows: 106-125: Missing. 157-157: D → DMSSYSIRHSISMPA | ||||||
| Isoform 5 (identifier: O43399-5) The sequence of this isoform differs from the canonical sequence as follows: 157-157: D → DMSSYSIRHSISMPA | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 6 (identifier: O43399-6) The sequence of this isoform differs from the canonical sequence as follows: 7-29: Missing. 106-125: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 206 | 206 | Tumor protein D54 | PRO_0000185744 | |||||
Regions | |||||||||
| Coiled coil | 38 – 82 | 45 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.13 Ref.15 | ||||||
| Modified residue | 3 | 1 | Phosphoserine Ref.11 Ref.15 | ||||||
| Modified residue | 12 | 1 | Phosphoserine Ref.8 Ref.10 Ref.11 Ref.13 Ref.15 | ||||||
| Modified residue | 19 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 21 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 96 | 1 | Phosphoserine Ref.11 Ref.12 Ref.13 | ||||||
| Modified residue | 149 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 166 | 1 | Phosphoserine Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 | ||||||
| Modified residue | 192 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 7 – 29 | 23 | Missing in isoform 6. | VSP_045154 | |||||
| Alternative sequence | 106 – 125 | 20 | Missing in isoform 2, isoform 3, isoform 4 and isoform 6. | VSP_006547 | |||||
| Alternative sequence | 157 | 1 | D → DMSSYSIRHSISMPA in isoform 4 and isoform 5. | VSP_038361 | |||||
| Alternative sequence | 159 | 1 | R → RAHPFSHSFSSYSIRHSISM PAMR in isoform 3. | VSP_036756 | |||||
Experimental info | |||||||||
| Sequence conflict | 72 | 1 | R → K in AAC98478. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning of a third member of the D52 gene family indicates alternative coding sequence usage in D52-like transcripts." Nourse C.R., Mattei M.-G., Gunning P., Byrne J.A. Biochim. Biophys. Acta 1443:155-168(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING. Tissue: Mammary gland. |
| [2] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6). Tissue: Brain and Kidney. |
| [3] | "Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). |
| [4] | "The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. Rogers J.Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | 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. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [6] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta. |
| [7] | "Identification of MAL2, a novel member of the mal proteolipid family, though interactions with TPD52-like proteins in the yeast two-hybrid system." Wilson S.H.D., Bailey A.M., Nourse C.R., Mattei M.-G., Byrne J.A. Genomics 76:81-88(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAL2. |
| [8] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-166, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [9] | "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, MASS SPECTROMETRY. Tissue: T-cell. |
| [10] | "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-166, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [11] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-12; SER-96 AND SER-166, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [12] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-149 AND SER-166, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [13] | "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-19; SER-21; SER-96 AND SER-166, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [14] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [15] | "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-12 AND SER-166, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF004429 mRNA. Translation: AAC98477.1. AF004430 mRNA. Translation: AAC98478.1. AK055068 mRNA. Translation: BAG51460.1. AK298366 mRNA. Translation: BAG60608.1. BT019631 mRNA. Translation: AAV38437.1. AL118506 Genomic DNA. Translation: CAC15492.1. AL118506 Genomic DNA. Translation: CAI21899.1. AL118506 Genomic DNA. Translation: CAI21900.1. AL118506 Genomic DNA. Translation: CAI21902.1. CH471077 Genomic DNA. Translation: EAW75195.1. CH471077 Genomic DNA. Translation: EAW75197.1. CH471077 Genomic DNA. Translation: EAW75198.1. CH471077 Genomic DNA. Translation: EAW75201.1. BC006804 mRNA. Translation: AAH06804.1. |
| IPI | IPI00221178. IPI00306825. IPI00399266. IPI00399267. IPI00399268. |
| RefSeq | NP_001230821.1. NM_001243892.1. NP_003279.2. NM_003288.3. NP_955393.1. NM_199361.2. NP_955394.1. NM_199362.2. NP_955395.1. NM_199363.2. |
| UniGene | Hs.473296. |
3D structure databases | |
| ProteinModelPortal | O43399. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O43399. 8 interactions. |
| STRING | 9606.ENSP00000217121. |
PTM databases | |
| PhosphoSite | O43399. |
2D gel databases | |
| OGP | O43399. |
Proteomic databases | |
| PaxDb | O43399. |
| PRIDE | O43399. |
Protocols and materials databases | |
| DNASU | 7165. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000346249; ENSP00000343547; ENSG00000101150. ENST00000348257; ENSP00000343554; ENSG00000101150. ENST00000351424; ENSP00000340006; ENSG00000101150. ENST00000352482; ENSP00000344647; ENSG00000101150. ENST00000358548; ENSP00000351350; ENSG00000101150. ENST00000369927; ENSP00000358943; ENSG00000101150. |
| GeneID | 7165. |
| KEGG | hsa:7165. |
| UCSC | uc002ygz.3. human. uc002yha.3. human. uc002yhb.3. human. uc002yhc.3. human. uc011abl.2. human. |
Organism-specific databases | |
| CTD | 7165. |
| GeneCards | GC20P062490. |
| HGNC | HGNC:12007. TPD52L2. |
| HPA | HPA047489. |
| MIM | 603747. gene. |
| neXtProt | NX_O43399. |
| PharmGKB | PA36688. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG329468. |
| HOGENOM | HOG000231968. |
| HOVERGEN | HBG058643. |
| OrthoDB | EOG4BP1CV. |
Enzyme and pathway databases | |
| SignaLink | O43399. |
Gene expression databases | |
| ArrayExpress | O43399. |
| Bgee | O43399. |
| CleanEx | HS_TPD52L2. |
| Genevestigator | O43399. |
| GermOnline | ENSG00000101150. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR007327. TPD52. [Graphical view] |
| PANTHER | PTHR19307. PTHR19307. 1 hit. |
| Pfam | PF04201. TPD52. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | TPD52L2. human. |
| GenomeRNAi | 7165. |
| NextBio | 28048. |
| SOURCE | Search... |
Entry information
| Entry name | TPD54_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O43399 Secondary accession number(s): B4DPJ6 Q9H3Z6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 20 Human chromosome 20: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
