Q16890 (TPD53_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tumor protein D53
Short name=hD53

Alternative name(s):
Tumor protein D52-like 1

Gene names

Name:

TPD52L1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	204 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Forms homodimer or heterodimer with other members of the family.
Sequence similarities	Belongs to the TPD52 family.
Sequence caution	The sequence AAC98475.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA fragmentation involved in apoptotic nuclear change Inferred from direct assay PubMed 14761963. Source: UniProtKB G2/M transition of mitotic cell cycle Inferred from direct assay PubMed 16112108. Source: UniProtKB induction of apoptosis Inferred from direct assay PubMed 14761963. Source: UniProtKB positive regulation of JNK cascade Inferred from direct assay PubMed 14761963. Source: UniProtKB positive regulation of MAP kinase activity Inferred from direct assay PubMed 14761963. Source: UniProtKB
Cellular component	perinuclear region of cytoplasm Inferred from direct assay PubMed 16112108PubMed 12963375. Source: UniProtKB
Molecular function	cysteine-type endopeptidase activator activity involved in apoptotic process Inferred from direct assay PubMed 14761963. Source: UniProtKB protein heterodimerization activity Inferred from direct assay Ref.2. Source: UniProtKB protein homodimerization activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-717470,EBI-717470
TPD52	P55327	3	EBI-717470,EBI-782581
Tpd52	Q62393	3	EBI-717470,EBI-782591	From a different organism.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q16890-1)

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: Q16890-2)

The sequence of this isoform differs from the canonical sequence as follows:
     143-144: NS → RK
     145-204: Missing.

Isoform 3 (identifier: Q16890-3)

The sequence of this isoform differs from the canonical sequence as follows:
     129-131: SYS → RRK
     132-204: Missing.

Isoform 4 (identifier: Q16890-4)

Also known as: +5hD53;

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.
     129-131: SYS → RRK
     132-204: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 204	204	Tumor protein D53		PRO_0000185741
Regions
	Coiled coil	22 – 73	52	Potential
Amino acid modifications
	Modified residue	149	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	1 – 29	29	Missing in isoform 4.		VSP_036751
	Alternative sequence	129 – 131	3	SYS → RRK in isoform 3 and isoform 4.		VSP_036752
	Alternative sequence	132 – 204	73	Missing in isoform 3 and isoform 4.		VSP_036753
	Alternative sequence	143 – 144	2	NS → RK in isoform 2.		VSP_036754
	Alternative sequence	145 – 204	60	Missing in isoform 2.		VSP_036755
	Natural variant	62	1	R → K. Corresponds to variant rs6905231 [ dbSNP | Ensembl ].		VAR_034568
Experimental info
	Sequence conflict	74	1	N → T in BAF84576. Ref.4
	Sequence conflict	107	1	G → E in BAF84561. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 6B3C336D5C0653C9	FASTA	204	22,449
	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
	Isoform 2 [UniParc]. Checksum: A1CEF878A98BAA63	FASTA	144	16,176
	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 ISKKFGDMSY SIRHSISMPA MRRK
	Isoform 3 [UniParc]. Checksum: ACBE38AD88FC4F52	FASTA	131	14,715
	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 ISKKFGDMRR K
	Isoform 4 (+5hD53) [UniParc]. Checksum: A2427192E12E4E62	FASTA	102	11,721
	10 20 30 40 50 60 MLSEEEKEEL KAELVQLEDE ITTLRQVLSA KERHLVEIKQ KLGMNLMNEL KQNFSKSWHD 70 80 90 100 MQTTTAYKKT HETLSHAGQK ATAAFSNVGT AISKKFGDMR RK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Definition of the tumor protein D52 (TPD52) gene family through cloning of D52 homologues in human (hD53) and mouse (mD52)." Byrne J.A., Mattei M.-G., Basset P. Genomics 35:523-532(1996) [PubMed: 8812487] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Mammary carcinoma.
[2]	"Identification of homo- and heteromeric interactions between members of the breast carcinoma-associated D52 protein family using the yeast two-hybrid system." Byrne J.A., Nourse C.R., Basset P., Gunning P. Oncogene 16:873-881(1998) [PubMed: 9484778] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), SELF-ASSOCIATION, INTERACTION WITH TPD52 AND TPD52L2.
[3]	Cho S., Kim J., Ryu S.E. Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[4]	"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. , 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). Tissue: Skeletal muscle.
[5]	"The DNA sequence and analysis of human chromosome 6." 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. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Lung.
[8]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U44427 mRNA. Translation: AAB40894.1. U44428 mRNA. Translation: AAB40895.1. AF004427 mRNA. Translation: AAC98475.1. Different initiation. AF208012 mRNA. Translation: AAG49634.1. AK291866 mRNA. Translation: BAF84555.1. AK291872 mRNA. Translation: BAF84561.1. AK291887 mRNA. Translation: BAF84576.1. AL121938 Genomic DNA. Translation: CAI19645.1. AL121938, AL136128 Genomic DNA. Translation: CAI19649.1. AL136128, AL121938 Genomic DNA. Translation: CAI23004.1. AL121938, AL136128 Genomic DNA. Translation: CAI19647.1. AL121938, AL136128 Genomic DNA. Translation: CAI19648.1. AL136128, AL121938 Genomic DNA. Translation: CAI23002.1. AL136128, AL121938 Genomic DNA. Translation: CAI23003.1. CH471051 Genomic DNA. Translation: EAW48142.1. BC002375 mRNA. Translation: AAH02375.1.
IPI	IPI00414728. IPI00457045. IPI00642078. IPI00976469.
RefSeq	NP_001003395.1. NM_001003395.1. NP_001003396.1. NM_001003396.1. NP_001003397.1. NM_001003397.1. NP_003278.1. NM_003287.2.
UniGene	Hs.591347.
3D structure databases
ProteinModelPortal	Q16890.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q16890. 10 interactions.
MINT	MINT-273476.
STRING	Q16890.
PTM databases
PhosphoSite	Q16890.
Polymorphism databases
DMDM	12585368.
Proteomic databases
PRIDE	Q16890.
Protocols and materials databases
DNASU	7164.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000304877; ENSP00000306285; ENSG00000111907. ENST00000368388; ENSP00000357373; ENSG00000111907. ENST00000368402; ENSP00000357387; ENSG00000111907.
GeneID	7164.
KEGG	hsa:7164.
UCSC	uc003pzu.1. human. uc003pzv.1. human. uc003pzw.1. human. uc003pzx.1. human.
Organism-specific databases
CTD	7164.
GeneCards	GC06P125516.
H-InvDB	HIX0006195.
HGNC	HGNC:12006. TPD52L1.
HPA	HPA027915. HPA027916.
MIM	604069. gene.
neXtProt	NX_Q16890.
PharmGKB	PA36687.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG268763.
GeneTree	ENSGT00390000015988.
HOVERGEN	HBG058643.
InParanoid	Q16890.
OMA	WHDVQTT.
OrthoDB	EOG4J6RS8.
PhylomeDB	Q16890.
Enzyme and pathway databases
Reactome	REACT_11123. Membrane Trafficking.
Gene expression databases
ArrayExpress	Q16890.
Bgee	Q16890.
CleanEx	HS_TPD52L1.
Genevestigator	Q16890.
GermOnline	ENSG00000111907. Homo sapiens.
Family and domain databases
InterPro	IPR007327. TPD52. [Graphical view]
PANTHER	PTHR19307. TPD52. 1 hit.
Pfam	PF04201. TPD52. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	28038.
SOURCE	Search...

Entry information

Entry name

TPD53_HUMAN

Accession

Primary (citable) accession number: Q16890
Secondary accession number(s): A8K757 , A8K772, A8MUD2, A8MUJ7, A8MW70, O43397, Q5TC99, Q5TDQ0, Q9BUQ6, Q9C054

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	November 1, 1996
Last modified:	April 18, 2012
This is version 91 of the entry and version 1 of the sequence. [Complete 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.