Reviewed, UniProtKB/Swiss-Prot P13693 (TCTP_HUMAN)

Names and origin

Protein names

Recommended name:
    Translationally-controlled tumor protein
      Short name=TCTP
Alternative name(s):
    p23
    Histamine-releasing factor
      Short name=HRF
    Fortilin

Gene names

Name:

TPT1

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	172 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in calcium binding and microtubule stabilization.
Subunit structure	Interacts with STEAP3. Ref.15
Subcellular location	Cytoplasm. Ref.13
Tissue specificity	Found in several healthy and tumoral cells including erythrocytes, hepatocytes, macrophages, platelets, keratinocytes, erythroleukemia cells, gliomas, melanomas, hepatoblastomas, and lymphomas. It cannot be detected in kidney and renal cell carcinoma (RCC). Expressed in placenta and prostate. Ref.13
Sequence similarities	Belongs to the TCTP family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Calcium
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: UniProtKB calcium ion transport Ref.17 Inferred by curator. Source: UniProtKB cellular calcium ion homeostasis Ref.17 Inferred by curator. Source: UniProtKB
Cellular component	extracellular space Ref.11 Ref.15 Inferred from direct assay. Source: MGI multivesicular body Ref.15 Inferred from direct assay. Source: MGI
Molecular function	calcium ion binding Ref.16 Ref.17 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CHFR	Q96EP1	2	EBI-1783169,EBI-718923
VHL	P40337	1	EBI-1783169,EBI-301246

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 172

172

Translationally-controlled tumor protein

PRO_0000211268

Amino acid modifications

Modified residue

46

1

Phosphoserine; by PLK1 Ref.14 Ref.18 Ref.19

Modified residue

53

1

Phosphoserine Ref.19

Modified residue

64

1

Phosphoserine; by PLK1 Ref.14

Natural variations

Natural variant

146

1

V → F: dbSNP rs3087989.

VAR_052273

Experimental info

Sequence conflict

53 – 54

2

SA → YG in AAH12431. Ref.7

Sequence conflict

168

1

E → K in AAQ01550. Ref.3

Secondary structure

1

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172

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Turn

7 – 9

3

Beta strand

12 – 15

4

Beta strand

18 – 23

6

Helix

24 – 26

3

Beta strand

28 – 32

5

Helix

71 – 75

5

Beta strand

79 – 81

3

Helix

85 – 106

22

Helix

108 – 110

3

Helix

111 – 127

17

Helix

129 – 131

3

Beta strand

133 – 136

4

Beta strand

146 – 151

6

Beta strand

158 – 163

6

Helix

164 – 166

3

Beta strand

167 – 171

5

Sequences

	Sequence		Length	Mass (Da)
	P13693-1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: BD31399B71CA62F9	FASTA	172	19,595
	10 20 30 40 50 60 MIIYRDLISH DEMFSDIYKI REIADGLCLE VEGKMVSRTE GNIDDSLIGG NASAEGPEGE 70 80 90 100 110 120 GTESTVITGV DIVMNHHLQE TSFTKEAYKK YIKDYMKSIK GKLEEQRPER VKPFMTGAAE 130 140 150 160 170 QIKHILANFK NYQFFIGENM NPDGMVALLD YREDGVTPYM IFFKDGLEME KC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA sequence coding for a translationally controlled human tumor protein." Gross B., Gaestel M., Boehm H., Bielka H. Nucleic Acids Res. 17:8367-8367(1989) [PubMed: 2813067] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Thiele H. Thesis (2000), Humboldt-University Berlin, Germany Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Cloning and characterization of TCTP from human eosinophils." Gnanasekar M., Ramaswamy K. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	Gao T.H., Duan F.L., Zhu W.L. Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] 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]. Tissue: Lung and Placenta.
[8]	"Human liver protein map: a reference database established by microsequencing and gel comparison." Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J. Electrophoresis 13:992-1001(1992) [PubMed: 1286669] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-10. Tissue: Liver.
[9]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-4; 22-31; 39-45 AND 103-109. Tissue: Keratinocyte.
[10]	"Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2." Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S. Electrophoresis 18:588-598(1997) [PubMed: 9150946] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-19. Tissue: Mammary carcinoma.
[11]	"Molecular identification of an IgE-dependent histamine-releasing factor." MacDonald S.M., Rafnar T., Langdon J., Lichtenstein L.M. Science 269:688-690(1995) [PubMed: 7542803] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-18.
[12]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 6-34; 111-123 AND 131-164, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[13]	"Translationally controlled tumor protein: a protein identified in several nontumoral cells including erythrocytes." Sanchez J.-C., Schaller D., Ravier F., Golaz O., Jaccoud S., Belet M., Wilkins M.R., James R., Deshusses J., Hochstrasser D.F. Electrophoresis 18:150-155(1997) [PubMed: 9059837] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[14]	"Plk phosphorylation regulates the microtubule-stabilizing protein TCTP." Yarm F.R. Mol. Cell. Biol. 22:6209-6221(2002) [PubMed: 12167714] [Abstract] Cited for: PHOSPHORYLATION AT SER-46 AND SER-64.
[15]	"TSAP6 facilitates the secretion of translationally controlled tumor protein/histamine-releasing factor via a nonclassical pathway." Amzallag N., Passer B.J., Allanic D., Segura E., Thery C., Goud B., Amson R., Telerman A. J. Biol. Chem. 279:46104-46112(2004) [PubMed: 15319436] [Abstract] Cited for: INTERACTION WITH STEAP3.
[16]	"Translationally controlled tumor protein (TCTP) in the human prostate and prostate cancer cells: expression, distribution, and calcium binding activity." Arcuri F., Papa S., Carducci A., Romagnoli R., Liberatori S., Riparbelli M.G., Sanchez J.-C., Tosi P., del Vecchio M.T. Prostate 60:130-140(2004) [PubMed: 15162379] [Abstract] Cited for: CALCIUM-BINDING.
[17]	"The translationally controlled tumor protein is a novel calcium binding protein of the human placenta and regulates calcium handling in trophoblast cells." Arcuri F., Papa S., Meini A., Carducci A., Romagnoli R., Bianchi L., Riparbelli M.G., Sanchez J.-C., Palmi M., Tosi P., Cintorino M. Biol. Reprod. 73:745-751(2005) [PubMed: 15958728] [Abstract] Cited for: CALCIUM-BINDING. Tissue: Placenta.
[18]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY.
[19]	"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-46 AND SER-53, MASS SPECTROMETRY.
[20]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[21]	"Solution structure of human translationally controlled tumor protein." Liu D.S., Feng Y.G., Wang J.F. Submitted (NOV-2004) to the PDB data bank Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X16064 mRNA. Translation: CAA34200.1.
AJ400717 Genomic DNA. Translation: CAB87812.1.
AY334563 mRNA. Translation: AAQ01550.1.
AY117678 mRNA. Translation: AAM51565.1.
CR457036 mRNA. Translation: CAG33317.1.
AL138963 Genomic DNA. Translation: CAH72034.1.
BC003352 mRNA. Translation: AAH03352.1.
BC012431 mRNA. Translation: AAH12431.1.
BC052333 mRNA. Translation: AAH52333.1.

IPI

IPI00550900.

PIR

S06590.

RefSeq

NP_003286.1.

UniGene

Hs.374596

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YZ1	X-ray	2.00	A/B/C/D	1-172	[»]
2HR9	NMR	-	A	1-172	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P13693. 8 interactions.

PTM databases

PhosphoSite

P13693.

2-D gel databases

SWISS-2DPAGE

P13693.

Aarhus/Ghent-2DPAGE

8114. IEF.
9119. IEF.

DOSAC-COBS-2DPAGE

P13693.

OGP

P13693.

REPRODUCTION-2DPAGE

IPI00550900.

Siena-2DPAGE

P13693.

Proteomic databases

PRIDE

P13693.

Genome annotation databases

Ensembl

ENSG00000133112. Homo sapiens. [Contig view]

GeneID

7178.

KEGG

hsa:7178.

Organism-specific databases

GeneCards

GC09M119885.
GC13M044827.

H-InvDB

HIX0011286.
HIX0028410.
HIX0034276.
HIX0035234.
HIX0077182.
HIX0092599.

HGNC

HGNC:12022. TPT1.

HPA

CAB008364.

MIM

600763. gene.

PharmGKB

PA36701.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P13693.

Gene expression databases

ArrayExpress

P13693.

Bgee

P13693.

CleanEx

HS_TPT1.

GermOnline

ENSG00000133112. Homo sapiens.

Family and domain databases

InterPro

IPR011323. Mss4/transl-control_tumor.
IPR001983. Translat-control_tumour-assoc.
IPR018103. Translation_control_tumour_CS.
IPR018105. Translational_control_tumour_p.
[Graphical view]

Gene3D

G3DSA:2.170.150.10. Mss4/transl-control_tumor. 1 hit.

PANTHER

PTHR11991. TCTP. 1 hit.

Pfam

PF00838. TCTP. 1 hit.
[Graphical view]

PRINTS

PR01653. TCTPROTEIN.

ProDom

PD004329. TCTP. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS01002. TCTP_1. 1 hit.
PS01003. TCTP_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

28136.

SOURCE

Search...

Entry information

Entry name

TCTP_HUMAN

Accession

Primary (citable) accession number: P13693
Secondary accession number(s): Q6YLS2 , Q7Z4J4, Q96EE2, Q9UC70

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	June 16, 2009
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)