P13693 (TCTP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Translationally-controlled tumor protein
Short name=TCTP

Alternative name(s):
Fortilin
Histamine-releasing factor
Short name=HRF
p23

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.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in calcium binding and microtubule stabilization.
Subunit structure	Interacts with STEAP3. Ref.17
Subcellular location	Cytoplasm Ref.15.
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.15
Induction	Down-regulated in response to enterovirus 71 (EV71) infection. Ref.20
Sequence similarities	Belongs to the TCTP family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Calcium
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: UniProtKB calcium ion transport Inferred by curator Ref.19. Source: UniProtKB cellular calcium ion homeostasis Inferred by curator Ref.19. Source: UniProtKB response to virus Inferred from expression pattern Ref.20. Source: UniProtKB
Cellular component	extracellular space Inferred from direct assay Ref.17. Source: MGI multivesicular body Inferred from direct assay Ref.17. Source: MGI
Molecular function	calcium ion binding Inferred from direct assay Ref.18Ref.19. Source: UniProtKB
Complete GO annotation...

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.16 Ref.21 Ref.22

Modified residue

53

1

Phosphoserine Ref.22

Modified residue

64

1

Phosphoserine; by PLK1 Ref.16

Modified residue

93

1

N6-acetyllysine Ref.23

Natural variations

Natural variant

146

1

V → F.
Corresponds to variant rs3087989 [ dbSNP | Ensembl ].

VAR_052273

Experimental info

Sequence conflict

53 – 54

2

SA → YG in AAH12431. Ref.9

Sequence conflict

168

1

E → K in AAQ01550. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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 [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]	"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]. Tissue: Trachea.
[7]	"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].
[8]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection." Leong W.F., Chow V.T. Cell. Microbiol. 8:565-580(2006) [PubMed: 16548883] [Abstract] Cited for: INDUCTION, MASS SPECTROMETRY.
[21]	"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. Tissue: Embryonic kidney.
[22]	"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. Tissue: Cervix carcinoma.
[23]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-93, MASS SPECTROMETRY.
[24]	"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].
[25]	"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

EMBL
GenBank
DDBJ

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.
AK312951 mRNA. Translation: BAG35792.1.
AL138963 Genomic DNA. Translation: CAH72034.1.
CH471075 Genomic DNA. Translation: EAX08732.1.
BC003352 mRNA. Translation: AAH03352.1.
BC012431 mRNA. Translation: AAH12431.1.
BC052333 mRNA. Translation: AAH52333.1.

IPI

IPI00550900.

PIR

S06590.

RefSeq

NP_003286.1. NM_003295.2.

UniGene

Hs.374596.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YZ1	X-ray	2.00	A/B/C/D	1-172	[»]
2HR9	NMR	-	A	1-172	[»]
3EBM	X-ray	2.60	A/B/C/D	1-172	[»]

ProteinModelPortal

P13693.

SMR

P13693. Positions 1-172.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13693. 23 interactions.

MINT

MINT-2634453.

STRING

P13693.

Protein family/group databases

Allergome

3816. Hom s TCTP.

PTM databases

PhosphoSite

P13693.

Polymorphism databases

DMDM

136479.

2D 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.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309246; ENSP00000339051; ENSG00000133112.
ENST00000379060; ENSP00000368350; ENSG00000133112.

GeneID

7178.

KEGG

hsa:7178.

UCSC

uc001uzy.1. human.

Organism-specific databases

CTD

7178.

GeneCards

GC13M045921.

H-InvDB

HIX0011286.
HIX0028410.
HIX0034276.

HGNC

HGNC:12022. TPT1.

HPA

CAB008364.

MIM

600763. gene.

neXtProt

NX_P13693.

PharmGKB

PA36701.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17188.

HOVERGEN

HBG002282.

InParanoid

P13693.

OrthoDB

EOG4FJ89Z.

PhylomeDB

P13693.

Gene expression databases

ArrayExpress

P13693.

Bgee

P13693.

CleanEx

HS_TPT1.

Genevestigator

P13693.

GermOnline

ENSG00000133112. Homo sapiens.

Family and domain databases

InterPro

IPR011057. Mss4-like.
IPR011323. Mss4/transl-control_tumor.
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.

SUPFAM

SSF51316. Mss4_like. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

NextBio

28136.

SOURCE

Search...

Entry information

Entry name

TCTP_HUMAN

Accession

Primary (citable) accession number: P13693
Secondary accession number(s): B2R7E5 , Q6YLS2, Q7Z4J4, Q96EE2, Q9UC70

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	January 25, 2012
This is version 132 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.