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Protein

Translationally-controlled tumor protein

Gene

TPT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in calcium binding and microtubule stabilization.

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • calcium ion transport Source: UniProtKB
  • cellular calcium ion homeostasis Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: MGI
  • regulation of apoptotic process Source: UniProtKB
  • response to virus Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Translationally-controlled tumor protein
Short name:
TCTP
Alternative name(s):
Fortilin
Histamine-releasing factor
Short name:
HRF
p23
Gene namesi
Name:TPT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:12022. TPT1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: MGI
  • multivesicular body Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36701.

Protein family/group databases

Allergomei3816. Hom s TCTP.

Polymorphism and mutation databases

DMDMi136479.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 172172Translationally-controlled tumor proteinPRO_0000211268Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 461Phosphoserine; by PLK1Combined sources1 Publication
Modified residuei53 – 531PhosphoserineCombined sources
Modified residuei64 – 641Phosphoserine; by PLK11 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP13693.
MaxQBiP13693.
PaxDbiP13693.
PRIDEiP13693.
TopDownProteomicsiP13693-1. [P13693-1]

2D gel databases

DOSAC-COBS-2DPAGEP13693.
OGPiP13693.
REPRODUCTION-2DPAGEIPI00550900.
SWISS-2DPAGEP13693.

PTM databases

iPTMnetiP13693.
PhosphoSiteiP13693.
SwissPalmiP13693.

Expressioni

Tissue specificityi

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.1 Publication

Inductioni

Down-regulated in response to enterovirus 71 (EV71) infection.1 Publication

Gene expression databases

BgeeiP13693.
CleanExiHS_TPT1.
ExpressionAtlasiP13693. baseline and differential.
GenevisibleiP13693. HS.

Organism-specific databases

HPAiCAB008364.
HPA039437.

Interactioni

Subunit structurei

Interacts with STEAP3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ATP1A1P050235EBI-1783169,EBI-358778
EEF1DP296923EBI-1783169,EBI-358607
EEF1DP29692-23EBI-1783169,EBI-5280572
HSPB1P047922EBI-1783169,EBI-352682
TP53P046375EBI-1783169,EBI-366083
TRIP13Q156453EBI-1783169,EBI-358993
TSC22D1Q157145EBI-1783169,EBI-712609

Protein-protein interaction databases

BioGridi113030. 32 interactions.
DIPiDIP-40097N.
IntActiP13693. 32 interactions.
MINTiMINT-2634453.
STRINGi9606.ENSP00000431872.

Structurei

Secondary structure

1
172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Turni7 – 93Combined sources
Beta strandi12 – 154Combined sources
Beta strandi18 – 236Combined sources
Helixi24 – 263Combined sources
Beta strandi28 – 325Combined sources
Helixi71 – 755Combined sources
Beta strandi79 – 813Combined sources
Helixi85 – 10622Combined sources
Helixi108 – 1103Combined sources
Helixi111 – 12717Combined sources
Helixi129 – 1313Combined sources
Beta strandi133 – 1364Combined sources
Beta strandi146 – 1516Combined sources
Beta strandi158 – 1636Combined sources
Helixi164 – 1663Combined sources
Beta strandi167 – 1715Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZ1X-ray2.00A/B/C/D1-172[»]
2HR9NMR-A1-172[»]
3EBMX-ray2.60A/B/C/D1-172[»]
4Z9VX-ray2.10C/D/E/F/G/H11-31[»]
ProteinModelPortaliP13693.
SMRiP13693. Positions 1-172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13693.

Family & Domainsi

Sequence similaritiesi

Belongs to the TCTP family.Curated

Phylogenomic databases

eggNOGiKOG1727. Eukaryota.
ENOG4111FVP. LUCA.
GeneTreeiENSGT00390000006051.
HOGENOMiHOG000203361.
HOVERGENiHBG002282.
InParanoidiP13693.
OrthoDBiEOG7SJD61.
PhylomeDBiP13693.
TreeFamiTF300238.

Family and domain databases

Gene3Di2.170.150.10. 1 hit.
InterProiIPR011057. Mss4-like.
IPR011323. Mss4/transl-control_tumor.
IPR018103. Translation_control_tumour_CS.
IPR018105. Translational_control_tumour_p.
[Graphical view]
PANTHERiPTHR11991. PTHR11991. 1 hit.
PfamiPF00838. TCTP. 1 hit.
[Graphical view]
PRINTSiPR01653. TCTPROTEIN.
SUPFAMiSSF51316. SSF51316. 1 hit.
PROSITEiPS01002. TCTP_1. 1 hit.
PS01003. TCTP_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P13693-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MIIYRDLISH DEMFSDIYKI REIADGLCLE VEGKMVSRTE GNIDDSLIGG
60 70 80 90 100
NASAEGPEGE GTESTVITGV DIVMNHHLQE TSFTKEAYKK YIKDYMKSIK
110 120 130 140 150
GKLEEQRPER VKPFMTGAAE QIKHILANFK NYQFFIGENM NPDGMVALLD
160 170
YREDGVTPYM IFFKDGLEME KC
Length:172
Mass (Da):19,595
Last modified:January 1, 1990 - v1
Checksum:iBD31399B71CA62F9
GO
Isoform 2 (identifier: P13693-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Show »
Length:138
Mass (Da):15,597
Checksum:iFD4A670AEFAC61FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 542SA → YG in AAH12431 (PubMed:15489334).Curated
Sequence conflicti168 – 1681E → K in AAQ01550 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti146 – 1461V → F.
Corresponds to variant rs3087989 [ dbSNP | Ensembl ].
VAR_052273

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3434Missing in isoform 2. 1 PublicationVSP_054838Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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: EAX08731.1.
CH471075 Genomic DNA. Translation: EAX08732.1.
BC003352 mRNA. Translation: AAH03352.1.
BC012431 mRNA. Translation: AAH12431.1.
BC022436 mRNA. Translation: AAH22436.1.
BC052333 mRNA. Translation: AAH52333.1.
CCDSiCCDS66538.1. [P13693-2]
CCDS9397.1. [P13693-1]
PIRiS06590.
RefSeqiNP_001273202.1. NM_001286273.1. [P13693-2]
NP_003286.1. NM_003295.3. [P13693-1]
UniGeneiHs.374596.
Hs.717316.

Genome annotation databases

EnsembliENST00000379055; ENSP00000368344; ENSG00000133112. [P13693-2]
ENST00000379056; ENSP00000368345; ENSG00000133112. [P13693-2]
ENST00000530705; ENSP00000431872; ENSG00000133112. [P13693-1]
GeneIDi7178.
UCSCiuc001uzy.3. human. [P13693-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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: EAX08731.1.
CH471075 Genomic DNA. Translation: EAX08732.1.
BC003352 mRNA. Translation: AAH03352.1.
BC012431 mRNA. Translation: AAH12431.1.
BC022436 mRNA. Translation: AAH22436.1.
BC052333 mRNA. Translation: AAH52333.1.
CCDSiCCDS66538.1. [P13693-2]
CCDS9397.1. [P13693-1]
PIRiS06590.
RefSeqiNP_001273202.1. NM_001286273.1. [P13693-2]
NP_003286.1. NM_003295.3. [P13693-1]
UniGeneiHs.374596.
Hs.717316.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZ1X-ray2.00A/B/C/D1-172[»]
2HR9NMR-A1-172[»]
3EBMX-ray2.60A/B/C/D1-172[»]
4Z9VX-ray2.10C/D/E/F/G/H11-31[»]
ProteinModelPortaliP13693.
SMRiP13693. Positions 1-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113030. 32 interactions.
DIPiDIP-40097N.
IntActiP13693. 32 interactions.
MINTiMINT-2634453.
STRINGi9606.ENSP00000431872.

Protein family/group databases

Allergomei3816. Hom s TCTP.

PTM databases

iPTMnetiP13693.
PhosphoSiteiP13693.
SwissPalmiP13693.

Polymorphism and mutation databases

DMDMi136479.

2D gel databases

DOSAC-COBS-2DPAGEP13693.
OGPiP13693.
REPRODUCTION-2DPAGEIPI00550900.
SWISS-2DPAGEP13693.

Proteomic databases

EPDiP13693.
MaxQBiP13693.
PaxDbiP13693.
PRIDEiP13693.
TopDownProteomicsiP13693-1. [P13693-1]

Protocols and materials databases

DNASUi7178.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379055; ENSP00000368344; ENSG00000133112. [P13693-2]
ENST00000379056; ENSP00000368345; ENSG00000133112. [P13693-2]
ENST00000530705; ENSP00000431872; ENSG00000133112. [P13693-1]
GeneIDi7178.
UCSCiuc001uzy.3. human. [P13693-1]

Organism-specific databases

CTDi7178.
GeneCardsiTPT1.
HGNCiHGNC:12022. TPT1.
HPAiCAB008364.
HPA039437.
MIMi600763. gene.
neXtProtiNX_P13693.
PharmGKBiPA36701.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1727. Eukaryota.
ENOG4111FVP. LUCA.
GeneTreeiENSGT00390000006051.
HOGENOMiHOG000203361.
HOVERGENiHBG002282.
InParanoidiP13693.
OrthoDBiEOG7SJD61.
PhylomeDBiP13693.
TreeFamiTF300238.

Miscellaneous databases

ChiTaRSiTPT1. human.
EvolutionaryTraceiP13693.
GeneWikiiTPT1.
Translationally-controlled_tumor_protein.
GenomeRNAii7178.
NextBioi28136.
PROiP13693.
SOURCEiSearch...

Gene expression databases

BgeeiP13693.
CleanExiHS_TPT1.
ExpressionAtlasiP13693. baseline and differential.
GenevisibleiP13693. HS.

Family and domain databases

Gene3Di2.170.150.10. 1 hit.
InterProiIPR011057. Mss4-like.
IPR011323. Mss4/transl-control_tumor.
IPR018103. Translation_control_tumour_CS.
IPR018105. Translational_control_tumour_p.
[Graphical view]
PANTHERiPTHR11991. PTHR11991. 1 hit.
PfamiPF00838. TCTP. 1 hit.
[Graphical view]
PRINTSiPR01653. TCTPROTEIN.
SUPFAMiSSF51316. SSF51316. 1 hit.
PROSITEiPS01002. TCTP_1. 1 hit.
PS01003. TCTP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. Thiele H.
    Thesis (2000), Humboldt-University Berlin, Germany
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  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] (ISOFORM 1).
  4. Gao T.H., Duan F.L., Zhu W.L.
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain, 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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.

Entry informationi

Entry nameiTCTP_HUMAN
AccessioniPrimary (citable) accession number: P13693
Secondary accession number(s): B2R7E5
, Q6YLS2, Q7Z4J4, Q8TBK7, Q96EE2, Q9UC70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 11, 2016
This is version 178 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.