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Protein

Tumor suppressor candidate 2

Gene

TUSC2

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

Functioni

May function as a tumor suppressor, inhibiting colony formation, causing G1 arrest and ultimately inducing apoptosis in homozygous 3p21.3 120-kb region-deficient cells.

GO - Biological processi

  1. cell-cell signaling Source: ProtInc
  2. cell cycle Source: UniProtKB-KW
  3. cell maturation Source: Ensembl
  4. cell proliferation Source: ProtInc
  5. chemokine (C-C motif) ligand 5 production Source: Ensembl
  6. inflammatory response Source: Ensembl
  7. interleukin-15 production Source: Ensembl
  8. natural killer cell differentiation Source: Ensembl
  9. negative regulation of interleukin-17 production Source: Ensembl
  10. neutrophil mediated killing of gram-negative bacterium Source: Ensembl
  11. phagocytosis Source: Ensembl
  12. positive regulation of interleukin-10 production Source: Ensembl
  13. regulation of mitochondrial membrane potential Source: Ensembl
  14. regulation of reactive oxygen species metabolic process Source: Ensembl
  15. response to defense-related host reactive oxygen species production Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell cycle

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor suppressor candidate 2
Alternative name(s):
Fusion 1 protein
Short name:
Fus-1 protein
PDGFA-associated protein 2
Gene namesi
Name:TUSC2
Synonyms:C3orf11, FUS1, LGCC, PDAP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:17034. TUSC2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

Organism-specific databases

PharmGKBiPA134968273.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 110109Tumor suppressor candidate 2PRO_0000148170Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine1 Publication
Modified residuei50 – 501Phosphoserine1 Publication

Post-translational modificationi

Myristoylation is required for tumor suppressor activity.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

MaxQBiO75896.
PaxDbiO75896.
PRIDEiO75896.

PTM databases

PhosphoSiteiO75896.

Expressioni

Tissue specificityi

Strong expression in heart, lung, skeletal muscle, kidney, and pancreas, followed by brain and liver, lowest levels in placenta.

Gene expression databases

BgeeiO75896.
CleanExiHS_TUSC2.
ExpressionAtlasiO75896. baseline and differential.
GenevestigatoriO75896.

Organism-specific databases

HPAiHPA030116.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ABLP005211EBI-1052725,EBI-1550592From a different organism.
GK006Q6P2I71EBI-1052725,EBI-1047027
HSPA4LO957571EBI-1052725,EBI-358652
LRBAP508511EBI-1052725,EBI-1052167
SGOL2Q562F61EBI-1052725,EBI-989213

Protein-protein interaction databases

BioGridi116462. 7 interactions.
IntActiO75896. 2 interactions.
STRINGi9606.ENSP00000232496.

Structurei

3D structure databases

ProteinModelPortaliO75896.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TUSC2 family.Curated

Phylogenomic databases

eggNOGiNOG71519.
GeneTreeiENSGT00390000008040.
HOGENOMiHOG000007342.
HOVERGENiHBG054202.
InParanoidiO75896.
OMAiTRRGSMY.
PhylomeDBiO75896.
TreeFamiTF314634.

Family and domain databases

InterProiIPR029393. FUS1.
[Graphical view]
PANTHERiPTHR15453. PTHR15453. 1 hit.
PfamiPF15000. TUSC2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O75896-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGASGSKARG LWPFASAAGG GGSEAAGAEQ ALVRPRGRAV PPFVFTRRGS
60 70 80 90 100
MFYDEDGDLA HEFYEETIVT KNGQKRAKLR RVHKNLIPQG IVKLDHPRIH
110
VDFPVILYEV
Length:110
Mass (Da):12,074
Last modified:January 23, 2007 - v3
Checksum:i9503BD10637C1504
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055479 mRNA. Translation: AAC35497.1.
AK311998 mRNA. Translation: BAG34936.1.
CH471055 Genomic DNA. Translation: EAW65097.1.
BC023976 mRNA. Translation: AAH23976.1.
CCDSiCCDS2819.1.
RefSeqiNP_009206.1. NM_007275.2.
UniGeneiHs.517981.

Genome annotation databases

EnsembliENST00000232496; ENSP00000232496; ENSG00000114383.
GeneIDi11334.
KEGGihsa:11334.
UCSCiuc003czy.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055479 mRNA. Translation: AAC35497.1.
AK311998 mRNA. Translation: BAG34936.1.
CH471055 Genomic DNA. Translation: EAW65097.1.
BC023976 mRNA. Translation: AAH23976.1.
CCDSiCCDS2819.1.
RefSeqiNP_009206.1. NM_007275.2.
UniGeneiHs.517981.

3D structure databases

ProteinModelPortaliO75896.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116462. 7 interactions.
IntActiO75896. 2 interactions.
STRINGi9606.ENSP00000232496.

PTM databases

PhosphoSiteiO75896.

Proteomic databases

MaxQBiO75896.
PaxDbiO75896.
PRIDEiO75896.

Protocols and materials databases

DNASUi11334.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000232496; ENSP00000232496; ENSG00000114383.
GeneIDi11334.
KEGGihsa:11334.
UCSCiuc003czy.1. human.

Organism-specific databases

CTDi11334.
GeneCardsiGC03M050357.
HGNCiHGNC:17034. TUSC2.
HPAiHPA030116.
MIMi607052. gene.
neXtProtiNX_O75896.
PharmGKBiPA134968273.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG71519.
GeneTreeiENSGT00390000008040.
HOGENOMiHOG000007342.
HOVERGENiHBG054202.
InParanoidiO75896.
OMAiTRRGSMY.
PhylomeDBiO75896.
TreeFamiTF314634.

Miscellaneous databases

GeneWikiiTUSC2.
GenomeRNAii11334.
NextBioi43061.
PROiO75896.
SOURCEiSearch...

Gene expression databases

BgeeiO75896.
CleanExiHS_TUSC2.
ExpressionAtlasiO75896. baseline and differential.
GenevestigatoriO75896.

Family and domain databases

InterProiIPR029393. FUS1.
[Graphical view]
PANTHERiPTHR15453. PTHR15453. 1 hit.
PfamiPF15000. TUSC2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Overexpression of candidate tumor suppressor gene FUS1 isolated from the 3p21.3 homozygous deletion region leads to G1 arrest and growth inhibition of lung cancer cells."
    Kondo M., Ji L., Kamibayashi C., Tomizawa Y., Randle D., Sekido Y., Yokota J., Kashuba V., Zabarovsky E., Kuzmin I., Lerman M., Roth J., Minna J.D.
    Oncogene 20:6258-6262(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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.
    , 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].
    Tissue: Subthalamic nucleus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Placenta.
  5. "Myristoylation of the fus1 protein is required for tumor suppression in human lung cancer cells."
    Uno F., Sasaki J., Nishizaki M., Carboni G., Xu K., Atkinson E.N., Kondo M., Minna J.D., Roth J.A., Ji L.
    Cancer Res. 64:2969-2976(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MYRISTOYLATION AT GLY-2.
  6. "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-50, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.

Entry informationi

Entry nameiTUSC2_HUMAN
AccessioniPrimary (citable) accession number: O75896
Secondary accession number(s): B2R4Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 109 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.