Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Tensin-4

Gene

TNS4

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

Functioni

May be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton (By similarity). May promote apoptosis, via its cleavage by caspase-3.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei570 – 5712Cleavage; by caspase-3

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. protein localization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

SignaLinkiQ8IZW8.

Names & Taxonomyi

Protein namesi
Recommended name:
Tensin-4
Alternative name(s):
C-terminal tensin-like protein
Gene namesi
Name:TNS4
Synonyms:CTEN
ORF Names:PP14434
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:24352. TNS4.

Subcellular locationi

Cell junctionfocal adhesion 1 Publication. Cytoplasmcytoskeleton 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. cytoskeleton Source: UniProtKB-SubCell
  3. focal adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi506 – 5061D → A: No effect on cleavage by caspase-3. 1 Publication
Mutagenesisi570 – 5701D → A: Abolishes cleavage by caspase-3. 1 Publication

Organism-specific databases

PharmGKBiPA142670717.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 715697Tensin-4PRO_0000248213Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei82 – 821Phosphoserine1 Publication
Modified residuei248 – 2481Phosphoserine1 Publication

Post-translational modificationi

Proteolytically cleaved by caspase-3 during apoptosis.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8IZW8.
PaxDbiQ8IZW8.
PRIDEiQ8IZW8.

PTM databases

PhosphoSiteiQ8IZW8.

Miscellaneous databases

PMAP-CutDBQ8IZW8.

Expressioni

Tissue specificityi

Prostate and placenta. Down regulated in prostate cancer.1 Publication

Gene expression databases

BgeeiQ8IZW8.
CleanExiHS_TNS4.
GenevestigatoriQ8IZW8.

Organism-specific databases

HPAiHPA021913.

Interactioni

Subunit structurei

Binds to actin filaments and interacts with phosphotyrosine-containing proteins.By similarity

Protein-protein interaction databases

BioGridi124383. 5 interactions.
IntActiQ8IZW8. 6 interactions.
MINTiMINT-1493010.
STRINGi9606.ENSP00000254051.

Structurei

3D structure databases

ProteinModelPortaliQ8IZW8.
SMRiQ8IZW8. Positions 443-557, 580-709.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini449 – 556108SH2PROSITE-ProRule annotationAdd
BLAST
Domaini548 – 714167Phosphatase tensin-typeAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi168 – 324157Ser-richAdd
BLAST

Sequence similaritiesi

Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, Signal

Phylogenomic databases

eggNOGiNOG254290.
GeneTreeiENSGT00760000119113.
HOGENOMiHOG000230981.
HOVERGENiHBG080039.
InParanoidiQ8IZW8.
KOiK18080.
OMAiLNQMILE.
OrthoDBiEOG7QG43J.
PhylomeDBiQ8IZW8.
TreeFamiTF315996.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR013625. PTB.
IPR000980. SH2.
[Graphical view]
PfamiPF08416. PTB. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8IZW8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQVMSSPLL AGGHAVSLAP CDEPRRTLHP APSPSLPPQC SYYTTEGWGA
60 70 80 90 100
QALMAPVPCM GPPGRLQQAP QVEAKATCFL PSPGEKALGT PEDLDSYIDF
110 120 130 140 150
SLESLNQMIL ELDPTFQLLP PGTGGSQAEL AQSTMSMRKK EESEALDIKY
160 170 180 190 200
IEVTSARSRC HDGPQHCSSP SVTPPFGSLR SGGLLLSRDV PRETRSSSES
210 220 230 240 250
LIFSGNQGRG HQRPLPPSEG LSPRPPNSPS ISIPCMGSKA SSPHGLGSPL
260 270 280 290 300
VASPRLEKRL GGLAPQRGSR ISVLSASPVS DVSYMFGSSQ SLLHSSNSSH
310 320 330 340 350
QSSSRSLESP ANSSSSLHSL GSVSLCTRPS DFQAPRNPTL TMGQPRTPHS
360 370 380 390 400
PPLAKEHASS CPPSITNSMV DIPIVLINGC PEPGSSPPQR TPGHQNSVQP
410 420 430 440 450
GAASPSNPCP ATRSNSQTLS DAPFTTCPEG PARDMQPTMK FVMDTSKYWF
460 470 480 490 500
KPNITREQAI ELLRKEEPGA FVIRDSSSYR GSFGLALKVQ EVPASAQSRP
510 520 530 540 550
GEDSNDLIRH FLIESSAKGV HLKGADEEPY FGSLSAFVCQ HSIMALALPC
560 570 580 590 600
KLTIPQRELG GADGASDSTD SPASCQKKSA GCHTLYLSSV SVETLTGALA
610 620 630 640 650
VQKAISTTFE RDILPTPTVV HFKVTEQGIT LTDVQRKVFF RRHYPLTTLR
660 670 680 690 700
FCGMDPEQRK WQKYCKPSWI FGFVAKSQTE PQENVCHLFA EYDMVQPASQ
710
VIGLVTALLQ DAERM
Length:715
Mass (Da):76,764
Last modified:May 4, 2009 - v3
Checksum:iE6AD7CB6B6DDA5D2
GO

Sequence cautioni

The sequence AAQ15257.1 differs from that shown. Reason: Frameshift at positions 85, 296, 472 and 602. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti163 – 1631G → W in AAN32666 (PubMed:12154022).Curated
Sequence conflicti360 – 3601S → I in AAN32666 (PubMed:12154022).Curated
Sequence conflicti360 – 3601S → I in BAB55413 (PubMed:14702039).Curated
Sequence conflicti623 – 6231K → E in AAN32666 (PubMed:12154022).Curated
Sequence conflicti623 – 6231K → E in BAB55413 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti179 – 1791L → P.1 Publication
Corresponds to variant rs3764424 [ dbSNP | Ensembl ].
VAR_027264
Natural varianti327 – 3271T → K.
Corresponds to variant rs33923045 [ dbSNP | Ensembl ].
VAR_055292
Natural varianti498 – 4981S → N.2 Publications
Corresponds to variant rs2290207 [ dbSNP | Ensembl ].
VAR_027265
Natural varianti642 – 6421R → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036515

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF417488 mRNA. Translation: AAN32666.1.
AF370421 mRNA. Translation: AAQ15257.1. Frameshift.
AK027856 mRNA. Translation: BAB55413.1.
AC018629 Genomic DNA. No translation available.
BC018706 mRNA. Translation: AAH18706.1.
CCDSiCCDS11368.1.
RefSeqiNP_116254.4. NM_032865.5.
UniGeneiHs.438292.

Genome annotation databases

EnsembliENST00000254051; ENSP00000254051; ENSG00000131746.
GeneIDi84951.
KEGGihsa:84951.
UCSCiuc010cxb.3. human.

Polymorphism databases

DMDMi229463025.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF417488 mRNA. Translation: AAN32666.1.
AF370421 mRNA. Translation: AAQ15257.1. Frameshift.
AK027856 mRNA. Translation: BAB55413.1.
AC018629 Genomic DNA. No translation available.
BC018706 mRNA. Translation: AAH18706.1.
CCDSiCCDS11368.1.
RefSeqiNP_116254.4. NM_032865.5.
UniGeneiHs.438292.

3D structure databases

ProteinModelPortaliQ8IZW8.
SMRiQ8IZW8. Positions 443-557, 580-709.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124383. 5 interactions.
IntActiQ8IZW8. 6 interactions.
MINTiMINT-1493010.
STRINGi9606.ENSP00000254051.

PTM databases

PhosphoSiteiQ8IZW8.

Polymorphism databases

DMDMi229463025.

Proteomic databases

MaxQBiQ8IZW8.
PaxDbiQ8IZW8.
PRIDEiQ8IZW8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254051; ENSP00000254051; ENSG00000131746.
GeneIDi84951.
KEGGihsa:84951.
UCSCiuc010cxb.3. human.

Organism-specific databases

CTDi84951.
GeneCardsiGC17M038632.
H-InvDBHIX0013799.
HGNCiHGNC:24352. TNS4.
HPAiHPA021913.
MIMi608385. gene.
neXtProtiNX_Q8IZW8.
PharmGKBiPA142670717.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG254290.
GeneTreeiENSGT00760000119113.
HOGENOMiHOG000230981.
HOVERGENiHBG080039.
InParanoidiQ8IZW8.
KOiK18080.
OMAiLNQMILE.
OrthoDBiEOG7QG43J.
PhylomeDBiQ8IZW8.
TreeFamiTF315996.

Enzyme and pathway databases

SignaLinkiQ8IZW8.

Miscellaneous databases

ChiTaRSiTNS4. human.
GeneWikiiTNS4.
GenomeRNAii84951.
NextBioi75438.
PMAP-CutDBQ8IZW8.
PROiQ8IZW8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IZW8.
CleanExiHS_TNS4.
GenevestigatoriQ8IZW8.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR013625. PTB.
IPR000980. SH2.
[Graphical view]
PfamiPF08416. PTB. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cten, a COOH-terminal tensin-like protein with prostate restricted expression, is down-regulated in prostate cancer."
    Lo S.H., Lo T.B.
    Cancer Res. 62:4217-4221(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS PRO-179 AND ASN-498.
  2. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
    Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
    , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
    Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-498.
    Tissue: Placenta.
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "Cleavage of cten by caspase-3 during apoptosis."
    Lo S.-S., Lo S.H., Lo S.H.
    Oncogene 24:4311-4314(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY CASPASE-3, MUTAGENESIS OF ASP-506 AND ASP-570.
  7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-642.

Entry informationi

Entry nameiTENS4_HUMAN
AccessioniPrimary (citable) accession number: Q8IZW8
Secondary accession number(s): A6NMJ7
, Q71RB7, Q8WV64, Q96JV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 4, 2006
Last sequence update: May 4, 2009
Last modified: January 6, 2015
This is version 98 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 17
    Human chromosome 17: 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. 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.