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Q04205

- TENS_CHICK

UniProt

Q04205 - TENS_CHICK

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Protein

Tensin

Gene

TNS

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

May be involved in cell migration, fibrillar adhesion formation, cartilage development and in linking signal transduction pathways to the cytoskeleton.

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tensin
Gene namesi
Name:TNS
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: UniProtKB-KW
  2. cytoplasm Source: UniProtKB-KW
  3. cytoskeleton Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17441744TensinPRO_0000215901Add
BLAST

Post-translational modificationi

Tyrosine phosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ04205.

Expressioni

Tissue specificityi

Heart, gizzard, lung and skeletal muscle.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAR1P569452EBI-2607590,EBI-702093From a different organism.

Protein-protein interaction databases

DIPiDIP-56927N.
IntActiQ04205. 1 interaction.

Structurei

Secondary structure

1
1744
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1607 – 161913
Helixi1623 – 163513
Beta strandi1644 – 16518
Beta strandi1654 – 16629
Beta strandi1667 – 16715
Helixi1672 – 16743
Beta strandi1675 – 16806
Beta strandi1686 – 16883
Beta strandi1690 – 16934
Beta strandi1695 – 17039
Beta strandi1706 – 17094
Beta strandi1712 – 17198
Helixi1726 – 173712

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WVHX-ray1.50A1605-1738[»]
2GJYNMR-A1605-1744[»]
ProteinModelPortaliQ04205.
SMRiQ04205. Positions 1605-1744.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04205.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 230173Phosphatase tensin-typePROSITE-ProRule annotationAdd
BLAST
Domaini235 – 361127C2 tensin-typePROSITE-ProRule annotationAdd
BLAST
Domaini1472 – 1581110SH2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 C2 tensin-type domain.PROSITE-ProRule annotation
Contains 1 phosphatase tensin-type domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000060090.
HOVERGENiHBG060186.
InParanoidiQ04205.
KOiK18080.
PhylomeDBiQ04205.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000008. C2_dom.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR013625. PTB.
IPR006020. PTB/PI_dom.
IPR000980. SH2.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
[Graphical view]
PfamiPF08416. PTB. 1 hit.
PF10409. PTEN_C2. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04205-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDFGSVMNQA ATPCSPAVNY ELPSPGQSIT KQVDTPDATR SPRGGQAHCK
60 70 80 90 100
ASRSMSVTAA MESSCELDLV YITERIIAVS YPSTAEEQSF RSNLREVAHM
110 120 130 140 150
LKSKHGDNYV LFNLSERRHD ISKLHPKVLD FGWPDLHTPA LEKICSICKA
160 170 180 190 200
MDTWLNAAAH NVVVLHNKGN RGRLGVVVAA YMHYSNISAS ADQALDRFAM
210 220 230 240 250
KRFYEDKVVP VGQPSQKRYI HYFSGLLSGS IKMNNKPLFL HHVIMHGIPN
260 270 280 290 300
FESKGGCRPF LKIYQAMQPV YTSGIYNVQG DSQTGICITI EPGLLLKGDI
310 320 330 340 350
LLKCYHKKFR SPTRDVIFRV QFHTCAVHDL DIVFGKEDLD EAFRDERFPE
360 370 380 390 400
YGKVEFVFSY GPEKIQGMEH LENGPSVSVD YNTSDPLIRW DSYENFNIQR
410 420 430 440 450
EDSAEGTWAE PALPGKHLEK EVGHTQGPLD GSLYAKVKKK DSLHGSIGAV
460 470 480 490 500
NTARLPLSAA PNHVEHTLSV SSDSGNSTAS TKTDRTDEPG APGAPTGHAV
510 520 530 540 550
LSPEEKRDVD RLLVGFGLES AAPMHNHAPG PAPARLPAGP GRHVVPAQVH
560 570 580 590 600
VNGAGTPLLA ERETDILDDE LPNQDGHSVG SLGTLSSLDG TTTASEAGFH
610 620 630 640 650
EAPRVGSLSS LPNGPASYNG AEKMLKEGLY EAEPLSNGAY PYSNQNTLMG
660 670 680 690 700
HHLRDPLAHL RPSRSAQEHL AGYPQRQPAS ASPAWLQPPV PQPYLYGYDL
710 720 730 740 750
PSAHRSQSFP AVGTAKYEAN LALPQAPARS TSSREAVQRG LNSWQQQGGS
760 770 780 790 800
RPPSQLHDGG LESHSPSLSS CSPQPSPLQP MPPHSHSMPE FPRAPSRREI
810 820 830 840 850
EQSIEALDVL MLDLAPSVHK SQSVPSAATR QDKPAAMLSS LSAQRLSGHY
860 870 880 890 900
AQPTPQVVQP RSFGTSVGTD PLAKPYSPGP LVPAARSTAE PDYTVHEYRE
910 920 930 940 950
TYTPYSYQPV PEPRSYGSAP ASILPLSASY SPAGSQQLLV SSPPSPTAPA
960 970 980 990 1000
QSQLPHKGLE SYEDLSRSGE EPLNLEGLVA HRVAGVQSRE KSPEESTVPA
1010 1020 1030 1040 1050
RRRTPSDSHY EKSSPEPGSP RSPTVLSPEV VSTIAANPGG RPKEPHLHSY
1060 1070 1080 1090 1100
KEAFEEMESA SPSSLTSGGV RSPPGLAKTP LSALGLKPHN PADILLHPVG
1110 1120 1130 1140 1150
ELEGEAGADS EEEPRSYVES VARTATTGRA GNLPAAQPVG LEVPARNGAF
1160 1170 1180 1190 1200
GNSFTVPSPV STSSPIHSVD GASLRSYPSE GSPHGTVTPP HAVAETAYRS
1210 1220 1230 1240 1250
PMVSQTPSAH SSYQTSSPSS FQAGTLGSPY ASPDYPDGRG GFQPDPQARQ
1260 1270 1280 1290 1300
QPQVSVVGVH ALPGSPRTLH RTVATNTPPS PGFGRRAANP AVASVPGSPG
1310 1320 1330 1340 1350
LGRHTVSPHA PPGSPSLARH QMAAVPPGSP MYGYSSPEER RPTLSRQSSA
1360 1370 1380 1390 1400
SGYQPPSTPS FPVSPAYYPG TSTPHSSSPD SAAYRQGSPT PQPALPEKRR
1410 1420 1430 1440 1450
MSAGERSNSL PNYATVNGKA SSPLSSGMSS PSSGSAVAFS HTLPDFSKFS
1460 1470 1480 1490 1500
MPDISPETRA NVKFVQDTSK YWYKPDISRE QAIALLKDRE PGAFIIRDSH
1510 1520 1530 1540 1550
SFRGAYGLAM KVASPPPTVM QQNKKGDITN ELVRHFLIET SPRGVKLKGC
1560 1570 1580 1590 1600
PNEPNFGCLS ALVYQHSIMP LALPCKLVIP DRDPMEEKKD AASTTNSATD
1610 1620 1630 1640 1650
LLKQGAACNV LFINSVEMES LTGPQAISKA VAETLVADPT PTATIVHFKV
1660 1670 1680 1690 1700
SAQGITLTDN QRKLFFRRHY PLNTVTFCDL DPQERKWTKT DGSGPAKLFG
1710 1720 1730 1740
FVARKQGSTT DNVCHLFAEL DPDQPAAAIV NFVSRVMLGS GQKR
Length:1,744
Mass (Da):187,214
Last modified:November 1, 1997 - v2
Checksum:i5C3C8B6211935524
GO

Sequence cautioni

The sequence AAA73949.1 differs from that shown. Reason: Erroneous initiation.
The sequence CAA79215.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491C → R in AAA73949. (PubMed:7896874)Curated
Sequence conflicti49 – 491C → R in CAA79215. (PubMed:7896874)Curated
Sequence conflicti61 – 611M → T in AAA73949. (PubMed:7896874)Curated
Sequence conflicti61 – 611M → T in CAA79215. (PubMed:7896874)Curated
Sequence conflicti88 – 881Q → PR in AAA49087. 1 PublicationCurated
Sequence conflicti404 – 4041A → T in AAA73949. (PubMed:7896874)Curated
Sequence conflicti404 – 4041A → T in CAA79215. (PubMed:7896874)Curated
Sequence conflicti452 – 4521T → A in AAA73949. (PubMed:7896874)Curated
Sequence conflicti452 – 4521T → A in CAA79215. (PubMed:7896874)Curated
Sequence conflicti508 – 5092DV → EL in AAA73949. (PubMed:7896874)Curated
Sequence conflicti508 – 5092DV → EL in CAA79215. (PubMed:7896874)Curated
Sequence conflicti522 – 5221A → P in AAA73949. (PubMed:7896874)Curated
Sequence conflicti522 – 5221A → P in CAA79215. (PubMed:7896874)Curated
Sequence conflicti664 – 6641R → A(PubMed:7896874)Curated
Sequence conflicti666 – 6661A → T(PubMed:7896874)Curated
Sequence conflicti875 – 8751P → A in AAA73949. (PubMed:7896874)Curated
Sequence conflicti875 – 8751P → A in CAA79215. (PubMed:7896874)Curated
Sequence conflicti909 – 9091P → T in AAA73949. (PubMed:7896874)Curated
Sequence conflicti909 – 9091P → T in CAA79215. (PubMed:7896874)Curated
Sequence conflicti1102 – 111312Missing1 PublicationCuratedAdd
BLAST
Sequence conflicti1240 – 12401G → A in AAA73949. (PubMed:7896874)Curated
Sequence conflicti1240 – 12401G → A in CAA79215. (PubMed:7896874)Curated
Sequence conflicti1480 – 14801E → D in AAA73949. (PubMed:7896874)Curated
Sequence conflicti1480 – 14801E → D in CAA79215. (PubMed:7896874)Curated
Sequence conflicti1711 – 17111D → E in AAA73949. (PubMed:7896874)Curated
Sequence conflicti1711 – 17111D → E in CAA79215. (PubMed:7896874)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M96625 mRNA. Translation: AAA59053.1.
L06662 mRNA. Translation: AAA73949.1. Different initiation.
Z18529 mRNA. Translation: CAA79215.1. Different initiation.
M74165 mRNA. Translation: AAA49087.1.
X66286 mRNA. Translation: CAA46992.1.
PIRiA54970.
A57075.
S27939.
RefSeqiNP_990786.1. NM_205455.1.
UniGeneiGga.4128.

Genome annotation databases

GeneIDi396439.
KEGGigga:396439.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M96625 mRNA. Translation: AAA59053.1 .
L06662 mRNA. Translation: AAA73949.1 . Different initiation.
Z18529 mRNA. Translation: CAA79215.1 . Different initiation.
M74165 mRNA. Translation: AAA49087.1 .
X66286 mRNA. Translation: CAA46992.1 .
PIRi A54970.
A57075.
S27939.
RefSeqi NP_990786.1. NM_205455.1.
UniGenei Gga.4128.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WVH X-ray 1.50 A 1605-1738 [» ]
2GJY NMR - A 1605-1744 [» ]
ProteinModelPortali Q04205.
SMRi Q04205. Positions 1605-1744.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-56927N.
IntActi Q04205. 1 interaction.

Proteomic databases

PaxDbi Q04205.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396439.
KEGGi gga:396439.

Organism-specific databases

CTDi 7145.

Phylogenomic databases

eggNOGi COG2453.
HOGENOMi HOG000060090.
HOVERGENi HBG060186.
InParanoidi Q04205.
KOi K18080.
PhylomeDBi Q04205.

Miscellaneous databases

EvolutionaryTracei Q04205.
NextBioi 20816480.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR000008. C2_dom.
IPR011993. PH_like_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR013625. PTB.
IPR006020. PTB/PI_dom.
IPR000980. SH2.
IPR014020. Tensin_C2-dom.
IPR029023. Tensin_lipid_phosphatase_dom.
[Graphical view ]
Pfami PF08416. PTB. 1 hit.
PF10409. PTEN_C2. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view ]
SMARTi SM00462. PTB. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of chick cardiac muscle tensin. Full-length cDNA sequence, expression, and characterization."
    Lo S.H., An Q., Bao S., Wong W.K., Liu Y., Janmey P.A., Hartwig J.H., Chen L.B.
    J. Biol. Chem. 269:22310-22319(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  2. "Molecular cloning, expression, and mapping of the high affinity actin-capping domain of chicken cardiac tensin."
    Chuang J.Z., Lin D.C., Lin S.
    J. Cell Biol. 128:1095-1109(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  3. Chen L.B.
    Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Modulation of tensin and vimentin expression in chick embryo developing cartilage and cultured differentiating chondrocytes."
    van de Werken R., Gennari M., Tavella S., Bet P., Molina F., Lin S., Cancedda R., Castagnola P.
    Eur. J. Biochem. 217:781-790(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1469-1744.
    Tissue: Embryonic chondrocyte and Embryonic heart.
  5. "Presence of an SH2 domain in the actin-binding protein tensin."
    Davis S., Lu M.L., Lo S.H., Lin S., Butler J.A., Druker B.J., Roberts T.M., An Q., Chen L.B.
    Science 252:712-715(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN SH2.

Entry informationi

Entry nameiTENS_CHICK
AccessioniPrimary (citable) accession number: Q04205
Secondary accession number(s): Q91007, Q92011
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3