Tumor Endothelial Marker Report: TEM24 (tensin)

TEM domain structure

	TEM domain structure

TEM Sequence Analysis

name from to source/E description

ABD-I 1 209 The homologous region is described as an actin binding domain in chicken tensin (proposed by similarity from chicken tensin - Lo, 1994).

ABD-II 210 395 The homologous region is described as an actin binding domain in chicken tensin (proposed by similarity from chicken tensin - Lo, 1994).

PTP II 53 167 SCOP-DB, E = 1e-09
SMART, E = 8.26e-03 (Phosphotyrosine) protein phosphatases II. The first 300aa show homology to PTEN (33%) in its phosphatase domain. PTEN is very active on highly acidic substrats, while otherwise being an inefficient protein phosphatase. PTEN specificity has been attributed to the fact that the catalytic side is surrounded by positively charged amino acids in the catlytic site (K125, K128, H93) which are partially conserved in tensin (K114, R117), opening up the posibility for a conservation in specificity.

unknown 395 1462 The central region of the protein (461-1445) is heavily interspersed by LCRs.

461 494 SEG25 LCR(SG)

630 710 SEG25 LCR(QP)

719 774 SEG25 LCR(AS), apolar:733-53/ toppred2=0.7

ABD-III 792 882 The homologous region is described as an actin binding domain in chicken tensin (proposed by similarity from chicken tensin - Lo, 1994).

813 874 SEG25 LCR(PS), apolar:813-33/ toppred2=0.8

877 915 SEG25 LCR(ERQ)

957 986 SEG25 LCR(P)

1066 1166 SEG25 LCR(S), apolar:1064-84/ toppred2=1.2

1201 1243 SEG25 LCR(PS), apolar:1214-34/ toppred2=0.6

1265 1313 SEG25 LCR(PG)

1320 1385 SEG25 LCR(SP), apolar:1346-66/ toppred2=0.9

1397 1442 SEG25 LCR(SP), apolar:1412-32/ toppred2=1.1

SH2 1462 1573 Pfam, E = 1.6e-14 SH2 domains function as regulatory modules of intracellular signalling cascades by interacting with high affinity to phosphotyrosine-containing target peptides in a sequence-specific and strictly phosphorylation-dependent manner.

PTB 1600 1734 Aravind SDB, E = 3e-18 It has been previously proposed that subunit self-association occurs via this C-terminal region as it is the case for other actin cross-linking proteins (with the N-terminus being involved in actin-binding).

1734

	TEM Sequence Analysis

name	from	to	source/E	description
ABD-I	1	209		The homologous region is described as an actin binding domain in chicken tensin (proposed by similarity from chicken tensin - Lo, 1994).
ABD-II	210	395		The homologous region is described as an actin binding domain in chicken tensin (proposed by similarity from chicken tensin - Lo, 1994).
PTP II	53	167	SCOP-DB, E = 1e-09 SMART, E = 8.26e-03	(Phosphotyrosine) protein phosphatases II. The first 300aa show homology to PTEN (33%) in its phosphatase domain. PTEN is very active on highly acidic substrats, while otherwise being an inefficient protein phosphatase. PTEN specificity has been attributed to the fact that the catalytic side is surrounded by positively charged amino acids in the catlytic site (K125, K128, H93) which are partially conserved in tensin (K114, R117), opening up the posibility for a conservation in specificity.
unknown	395	1462		The central region of the protein (461-1445) is heavily interspersed by LCRs.
	461	494	SEG25	LCR(SG)
	630	710	SEG25	LCR(QP)
	719	774	SEG25	LCR(AS), apolar:733-53/ toppred2=0.7
ABD-III	792	882		The homologous region is described as an actin binding domain in chicken tensin (proposed by similarity from chicken tensin - Lo, 1994).
	813	874	SEG25	LCR(PS), apolar:813-33/ toppred2=0.8
	877	915	SEG25	LCR(ERQ)
	957	986	SEG25	LCR(P)
	1066	1166	SEG25	LCR(S), apolar:1064-84/ toppred2=1.2
	1201	1243	SEG25	LCR(PS), apolar:1214-34/ toppred2=0.6
	1265	1313	SEG25	LCR(PG)
	1320	1385	SEG25	LCR(SP), apolar:1346-66/ toppred2=0.9
	1397	1442	SEG25	LCR(SP), apolar:1412-32/ toppred2=1.1
SH2	1462	1573	Pfam, E = 1.6e-14	SH2 domains function as regulatory modules of intracellular signalling cascades by interacting with high affinity to phosphotyrosine-containing target peptides in a sequence-specific and strictly phosphorylation-dependent manner.
PTB	1600	1734	Aravind SDB, E = 3e-18	It has been previously proposed that subunit self-association occurs via this C-terminal region as it is the case for other actin cross-linking proteins (with the N-terminus being involved in actin-binding).
1734

Remarks

	Remarks

HOMOLOGUES: The overall sequence similarity between chicken and human tensin is 60%. The central region of the protein is LCR-rich and less conserved (down to 40% identity), while the identity increases above 80% close to the N- and C-termini.
DOMAIN ARCHITECTURE: The N-terminal (1-460) and C-terminal (1403-1735) regions contain known domains: PTPII in the N-terminus, SH2 and PTB in the C-terminus. These regions are devoid of LCRs (SEG25), while the central region is heavily interspersed by LCRs.
Three regions with actin binding activity can be proposed by similarity to chicken tensin:
- ABD-I ranging from 1 to 209, binds the side of F-actin. Due to the 55aa shorter N-terminus in human tensin there are 55aa missing compared to the chicken ABD-I. This region shows 87% identity to chicken tensin.
- ABD-II ranging from 210 to 395, binds the side of F-actin. This region shows 80% identity to chicken tensin.
- ABD-III ranging from 792 to 882, binds the side of barbed ends of actin-filaments. This region shows 48% identity to chicken tensin, and contains a PS-LCR in which the conservation is weak. Note that the region ranging from 767 to 1136 is homologous (51% identical) to insertin (12-346) a proposed proteolytic fragment of tensin found to retard actin assembly at high ratios.
LOCALIZATION: Tensin has been shown to be associated with the cytoskeleton. Effects on the cytoskeleton may have an important role in regulating cell growth by controlling spreading and shape change at the cell surface.
FUNCTION: MOSTLY DERIVED FROM CHICKEN TENSIN: Tensin/TEM24 is proposed to harbor an integrative function for signal transductions with the cytoskeleton. It localizes to the focal adhesion where it binds both actin filaments and tyrosine-phosphorylated proteins, potentially providing a nucleus around which signalling complexes can assemble.
   The focal adhesion is a structure that is formed when a cell comes into contact with the extracellular matrix. Various protein components of the focal adhesion are linked to signal transduction pathways eg. the catalytically active p125FAK, SH2-containing tensin, and the multifunctional LIM domain-containing paxillin. pp125FAK, paxillin and tensin show increased tyrosine phosphorylation upon adhesion of cells to the extracellular matrix.
   Tensin contains N-terminally a phosphatase domain embedded within an actin-binding motif. The protein phosphatase domain has similarity to dual specificity phosphatases. Dual specificity phosphatases act both on serine/threonine and tyrosine phosphotyrosine residues. Despite its homology with dual-specificity PTEN is an inefficient protein phosphatase in vitro, being very active on highly acidic substrats. Its specificity for acidic substrats like PIP-3 has been attributed to the fact that the catalytic side is surrounded by positively charged amino acids, which are partially conserved in tensins. Recently it has been suggested that PTEN might interact and dephosphorylate FAK and Shc.
   The targets of the SH2 domain of PTEN have been localized specifically to the focal adhesions (while GRB2, GAP, PLC-g SH2 domains do not), consistent with the fact that many phosphorylated tyrosine-containing proteins are concentrated at focal adhesions. PI 3 kinase activity associated with the SH2 domain of chicken tensin and the optimal phosphopeptide binding specificity of the SH2 domain of tensin was determined to be phospho-Y (E or D) , N, (I, V, or F).
   Tensin is phosphorylated on serine, threonine, tyrosine. It has been shown that tyrosine kinases Src, FAK, EGFR and serin-threonine kinases cdc 2 kinase and protein kinase C phosphorylate chicken tensin in vitro. It is hypothesized that tensin could as well provide binding sites for other SH2-containing proteins.
REMARKS: 89% of the Unigen SAGE libraries that show expression of the TEM24 tag (AGACATACTG), show expression of the TEM5 tag (TATTAACTCT) as well.

Sequence Information

TEM TEM24

Reliability of Gen2Tag mapping

Cid->tag (Hs.59378) frequency:
tem24: CATG-AGACATACTG=3/4 (cDNA)
tem24: CATG-AGACATACTG=11/11 (ESTS oriented)

Analysis
BlastP against nr

Output Created by a Suite of Single Sequence Analysis Techniques

Protein Description

SEQ.SOURCE: gi|11275669|gb|AAG33700.1| tensin [Homo sapiens]

Protein Sequence

MSVSRTMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKL HAKVLEFGWPDLHTPALEKICSICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQA LDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGLLSGSIKINNKPLFLHHVIMHGIPNFESKGGCRPFLRIY QAMQPVYTSGIYNIPGDSQTSVCITIEPGLLLKGDILLKCYHKKFRSPARDVIFRVQFHTCAIHDLGVVF GKEDLDDAFKDDRFPEYGKVEFVFSYGPEKIQGMEHLENGPSVSVDYNTSDPLIRWDSYDNFSGHRDDGM EEVVGHTQGPLDGSLYAKVKKKDSLHGSTGAVNATRPTLSATPNHVEHTLSVSSDSGNSTASTKTDKTDE PVPGASSATAALSPQEKRELDRLLSGFGLEREKQGAMYHTQHLRSRPAGGSAVPSSGRHVVPAQVHVNGG ALASERETDILDDELPNQDGHSAGSMGTLSSLDGVTNTSEGGYPEALSPLTNGLDKSYPMEPMVNGGGYP YESASRAGPAHAGHTAPMRPSYSAQEGLAGYQREGPHPAWPQPVTTSHYAHDPSGMFRSQSFSEAEPQLP PAPVRGGSSREAVQRGLNSWQQQQQQQQQPRPPPRQQERAHLESLVASRPSPQPLAETPIPSLPEFPRAA SQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLSGSSRQSHPLTQSRSGYIPSG HSLGTPEPAPRASLESVPPGRSYSPYDYQPCLAGPNQDFHSKSPASSSLPAFLPTTHSPPGPQQPPASLP GLTAQPLLSPKEATSDPSRTPEEEPLNLEGLVAHRVAGVQAREKQPAEPPAPLRRRAASDGQYENQSPEA TSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLHSYKEAFEEMEGTSPSSPPPSGVRSPPGLAKTPL SALGLKPHNPADILLHPTGVTRRRIQPEEDEGKVVVRLSEEPRSYVESVARTAVAGPRAQDSEPKSFSAP ATQAYGHEIPLRNGTLGGSFVSPSPLSTSSPILSADSTSVGSFPSGESSDQGPRTPTQPLLESGFRSGSL GQPSPSAQRNYQSSSPLPTVGSSYSSPDYSLQHFSSSPESQARAQFSVAGVHTVPGSPQARHRTVGTNTP PSPGFGRRAINPSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSPQSSAATTPGSPSLCRHPAGVYQVSGLH NKVATTPGSPSLGRHPGAHQGNLASGLHSNAIASPGSPSLGRHLGGSGSVVPGSPCLDRHVAYGGYSTPE DRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEKRRMSVGDRAGS LPNYATINGKVASPVPSGMSSPSGGSTVSFSHTLPDFSKYSMPDNSPETRAKVKFVQDTSKYWYKPEISR EQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTIMQQNKKGDMTHELVRHFLIETGPRGVKLKG CPNEPNFGSLSALVYQHSIIPLALPCKLVIPNRDPTDESKDSSGPANSTADLLKQGAACNVLFINSVDME SLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQERKWMK TEGGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVMLNAGQKR

SAGE-Tag CATG-AGACATACTGA

EST/cluster Description

UNIGEN CLUSTER: Hs.59378 : DKFZP434G162 protein

SEQ.SOURCE: gi|11275668|gb|AF225896.1|AF225896 Homo sapiens tensin mRNA and
gi|5912066|emb|AL117537.1|HSM801062 Homo sapiens mRNA; cDNA DKFZp434G162

EST/cluster Sequence

CAATCCTTTAACGAGGATCCATTGGAGGGCAAGTCTGGTGCCAGCAGCCGCGGTAATTCCAGCTCCAATA GCGTATATTAAAGTTGCTGCAGTTAAAAAGCTCGTAGTTGGATCTTGGGAGCGGGCGGGCGGTCCGCCGC GAGGCGAGCCACCGCCCGTCCCCGCCCCTTGCCTCTCGGCGCCCCCTCGATGCTCTTAGCTGAGTGTCCC GCGGGGCCCGAAGCGTTTACTTTGAAAAAATTAGAGTGTTCAAAGCAGGCCCGAGCCGCCTGGATACCGC AGCTAGGAATAATGGAATAGGACCGCGGTTCTATTTTGTTGGTTTTCGGAACTGAGGCCATGATTAAGAG GGACGGCCGGGGGCATTCGTATTGCGCCGCTAGAGGTGAAATTCTTGGACCGGCGCAAGACGGACCAGAG CGAAAGCATTTGCCAAGAATGTTTTCATTAATCAAGAACGAAAGTCGGAGGTTCGAAGACGATCAGATAC CGTCGTAGTTCCGACCATAAACGATGCCGACCGGGCATGCGGCGGCGTTATTCCCATGACCCGCCGGCAG CTTCCGGGAAACCAAAGTCTTTGGGTTCCGGGGGGAGTATGGTTGCAAAGCTGAAACTTAAAGGAATTGA CGGAAGGGCACCACCAGGAGTGGAGCCTGGCGGCTTAATTTGACCCAACACGGGAAACCTCACCCGGCCC GGACACGGACAGGATTGACAGATTGACAGCTCTTTCTCGATTCCGTGGGTGGTGGTGCATGGCCGTTCTT AGTTGGTGGAGCGATTTGTCTGGTTAATTCCGATAACGAACGAGACTCTGGCATGCTAACTAGTTACGCG ACCCCCGAGCGGTCGGCGTCCCCCAACTTCTTAGAGGGACAAGTGGCGTTCAGCCACCCGAGATTGAGCA ATAACAGGTCTGTGATGCCCTTAGATGTCCGGGGCTGCACGCGCGCTACACTGACTGGCTCAGCGTGTGC CTACCCTACGCCGGCAGGCGCGGGTAACCCGTTGAACCCCATTCGTGATGGGGATCGGGGATTGCAATTA TTCCCCATGAACGAGGAATTCCCAGTAAGTGCGGGTCATAAGCTTGCGTTGATTAAGTCCCTGCCCTTTG TACACACCGCCCGTCGCTACTACCGATTGGATGGTTTAGTGAGGCCCGGATAACATGGAAATAATTTGAA CAGGAAAATATTACTCCACCCAGAAATCCAAGAACTGGAAGGATCTTCAATTTTATTTCTAGAATAGGAA TCGTATAGTCCCACATTGTTGCTCCTCCAAATGCAGACAACACAAAGACAATCACTAAAGCTATCTGAAT TTCAGTTACATCCACTTTTCCAAATCTCAACATGCCTGAAACATAAGTCTGCCAATGAGCGCAATAAAAC ACAAACATCGGAATTCCGGGTCCTCCCCCGCCCCCCCCCCCCACGCCTCCTCCCCTCCTCCCGCCCTCAT CTCTCTCCCCACCCCCGGAGCCCCGCGACGCTACGCCGCGACGAGTAGGAGGGCCGCTGCGGTGAGCCTT GAAGCCTAGGGCGCGGGCCCGGGTGGAGCCGCCGCAGGTGCAGATCTTGGTGGTAGTAGCAAATATTCAA ACGAGAACTTTGAAGGGGAATTCCCCACTGCTCCTTGCACCCCGCTCCCTGCCTGGACACAGGCTCACTC GCTGCCTTCTTCTGGGGGAAACCAGCTTCTTGCCAGCCACAGCTGCTGCCTCCGCCACTGGCCACCGCCC CTGTCCTGGGAGTCCCTTGGCCCAGACACCCACCTGACTTAGTGGCTCCTCTGCAGGAAAGGTGGCTGCC CCCTGCGTTCCTCCATCCAACCATGAGCTGGTGCCCATCACCACTGAGAATGCACCAAAGAATGTAGTGG ACAAGGGAGAAGGAGCCTCCCGGGGTGGAAACACACGGAAAAGCCTCGAGGACAACGGCTCCACCAGGGT CACCCCGAGTGTCCAGCCCCACCTCCAGCCCATCAGAAACATGAGTGTGAGCCGGACCATGGAGGACAGC TGTGAGCTGGACCTGGTGTACGTCACAGAGAGGATCATCGCTGTCTCCTTCCCCAGCACAGCCAATGAGG AGAACTTCCGGAGCAACCTCCGTGAGGTGGCGCAGATGCTCAAGTCCAAACATGGAGGCAACTACCTGCT GTTCAACCTCTCTGAGCGGAGACCTGACATCACGAAGCTCCATGCCAAGGTACTGGAATTTGGCTGGCCC GACCTCCACACCCCAGCCCTGGAGAAGATCTGCAGCATCTGTAAGGCCATGGACACATGGCTCAATGCAG ACCCTCACAATGTCGTTGTTCTACACAACAAGGGAAACCGAGGCAGGATAGGAGTTGTCATCGCGGCTTA CATGCACTACAGCAACATTTCTGCCAGTGCGGACCAGGCTCTGGACCGGTTTGCAATGAAGCGGTTCTAT GAGGATAAGATTGTGCCCATTGGCCAGCCATCCCAAAGAAGGTACGTGCATTACTTCAGTGGCCTGCTCT CCGGCTCCATCAAAATAAACAACAAGCCCTTGTTTCTGCACCACGTGATCATGCACGGCATCCCCAACTT TGAGTCTAAAGGAGGATGTCGGCCATTTCTCCGCATCTACCAGGCCATGCAACCTGTGTACACATCTGGC ATCTACAACATCCCAGGAGACAGCCAGACTAGCGTCTGCATCACCATCGAGCCAGGACTGCTCTTGAAGG GAGACATCTTGCTGAAGTGCTACCACAAGAAGTTCCGAAGCCCAGCCCGAGACGTCATCTTCCGTGTGCA GTTCCACACCTGTGCCATCCATGACCTGGGGGTTGTCTTTGGGAAGGAGGACCTTGATGATGCTTTCAAA GATGATCGATTTCCAGAGTATGGCAAAGTGGAGTTTGTATTTTCTTATGGGCCAGAGAAAATTCAAGGCA TGGAGCACCTGGAGAACGGGCCGAGCGTGTCTGTGGACTATAACACCTCTGACCCCCTCATCCGCTGGGA CTCCTACGACAACTTCAGTGGGCATCGAGATGACGGCATGGAGGAGGTGGTGGGACACACGCAGGGGCCA CTAGATGGGAGCCTGTATGCTAAGGTGAAGAAGAAAGACTCCCTGCACGGCAGCACCGGGGCTGTTAATG CCACACGTCCTACACTGTCGGCCACCCCCAACCACGTGGAACACACGCTTTCTGTGAGCAGCGACTCGGG CAACTCCACAGCCTCCACCAAGACCGACAAGACCGACGAGCCTGTCCCCGGGGCCTCCAGTGCCACTGCT GCCTTGAGTCCCCAGGAGAAGCGGGAGCTGGACCGCCTGCTGAGTGGCTTTGGCTTAGAGCGAGAGAAGC AAGGCGCCATGTACCACACCCAGCACCTCAGGTCCCGCCCAGCAGGGGGCTCGGCTGTGCCCTCCTCTGG ACGCCACGTTGTCCCAGCCCAGGTTCATGTCAATGGTGGGGCGTTAGCATCTGAGCGGGAGACAGACATC CTGGACGATGAATTGCCAAACCAGGATGGTCACAGTGCGGGCAGCATGGGCACACTCTCTTCTCTGGACG GGGTCACCAACACCAGTGAGGGGGGCTACCCAGAGGCCCTGTCCCCACTGACCAACGGTCTGGACAAGTC CTACCCCATGGAGCCTATGGTCAATGGAGGAGGCTACCCCTACGAGTCTGCCAGCCGGGCGGGGCCTGCC CATGCTGGCCACACGGCCCCCATGCGGCCCTCCTACTCTGCACAGGAGGGTTTAGCTGGCTACCAGAGGG AGGGGCCCCACCCAGCCTGGCCACAGCCAGTGACCACCTCCCACTATGCCCATGACCCCAGCGGTATGTT CCGCTCTCAATCCTTTTCGGAAGCTGAACCCCAGCTGCCCCCAGCTCCGGTCCGAGGGGGAAGCAGCCGG GAGGCTGTGCAAAGGGGACTGAATTCGTGGCAGCAGCAGCAGCAGCAGCAGCAGCAGCCTCGCCCACCTC CACGCCAGCAGGAAAGAGCCCACTTGGAGAGTCTTGTAGCCAGCAGGCCCAGCCCTCAGCCATTGGCAGA GACCCCCATCCCCAGTCTCCCTGAGTTCCCGCGAGCAGCCTCCCAGCAGGAGATTGAACAGTCCATCGAA ACACTCAATATGCTGATGCTGGACCTGGAGCCAGCCTCCGCTGCTGCCCCACTACACAAGTCCCAGAGTG TCCCCGGGGCCTGGCCAGGGGCTTCTCCACTCTCCTCCCAGCCCCTCTCTGGATCCTCCCGTCAGTCCCA TCCACTGACCCAGTCCAGATCTGGCTATATCCCCAGTGGGCATTCGTTGGGAACCCCTGAGCCAGCCCCA CGGGCCTCTCTGGAGTCTGTCCCTCCTGGCAGGTCTTACTCACCTTATGACTATCAGCCATGTTTGGCTG GGCCTAACCAGGATTTCCATTCAAAGAGCCCAGCCTCTTCCTCCTTGCCTGCCTTCCTTCCGACCACCCA CAGCCCTCCAGGGCCTCAGCAACCCCCAGCCTCTCTCCCTGGCCTCACTGCTCAGCCTCTGCTCTCACCA AAGGAAGCGACTTCAGACCCCTCCCGGACTCCAGAGGAGGAGCCATTGAATTTAGAAGGGCTGGTGGCCC ACAGGGTAGCAGGGGTACAGGCTCGGGAGAAGCAGCCTGCAGAGCCCCCAGCCCCTCTGCGGAGGCGGGC GGCCAGTGATGGACAGTATGAGAACCAGTCTCCAGAAGCCACATCCCCTCGTAGCCCTGGGGTTCGCTCC CCTGTCCAGTGTGTCTCCCCGGAGCTGGCTCTTACCATCGCTCTCAATCCTGGAGGGCGGCCCAAAGAGC CCCATTTGCACAGCTACAAGGAGGCCTTCGAGGAGATGGAGGGAACCTCCCCGAGCAGCCCACCACCCAG TGGGGTGCGGTCCCCCCCGGGTCTGGCCAAGACACCCCTGTCTGCTCTGGGCCTGAAACCTCACAACCCA GCGGACATCCTGTTGCACCCCACAGGAGTTACCAGAAGACGGATCCAGCCAGAGGAAGATGAGGGGAAGG TGGTGGTCAGGCTGTCAGAAGAGCCCCGGAGCTATGTGGAGTCTGTGGCACGGACAGCGGTGGCTGGACC CCGAGCTCAGGACTCTGAGCCCAAGAGCTTTAGTGCTCCAGCCACCCAGGCCTATGGCCATGAGATACCC CTGAGGAACGGGACCCTGGGTGGCTCCTTTGTCTCCCCCAGCCCCCTCTCCACCAGCAGCCCCATCCTCA GTGCTGACAGCACTTCAGTGGGGAGTTTCCCGTCGGGAGAGAGCAGTGACCAGGGTCCCCGGACGCCCAC CCAGCCTCTGTTGGAGTCTGGCTTCCGCTCAGGCAGCCTGGGACAGCCCAGCCCATCTGCCCAGAGAAAC TACCAGAGCTCTTCTCCTCTCCCGACTGTGGGCAGTAGCTACAGCAGCCCCGACTACTCACTTCAGCATT TCAGCTCCTCTCCGGAAAGCCAGGCCCGAGCTCAGTTCAGTGTGGCTGGCGTCCACACGGTGCCTGGGAG CCCTCAGGCGCGCCACAGAACAGTGGGCACCAACACTCCCCCTAGTCCTGGCTTCGGCCGGCGGGCCATC AATCCCAGCATGGCTGCCCCCAGCAGTCCCAGTTTGAGCCATCACCAGATGATGGGTCCACCAGGCACTG GCTTCCATGGTAGCACTGTCTCCAGCCCCCAGAGCAGTGCAGCGACCACCCCGGGGAGCCCCAGCCTGTG TCGGCACCCAGCAGGGGTCTACCAGGTTTCTGGCCTCCACAACAAAGTGGCCACCACCCCGGGGAGTCCC AGCCTGGGCCGGCACCCTGGGGCTCACCAAGGCAACCTGGCCTCCGGTCTTCATAGCAATGCAATAGCCA GCCCTGGAAGCCCCAGCCTGGGCCGTCACCTCGGAGGGTCTGGATCTGTGGTTCCCGGCAGCCCCTGCTT GGACCGGCATGTGGCCTATGGCGGCTATTCTACCCCGGAGGATCGGAGACCCACACTGTCCCGGCAGAGC AGTGCCTCTGGCTACCAGGCTCCTTCCACGCCCTCCTTCCCTGTCTCCCCTGCCTACTACCCTGGCCTGA GCAGCCCTGCCACCTCCCCGTCACCAGACTCCGCAGCCTTCCGGCAAGGGAGCCCAACACCAGCCTTGCC AGAGAAGCGAAGGATGTCAGTGGGAGACCGGGCAGGCAGCCTCCCCAACTATGCCACCATCAATGGGAAG GTTGCTTCGCCTGTGCCCAGCGGCATGTCCAGTCCCAGCGGGGGCAGCACCGTCTCCTTCTCCCACACTC TGCCCGACTTCTCCAAGTACTCCATGCCAGACAACAGCCCGGAGACGCGGGCTAAAGTGAAGTTTGTCCA GGACACTTCTAAGTATTGGTACAAGCCTGAGATCTCCAGGGAGCAGGCCATCGCGCTCCTCAAGGACCAG GAGCCGGGGGCCTTCATCATCCGCGACAGTCACTCCTTCCGAGGCGCGTACGGGCTGGCCATGAAGGTGT CTTCGCCACCTCCAACCATCATGCAGCAGAATAAAAAAGGAGACATGACCCATGAGCTGGTCAGGCATTT TCTGATAGAGACTGGCCCCAGAGGAGTCAAGCTCAAGGGCTGCCCCAATGAGCCAAACTTCGGATCGCTG TCTGCCCTGGTCTACCAGCACTCCATCATCCCATTGGCCCTGCCTTGCAAGCTGGTCATTCCAAACCGAG ACCCCACAGATGAATCGAAAGATAGCTCCGGCCCTGCCAACTCAACTGCAGACCTGCTGAAACAAGGGGC AGCCTGCAATGTGCTCTTCGTCAACTCTGTGGACATGGAGTCACTCACTGGGCCACAGGCCATCTCTAAA GCCACATCTGAGACGTTGGCTGCAGACCCCACGCCAGCTGCCACCATCGTTCACTTCAAAGTCTCTGCCC AGGGAATCACTCTGACTGACAACCAGAGAAAGCTCTTTTTCAGACGCCACTACCCTCTCAACACTGTCAC CTTCTGTGACCTGGATCCACAGGAAAGAAAGTGGATGAAAACAGAGGGTGGTGCCCCTGCTAAGCTCTTC GGCTTCGTGGCCCGGAAGCAGGGCAGCACCACGGACAACGCCTGCCACCTCTTTGCTGAGCTTGACCCCA ACCAGCCGGCCTCTGCCATCGTCAACTTCGTCTCCAAGGTCATGCTGAATGCCGGCCAAAAGAGATGAAC CCTGCCCCTTGCCCAGGGCCAGTGCCATGGGGAAGGGGCTTGTGGGGAGGGGACCCATGAATCCTGACCA CTCTTGAACCCAGAAGGAGGACTTTGGGCCAATTTCGGAGGAGAGAAGAAAGTGCAACGTGGGGAGAGGG AAGTGAATTGCAGAGGGGAGGGGGAAAAGAGAGAGAGAGAGAGAGAGAGAGAGAGAGAGAAAGATGGAGG AGAAGAACTTGGATTCCCCTGGGTAGATGGAAACTGCAAAAACCCAAAGCCTCCAAAACTAACCAGGTCC ACCTAACACCCCCTCCCTCCCCTAAGAAGATGGATGTCCTCAAAAGAGAAGGAACAAACCTCCTTGGGAA TCCACATTTTTTGGGGGAATGGAAAAGCTCTGTCTCCCTAACTCAACTGCTTTGCAAGGGGAAATCAAGC TGGGAGAATCTTTTTCTGGCCACCTGTGGGGTAGGTTGTCAAACCAAACAGAGCCACCGTGGGACATCAA GTGGAAGAACTTGTTTGCTTGAAAGTATCTCAGACCCAAGGCACCTCAGGTCTCTTTGCTGTGCCTCCAC TATATTGTCGTGTGGGTGTGTGTCTGCACCCACATCCTCACACATTGATCTAGATCTGCCTTTATCCACT CGAATTATAAACAGCTCGGCTTGTCCTTGTCCCATGTGTTTGTAGACACACATGCATACTGTCCAAAGAT TAGGGTTGGTGGTGGCAGTGCAGCAGGGGAGGGACAAACAACCAAGCTATGGGTGACAGAGGCTCTCTCC TGGTGCCTGCACCTGCACTCTAGTGACCCTGGGTGCCGCCAGACCCTTCTCTTCTACAAAGACCCCAGCA GGAGTGGGAGGGTCTGCAATGGCATCGCCCTGTCCTGCCTTGGCCAGAAGCCTGGAGCTTTGGTTTGAGG AGGTAGAGATATGTGTATCCATAGGAAGAGATCTGTCAGAACAGGCAGCTGTTGAGCTCGGGGTGTCTTC CCCAAGGCATGTGGCTCAGCAGCAAGAAAGGCAAGTTGCTCCTGCTGGGGCCCTGGACTCTGCCTTAGCT CCCACCTCTCAGCCTTGTTATTGGGTTTCATGCCCCTGGACCAGCCTTATCTCAGACCTGCTTACCTGCA TGATGCCTTTTTGGGGGCTGGGGATTGAGTCTTGCTGCTCTGCCCAGCCCTGTTCTATTCTGCAGGGTCC CTGTGTTGGAATTCTCCCTGGGGAACCTACTTTCTGCTCAGTGAGGCTCCGGCCAGAAACCTGGAGTCCT TATCCTCCCCTCTGTAAGTGTTTTAGGGTCTGGCTTTTGCAGGCACCCTCTGACCTCAGCAGAGCTCCTG GGCCTGCTGCCTGCACACCACATCGCCTACCTACAATGCCAAAGCCTCACTGTCACCCTTTCTGCCTTGG TTTCCCTAGCTGAGCCACGCTGCCCATGCAGCAGAGGGCAGAAGGCTTGCACTTGGGCCAAAGGGCCTAA GGTCCACTGGACAGTTGGGAAAACACCTGACCACCATTTAAGGACTCTAAGCCAGAATGGAAAATTCACC AGGACTCCATTCTTAAGCCTATGCGAGTCCCCTAGAGAGAGGCATTGTACTGATATATAAATATTATATA ATATATACATGAGACATACTGACAGAATCTGTAAGCTAATAAAATGTAAGAAAAGGTTAAAAAAAGAAAA AAAAAAAA

Genomic Sequence Description

Genomic Sequence

	Sequence Information

Literature

	Literature

PubMed: 11023826 Molecular characterization of human tensin.
Chen H, Ishii A, Wong WK, Chen LB, Lo SH.
Biochem J. 2000 Oct 15;351 Pt 2:403-11.

PubMed: 10860821 Tensin can induce JNK and p38 activation.
Katz BZ, Zohar M, Teramoto H, Matsumoto K, Gutkind JS, Lin DC, Lin S, Yamada KM.
Biochem Biophys Res Commun. 2000 Jun 16;272(3):717-20.

PubMed: 10704455 Integrin dynamics and matrix assembly: tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis.
Pankov R, Cukierman E, Katz BZ, Matsumoto K, Lin DC, Lin S, Hahn C, Yamada KM.
J Cell Biol. 2000 Mar 6;148(5):1075-90.

PubMed: 7840759 Tensin: a potential link between the cytoskeleton and signal transduction.
Lo SH, Weisberg E, Chen LB.
Bioessays. 1994 Nov;16(11):817-23.

FAQ

PubMed: 11023826	Molecular characterization of human tensin. Chen H, Ishii A, Wong WK, Chen LB, Lo SH. Biochem J. 2000 Oct 15;351 Pt 2:403-11.
PubMed: 10860821	Tensin can induce JNK and p38 activation. Katz BZ, Zohar M, Teramoto H, Matsumoto K, Gutkind JS, Lin DC, Lin S, Yamada KM. Biochem Biophys Res Commun. 2000 Jun 16;272(3):717-20.
PubMed: 10704455	Integrin dynamics and matrix assembly: tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis. Pankov R, Cukierman E, Katz BZ, Matsumoto K, Lin DC, Lin S, Hahn C, Yamada KM. J Cell Biol. 2000 Mar 6;148(5):1075-90.
PubMed: 7840759	Tensin: a potential link between the cytoskeleton and signal transduction. Lo SH, Weisberg E, Chen LB. Bioessays. 1994 Nov;16(11):817-23.