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Q68CZ2 (TENS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tensin-3
Alternative name(s):
Tensin-like SH2 domain-containing protein 1
Tumor endothelial marker 6
Gene names
Name:TNS3
Synonyms:TEM6, TENS1, TPP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1445 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in actin remodeling. Involved in the dissociation of the integrin-tensin-actin complex. EGF activates TNS4 and down-regulates TNS3 which results in capping the tail of ITGB1. Seems to be involved in mammary cell migration. May be involved in cell migration and bone development By similarity. Ref.9

Subunit structure

EGF promotes the interaction with EGFR. Interacts with PTK2/FAK1 and BCAR1. Tyrosine phosphorylation is critical for these interactions. Ref.2

Subcellular location

Cell junctionfocal adhesion Ref.2 Ref.9.

Tissue specificity

Expressed in umbilical vein endothelial cells, epithelial cells, and fibroblasts cells (at protein level). Highly expressed in thyroid, kidney and placenta. Low expression in heart, skeletal muscle, spleen, liver, and lung. Expressed in tumor endothelial cells. Expression seems to be down-regulated in thyroid tumor tissues and in anaplastic carcinomas. Ref.1 Ref.2 Ref.8

Induction

Down-regulated by EGF. Ref.2 Ref.9

Post-translational modification

EGF/epidermal growth factor induces tyrosine phosphorylation in a time- and dose-dependent manner.

Sequence similarities

Contains 1 C2 tensin-type domain.

Contains 1 phosphatase tensin-type domain.

Contains 1 SH2 domain.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q68CZ2-1)

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.
Isoform 2 (identifier: Q68CZ2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     241-480: Missing.
Isoform 3 (identifier: Q68CZ2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     381-391: DHSDHTLSVSS → ANVLFELIGQV
     392-1445: Missing.
Isoform 4 (identifier: Q68CZ2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     243-250: KCYHKKYR → MNYNIANI
     251-1445: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14451445Tensin-3
PRO_0000295915

Regions

Domain1 – 170170Phosphatase tensin-type
Domain175 – 301127C2 tensin-type
Domain1172 – 1282111SH2
Compositional bias941 – 9444Poly-Ser

Amino acid modifications

Modified residue3321Phosphoserine Ref.11
Modified residue6321Phosphothreonine Ref.11
Modified residue6491Phosphoserine Ref.13
Modified residue6601Phosphoserine Ref.11 Ref.13
Modified residue6871Phosphoserine By similarity
Modified residue6901Phosphoserine By similarity
Modified residue7351Phosphoserine Ref.13
Modified residue7761Phosphoserine Ref.11 Ref.13
Modified residue7801Phosphotyrosine Ref.13
Modified residue8111Phosphoserine Ref.13
Modified residue8661Phosphoserine Ref.11
Modified residue9011Phosphoserine Ref.11
Modified residue11491Phosphoserine Ref.11 Ref.13
Modified residue11541Phosphoserine Ref.11 Ref.13
Modified residue12931Phosphoserine Ref.11

Natural variations

Alternative sequence241 – 480240Missing in isoform 2.
VSP_027123
Alternative sequence243 – 2508KCYHKKYR → MNYNIANI in isoform 4.
VSP_027124
Alternative sequence251 – 14451195Missing in isoform 4.
VSP_027125
Alternative sequence381 – 39111DHSDHTLSVSS → ANVLFELIGQV in isoform 3.
VSP_027126
Alternative sequence392 – 14451054Missing in isoform 3.
VSP_027127
Natural variant6001Q → H.
Corresponds to variant rs2293362 [ dbSNP | Ensembl ].
VAR_034593
Natural variant6791G → S.
Corresponds to variant rs7808646 [ dbSNP | Ensembl ].
VAR_034594
Natural variant10341E → K.
Corresponds to variant rs3807590 [ dbSNP | Ensembl ].
VAR_052548

Experimental info

Sequence conflict311L → P in AAN32667. Ref.2
Sequence conflict4581V → A in CAH18438. Ref.4
Sequence conflict5051A → V in AAN32667. Ref.2
Sequence conflict9171T → A in CAH18438. Ref.4
Sequence conflict10471A → T in CAH18438. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 40B02C6269899320

FASTA1,445155,266
        10         20         30         40         50         60 
MEEGHGLDLT YITERIIAVS FPAGCSEESY LHNLQEVTRM LKSKHGDNYL VLNLSEKRYD 

        70         80         90        100        110        120 
LTKLNPKIMD VGWPELHAPP LDKMCTICKA QESWLNSNLQ HVVVIHCRGG KGRIGVVISS 

       130        140        150        160        170        180 
YMHFTNVSAS ADQALDRFAM KKFYDDKVSA LMQPSQKRYV QFLSGLLSGS VKMNASPLFL 

       190        200        210        220        230        240 
HFVILHGTPN FDTGGVCRPF LKLYQAMQPV YTSGIYNVGP ENPSRICIVI EPAQLLKGDV 

       250        260        270        280        290        300 
MVKCYHKKYR SATRDVIFRL QFHTGAVQGY GLVFGKEDLD NASKDDRFPD YGKVELVFSA 

       310        320        330        340        350        360 
TPEKIQGSEH LYNDHGVIVD YNTTDPLIRW DSYENLSADG EVLHTQGPVD GSLYAKVRKK 

       370        380        390        400        410        420 
SSSDPGIPGG PQAIPATNSP DHSDHTLSVS SDSGHSTASA RTDKTEERLA PGTRRGLSAQ 

       430        440        450        460        470        480 
EKAELDQLLS GFGLEDPGSS LKEMTDARSK YSGTRHVVPA QVHVNGDAAL KDRETDILDD 

       490        500        510        520        530        540 
EMPHHDLHSV DSLGTLSSSE GPQSAHLGPF TCHKSSQNSL LSDGFGSNVG EDPQGTLVPD 

       550        560        570        580        590        600 
LGLGMDGPYE RERTFGSREP KQPQPLLRKP SVSAQMQAYG QSSYSTQTWV RQQQMVVAHQ 

       610        620        630        640        650        660 
YSFAPDGEAR LVSRCPADNP GLVQAQPRVP LTPTRGTSSR VAVQRGVGSG PHPPDTQQPS 

       670        680        690        700        710        720 
PSKAFKPRFP GDQVVNGAGP ELSTGPSPGS PTLDIDQSIE QLNRLILELD PTFEPIPTHM 

       730        740        750        760        770        780 
NALGSQANGS VSPDSVGGGL RASSRLPDTG EGPSRATGRQ GSSAEQPLGG RLRKLSLGQY 

       790        800        810        820        830        840 
DNDAGGQLPF SKCAWGKAGV DYAPNLPPFP SPADVKETMT PGYPQDLDII DGRILSSKES 

       850        860        870        880        890        900 
MCSTPAFPVS PETPYVKTAL RHPPFSPPEP PLSSPASQHK GGREPRSCPE TLTHAVGMSE 

       910        920        930        940        950        960 
SPIGPKSTML RADASSTPSF QQAFASSCTI SSNGPGQRRE SSSSAERQWV ESSPKPMVSL 

       970        980        990       1000       1010       1020 
LGSGRPTGSP LSAEFSGTRK DSPVLSCFPP SELQAPFHSH ELSLAEPPDS LAPPSSQAFL 

      1030       1040       1050       1060       1070       1080 
GFGTAPVGSG LPPEEDLGAL LANSHGASPT PSIPLTATGA ADNGFLSHNF LTVAPGHSSH 

      1090       1100       1110       1120       1130       1140 
HSPGLQGQGV TLPGQPPLPE KKRASEGDRS LGSVSPSSSG FSSPHSGSTI SIPFPNVLPD 

      1150       1160       1170       1180       1190       1200 
FSKASEAASP LPDSPGDKLV IVKFVQDTSK FWYKADISRE QAIAMLKDKE PGSFIVRDSH 

      1210       1220       1230       1240       1250       1260 
SFRGAYGLAM KVATPPPSVL QLNKKAGDLA NELVRHFLIE CTPKGVRLKG CSNEPYFGSL 

      1270       1280       1290       1300       1310       1320 
TALVCQHSIT PLALPCKLLI PERDPLEEIA ESSPQTAANS AAELLKQGAA CNVWYLNSVE 

      1330       1340       1350       1360       1370       1380 
MESLTGHQAI QKALSITLVQ EPPPVSTVVH FKVSAQGITL TDNQRKLFFR RHYPVNSVIF 

      1390       1400       1410       1420       1430       1440 
CALDPQDRKW IKDGPSSKVF GFVARKQGSA TDNVCHLFAE HDPEQPASAI VNFVSKVMIG 


SPKKV 

« Hide

Isoform 2 [UniParc].

Checksum: 7E02E291D5DF030D
Show »

FASTA1,205129,066
Isoform 3 [UniParc].

Checksum: B35A18476C52C6F3
Show »

FASTA39143,549
Isoform 4 [UniParc].

Checksum: 35E9ABB42FF739A5
Show »

FASTA25028,043

References

« Hide 'large scale' references
[1]"Cell surface tumor endothelial markers are conserved in mice and humans."
Carson-Walter E.B., Watkins D.N., Nanda A., Vogelstein B., Kinzler K.W., St Croix B.
Cancer Res. 61:6649-6655(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
[2]"Epidermal growth factor modulates tyrosine phosphorylation of a novel tensin family member, tensin3."
Cui Y., Liao Y.-C., Lo S.H.
Mol. Cancer Res. 2:225-232(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, INTERACTION WITH EGFR; PTK2/FAK1 AND BCAR1.
[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. expand/collapse author list , 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 3).
Tissue: Spleen.
[4]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Amygdala.
[5]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 4).
Tissue: Brain and Kidney.
[8]"Tensin3 is a novel thyroid-specific gene."
Maeda I., Takano T., Yoshida H., Matsuzuka F., Amino N., Miyauchi A.
J. Mol. Endocrinol. 36:R1-R8(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 749-1445, TISSUE SPECIFICITY.
[9]"A reciprocal tensin-3-cten switch mediates EGF-driven mammary cell migration."
Katz M., Amit I., Citri A., Shay T., Carvalho S., Lavi S., Milanezi F., Lyass L., Amariglio N., Jacob-Hirsch J., Ben-Chetrit N., Tarcic G., Lindzen M., Avraham R., Liao Y.C., Trusk P., Lyass A., Rechavi G. expand/collapse author list , Spector N.L., Lo S.H., Schmitt F., Bacus S.S., Yarden Y.
Nat. Cell Biol. 9:961-969(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, KNOCKDOWN IN MCF10A CELLS.
[10]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; THR-632; SER-660; SER-776; SER-866; SER-901; SER-1149; SER-1154 AND SER-1293, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; SER-660; SER-735; SER-776; TYR-780; SER-811; SER-1149 AND SER-1154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF378756 mRNA. Translation: AAL11993.1.
AF417489 mRNA. Translation: AAN32667.1.
AK092864 mRNA. Translation: BAC03993.1.
CR749644 mRNA. Translation: CAH18438.1.
AC073341 Genomic DNA. Translation: AAQ96841.1.
CH471128 Genomic DNA. Translation: EAW61011.1.
BC071791 mRNA. Translation: AAH71791.1.
BC137133 mRNA. Translation: AAI37134.1.
BC137134 mRNA. Translation: AAI37135.1.
AB062750 mRNA. Translation: BAB60681.1.
CCDSCCDS5506.2. [Q68CZ2-1]
RefSeqNP_073585.8. NM_022748.11. [Q68CZ2-1]
UniGeneHs.520814.

3D structure databases

ProteinModelPortalQ68CZ2.
SMRQ68CZ2. Positions 2-301, 1167-1284, 1309-1439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122272. 10 interactions.
IntActQ68CZ2. 16 interactions.
MINTMINT-1494711.
STRING9606.ENSP00000312143.

PTM databases

PhosphoSiteQ68CZ2.

Polymorphism databases

DMDM156637424.

Proteomic databases

MaxQBQ68CZ2.
PaxDbQ68CZ2.
PRIDEQ68CZ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311160; ENSP00000312143; ENSG00000136205. [Q68CZ2-1]
ENST00000398879; ENSP00000381854; ENSG00000136205. [Q68CZ2-1]
ENST00000442536; ENSP00000389285; ENSG00000136205. [Q68CZ2-4]
ENST00000458317; ENSP00000388318; ENSG00000136205. [Q68CZ2-4]
GeneID64759.
KEGGhsa:64759.
UCSCuc003tnw.3. human. [Q68CZ2-1]
uc010kyo.1. human. [Q68CZ2-4]

Organism-specific databases

CTD64759.
GeneCardsGC07M047281.
HGNCHGNC:21616. TNS3.
HPAHPA055338.
HPA056015.
MIM606825. gene.
neXtProtNX_Q68CZ2.
PharmGKBPA134888115.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOVERGENHBG060186.
InParanoidQ68CZ2.
KOK18080.
OMAKWIKDGP.
PhylomeDBQ68CZ2.
TreeFamTF315996.

Enzyme and pathway databases

SignaLinkQ68CZ2.

Gene expression databases

ArrayExpressQ68CZ2.
BgeeQ68CZ2.
CleanExHS_TNS3.
GenevestigatorQ68CZ2.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
3.90.190.10. 1 hit.
InterProIPR000008. 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]
PfamPF08416. PTB. 1 hit.
PF10409. PTEN_C2. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTSM00462. PTB. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
SSF52799. SSF52799. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS51182. C2_TENSIN. 1 hit.
PS51181. PPASE_TENSIN. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTNS3. human.
GenomeRNAi64759.
NextBio66735.
PROQ68CZ2.
SOURCESearch...

Entry information

Entry nameTENS3_HUMAN
AccessionPrimary (citable) accession number: Q68CZ2
Secondary accession number(s): B2RNV1 expand/collapse secondary AC list , Q6IPQ2, Q8IZW7, Q8NAD0, Q96PE0, Q96S48
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: July 9, 2014
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM