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Q68CZ2

- TENS3_HUMAN

UniProt

Q68CZ2 - TENS3_HUMAN

Protein

Tensin-3

Gene

TNS3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (24 Jul 2007)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell migration Source: Ensembl
    2. lung alveolus development Source: Ensembl
    3. positive regulation of cell proliferation Source: Ensembl

    Enzyme and pathway databases

    SignaLinkiQ68CZ2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tensin-3
    Alternative name(s):
    Tensin-like SH2 domain-containing protein 1
    Tumor endothelial marker 6
    Gene namesi
    Name:TNS3
    Synonyms:TEM6, TENS1, TPP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:21616. TNS3.

    Subcellular locationi

    Cell junctionfocal adhesion 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. focal adhesion Source: HPA

    Keywords - Cellular componenti

    Cell junction

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134888115.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14451445Tensin-3PRO_0000295915Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei332 – 3321Phosphoserine1 Publication
    Modified residuei632 – 6321Phosphothreonine1 Publication
    Modified residuei649 – 6491Phosphoserine1 Publication
    Modified residuei660 – 6601Phosphoserine2 Publications
    Modified residuei687 – 6871PhosphoserineBy similarity
    Modified residuei690 – 6901PhosphoserineBy similarity
    Modified residuei735 – 7351Phosphoserine1 Publication
    Modified residuei776 – 7761Phosphoserine2 Publications
    Modified residuei780 – 7801Phosphotyrosine1 Publication
    Modified residuei811 – 8111Phosphoserine1 Publication
    Modified residuei866 – 8661Phosphoserine1 Publication
    Modified residuei901 – 9011Phosphoserine1 Publication
    Modified residuei1149 – 11491Phosphoserine2 Publications
    Modified residuei1154 – 11541Phosphoserine2 Publications
    Modified residuei1293 – 12931Phosphoserine1 Publication

    Post-translational modificationi

    EGF/epidermal growth factor induces tyrosine phosphorylation in a time- and dose-dependent manner.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ68CZ2.
    PaxDbiQ68CZ2.
    PRIDEiQ68CZ2.

    PTM databases

    PhosphoSiteiQ68CZ2.

    Expressioni

    Tissue specificityi

    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.3 Publications

    Inductioni

    Down-regulated by EGF.2 Publications

    Gene expression databases

    ArrayExpressiQ68CZ2.
    BgeeiQ68CZ2.
    CleanExiHS_TNS3.
    GenevestigatoriQ68CZ2.

    Organism-specific databases

    HPAiHPA055338.
    HPA056015.

    Interactioni

    Subunit structurei

    EGF promotes the interaction with EGFR. Interacts with PTK2/FAK1 and BCAR1. Tyrosine phosphorylation is critical for these interactions.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BCAR1P569458EBI-1220488,EBI-702093
    CDH1P128302EBI-1220488,EBI-727477
    ERBB2P046262EBI-1220488,EBI-641062
    ERBB3P218602EBI-1220488,EBI-720706
    KITP107215EBI-1220488,EBI-1379503
    METP085813EBI-1220488,EBI-1039152
    PTK2Q053973EBI-1220488,EBI-702142
    SRCP1293113EBI-1220488,EBI-621482

    Protein-protein interaction databases

    BioGridi122272. 10 interactions.
    IntActiQ68CZ2. 16 interactions.
    MINTiMINT-1494711.
    STRINGi9606.ENSP00000312143.

    Structurei

    3D structure databases

    ProteinModelPortaliQ68CZ2.
    SMRiQ68CZ2. Positions 2-301, 1167-1284, 1309-1439.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 170170Phosphatase tensin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini175 – 301127C2 tensin-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini1172 – 1282111SH2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi941 – 9444Poly-Ser

    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.
    HOVERGENiHBG060186.
    InParanoidiQ68CZ2.
    KOiK18080.
    OMAiKWIKDGP.
    PhylomeDBiQ68CZ2.
    TreeFamiTF315996.

    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]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q68CZ2-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MEEGHGLDLT YITERIIAVS FPAGCSEESY LHNLQEVTRM LKSKHGDNYL     50
    VLNLSEKRYD LTKLNPKIMD VGWPELHAPP LDKMCTICKA QESWLNSNLQ 100
    HVVVIHCRGG KGRIGVVISS YMHFTNVSAS ADQALDRFAM KKFYDDKVSA 150
    LMQPSQKRYV QFLSGLLSGS VKMNASPLFL HFVILHGTPN FDTGGVCRPF 200
    LKLYQAMQPV YTSGIYNVGP ENPSRICIVI EPAQLLKGDV MVKCYHKKYR 250
    SATRDVIFRL QFHTGAVQGY GLVFGKEDLD NASKDDRFPD YGKVELVFSA 300
    TPEKIQGSEH LYNDHGVIVD YNTTDPLIRW DSYENLSADG EVLHTQGPVD 350
    GSLYAKVRKK SSSDPGIPGG PQAIPATNSP DHSDHTLSVS SDSGHSTASA 400
    RTDKTEERLA PGTRRGLSAQ EKAELDQLLS GFGLEDPGSS LKEMTDARSK 450
    YSGTRHVVPA QVHVNGDAAL KDRETDILDD EMPHHDLHSV DSLGTLSSSE 500
    GPQSAHLGPF TCHKSSQNSL LSDGFGSNVG EDPQGTLVPD LGLGMDGPYE 550
    RERTFGSREP KQPQPLLRKP SVSAQMQAYG QSSYSTQTWV RQQQMVVAHQ 600
    YSFAPDGEAR LVSRCPADNP GLVQAQPRVP LTPTRGTSSR VAVQRGVGSG 650
    PHPPDTQQPS PSKAFKPRFP GDQVVNGAGP ELSTGPSPGS PTLDIDQSIE 700
    QLNRLILELD PTFEPIPTHM NALGSQANGS VSPDSVGGGL RASSRLPDTG 750
    EGPSRATGRQ GSSAEQPLGG RLRKLSLGQY DNDAGGQLPF SKCAWGKAGV 800
    DYAPNLPPFP SPADVKETMT PGYPQDLDII DGRILSSKES MCSTPAFPVS 850
    PETPYVKTAL RHPPFSPPEP PLSSPASQHK GGREPRSCPE TLTHAVGMSE 900
    SPIGPKSTML RADASSTPSF QQAFASSCTI SSNGPGQRRE SSSSAERQWV 950
    ESSPKPMVSL LGSGRPTGSP LSAEFSGTRK DSPVLSCFPP SELQAPFHSH 1000
    ELSLAEPPDS LAPPSSQAFL GFGTAPVGSG LPPEEDLGAL LANSHGASPT 1050
    PSIPLTATGA ADNGFLSHNF LTVAPGHSSH HSPGLQGQGV TLPGQPPLPE 1100
    KKRASEGDRS LGSVSPSSSG FSSPHSGSTI SIPFPNVLPD FSKASEAASP 1150
    LPDSPGDKLV IVKFVQDTSK FWYKADISRE QAIAMLKDKE PGSFIVRDSH 1200
    SFRGAYGLAM KVATPPPSVL QLNKKAGDLA NELVRHFLIE CTPKGVRLKG 1250
    CSNEPYFGSL TALVCQHSIT PLALPCKLLI PERDPLEEIA ESSPQTAANS 1300
    AAELLKQGAA CNVWYLNSVE MESLTGHQAI QKALSITLVQ EPPPVSTVVH 1350
    FKVSAQGITL TDNQRKLFFR RHYPVNSVIF CALDPQDRKW IKDGPSSKVF 1400
    GFVARKQGSA TDNVCHLFAE HDPEQPASAI VNFVSKVMIG SPKKV 1445
    Length:1,445
    Mass (Da):155,266
    Last modified:July 24, 2007 - v2
    Checksum:i40B02C6269899320
    GO
    Isoform 2 (identifier: Q68CZ2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         241-480: Missing.

    Show »
    Length:1,205
    Mass (Da):129,066
    Checksum:i7E02E291D5DF030D
    GO
    Isoform 3 (identifier: Q68CZ2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         381-391: DHSDHTLSVSS → ANVLFELIGQV
         392-1445: Missing.

    Show »
    Length:391
    Mass (Da):43,549
    Checksum:iB35A18476C52C6F3
    GO
    Isoform 4 (identifier: Q68CZ2-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:250
    Mass (Da):28,043
    Checksum:i35E9ABB42FF739A5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311L → P in AAN32667. (PubMed:15140944)Curated
    Sequence conflicti458 – 4581V → A in CAH18438. (PubMed:11230166)Curated
    Sequence conflicti505 – 5051A → V in AAN32667. (PubMed:15140944)Curated
    Sequence conflicti917 – 9171T → A in CAH18438. (PubMed:11230166)Curated
    Sequence conflicti1047 – 10471A → T in CAH18438. (PubMed:11230166)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti600 – 6001Q → H.
    Corresponds to variant rs2293362 [ dbSNP | Ensembl ].
    VAR_034593
    Natural varianti679 – 6791G → S.
    Corresponds to variant rs7808646 [ dbSNP | Ensembl ].
    VAR_034594
    Natural varianti1034 – 10341E → K.
    Corresponds to variant rs3807590 [ dbSNP | Ensembl ].
    VAR_052548

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei241 – 480240Missing in isoform 2. 1 PublicationVSP_027123Add
    BLAST
    Alternative sequencei243 – 2508KCYHKKYR → MNYNIANI in isoform 4. 1 PublicationVSP_027124
    Alternative sequencei251 – 14451195Missing in isoform 4. 1 PublicationVSP_027125Add
    BLAST
    Alternative sequencei381 – 39111DHSDHTLSVSS → ANVLFELIGQV in isoform 3. 1 PublicationVSP_027126Add
    BLAST
    Alternative sequencei392 – 14451054Missing in isoform 3. 1 PublicationVSP_027127Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS5506.2. [Q68CZ2-1]
    RefSeqiNP_073585.8. NM_022748.11. [Q68CZ2-1]
    UniGeneiHs.520814.

    Genome annotation databases

    EnsembliENST00000311160; ENSP00000312143; ENSG00000136205. [Q68CZ2-1]
    ENST00000442536; ENSP00000389285; ENSG00000136205. [Q68CZ2-4]
    ENST00000458317; ENSP00000388318; ENSG00000136205. [Q68CZ2-4]
    GeneIDi64759.
    KEGGihsa:64759.
    UCSCiuc003tnw.3. human. [Q68CZ2-1]
    uc010kyo.1. human. [Q68CZ2-4]

    Polymorphism databases

    DMDMi156637424.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS5506.2. [Q68CZ2-1 ]
    RefSeqi NP_073585.8. NM_022748.11. [Q68CZ2-1 ]
    UniGenei Hs.520814.

    3D structure databases

    ProteinModelPortali Q68CZ2.
    SMRi Q68CZ2. Positions 2-301, 1167-1284, 1309-1439.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122272. 10 interactions.
    IntActi Q68CZ2. 16 interactions.
    MINTi MINT-1494711.
    STRINGi 9606.ENSP00000312143.

    PTM databases

    PhosphoSitei Q68CZ2.

    Polymorphism databases

    DMDMi 156637424.

    Proteomic databases

    MaxQBi Q68CZ2.
    PaxDbi Q68CZ2.
    PRIDEi Q68CZ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311160 ; ENSP00000312143 ; ENSG00000136205 . [Q68CZ2-1 ]
    ENST00000442536 ; ENSP00000389285 ; ENSG00000136205 . [Q68CZ2-4 ]
    ENST00000458317 ; ENSP00000388318 ; ENSG00000136205 . [Q68CZ2-4 ]
    GeneIDi 64759.
    KEGGi hsa:64759.
    UCSCi uc003tnw.3. human. [Q68CZ2-1 ]
    uc010kyo.1. human. [Q68CZ2-4 ]

    Organism-specific databases

    CTDi 64759.
    GeneCardsi GC07M047281.
    HGNCi HGNC:21616. TNS3.
    HPAi HPA055338.
    HPA056015.
    MIMi 606825. gene.
    neXtProti NX_Q68CZ2.
    PharmGKBi PA134888115.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOVERGENi HBG060186.
    InParanoidi Q68CZ2.
    KOi K18080.
    OMAi KWIKDGP.
    PhylomeDBi Q68CZ2.
    TreeFami TF315996.

    Enzyme and pathway databases

    SignaLinki Q68CZ2.

    Miscellaneous databases

    ChiTaRSi TNS3. human.
    GenomeRNAii 64759.
    NextBioi 66735.
    PROi Q68CZ2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q68CZ2.
    Bgeei Q68CZ2.
    CleanExi HS_TNS3.
    Genevestigatori Q68CZ2.

    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. "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.
      , 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. 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.
      , 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. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 749-1445, TISSUE SPECIFICITY.
    9. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTENS3_HUMAN
    AccessioniPrimary (citable) accession number: Q68CZ2
    Secondary accession number(s): B2RNV1
    , Q6IPQ2, Q8IZW7, Q8NAD0, Q96PE0, Q96S48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 24, 2007
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 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 7
      Human chromosome 7: 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