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Q9NS15

- LTBP3_HUMAN

UniProt

Q9NS15 - LTBP3_HUMAN

Protein

Latent-transforming growth factor beta-binding protein 3

Gene

LTBP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 4 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extra cellular matrix (ECM).

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. transforming growth factor beta binding Source: UniProt

    GO - Biological processi

    1. bone morphogenesis Source: Ensembl
    2. bone remodeling Source: Ensembl
    3. extracellular matrix organization Source: Reactome
    4. lung saccule development Source: Ensembl
    5. negative regulation of bone mineralization Source: Ensembl
    6. negative regulation of chondrocyte differentiation Source: Ensembl
    7. positive regulation of bone resorption Source: Ensembl
    8. positive regulation of mesenchymal stem cell differentiation Source: UniProt
    9. positive regulation of mesenchymal stem cell proliferation Source: UniProt
    10. transforming growth factor beta activation Source: UniProt
    11. transforming growth factor beta receptor signaling pathway Source: Ensembl

    Keywords - Ligandi

    Growth factor binding

    Enzyme and pathway databases

    ReactomeiREACT_150331. Molecules associated with elastic fibres.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Latent-transforming growth factor beta-binding protein 3
    Short name:
    LTBP-3
    Gene namesi
    Name:LTBP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:6716. LTBP3.

    Subcellular locationi

    Secreted By similarity
    Note: Secretion occurs after coexpression with TGFB1 and requires complexing with 'Cys-33' of the TGFB1 propeptide.By similarity

    GO - Cellular componenti

    1. extracellular matrix Source: UniProt
    2. extracellular region Source: Reactome
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Tooth agenesis selective 6 (STHAG6) [MIM:613097]: A form of selective tooth agenesis, a common anomaly characterized by the congenital absence of one or more teeth. Selective tooth agenesis without associated systemic disorders has sometimes been divided into 2 types: oligodontia, defined as agenesis of 6 or more permanent teeth, and hypodontia, defined as agenesis of less than 6 teeth. The number in both cases does not include absence of third molars (wisdom teeth). In tooth agenesis selective type 6, alveolar bone is absent where the teeth are missing. Some individuals have short stature.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi613097. phenotype.
    Orphaneti2227. Hypodontia.
    99798. Oligodontia.
    PharmGKBiPA30479.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4343Sequence AnalysisAdd
    BLAST
    Chaini44 – 13031260Latent-transforming growth factor beta-binding protein 3PRO_0000007646Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi113 ↔ 123PROSITE-ProRule annotation
    Disulfide bondi117 ↔ 129PROSITE-ProRule annotation
    Disulfide bondi131 ↔ 140PROSITE-ProRule annotation
    Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi359 ↔ 370PROSITE-ProRule annotation
    Disulfide bondi365 ↔ 379PROSITE-ProRule annotation
    Disulfide bondi381 ↔ 394PROSITE-ProRule annotation
    Disulfide bondi578 ↔ 590PROSITE-ProRule annotation
    Disulfide bondi585 ↔ 599PROSITE-ProRule annotation
    Disulfide bondi601 ↔ 614PROSITE-ProRule annotation
    Disulfide bondi620 ↔ 632PROSITE-ProRule annotation
    Disulfide bondi625 ↔ 641PROSITE-ProRule annotation
    Disulfide bondi643 ↔ 658PROSITE-ProRule annotation
    Disulfide bondi664 ↔ 676PROSITE-ProRule annotation
    Disulfide bondi670 ↔ 685PROSITE-ProRule annotation
    Disulfide bondi687 ↔ 701PROSITE-ProRule annotation
    Disulfide bondi748 ↔ 759PROSITE-ProRule annotation
    Disulfide bondi754 ↔ 768PROSITE-ProRule annotation
    Disulfide bondi770 ↔ 783PROSITE-ProRule annotation
    Disulfide bondi789 ↔ 800PROSITE-ProRule annotation
    Disulfide bondi795 ↔ 809PROSITE-ProRule annotation
    Disulfide bondi811 ↔ 824PROSITE-ProRule annotation
    Disulfide bondi830 ↔ 841PROSITE-ProRule annotation
    Disulfide bondi836 ↔ 850PROSITE-ProRule annotation
    Glycosylationi845 – 8451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi852 ↔ 864PROSITE-ProRule annotation
    Disulfide bondi870 ↔ 883PROSITE-ProRule annotation
    Disulfide bondi877 ↔ 892PROSITE-ProRule annotation
    Disulfide bondi894 ↔ 907PROSITE-ProRule annotation
    Glycosylationi936 – 9361N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi997 ↔ 1010PROSITE-ProRule annotation
    Disulfide bondi1005 ↔ 1019PROSITE-ProRule annotation
    Disulfide bondi1021 ↔ 1034PROSITE-ProRule annotation
    Disulfide bondi1040 ↔ 1051PROSITE-ProRule annotation
    Disulfide bondi1046 ↔ 1060PROSITE-ProRule annotation
    Disulfide bondi1062 ↔ 1075PROSITE-ProRule annotation
    Disulfide bondi1086 ↔ 1097PROSITE-ProRule annotation
    Disulfide bondi1092 ↔ 1106PROSITE-ProRule annotation
    Disulfide bondi1108 ↔ 1121PROSITE-ProRule annotation
    Disulfide bondi1258 ↔ 1273PROSITE-ProRule annotation
    Disulfide bondi1268 ↔ 1282PROSITE-ProRule annotation
    Glycosylationi1275 – 12751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1284 ↔ 1297PROSITE-ProRule annotation

    Post-translational modificationi

    Contains hydroxylated asparagine residues.By similarity
    Two intrachain disulfide bonds from the TB3 domain are rearranged upon TGFB1 binding, and form interchain bonds with TGFB1 propeptide, anchoring it to the extracellular matrix.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9NS15.
    PaxDbiQ9NS15.
    PRIDEiQ9NS15.

    PTM databases

    PhosphoSiteiQ9NS15.

    Expressioni

    Tissue specificityi

    Isoform 2 is expressed prominently in heart, skeletal muscle, prostate, testis, small intestine and ovary. Isoform 1 is strongly expressed in pancreas and liver.

    Gene expression databases

    ArrayExpressiQ9NS15.
    BgeeiQ9NS15.
    CleanExiHS_LTBP3.
    GenevestigatoriQ9NS15.

    Interactioni

    Subunit structurei

    Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex.

    Protein-protein interaction databases

    BioGridi110232. 8 interactions.
    IntActiQ9NS15. 6 interactions.
    MINTiMINT-1184940.
    STRINGi9606.ENSP00000301873.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NS15.
    SMRiQ9NS15. Positions 296-461, 573-1122, 1234-1297.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini109 – 14133EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini277 – 33155TB 1Add
    BLAST
    Domaini355 – 39541EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini403 – 45553TB 2Add
    BLAST
    Domaini574 – 61542EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini616 – 65944EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini660 – 70243EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini744 – 78441EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini785 – 82541EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini826 – 86540EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini866 – 90843EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini917 – 97155TB 3Add
    BLAST
    Domaini993 – 103543EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1036 – 107641EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1082 – 112241EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1136 – 118651TB 4Add
    BLAST
    Domaini1254 – 129845EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi3 – 167165Gly-richAdd
    BLAST
    Compositional biasi578 – 894317Cys-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the LTBP family.Curated
    Contains 13 EGF-like domains.PROSITE-ProRule annotation
    Contains 4 TB (TGF-beta binding) domains.Curated

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG261244.
    HOGENOMiHOG000293153.
    HOVERGENiHBG052370.
    InParanoidiQ9NS15.
    KOiK08023.
    OMAiEGPPAQH.
    PhylomeDBiQ9NS15.
    TreeFamiTF317514.

    Family and domain databases

    Gene3Di3.90.290.10. 5 hits.
    InterProiIPR026823. cEGF.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR017878. TB_dom.
    [Graphical view]
    PfamiPF12662. cEGF. 1 hit.
    PF07645. EGF_CA. 10 hits.
    PF00683. TB. 4 hits.
    [Graphical view]
    SMARTiSM00181. EGF. 3 hits.
    SM00179. EGF_CA. 12 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 4 hits.
    SSF57581. SSF57581. 4 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 11 hits.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 8 hits.
    PS50026. EGF_3. 13 hits.
    PS01187. EGF_CA. 12 hits.
    PS51364. TB. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NS15-1) [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

    MPGPRGAAGG LAPEMRGAGA AGLLALLLLL LLLLLGLGGR VEGGPAGERG     50
    AGGGGALARE RFKVVFAPVI CKRTCLKGQC RDSCQQGSNM TLIGENGHST 100
    DTLTGSGFRV VVCPLPCMNG GQCSSRNQCL CPPDFTGRFC QVPAGGAGGG 150
    TGGSGPGLSR TGALSTGALP PLAPEGDSVA SKHAIYAVQV IADPPGPGEG 200
    PPAQHAAFLV PLGPGQISAE VQAPPPVVNV RVHHPPEASV QVHRIESSNA 250
    ESAAPSQHLL PHPKPSHPRP PTQKPLGRCF QDTLPKQPCG SNPLPGLTKQ 300
    EDCCGSIGTA WGQSKCHKCP QLQYTGVQKP GPVRGEVGAD CPQGYKRLNS 350
    THCQDINECA MPGVCRHGDC LNNPGSYRCV CPPGHSLGPS RTQCIADKPE 400
    EKSLCFRLVS PEHQCQHPLT TRLTRQLCCC SVGKAWGARC QRCPTDGTAA 450
    FKEICPAGKG YHILTSHQTL TIQGESDFSL FLHPDGPPKP QQLPESPSQA 500
    PPPEDTEEER GVTTDSPVSE ERSVQQSHPT ATTTPARPYP ELISRPSPPT 550
    MRWFLPDLPP SRSAVEIAPT QVTETDECRL NQNICGHGEC VPGPPDYSCH 600
    CNPGYRSHPQ HRYCVDVNEC EAEPCGPGRG ICMNTGGSYN CHCNRGYRLH 650
    VGAGGRSCVD LNECAKPHLC GDGGFCINFP GHYKCNCYPG YRLKASRPPV 700
    CEDIDECRDP SSCPDGKCEN KPGSFKCIAC QPGYRSQGGG ACRDVNECAE 750
    GSPCSPGWCE NLPGSFRCTC AQGYAPAPDG RSCLDVDECE AGDVCDNGIC 800
    SNTPGSFQCQ CLSGYHLSRD RSHCEDIDEC DFPAACIGGD CINTNGSYRC 850
    LCPQGHRLVG GRKCQDIDEC SQDPSLCLPH GACKNLQGSY VCVCDEGFTP 900
    TQDQHGCEEV EQPHHKKECY LNFDDTVFCD SVLATNVTQQ ECCCSLGAGW 950
    GDHCEIYPCP VYSSAEFHSL CPDGKGYTQD NNIVNYGIPA HRDIDECMLF 1000
    GSEICKEGKC VNTQPGYECY CKQGFYYDGN LLECVDVDEC LDESNCRNGV 1050
    CENTRGGYRC ACTPPAEYSP AQRQCLSPEE MDVDECQDPA ACRPGRCVNL 1100
    PGSYRCECRP PWVPGPSGRD CQLPESPAER APERRDVCWS QRGEDGMCAG 1150
    PLAGPALTFD DCCCRQGRGW GAQCRPCPPR GAGSHCPTSQ SESNSFWDTS 1200
    PLLLGKPPRD EDSSEEDSDE CRCVSGRCVP RPGGAVCECP GGFQLDASRA 1250
    RCVDIDECRE LNQRGLLCKS ERCVNTSGSF RCVCKAGFAR SRPHGACVPQ 1300
    RRR 1303
    Length:1,303
    Mass (Da):139,359
    Last modified:October 17, 2006 - v4
    Checksum:i3BC6B1EE19198414
    GO
    Isoform 2 (identifier: Q9NS15-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1082-1128: Missing.

    Show »
    Length:1,256
    Mass (Da):134,292
    Checksum:i1D930E5D208601E2
    GO

    Sequence cautioni

    The sequence BAB15767.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 351Missing in BAB15767. 1 PublicationCurated
    Sequence conflicti477 – 4771D → H in AAB64201. (PubMed:9620332)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1082 – 112847Missing in isoform 2. 1 PublicationVSP_009241Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF135960 mRNA. Translation: AAF62352.3.
    AK024477 mRNA. Translation: BAB15767.1. Different initiation.
    AF011407 mRNA. Translation: AAB64201.1.
    BC008761 mRNA. Translation: AAH08761.2.
    AL117551 mRNA. Translation: CAB55988.1.
    CCDSiCCDS44647.1. [Q9NS15-1]
    CCDS8103.1. [Q9NS15-2]
    PIRiT17298.
    RefSeqiNP_001123616.1. NM_001130144.2. [Q9NS15-1]
    NP_001157738.1. NM_001164266.1.
    NP_066548.2. NM_021070.4. [Q9NS15-2]
    UniGeneiHs.289019.

    Genome annotation databases

    EnsembliENST00000301873; ENSP00000301873; ENSG00000168056. [Q9NS15-1]
    ENST00000322147; ENSP00000326647; ENSG00000168056. [Q9NS15-2]
    GeneIDi4054.
    KEGGihsa:4054.
    UCSCiuc001oei.3. human. [Q9NS15-2]
    uc001oej.3. human. [Q9NS15-1]

    Polymorphism databases

    DMDMi116242623.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF135960 mRNA. Translation: AAF62352.3 .
    AK024477 mRNA. Translation: BAB15767.1 . Different initiation.
    AF011407 mRNA. Translation: AAB64201.1 .
    BC008761 mRNA. Translation: AAH08761.2 .
    AL117551 mRNA. Translation: CAB55988.1 .
    CCDSi CCDS44647.1. [Q9NS15-1 ]
    CCDS8103.1. [Q9NS15-2 ]
    PIRi T17298.
    RefSeqi NP_001123616.1. NM_001130144.2. [Q9NS15-1 ]
    NP_001157738.1. NM_001164266.1.
    NP_066548.2. NM_021070.4. [Q9NS15-2 ]
    UniGenei Hs.289019.

    3D structure databases

    ProteinModelPortali Q9NS15.
    SMRi Q9NS15. Positions 296-461, 573-1122, 1234-1297.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110232. 8 interactions.
    IntActi Q9NS15. 6 interactions.
    MINTi MINT-1184940.
    STRINGi 9606.ENSP00000301873.

    PTM databases

    PhosphoSitei Q9NS15.

    Polymorphism databases

    DMDMi 116242623.

    Proteomic databases

    MaxQBi Q9NS15.
    PaxDbi Q9NS15.
    PRIDEi Q9NS15.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301873 ; ENSP00000301873 ; ENSG00000168056 . [Q9NS15-1 ]
    ENST00000322147 ; ENSP00000326647 ; ENSG00000168056 . [Q9NS15-2 ]
    GeneIDi 4054.
    KEGGi hsa:4054.
    UCSCi uc001oei.3. human. [Q9NS15-2 ]
    uc001oej.3. human. [Q9NS15-1 ]

    Organism-specific databases

    CTDi 4054.
    GeneCardsi GC11M065306.
    HGNCi HGNC:6716. LTBP3.
    MIMi 602090. gene.
    613097. phenotype.
    neXtProti NX_Q9NS15.
    Orphaneti 2227. Hypodontia.
    99798. Oligodontia.
    PharmGKBi PA30479.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG261244.
    HOGENOMi HOG000293153.
    HOVERGENi HBG052370.
    InParanoidi Q9NS15.
    KOi K08023.
    OMAi EGPPAQH.
    PhylomeDBi Q9NS15.
    TreeFami TF317514.

    Enzyme and pathway databases

    Reactomei REACT_150331. Molecules associated with elastic fibres.

    Miscellaneous databases

    ChiTaRSi LTBP3. human.
    GeneWikii LTBP3.
    GenomeRNAii 4054.
    NextBioi 15884.
    PROi Q9NS15.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NS15.
    Bgeei Q9NS15.
    CleanExi HS_LTBP3.
    Genevestigatori Q9NS15.

    Family and domain databases

    Gene3Di 3.90.290.10. 5 hits.
    InterProi IPR026823. cEGF.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR017878. TB_dom.
    [Graphical view ]
    Pfami PF12662. cEGF. 1 hit.
    PF07645. EGF_CA. 10 hits.
    PF00683. TB. 4 hits.
    [Graphical view ]
    SMARTi SM00181. EGF. 3 hits.
    SM00179. EGF_CA. 12 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 4 hits.
    SSF57581. SSF57581. 4 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 11 hits.
    PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 8 hits.
    PS50026. EGF_3. 13 hits.
    PS01187. EGF_CA. 12 hits.
    PS51364. TB. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Secretion of human latent TGF-beta-binding protein-3 (LTBP-3) is dependent on co-expression of TGF-beta."
      Penttinen C., Saharinen J., Weikkolainen K., Hyytiainen M., Keski-Oja J.
      J. Cell Sci. 115:3457-3468(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION (ISOFORM 2).
    2. "The nucleotide sequence of a long cDNA clone isolated from human spleen."
      Ohara O., Nagase T., Kikuno R., Okumura K.
      Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Spleen.
    3. "Analysis of the expression pattern of the latent transforming growth factor beta binding protein isoforms in normal and diseased human liver reveals a new splice variant missing the proteinase-sensitive hinge region."
      Michel K., Roth S., Trautwein C., Gong W., Flemming P., Gressner A.M.
      Hepatology 27:1592-1599(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 394-573.
      Tissue: Liver.
    4. "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] OF 514-1303 (ISOFORM 2).
      Tissue: Colon.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 793-1303.
      Tissue: Uterus.
    6. "Specific sequence motif of 8-Cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGF-beta."
      Saharinen J., Keski-Oja J.
      Mol. Biol. Cell 11:2691-2704(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TGFB1.
    7. "Latent transforming growth factor-beta binding proteins (LTBPs) --structural extracellular matrix proteins for targeting TGF-beta action."
      Saharinen J., Hyytiainen M., Taipale J., Keski-Oja J.
      Cytokine Growth Factor Rev. 10:99-117(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    8. "The latent transforming growth factor beta binding protein (LTBP) family."
      Oklu R., Hesketh R.
      Biochem. J. 352:601-610(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    9. "Oligodontia is caused by mutation in LTBP3, the gene encoding latent TGF-beta binding protein 3."
      Noor A., Windpassinger C., Vitcu I., Orlic M., Rafiq M.A., Khalid M., Malik M.N., Ayub M., Alman B., Vincent J.B.
      Am. J. Hum. Genet. 84:519-523(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN STHAG6.

    Entry informationi

    Entry nameiLTBP3_HUMAN
    AccessioniPrimary (citable) accession number: Q9NS15
    Secondary accession number(s): O15107
    , Q96HB9, Q9H7K2, Q9UFN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 128 of the entry and version 4 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 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3