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Q14766

- LTBP1_HUMAN

UniProt

Q14766 - LTBP1_HUMAN

Protein

Latent-transforming growth factor beta-binding protein 1

Gene

LTBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 4 (02 Mar 2010)
      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. protein binding Source: BHF-UCL
    3. transforming growth factor beta-activated receptor activity Source: UniProtKB
    4. transforming growth factor beta binding Source: UniProt

    GO - Biological processi

    1. extracellular matrix organization Source: Reactome
    2. sequestering of TGFbeta in extracellular matrix Source: BHF-UCL
    3. transmembrane receptor protein serine/threonine kinase signaling pathway Source: GOC

    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 1
    Short name:
    LTBP-1
    Alternative name(s):
    Transforming growth factor beta-1-binding protein 1
    Short name:
    TGF-beta1-BP-1
    Gene namesi
    Name:LTBP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6714. LTBP1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular matrix Source: UniProt
    2. extracellular region Source: Reactome
    3. proteinaceous extracellular matrix Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1385 – 13884EIFP → DL: Loss of binding to TGFB1. 1 Publication

    Organism-specific databases

    PharmGKBiPA30477.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 17211698Latent-transforming growth factor beta-binding protein 1PRO_0000007635Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi191 ↔ 201PROSITE-ProRule annotation
    Disulfide bondi195 ↔ 207PROSITE-ProRule annotation
    Disulfide bondi209 ↔ 218PROSITE-ProRule annotation
    Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi403 ↔ 413PROSITE-ProRule annotation
    Disulfide bondi407 ↔ 419PROSITE-ProRule annotation
    Disulfide bondi421 ↔ 430PROSITE-ProRule annotation
    Glycosylationi424 – 4241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi620 – 6201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi630 ↔ 641PROSITE-ProRule annotation
    Disulfide bondi636 ↔ 650PROSITE-ProRule annotation
    Disulfide bondi652 ↔ 665PROSITE-ProRule annotation
    Disulfide bondi877 ↔ 889PROSITE-ProRule annotation
    Disulfide bondi884 ↔ 898PROSITE-ProRule annotation
    Disulfide bondi900 ↔ 913PROSITE-ProRule annotation
    Disulfide bondi919 ↔ 931PROSITE-ProRule annotation
    Disulfide bondi926 ↔ 940PROSITE-ProRule annotation
    Disulfide bondi942 ↔ 955PROSITE-ProRule annotation
    Disulfide bondi961 ↔ 972PROSITE-ProRule annotation
    Disulfide bondi967 ↔ 981PROSITE-ProRule annotation
    Modified residuei974 – 9741(3R)-3-hydroxyasparagine1 Publication
    Disulfide bondi984 ↔ 996PROSITE-ProRule annotation
    Disulfide bondi1002 ↔ 1013PROSITE-ProRule annotation
    Disulfide bondi1008 ↔ 1022PROSITE-ProRule annotation
    Disulfide bondi1025 ↔ 1036PROSITE-ProRule annotation
    Disulfide bondi1042 ↔ 1053PROSITE-ProRule annotation
    Disulfide bondi1048 ↔ 1062PROSITE-ProRule annotation
    Disulfide bondi1064 ↔ 1077PROSITE-ProRule annotation
    Disulfide bondi1083 ↔ 1094PROSITE-ProRule annotation
    Disulfide bondi1089 ↔ 1103PROSITE-ProRule annotation
    Disulfide bondi1105 ↔ 1118PROSITE-ProRule annotation
    Disulfide bondi1124 ↔ 1135PROSITE-ProRule annotation
    Disulfide bondi1130 ↔ 1144PROSITE-ProRule annotation
    Modified residuei1137 – 11371(3R)-3-hydroxyasparagine1 Publication
    Disulfide bondi1146 ↔ 1159PROSITE-ProRule annotation
    Disulfide bondi1165 ↔ 1177PROSITE-ProRule annotation
    Disulfide bondi1172 ↔ 1186PROSITE-ProRule annotation
    Disulfide bondi1188 ↔ 1200PROSITE-ProRule annotation
    Glycosylationi1197 – 11971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1206 ↔ 1218PROSITE-ProRule annotation
    Disulfide bondi1212 ↔ 1227PROSITE-ProRule annotation
    Disulfide bondi1229 ↔ 1242PROSITE-ProRule annotation
    Disulfide bondi1248 ↔ 1260PROSITE-ProRule annotation
    Glycosylationi1250 – 12501N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1254 ↔ 1269PROSITE-ProRule annotation
    Disulfide bondi1349 ↔ 13721 PublicationPROSITE-ProRule annotation
    Disulfide bondi1359 ↔ 13841 PublicationPROSITE-ProRule annotation
    Disulfide bondi1359 – 1359Interchain (with C-33 in TGFB1); in linked formPROSITE-ProRule annotation
    Glycosylationi1366 – 13661N-linked (GlcNAc...)1 PublicationCAR_000184
    Disulfide bondi1373 ↔ 13891 PublicationPROSITE-ProRule annotation
    Disulfide bondi1374 ↔ 14011 PublicationPROSITE-ProRule annotation
    Disulfide bondi1384 – 1384Interchain (with C-33 in TGFB1); in linked formPROSITE-ProRule annotation
    Disulfide bondi1471 ↔ 1482PROSITE-ProRule annotation
    Disulfide bondi1477 ↔ 1491PROSITE-ProRule annotation
    Modified residuei1597 – 15971Phosphoserine1 Publication
    Disulfide bondi1625 ↔ 1636PROSITE-ProRule annotation
    Disulfide bondi1631 ↔ 1645PROSITE-ProRule annotation
    Disulfide bondi1666 ↔ 1681PROSITE-ProRule annotation
    Disulfide bondi1676 ↔ 1690PROSITE-ProRule annotation
    Disulfide bondi1692 ↔ 1705PROSITE-ProRule annotation

    Post-translational modificationi

    Contains hydroxylated asparagine residues.1 Publication
    Isoform Short N-terminus is blocked.
    The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.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, Hydroxylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ14766.
    PaxDbiQ14766.
    PRIDEiQ14766.

    PTM databases

    PhosphoSiteiQ14766.
    UniCarbKBiQ14766.

    Expressioni

    Tissue specificityi

    Isoform Long is found in fibroblasts.

    Gene expression databases

    ArrayExpressiQ14766.
    BgeeiQ14766.
    CleanExiHS_LTBP1.
    GenevestigatoriQ14766.

    Organism-specific databases

    HPAiCAB025428.
    HPA005707.
    HPA006221.

    Interactioni

    Subunit structurei

    The large latent complex of TGFB1 from platelets is composed of the TGFB1 molecule non-covalently associated with a disulfide-bonded complex of a dimer of the N-terminal propeptide of the TGFB1 precursor and LTBP1. LTBP1 does not bind directly to active TGFB1. Binds to FBN1 and FBN2. Interacts with ADAMTSL2.3 Publications

    Protein-protein interaction databases

    BioGridi110230. 5 interactions.
    DIPiDIP-50011N.
    IntActiQ14766. 2 interactions.
    MINTiMINT-1522113.
    STRINGi9606.ENSP00000346467.

    Structurei

    Secondary structure

    1
    1721
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1340 – 13423
    Beta strandi1346 – 13538
    Turni1355 – 13584
    Beta strandi1366 – 13683
    Helixi1369 – 13746
    Beta strandi1378 – 13825
    Beta strandi1385 – 13884
    Beta strandi1392 – 13943
    Helixi1395 – 14006
    Beta strandi1408 – 14103

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KSQNMR-A1340-1412[»]
    ProteinModelPortaliQ14766.
    SMRiQ14766. Positions 550-739, 872-1506, 1621-1700.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14766.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini187 – 21933EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini399 – 43133EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini557 – 60953TB 1Add
    BLAST
    Domaini626 – 66338EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini677 – 72953TB 2Add
    BLAST
    Domaini873 – 91038EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini915 – 95642EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini957 – 99741EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini998 – 103740EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1038 – 107841EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1079 – 111941EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1120 – 116041EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1161 – 120141EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1202 – 124342EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1244 – 128138EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1286 – 132843EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1347 – 140155TB 3Add
    BLAST
    Domaini1424 – 146643EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1467 – 150337EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1524 – 157754TB 4Add
    BLAST
    Domaini1621 – 165737EGF-like 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini1662 – 170645EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1174 – 11763Cell attachment siteSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi100 – 13031Pro-richAdd
    BLAST

    Domaini

    Associates covalently with small latent TGF-beta complex via domain TB 3.

    Sequence similaritiesi

    Belongs to the LTBP family.Curated
    Contains 18 EGF-like domains.PROSITE-ProRule annotation
    Contains 4 TB (TGF-beta binding) domains.Curated

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG318792.
    KOiK08023.
    OMAiKHPPEAS.
    OrthoDBiEOG7FR7FP.
    PhylomeDBiQ14766.
    TreeFamiTF317514.

    Family and domain databases

    Gene3Di3.90.290.10. 5 hits.
    InterProiIPR000742. 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]
    PfamiPF07645. EGF_CA. 12 hits.
    PF00683. TB. 4 hits.
    [Graphical view]
    SMARTiSM00181. EGF. 5 hits.
    SM00179. EGF_CA. 13 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 5 hits.
    SSF57581. SSF57581. 4 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 13 hits.
    PS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 11 hits.
    PS50026. EGF_3. 14 hits.
    PS01187. EGF_CA. 15 hits.
    PS51364. TB. 4 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q14766-1) [UniParc]FASTAAdd to Basket

    Also known as: LTBP-1L

    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

    MAGAWLRWGL LLWAGLLASS AHGRLRRITY VVHPGPGLAA GALPLSGPPR     50
    SRTFNVALNA RYSRSSAAAG APSRASPGVP SERTRRTSKP GGAALQGLRP 100
    PPPPPPEPAR PAVPGGQLHP NPGGHPAAAP FTKQGRQVVR SKVPQETQSG 150
    GGSRLQVHQK QQLQGVNVCG GRCCHGWSKA PGSQRCTKPS CVPPCQNGGM 200
    CLRPQLCVCK PGTKGKACET IAAQDTSSPV FGGQSPGAAS SWGPPEQAAK 250
    HTSSKKADTL PRVSPVAQMT LTLKPKPSVG LPQQIHSQVT PLSSQSVVIH 300
    HGQTQEYVLK PKYFPAQKGI SGEQSTEGSF PLRYVQDQVA APFQLSNHTG 350
    RIKVVFTPSI CKVTCTKGSC QNSCEKGNTT TLISENGHAA DTLTATNFRV 400
    VICHLPCMNG GQCSSRDKCQ CPPNFTGKLC QIPVHGASVP KLYQHSQQPG 450
    KALGTHVIHS THTLPLTVTS QQGVKVKFPP NIVNIHVKHP PEASVQIHQV 500
    SRIDGPTGQK TKEAQPGQSQ VSYQGLPVQK TQTIHSTYSH QQVIPHVYPV 550
    AAKTQLGRCF QETIGSQCGK ALPGLSKQED CCGTVGTSWG FNKCQKCPKK 600
    PSYHGYNQMM ECLPGYKRVN NTFCQDINEC QLQGVCPNGE CLNTMGSYRC 650
    TCKIGFGPDP TFSSCVPDPP VISEEKGPCY RLVSSGRQCM HPLSVHLTKQ 700
    LCCCSVGKAW GPHCEKCPLP GTAAFKEICP GGMGYTVSGV HRRRPIHHHV 750
    GKGPVFVKPK NTQPVAKSTH PPPLPAKEEP VEALTFSREH GPGVAEPEVA 800
    TAPPEKEIPS LDQEKTKLEP GQPQLSPGIS TIHLHPQFPV VIEKTSPPVP 850
    VEVAPEASTS SASQVIAPTQ VTEINECTVN PDICGAGHCI NLPVRYTCIC 900
    YEGYRFSEQQ RKCVDIDECT QVQHLCSQGR CENTEGSFLC ICPAGFMASE 950
    EGTNCIDVDE CLRPDVCGEG HCVNTVGAFR CEYCDSGYRM TQRGRCEDID 1000
    ECLNPSTCPD EQCVNSPGSY QCVPCTEGFR GWNGQCLDVD ECLEPNVCAN 1050
    GDCSNLEGSY MCSCHKGYTR TPDHKHCRDI DECQQGNLCV NGQCKNTEGS 1100
    FRCTCGQGYQ LSAAKDQCED IDECQHRHLC AHGQCRNTEG SFQCVCDQGY 1150
    RASGLGDHCE DINECLEDKS VCQRGDCINT AGSYDCTCPD GFQLDDNKTC 1200
    QDINECEHPG LCGPQGECLN TEGSFHCVCQ QGFSISADGR TCEDIDECVN 1250
    NTVCDSHGFC DNTAGSFRCL CYQGFQAPQD GQGCVDVNEC ELLSGVCGEA 1300
    FCENVEGSFL CVCADENQEY SPMTGQCRSR TSTDLDVDVD QPKEEKKECY 1350
    YNLNDASLCD NVLAPNVTKQ ECCCTSGVGW GDNCEIFPCP VLGTAEFTEM 1400
    CPKGKGFVPA GESSSEAGGE NYKDADECLL FGQEICKNGF CLNTRPGYEC 1450
    YCKQGTYYDP VKLQCFDMDE CQDPSSCIDG QCVNTEGSYN CFCTHPMVLD 1500
    ASEKRCIRPA ESNEQIEETD VYQDLCWEHL SDEYVCSRPL VGKQTTYTEC 1550
    CCLYGEAWGM QCALCPLKDS DDYAQLCNIP VTGRRQPYGR DALVDFSEQY 1600
    TPEADPYFIQ DRFLNSFEEL QAEECGILNG CENGRCVRVQ EGYTCDCFDG 1650
    YHLDTAKMTC VDVNECDELN NRMSLCKNAK CINTDGSYKC LCLPGYVPSD 1700
    KPNYCTPLNT ALNLEKDSDL E 1721
    Length:1,721
    Mass (Da):186,796
    Last modified:March 2, 2010 - v4
    Checksum:i432489CAC3023754
    GO
    Isoform Short (identifier: Q14766-2) [UniParc] [UniParc]FASTAAdd to Basket

    Also known as: LTBP-1S

    The sequence of this isoform differs from the canonical sequence as follows:
         1-326: Missing.
         327-345: EGSFPLRYVQDQVAAPFQL → MDTKLMCLLFFFSLPPLLV

    Show »
    Length:1,395
    Mass (Da):152,935
    Checksum:i69C41A7EC71FE8D2
    GO
    Isoform 3 (identifier: Q14766-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-326: Missing.
         327-345: EGSFPLRYVQDQVAAPFQL → MDTKLMCLLFFFSLPPLLV
         724-776: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,342
    Mass (Da):147,235
    Checksum:i616E9947D00D3200
    GO
    Isoform 4 (identifier: Q14766-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         839-840: PV → PGI

    Show »
    Length:1,722
    Mass (Da):186,867
    Checksum:iD59CED455F79E348
    GO
    Isoform 5 (identifier: Q14766-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-326: Missing.
         327-345: EGSFPLRYVQDQVAAPFQL → MDTKLMCLLFFFSLPPLLV
         839-840: PV → PGI

    Note: No experimental confirmation available.

    Show »
    Length:1,396
    Mass (Da):153,006
    Checksum:i08160DD6EB7DFE97
    GO

    Sequence cautioni

    The sequence BAD92038.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti50 – 501R → AS in AAA96327. (PubMed:8537398)Curated
    Sequence conflicti691 – 6911H → Y in AAA61160. (PubMed:2350783)Curated
    Sequence conflicti694 – 6941S → P in BP291349. 1 PublicationCurated
    Sequence conflicti710 – 7101Missing in AAA61160. (PubMed:2350783)Curated
    Sequence conflicti710 – 7101Missing in AAM03124. 1 PublicationCurated
    Sequence conflicti744 – 7441R → M in BP291349. 1 PublicationCurated
    Sequence conflicti792 – 7943PGV → ARS in AAA61160. (PubMed:2350783)Curated
    Sequence conflicti792 – 7943PGV → ARS in AAM03124. 1 PublicationCurated
    Sequence conflicti831 – 8311T → A in AAA61160. (PubMed:2350783)Curated
    Sequence conflicti1378 – 13781V → A in AAA61160. (PubMed:2350783)Curated
    Sequence conflicti1378 – 13781V → A in AAM03124. 1 PublicationCurated
    Sequence conflicti1378 – 13781V → A in BAD92038. 1 PublicationCurated
    Sequence conflicti1378 – 13781V → A in EAX00437. 1 PublicationCurated
    Sequence conflicti1378 – 13781V → A in AAI30290. (PubMed:15489334)Curated
    Sequence conflicti1648 – 16481F → L in AAA61160. (PubMed:2350783)Curated
    Sequence conflicti1648 – 16481F → L in AAM03124. 1 PublicationCurated
    Sequence conflicti1661 – 16611V → F in AAA61160. (PubMed:2350783)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 326326Missing in isoform Short, isoform 3 and isoform 5. 5 PublicationsVSP_036963Add
    BLAST
    Alternative sequencei327 – 34519EGSFP…APFQL → MDTKLMCLLFFFSLPPLLV in isoform Short, isoform 3 and isoform 5. 5 PublicationsVSP_036964Add
    BLAST
    Alternative sequencei724 – 77653Missing in isoform 3. 1 PublicationVSP_036965Add
    BLAST
    Alternative sequencei839 – 8402PV → PGI in isoform 4 and isoform 5. 1 PublicationVSP_040125

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34057 mRNA. Translation: AAA61160.1.
    AF489528 mRNA. Translation: AAM03124.1.
    AB208801 mRNA. Translation: BAD92038.1. Different initiation.
    AC019195 Genomic DNA. Translation: AAY14953.1.
    AC019127 Genomic DNA. Translation: AAY24260.1.
    AC020594 Genomic DNA. Translation: AAY15036.1.
    CH471053 Genomic DNA. Translation: EAX00437.1.
    BC130289 mRNA. Translation: AAI30290.1.
    L48925 Genomic DNA. Translation: AAA96327.1.
    BP291349 mRNA. No translation available.
    CCDSiCCDS33177.2. [Q14766-1]
    CCDS33178.2. [Q14766-2]
    CCDS54345.1. [Q14766-3]
    PIRiA35626.
    RefSeqiNP_000618.3. NM_000627.3.
    NP_001159736.1. NM_001166264.1.
    NP_001159737.1. NM_001166265.1.
    NP_001159738.1. NM_001166266.1.
    NP_996826.2. NM_206943.2.
    UniGeneiHs.619315.

    Genome annotation databases

    EnsembliENST00000404525; ENSP00000385359; ENSG00000049323. [Q14766-3]
    ENST00000404816; ENSP00000386043; ENSG00000049323. [Q14766-1]
    ENST00000407925; ENSP00000384091; ENSG00000049323. [Q14766-2]
    GeneIDi4052.
    KEGGihsa:4052.
    UCSCiuc002rou.3. human. [Q14766-2]
    uc002rov.3. human. [Q14766-3]
    uc021vft.1. human. [Q14766-1]

    Polymorphism databases

    DMDMi290457687.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M34057 mRNA. Translation: AAA61160.1 .
    AF489528 mRNA. Translation: AAM03124.1 .
    AB208801 mRNA. Translation: BAD92038.1 . Different initiation.
    AC019195 Genomic DNA. Translation: AAY14953.1 .
    AC019127 Genomic DNA. Translation: AAY24260.1 .
    AC020594 Genomic DNA. Translation: AAY15036.1 .
    CH471053 Genomic DNA. Translation: EAX00437.1 .
    BC130289 mRNA. Translation: AAI30290.1 .
    L48925 Genomic DNA. Translation: AAA96327.1 .
    BP291349 mRNA. No translation available.
    CCDSi CCDS33177.2. [Q14766-1 ]
    CCDS33178.2. [Q14766-2 ]
    CCDS54345.1. [Q14766-3 ]
    PIRi A35626.
    RefSeqi NP_000618.3. NM_000627.3.
    NP_001159736.1. NM_001166264.1.
    NP_001159737.1. NM_001166265.1.
    NP_001159738.1. NM_001166266.1.
    NP_996826.2. NM_206943.2.
    UniGenei Hs.619315.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KSQ NMR - A 1340-1412 [» ]
    ProteinModelPortali Q14766.
    SMRi Q14766. Positions 550-739, 872-1506, 1621-1700.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110230. 5 interactions.
    DIPi DIP-50011N.
    IntActi Q14766. 2 interactions.
    MINTi MINT-1522113.
    STRINGi 9606.ENSP00000346467.

    PTM databases

    PhosphoSitei Q14766.
    UniCarbKBi Q14766.

    Polymorphism databases

    DMDMi 290457687.

    Proteomic databases

    MaxQBi Q14766.
    PaxDbi Q14766.
    PRIDEi Q14766.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000404525 ; ENSP00000385359 ; ENSG00000049323 . [Q14766-3 ]
    ENST00000404816 ; ENSP00000386043 ; ENSG00000049323 . [Q14766-1 ]
    ENST00000407925 ; ENSP00000384091 ; ENSG00000049323 . [Q14766-2 ]
    GeneIDi 4052.
    KEGGi hsa:4052.
    UCSCi uc002rou.3. human. [Q14766-2 ]
    uc002rov.3. human. [Q14766-3 ]
    uc021vft.1. human. [Q14766-1 ]

    Organism-specific databases

    CTDi 4052.
    GeneCardsi GC02P033172.
    HGNCi HGNC:6714. LTBP1.
    HPAi CAB025428.
    HPA005707.
    HPA006221.
    MIMi 150390. gene.
    neXtProti NX_Q14766.
    PharmGKBi PA30477.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG318792.
    KOi K08023.
    OMAi KHPPEAS.
    OrthoDBi EOG7FR7FP.
    PhylomeDBi Q14766.
    TreeFami TF317514.

    Enzyme and pathway databases

    Reactomei REACT_150331. Molecules associated with elastic fibres.

    Miscellaneous databases

    ChiTaRSi LTBP1. human.
    EvolutionaryTracei Q14766.
    GeneWikii LTBP1_(gene).
    GenomeRNAii 4052.
    NextBioi 15874.
    PROi Q14766.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14766.
    Bgeei Q14766.
    CleanExi HS_LTBP1.
    Genevestigatori Q14766.

    Family and domain databases

    Gene3Di 3.90.290.10. 5 hits.
    InterProi 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 PF07645. EGF_CA. 12 hits.
    PF00683. TB. 4 hits.
    [Graphical view ]
    SMARTi SM00181. EGF. 5 hits.
    SM00179. EGF_CA. 13 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 5 hits.
    SSF57581. SSF57581. 4 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 13 hits.
    PS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 11 hits.
    PS50026. EGF_3. 14 hits.
    PS01187. EGF_CA. 15 hits.
    PS51364. TB. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "TGF-beta 1 binding protein: a component of the large latent complex of TGF-beta 1 with multiple repeat sequences."
      Kanzaki T., Olofsson A., Moren A., Wernstedt C., Hellman U., Miyazono K., Claesson-Welsh L., Heldin C.-H.
      Cell 61:1051-1061(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), PARTIAL PROTEIN SEQUENCE, HYDROXYLATION AT ASN-974 AND ASN-1137.
      Tissue: Fibroblast and Platelet.
    2. "Major alternative spliced-form of LTBP1 mRNA in human glomerular endothelial cell."
      Kwak J.H., Shin K.Y., Kim S.I.
      Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM SHORT).
      Tissue: Brain.
    7. "Efficient association of an amino-terminally extended form of human latent transforming growth factor-beta binding protein with the extracellular matrix."
      Olofsson A., Ichijo H., Moren A., ten Dijke P., Miyazono K., Heldin C.-H.
      J. Biol. Chem. 270:31294-31297(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-346.
      Tissue: Blood.
    8. Suzuki Y., Yamashita R., Shirota M., Sakakibara Y., Chiba J., Nakai K., Sugano S.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 684-875 (ISOFORMS 4 AND 5).
    9. "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.
    10. "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.
    11. "Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells."
      Rudd P.M., Downing A.K., Cadene M., Harvey D.J., Wormald M.R., Weir I., Dwek R.A., Rifkin D.B., Gleizes P.E.
      Biochemistry 39:1596-1603(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-1366.
    12. "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, MUTAGENESIS OF 1385-GLU--PRO-1388.
    13. "Latent transforming growth factor beta-binding protein 1 interacts with fibrillin and is a microfibril-associated protein."
      Isogai Z., Ono R.N., Ushiro S., Keene D.R., Chen Y., Mazzieri R., Charbonneau N.L., Reinhardt D.P., Rifkin D.B., Sakai L.Y.
      J. Biol. Chem. 278:2750-2757(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FBN1.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    15. "ADAMTSL2 mutations in geleophysic dysplasia demonstrate a role for ADAMTS-like proteins in TGF-beta bioavailability regulation."
      Le Goff C., Morice-Picard F., Dagoneau N., Wang L.W., Perrot C., Crow Y.J., Bauer F., Flori E., Prost-Squarcioni C., Krakow D., Ge G., Greenspan D.S., Bonnet D., Le Merrer M., Munnich A., Apte S.S., Cormier-Daire V.
      Nat. Genet. 40:1119-1123(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ADAMTSL2.
    16. "Solution structure of the third TB domain from LTBP1 provides insight into assembly of the large latent complex that sequesters latent TGF-beta."
      Lack J., O'Leary J.M., Knott V., Yuan X., Rifkin D.B., Handford P.A., Downing A.K.
      J. Mol. Biol. 334:281-291(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1340-1412, DISULFIDE BONDS.

    Entry informationi

    Entry nameiLTBP1_HUMAN
    AccessioniPrimary (citable) accession number: Q14766
    Secondary accession number(s): A1L3V1
    , P22064, Q53SD8, Q53SF3, Q53SG1, Q59HF7, Q8TD95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: March 2, 2010
    Last modified: October 1, 2014
    This is version 140 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3