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Q14767

- LTBP2_HUMAN

UniProt

Q14767 - LTBP2_HUMAN

Protein

Latent-transforming growth factor beta-binding protein 2

Gene

LTBP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    May play an integral structural role in elastic-fiber architectural organization and/or assembly.

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. heparin binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. protein secretion Source: ProtInc
    2. protein targeting Source: ProtInc
    3. transforming growth factor beta receptor signaling pathway Source: ProtInc

    Keywords - Ligandi

    Growth factor binding, Heparin-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 2
    Short name:
    LTBP-2
    Gene namesi
    Name:LTBP2
    Synonyms:C14orf141, LTBP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:6715. LTBP2.

    Subcellular locationi

    Secreted By similarity
    Note: Localized in nuchal ligament and aorta to the fibrillin-containing, microfibrillar component of elastic fibers.By similarity

    GO - Cellular componenti

    1. extracellular space Source: BHF-UCL
    2. extracellular vesicular exosome Source: UniProtKB
    3. proteinaceous extracellular matrix Source: ProtInc

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Glaucoma 3, primary congenital, D (GLC3D) [MIM:613086]: An autosomal recessive form of primary congenital glaucoma (PCG). PCG is characterized by marked increase of intraocular pressure at birth or early childhood, large ocular globes (buphthalmos) and corneal edema. It results from developmental defects of the trabecular meshwork and anterior chamber angle of the eye that prevent adequate drainage of aqueous humor.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Microspherophakia and/or megalocornea, with ectopia lentis and with or without secondary glaucoma (MSPKA) [MIM:251750]: A rare disease characterized by smaller and more spherical lenses than normal bilaterally, an increased anteroposterior thickness of the lens, and highly myopic eyes. Lens dislocation or subluxation may occur, leading to defective accommodation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Weill-Marchesani syndrome 3 (WMS3) [MIM:614819]: A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1177 – 11771V → M in WMS3. 1 Publication
    VAR_068647

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1449 – 14502DL → EIFP: Gain-of-function. Forms a complex with TGFB1. 1 Publication

    Keywords - Diseasei

    Disease mutation, Dwarfism, Glaucoma

    Organism-specific databases

    MIMi251750. phenotype.
    613086. phenotype.
    614819. phenotype.
    Orphaneti98976. Congenital glaucoma.
    238763. Glaucoma secondary to spherophakia/ectopia lentis and megalocornea.
    3449. Weill-Marchesani syndrome.
    PharmGKBiPA164741922.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535Sequence AnalysisAdd
    BLAST
    Chaini36 – 18211786Latent-transforming growth factor beta-binding protein 2PRO_0000007643Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi191 ↔ 201PROSITE-ProRule annotation
    Disulfide bondi195 ↔ 207PROSITE-ProRule annotation
    Disulfide bondi209 ↔ 218PROSITE-ProRule annotation
    Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi400 ↔ 410PROSITE-ProRule annotation
    Disulfide bondi404 ↔ 416PROSITE-ProRule annotation
    Disulfide bondi418 ↔ 427PROSITE-ProRule annotation
    Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi616 – 6161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi626 ↔ 637PROSITE-ProRule annotation
    Disulfide bondi632 ↔ 646PROSITE-ProRule annotation
    Disulfide bondi648 ↔ 661PROSITE-ProRule annotation
    Glycosylationi811 – 8111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi848 ↔ 861PROSITE-ProRule annotation
    Disulfide bondi856 ↔ 870PROSITE-ProRule annotation
    Disulfide bondi872 ↔ 885PROSITE-ProRule annotation
    Disulfide bondi891 ↔ 902PROSITE-ProRule annotation
    Disulfide bondi896 ↔ 911PROSITE-ProRule annotation
    Disulfide bondi913 ↔ 928PROSITE-ProRule annotation
    Disulfide bondi934 ↔ 945PROSITE-ProRule annotation
    Disulfide bondi940 ↔ 954PROSITE-ProRule annotation
    Disulfide bondi956 ↔ 968PROSITE-ProRule annotation
    Disulfide bondi974 ↔ 985PROSITE-ProRule annotation
    Disulfide bondi980 ↔ 994PROSITE-ProRule annotation
    Disulfide bondi997 ↔ 1008PROSITE-ProRule annotation
    Disulfide bondi1014 ↔ 1025PROSITE-ProRule annotation
    Disulfide bondi1020 ↔ 1034PROSITE-ProRule annotation
    Disulfide bondi1036 ↔ 1049PROSITE-ProRule annotation
    Disulfide bondi1055 ↔ 1066PROSITE-ProRule annotation
    Disulfide bondi1061 ↔ 1075PROSITE-ProRule annotation
    Disulfide bondi1078 ↔ 1091PROSITE-ProRule annotation
    Disulfide bondi1097 ↔ 1108PROSITE-ProRule annotation
    Disulfide bondi1103 ↔ 1117PROSITE-ProRule annotation
    Disulfide bondi1120 ↔ 1133PROSITE-ProRule annotation
    Disulfide bondi1139 ↔ 1151PROSITE-ProRule annotation
    Disulfide bondi1146 ↔ 1160PROSITE-ProRule annotation
    Disulfide bondi1162 ↔ 1174PROSITE-ProRule annotation
    Glycosylationi1170 – 11701N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1180 ↔ 1192PROSITE-ProRule annotation
    Disulfide bondi1186 ↔ 1201PROSITE-ProRule annotation
    Disulfide bondi1203 ↔ 1216PROSITE-ProRule annotation
    Disulfide bondi1222 ↔ 1233PROSITE-ProRule annotation
    Disulfide bondi1228 ↔ 1242PROSITE-ProRule annotation
    Disulfide bondi1244 ↔ 1257PROSITE-ProRule annotation
    Disulfide bondi1263 ↔ 1276PROSITE-ProRule annotation
    Disulfide bondi1271 ↔ 1285PROSITE-ProRule annotation
    Disulfide bondi1289 ↔ 1301PROSITE-ProRule annotation
    Disulfide bondi1307 ↔ 1319PROSITE-ProRule annotation
    Glycosylationi1309 – 13091N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1313 ↔ 1328PROSITE-ProRule annotation
    Disulfide bondi1330 ↔ 1343PROSITE-ProRule annotation
    Disulfide bondi1349 ↔ 1361PROSITE-ProRule annotation
    Disulfide bondi1356 ↔ 1370PROSITE-ProRule annotation
    Disulfide bondi1372 ↔ 1386PROSITE-ProRule annotation
    Glycosylationi1430 – 14301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1489 ↔ 1502PROSITE-ProRule annotation
    Disulfide bondi1497 ↔ 1511PROSITE-ProRule annotation
    Disulfide bondi1513 ↔ 1526PROSITE-ProRule annotation
    Disulfide bondi1532 ↔ 1542PROSITE-ProRule annotation
    Disulfide bondi1537 ↔ 1551PROSITE-ProRule annotation
    Disulfide bondi1553 ↔ 1566PROSITE-ProRule annotation
    Glycosylationi1568 – 15681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1737 ↔ 1748PROSITE-ProRule annotation
    Disulfide bondi1743 ↔ 1757PROSITE-ProRule annotation
    Disulfide bondi1759 ↔ 1772PROSITE-ProRule annotation
    Disulfide bondi1778 ↔ 1793PROSITE-ProRule annotation
    Disulfide bondi1788 ↔ 1802PROSITE-ProRule annotation
    Disulfide bondi1804 ↔ 1817PROSITE-ProRule annotation

    Post-translational modificationi

    Contains hydroxylated asparagine residues.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiQ14767.
    PRIDEiQ14767.

    PTM databases

    PhosphoSiteiQ14767.

    Expressioni

    Tissue specificityi

    Expressed in lung, weakly expressed in heart, placenta, liver and skeletal muscle.

    Gene expression databases

    ArrayExpressiQ14767.
    BgeeiQ14767.
    CleanExiHS_LTBP2.
    HS_LTBP3.
    GenevestigatoriQ14767.

    Organism-specific databases

    HPAiHPA003415.

    Interactioni

    Subunit structurei

    Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex. Interacts with SDC4.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FBLN5Q9UBX52EBI-1546118,EBI-947897

    Protein-protein interaction databases

    IntActiQ14767. 3 interactions.
    MINTiMINT-2806977.
    STRINGi9606.ENSP00000261978.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14767.
    SMRiQ14767. Positions 171-221, 552-736, 855-1624, 1735-1819.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini187 – 21933EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini396 – 42833EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini552 – 60453TB 1Add
    BLAST
    Domaini622 – 66241EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini672 – 72453TB 2Add
    BLAST
    Domaini844 – 88643EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini887 – 92943EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini930 – 96940EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini970 – 100940EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1010 – 105041EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1051 – 109242EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1093 – 113442EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1135 – 117541EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1176 – 121742EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1218 – 125841EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1259 – 130244EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1303 – 134442EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1345 – 138743EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1411 – 146353TB 3Add
    BLAST
    Domaini1485 – 152743EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1528 – 156740EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1584 – 163653TB 4Add
    BLAST
    Domaini1733 – 177341EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1774 – 181845EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni94 – 11522Heparin-bindingAdd
    BLAST
    Regioni232 – 24918Heparin-bindingAdd
    BLAST
    Regioni344 – 35411Heparin-bindingAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi375 – 3773Cell attachment siteSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi856 – 1372517Cys-richAdd
    BLAST

    Domaini

    Associates covalently with small latent TGF-beta complex via Repeat B and Repeat C.By similarity

    Sequence similaritiesi

    Belongs to the LTBP family.Curated
    Contains 20 EGF-like domains.PROSITE-ProRule annotation
    Contains 4 TB (TGF-beta binding) domains.Curated

    Keywords - Domaini

    EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG318792.
    HOGENOMiHOG000293153.
    HOVERGENiHBG052370.
    InParanoidiQ14767.
    KOiK08023.
    OMAiYFCQIPC.
    OrthoDBiEOG7FR7FP.
    PhylomeDBiQ14767.

    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]
    PfamiPF00008. EGF. 1 hit.
    PF07645. EGF_CA. 17 hits.
    PF00683. TB. 4 hits.
    [Graphical view]
    SMARTiSM00181. EGF. 4 hits.
    SM00179. EGF_CA. 16 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 5 hits.
    SSF57581. SSF57581. 5 hits.
    PROSITEiPS00010. ASX_HYDROXYL. 13 hits.
    PS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 11 hits.
    PS50026. EGF_3. 15 hits.
    PS01187. EGF_CA. 16 hits.
    PS51364. TB. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q14767-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPRTKARSP GRALRNPWRG FLPLTLALFV GAGHAQRDPV GRYEPAGGDA     50
    NRLRRPGGSY PAAAAAKVYS LFREQDAPVA GLQPVERAQP GWGSPRRPTE 100
    AEARRPSRAQ QSRRVQPPAQ TRRSTPLGQQ QPAPRTRAAP ALPRLGTPQR 150
    SGAAPPTPPR GRLTGRNVCG GQCCPGWTTA NSTNHCIKPV CEPPCQNRGS 200
    CSRPQLCVCR SGFRGARCEE VIPDEEFDPQ NSRLAPRRWA ERSPNLRRSS 250
    AAGEGTLARA QPPAPQSPPA PQSPPAGTLS GLSQTHPSQQ HVGLSRTVRL 300
    HPTATASSQL SSNALPPGPG LEQRDGTQQA VPLEHPSSPW GLNLTEKIKK 350
    IKIVFTPTIC KQTCARGHCA NSCERGDTTT LYSQGGHGHD PKSGFRIYFC 400
    QIPCLNGGRC IGRDECWCPA NSTGKFCHLP IPQPDREPPG RGSRPRALLE 450
    APLKQSTFTL PLSNQLASVN PSLVKVHIHH PPEASVQIHQ VAQVRGGVEE 500
    ALVENSVETR PPPWLPASPG HSLWDSNNIP ARSGEPPRPL PPAAPRPRGL 550
    LGRCYLNTVN GQCANPLLEL TTQEDCCGSV GAFWGVTLCA PCPPRPASPV 600
    IENGQLECPQ GYKRLNLTHC QDINECLTLG LCKDAECVNT RGSYLCTCRP 650
    GLMLDPSRSR CVSDKAISML QGLCYRSLGP GTCTLPLAQR ITKQICCCSR 700
    VGKAWGSECE KCPLPGTEAF REICPAGHGY TYASSDIRLS MRKAEEEELA 750
    RPPREQGQRS SGALPGPAER QPLRVVTDTW LEAGTIPDKG DSQAGQVTTS 800
    VTHAPAWVTG NATTPPMPEQ GIAEIQEEQV TPSTDVLVTL STPGIDRCAA 850
    GATNVCGPGT CVNLPDGYRC VCSPGYQLHP SQAYCTDDNE CLRDPCKGKG 900
    RCINRVGSYS CFCYPGYTLA TSGATQECQD INECEQPGVC SGGQCTNTEG 950
    SYHCECDQGY IMVRKGHCQD INECRHPGTC PDGRCVNSPG SYTCLACEEG 1000
    YRGQSGSCVD VNECLTPGVC AHGKCTNLEG SFRCSCEQGY EVTSDEKGCQ 1050
    DVDECASRAS CPTGLCLNTE GSFACSACEN GYWVNEDGTA CEDLDECAFP 1100
    GVCPSGVCTN TAGSFSCKDC DGGYRPSPLG DSCEDVDECE DPQSSCLGGE 1150
    CKNTVGSYQC LCPQGFQLAN GTVCEDVNEC MGEEHCAPHG ECLNSHGSFF 1200
    CLCAPGFVSA EGGTSCQDVD ECATTDPCVG GHCVNTEGSF NCLCETGFQP 1250
    SPESGECVDI DECEDYGDPV CGTWKCENSP GSYRCVLGCQ PGFHMAPNGD 1300
    CIDIDECAND TMCGSHGFCD NTDGSFRCLC DQGFEISPSG WDCVDVNECE 1350
    LMLAVCGAAL CENVEGSFLC LCASDLEEYD AQEGHCRPRG AGGQSMSEAP 1400
    TGDHAPAPTR MDCYSGQKGH APCSSVLGRN TTQAECCCTQ GASWGDACDL 1450
    CPSEDSAEFS EICPSGKGYI PVEGAWTFGQ TMYTDADECV IFGPGLCPNG 1500
    RCLNTVPGYV CLCNPGFHYD ASHKKCEDHD ECQDLACENG ECVNTEGSFH 1550
    CFCSPPLTLD LSQQRCMNST SSTEDLPDHD IHMDICWKKV TNDVCSEPLR 1600
    GHRTTYTECC CQDGEAWSQQ CALCPPRSSE VYAQLCNVAR IEAEREAGVH 1650
    FRPGYEYGPG PDDLHYSIYG PDGAPFYNYL GPEDTVPEPA FPNTAGHSAD 1700
    RTPILESPLQ PSELQPHYVA SHPEPPAGFE GLQAEECGIL NGCENGRCVR 1750
    VREGYTCDCF EGFQLDAAHM ACVDVNECDD LNGPAVLCVH GYCENTEGSY 1800
    RCHCSPGYVA EAGPPHCTAK E 1821
    Length:1,821
    Mass (Da):195,052
    Last modified:May 18, 2010 - v3
    Checksum:i3D6952B39885E1A6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti897 – 8971K → Q in CAA86030. (PubMed:7798248)Curated
    Sequence conflicti1443 – 14431S → T in CAA86030. (PubMed:7798248)Curated
    Sequence conflicti1615 – 16151E → K in CAA86030. (PubMed:7798248)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371R → M.
    Corresponds to variant rs934996 [ dbSNP | Ensembl ].
    VAR_059270
    Natural varianti319 – 3191P → Q.
    Corresponds to variant rs2304707 [ dbSNP | Ensembl ].
    VAR_055752
    Natural varianti591 – 5911P → S.
    Corresponds to variant rs2196862 [ dbSNP | Ensembl ].
    VAR_060337
    Natural varianti1177 – 11771V → M in WMS3. 1 Publication
    VAR_068647

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z37976 mRNA. Translation: CAA86030.1.
    S82451 mRNA. Translation: AAB37459.1.
    AC013451 Genomic DNA. Translation: AAF87081.1.
    CCDSiCCDS9831.1.
    PIRiA55494.
    RefSeqiNP_000419.1. NM_000428.2.
    UniGeneiHs.512776.
    Hs.597522.

    Genome annotation databases

    EnsembliENST00000261978; ENSP00000261978; ENSG00000119681.
    GeneIDi4053.
    KEGGihsa:4053.
    UCSCiuc001xqa.3. human.

    Polymorphism databases

    DMDMi296439311.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z37976 mRNA. Translation: CAA86030.1 .
    S82451 mRNA. Translation: AAB37459.1 .
    AC013451 Genomic DNA. Translation: AAF87081.1 .
    CCDSi CCDS9831.1.
    PIRi A55494.
    RefSeqi NP_000419.1. NM_000428.2.
    UniGenei Hs.512776.
    Hs.597522.

    3D structure databases

    ProteinModelPortali Q14767.
    SMRi Q14767. Positions 171-221, 552-736, 855-1624, 1735-1819.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q14767. 3 interactions.
    MINTi MINT-2806977.
    STRINGi 9606.ENSP00000261978.

    PTM databases

    PhosphoSitei Q14767.

    Polymorphism databases

    DMDMi 296439311.

    Proteomic databases

    PaxDbi Q14767.
    PRIDEi Q14767.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261978 ; ENSP00000261978 ; ENSG00000119681 .
    GeneIDi 4053.
    KEGGi hsa:4053.
    UCSCi uc001xqa.3. human.

    Organism-specific databases

    CTDi 4053.
    GeneCardsi GC14M074965.
    GeneReviewsi LTBP2.
    HGNCi HGNC:6715. LTBP2.
    HPAi HPA003415.
    MIMi 251750. phenotype.
    602091. gene.
    613086. phenotype.
    614819. phenotype.
    neXtProti NX_Q14767.
    Orphaneti 98976. Congenital glaucoma.
    238763. Glaucoma secondary to spherophakia/ectopia lentis and megalocornea.
    3449. Weill-Marchesani syndrome.
    PharmGKBi PA164741922.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG318792.
    HOGENOMi HOG000293153.
    HOVERGENi HBG052370.
    InParanoidi Q14767.
    KOi K08023.
    OMAi YFCQIPC.
    OrthoDBi EOG7FR7FP.
    PhylomeDBi Q14767.

    Enzyme and pathway databases

    Reactomei REACT_150331. Molecules associated with elastic fibres.

    Miscellaneous databases

    ChiTaRSi LTBP2. human.
    GeneWikii LTBP2.
    GenomeRNAii 4053.
    NextBioi 15880.
    PROi Q14767.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14767.
    Bgeei Q14767.
    CleanExi HS_LTBP2.
    HS_LTBP3.
    Genevestigatori Q14767.

    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 PF00008. EGF. 1 hit.
    PF07645. EGF_CA. 17 hits.
    PF00683. TB. 4 hits.
    [Graphical view ]
    SMARTi SM00181. EGF. 4 hits.
    SM00179. EGF_CA. 16 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 5 hits.
    SSF57581. SSF57581. 5 hits.
    PROSITEi PS00010. ASX_HYDROXYL. 13 hits.
    PS00022. EGF_1. 2 hits.
    PS01186. EGF_2. 11 hits.
    PS50026. EGF_3. 15 hits.
    PS01187. EGF_CA. 16 hits.
    PS51364. TB. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and characterization of LTBP-2, a novel latent transforming growth factor-beta-binding protein."
      Moren A., Olofsson A., Stenman G., Sahlin P., Kanzaki T., Claesson-Welsh L., ten Dijke P., Miyazono K., Heldin C.
      J. Biol. Chem. 269:32469-32478(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
      Tissue: Foreskin fibroblast.
    2. "Analysis of the human gene encoding latent transforming growth factor-beta-binding protein-2."
      Bashir M.M., Han M.-D., Abrams W.R., Tucker T., Ma R.-I., Gibson M., Ritty T., Mecham R., Rosenbloom J.
      Int. J. Biochem. Cell Biol. 28:531-542(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: LACK OF INTERACTION WITH TGFB1, MUTAGENESIS OF 1449-ASP-LEU-1450.
    5. "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.
    6. "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.
    7. Cited for: INVOLVEMENT IN GLC3D.
    8. "A homozygous mutation in LTBP2 causes isolated microspherophakia."
      Kumar A., Duvvari M.R., Prabhakaran V.C., Shetty J.S., Murthy G.J., Blanton S.H.
      Hum. Genet. 128:365-371(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN MSPKA.
    9. "LTBP-2 has multiple heparin/heparan sulfate binding sites."
      Parsi M.K., Adams J.R., Whitelock J., Gibson M.A.
      Matrix Biol. 29:393-401(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: HEPARIN-BINDING REGIONS, INTERACTION WITH SDC4.
    10. Cited for: VARIANT WMS3 MET-1177.

    Entry informationi

    Entry nameiLTBP2_HUMAN
    AccessioniPrimary (citable) accession number: Q14767
    Secondary accession number(s): Q99907, Q9NS51
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 136 of the entry and version 3 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

    Caution

    PubMed:7798248 reported that a complex is formed with TGFB1. PubMed:10930463 has shown that there is no association with TGFB1.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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