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Q14767

- LTBP2_HUMAN

UniProt

Q14767 - LTBP2_HUMAN

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Protein

Latent-transforming growth factor beta-binding protein 2

Gene
LTBP2, C14orf141, LTBP3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 – 3535 Reviewed predictionAdd
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...) Reviewed prediction
Disulfide bondi191 ↔ 201 By similarity
Disulfide bondi195 ↔ 207 By similarity
Disulfide bondi209 ↔ 218 By similarity
Glycosylationi343 – 3431N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi400 ↔ 410 By similarity
Disulfide bondi404 ↔ 416 By similarity
Disulfide bondi418 ↔ 427 By similarity
Glycosylationi421 – 4211N-linked (GlcNAc...) Reviewed prediction
Glycosylationi616 – 6161N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi626 ↔ 637 By similarity
Disulfide bondi632 ↔ 646 By similarity
Disulfide bondi648 ↔ 661 By similarity
Glycosylationi811 – 8111N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi848 ↔ 861 By similarity
Disulfide bondi856 ↔ 870 By similarity
Disulfide bondi872 ↔ 885 By similarity
Disulfide bondi891 ↔ 902 By similarity
Disulfide bondi896 ↔ 911 By similarity
Disulfide bondi913 ↔ 928 By similarity
Disulfide bondi934 ↔ 945 By similarity
Disulfide bondi940 ↔ 954 By similarity
Disulfide bondi956 ↔ 968 By similarity
Disulfide bondi974 ↔ 985 By similarity
Disulfide bondi980 ↔ 994 By similarity
Disulfide bondi997 ↔ 1008 By similarity
Disulfide bondi1014 ↔ 1025 By similarity
Disulfide bondi1020 ↔ 1034 By similarity
Disulfide bondi1036 ↔ 1049 By similarity
Disulfide bondi1055 ↔ 1066 By similarity
Disulfide bondi1061 ↔ 1075 By similarity
Disulfide bondi1078 ↔ 1091 By similarity
Disulfide bondi1097 ↔ 1108 By similarity
Disulfide bondi1103 ↔ 1117 By similarity
Disulfide bondi1120 ↔ 1133 By similarity
Disulfide bondi1139 ↔ 1151 By similarity
Disulfide bondi1146 ↔ 1160 By similarity
Disulfide bondi1162 ↔ 1174 By similarity
Glycosylationi1170 – 11701N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1180 ↔ 1192 By similarity
Disulfide bondi1186 ↔ 1201 By similarity
Disulfide bondi1203 ↔ 1216 By similarity
Disulfide bondi1222 ↔ 1233 By similarity
Disulfide bondi1228 ↔ 1242 By similarity
Disulfide bondi1244 ↔ 1257 By similarity
Disulfide bondi1263 ↔ 1276 By similarity
Disulfide bondi1271 ↔ 1285 By similarity
Disulfide bondi1289 ↔ 1301 By similarity
Disulfide bondi1307 ↔ 1319 By similarity
Glycosylationi1309 – 13091N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1313 ↔ 1328 By similarity
Disulfide bondi1330 ↔ 1343 By similarity
Disulfide bondi1349 ↔ 1361 By similarity
Disulfide bondi1356 ↔ 1370 By similarity
Disulfide bondi1372 ↔ 1386 By similarity
Glycosylationi1430 – 14301N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1489 ↔ 1502 By similarity
Disulfide bondi1497 ↔ 1511 By similarity
Disulfide bondi1513 ↔ 1526 By similarity
Disulfide bondi1532 ↔ 1542 By similarity
Disulfide bondi1537 ↔ 1551 By similarity
Disulfide bondi1553 ↔ 1566 By similarity
Glycosylationi1568 – 15681N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1737 ↔ 1748 By similarity
Disulfide bondi1743 ↔ 1757 By similarity
Disulfide bondi1759 ↔ 1772 By similarity
Disulfide bondi1778 ↔ 1793 By similarity
Disulfide bondi1788 ↔ 1802 By similarity
Disulfide bondi1804 ↔ 1817 By similarity

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 SDC4.2 Publications

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.

Family & Domainsi

Domains and Repeats

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

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.
Contains 20 EGF-like domains.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti897 – 8971K → Q in CAA86030. 1 Publication
Sequence conflicti1443 – 14431S → T in CAA86030. 1 Publication
Sequence conflicti1615 – 16151E → K in CAA86030. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 135 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

1 Publication reported that a complex is formed with TGFB1. 1 Publication has shown that there is no association with TGFB1.

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

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