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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

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

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.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

BgeeiQ14767.
CleanExiHS_LTBP2.
HS_LTBP3.
ExpressionAtlasiQ14767. baseline and differential.
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, 403-428, 552-736, 856-1624, 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.
GeneTreeiENSGT00760000118806.
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 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MRPRTKARSP GRALRNPWRG FLPLTLALFV GAGHAQRDPV GRYEPAGGDA
60 70 80 90 100
NRLRRPGGSY PAAAAAKVYS LFREQDAPVA GLQPVERAQP GWGSPRRPTE
110 120 130 140 150
AEARRPSRAQ QSRRVQPPAQ TRRSTPLGQQ QPAPRTRAAP ALPRLGTPQR
160 170 180 190 200
SGAAPPTPPR GRLTGRNVCG GQCCPGWTTA NSTNHCIKPV CEPPCQNRGS
210 220 230 240 250
CSRPQLCVCR SGFRGARCEE VIPDEEFDPQ NSRLAPRRWA ERSPNLRRSS
260 270 280 290 300
AAGEGTLARA QPPAPQSPPA PQSPPAGTLS GLSQTHPSQQ HVGLSRTVRL
310 320 330 340 350
HPTATASSQL SSNALPPGPG LEQRDGTQQA VPLEHPSSPW GLNLTEKIKK
360 370 380 390 400
IKIVFTPTIC KQTCARGHCA NSCERGDTTT LYSQGGHGHD PKSGFRIYFC
410 420 430 440 450
QIPCLNGGRC IGRDECWCPA NSTGKFCHLP IPQPDREPPG RGSRPRALLE
460 470 480 490 500
APLKQSTFTL PLSNQLASVN PSLVKVHIHH PPEASVQIHQ VAQVRGGVEE
510 520 530 540 550
ALVENSVETR PPPWLPASPG HSLWDSNNIP ARSGEPPRPL PPAAPRPRGL
560 570 580 590 600
LGRCYLNTVN GQCANPLLEL TTQEDCCGSV GAFWGVTLCA PCPPRPASPV
610 620 630 640 650
IENGQLECPQ GYKRLNLTHC QDINECLTLG LCKDAECVNT RGSYLCTCRP
660 670 680 690 700
GLMLDPSRSR CVSDKAISML QGLCYRSLGP GTCTLPLAQR ITKQICCCSR
710 720 730 740 750
VGKAWGSECE KCPLPGTEAF REICPAGHGY TYASSDIRLS MRKAEEEELA
760 770 780 790 800
RPPREQGQRS SGALPGPAER QPLRVVTDTW LEAGTIPDKG DSQAGQVTTS
810 820 830 840 850
VTHAPAWVTG NATTPPMPEQ GIAEIQEEQV TPSTDVLVTL STPGIDRCAA
860 870 880 890 900
GATNVCGPGT CVNLPDGYRC VCSPGYQLHP SQAYCTDDNE CLRDPCKGKG
910 920 930 940 950
RCINRVGSYS CFCYPGYTLA TSGATQECQD INECEQPGVC SGGQCTNTEG
960 970 980 990 1000
SYHCECDQGY IMVRKGHCQD INECRHPGTC PDGRCVNSPG SYTCLACEEG
1010 1020 1030 1040 1050
YRGQSGSCVD VNECLTPGVC AHGKCTNLEG SFRCSCEQGY EVTSDEKGCQ
1060 1070 1080 1090 1100
DVDECASRAS CPTGLCLNTE GSFACSACEN GYWVNEDGTA CEDLDECAFP
1110 1120 1130 1140 1150
GVCPSGVCTN TAGSFSCKDC DGGYRPSPLG DSCEDVDECE DPQSSCLGGE
1160 1170 1180 1190 1200
CKNTVGSYQC LCPQGFQLAN GTVCEDVNEC MGEEHCAPHG ECLNSHGSFF
1210 1220 1230 1240 1250
CLCAPGFVSA EGGTSCQDVD ECATTDPCVG GHCVNTEGSF NCLCETGFQP
1260 1270 1280 1290 1300
SPESGECVDI DECEDYGDPV CGTWKCENSP GSYRCVLGCQ PGFHMAPNGD
1310 1320 1330 1340 1350
CIDIDECAND TMCGSHGFCD NTDGSFRCLC DQGFEISPSG WDCVDVNECE
1360 1370 1380 1390 1400
LMLAVCGAAL CENVEGSFLC LCASDLEEYD AQEGHCRPRG AGGQSMSEAP
1410 1420 1430 1440 1450
TGDHAPAPTR MDCYSGQKGH APCSSVLGRN TTQAECCCTQ GASWGDACDL
1460 1470 1480 1490 1500
CPSEDSAEFS EICPSGKGYI PVEGAWTFGQ TMYTDADECV IFGPGLCPNG
1510 1520 1530 1540 1550
RCLNTVPGYV CLCNPGFHYD ASHKKCEDHD ECQDLACENG ECVNTEGSFH
1560 1570 1580 1590 1600
CFCSPPLTLD LSQQRCMNST SSTEDLPDHD IHMDICWKKV TNDVCSEPLR
1610 1620 1630 1640 1650
GHRTTYTECC CQDGEAWSQQ CALCPPRSSE VYAQLCNVAR IEAEREAGVH
1660 1670 1680 1690 1700
FRPGYEYGPG PDDLHYSIYG PDGAPFYNYL GPEDTVPEPA FPNTAGHSAD
1710 1720 1730 1740 1750
RTPILESPLQ PSELQPHYVA SHPEPPAGFE GLQAEECGIL NGCENGRCVR
1760 1770 1780 1790 1800
VREGYTCDCF EGFQLDAAHM ACVDVNECDD LNGPAVLCVH GYCENTEGSY
1810 1820
RCHCSPGYVA EAGPPHCTAK E
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, 403-428, 552-736, 856-1624, 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.
GeneTreei ENSGT00760000118806.
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

Bgeei Q14767.
CleanExi HS_LTBP2.
HS_LTBP3.
ExpressionAtlasi Q14767. baseline and differential.
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: October 29, 2014
This is version 137 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