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Protein

Latent-transforming growth factor beta-binding protein 2

Gene

LTBP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • extracellular fibril organization Source: MGI
  • protein secretion Source: ProtInc
  • protein targeting Source: ProtInc
  • transforming growth factor beta receptor signaling pathway Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Growth factor binding, Heparin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000119681-MONOMER.
ReactomeiR-HSA-2129379. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:6715. LTBP2.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular space Source: BHF-UCL
  • intracellular Source: GOC
  • proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Glaucoma 3, primary congenital, D (GLC3D)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:613086
Microspherophakia and/or megalocornea, with ectopia lentis and with or without secondary glaucoma (MSPKA)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:251750
Weill-Marchesani syndrome 3 (WMS3)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma.
See also OMIM:614819
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0686471177V → M in WMS3. 1 PublicationCorresponds to variant rs137854856dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1449 – 1450DL → EIFP: Gain-of-function. Forms a complex with TGFB1. 1 Publication2

Keywords - Diseasei

Disease mutation, Dwarfism, Glaucoma

Organism-specific databases

DisGeNETi4053.
MalaCardsiLTBP2.
MIMi251750. phenotype.
613086. phenotype.
614819. phenotype.
OpenTargetsiENSG00000119681.
Orphaneti98976. Congenital glaucoma.
238763. Glaucoma secondary to spherophakia/ectopia lentis and megalocornea.
3449. Weill-Marchesani syndrome.
PharmGKBiPA164741922.

Polymorphism and mutation databases

BioMutaiLTBP2.
DMDMi296439311.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 35By similarityAdd BLAST35
ChainiPRO_000000764336 – 1821Latent-transforming growth factor beta-binding protein 2Add BLAST1786

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi181N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi191 ↔ 201PROSITE-ProRule annotation
Disulfide bondi195 ↔ 207PROSITE-ProRule annotation
Disulfide bondi209 ↔ 218PROSITE-ProRule annotation
Glycosylationi343N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi400 ↔ 410PROSITE-ProRule annotation
Disulfide bondi404 ↔ 416PROSITE-ProRule annotation
Disulfide bondi418 ↔ 427PROSITE-ProRule annotation
Glycosylationi421N-linked (GlcNAc...)Sequence analysis1
Modified residuei506PhosphoserineBy similarity1
Disulfide bondi554 ↔ 576PROSITE-ProRule annotation
Disulfide bondi563 ↔ 589PROSITE-ProRule annotation
Disulfide bondi577 ↔ 592PROSITE-ProRule annotation
Glycosylationi616N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi626 ↔ 637PROSITE-ProRule annotation
Disulfide bondi632 ↔ 646PROSITE-ProRule annotation
Disulfide bondi648 ↔ 661PROSITE-ProRule annotation
Disulfide bondi674 ↔ 696PROSITE-ProRule annotation
Disulfide bondi683 ↔ 709PROSITE-ProRule annotation
Disulfide bondi697 ↔ 712PROSITE-ProRule annotation
Disulfide bondi698 ↔ 724PROSITE-ProRule annotation
Glycosylationi811N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi1170N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi1309N-linked (GlcNAc...)Sequence analysis1
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
Disulfide bondi1413 ↔ 1436PROSITE-ProRule annotation
Disulfide bondi1423 ↔ 1448PROSITE-ProRule annotation
Glycosylationi1430N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1437 ↔ 1451PROSITE-ProRule annotation
Disulfide bondi1438 ↔ 1463PROSITE-ProRule annotation
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
Glycosylationi1568N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1586 ↔ 1609PROSITE-ProRule annotation
Disulfide bondi1595 ↔ 1621PROSITE-ProRule annotation
Disulfide bondi1610 ↔ 1624PROSITE-ProRule annotation
Disulfide bondi1611 ↔ 1636PROSITE-ProRule annotation
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

N-Glycosylated.1 Publication
Contains hydroxylated asparagine residues.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

PaxDbiQ14767.
PeptideAtlasiQ14767.
PRIDEiQ14767.

PTM databases

iPTMnetiQ14767.
PhosphoSitePlusiQ14767.

Expressioni

Tissue specificityi

Expressed in the aorta (at protein level). Expressed in lung, weakly expressed in heart, placenta, liver and skeletal muscle.2 Publications

Gene expression databases

BgeeiENSG00000119681.
CleanExiHS_LTBP2.
HS_LTBP3.
ExpressionAtlasiQ14767. baseline and differential.
GenevisibleiQ14767. HS.

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 (PubMed:7798248). Interacts with SDC4 (PubMed:20382221). Interacts (via C-terminal domain) with FBN1 (via N-terminal domain) in a Ca(+2)-dependent manner (PubMed:17293099).3 Publications

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ14767.
SMRiQ14767.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini187 – 219EGF-like 1PROSITE-ProRule annotationAdd BLAST33
Domaini396 – 428EGF-like 2PROSITE-ProRule annotationAdd BLAST33
Domaini552 – 604TB 1PROSITE-ProRule annotationAdd BLAST53
Domaini622 – 662EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini672 – 724TB 2PROSITE-ProRule annotationAdd BLAST53
Domaini844 – 886EGF-like 4PROSITE-ProRule annotationAdd BLAST43
Domaini887 – 929EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini930 – 969EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini970 – 1009EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini1010 – 1050EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1051 – 1092EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1093 – 1134EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1135 – 1175EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1176 – 1217EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1218 – 1258EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1259 – 1302EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST44
Domaini1303 – 1344EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1345 – 1387EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1411 – 1463TB 3PROSITE-ProRule annotationAdd BLAST53
Domaini1485 – 1527EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1528 – 1567EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini1584 – 1636TB 4PROSITE-ProRule annotationAdd BLAST53
Domaini1733 – 1773EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1774 – 1818EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni94 – 115Heparin-bindingAdd BLAST22
Regioni232 – 249Heparin-bindingAdd BLAST18
Regioni344 – 354Heparin-bindingAdd BLAST11
Regioni1639 – 1821C-terminal domain1 PublicationAdd BLAST183

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi375 – 377Cell attachment siteSequence analysis3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi856 – 1372Cys-richAdd BLAST517

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.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IR7H. Eukaryota.
ENOG410XSTY. LUCA.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiQ14767.
KOiK08023.
OMAiGHDPKSG.
OrthoDBiEOG091G008S.
PhylomeDBiQ14767.

Family and domain databases

Gene3Di3.90.290.10. 5 hits.
InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF07645. EGF_CA. 17 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 20 hits.
SM00179. EGF_CA. 18 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

        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)DescriptionActionsGraphical viewLength
Sequence conflicti897K → Q in CAA86030 (PubMed:7798248).Curated1
Sequence conflicti1443S → T in CAA86030 (PubMed:7798248).Curated1
Sequence conflicti1615E → K in CAA86030 (PubMed:7798248).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05927037R → M.Corresponds to variant rs934996dbSNPEnsembl.1
Natural variantiVAR_055752319P → Q.Corresponds to variant rs2304707dbSNPEnsembl.1
Natural variantiVAR_060337591P → S.Corresponds to variant rs2196862dbSNPEnsembl.1
Natural variantiVAR_0686471177V → M in WMS3. 1 PublicationCorresponds to variant rs137854856dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ14767.
SMRiQ14767.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ14767.
PhosphoSitePlusiQ14767.

Polymorphism and mutation databases

BioMutaiLTBP2.
DMDMi296439311.

Proteomic databases

PaxDbiQ14767.
PeptideAtlasiQ14767.
PRIDEiQ14767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261978; ENSP00000261978; ENSG00000119681.
GeneIDi4053.
KEGGihsa:4053.
UCSCiuc001xqa.4. human.

Organism-specific databases

CTDi4053.
DisGeNETi4053.
GeneCardsiLTBP2.
GeneReviewsiLTBP2.
HGNCiHGNC:6715. LTBP2.
HPAiHPA003415.
MalaCardsiLTBP2.
MIMi251750. phenotype.
602091. gene.
613086. phenotype.
614819. phenotype.
neXtProtiNX_Q14767.
OpenTargetsiENSG00000119681.
Orphaneti98976. Congenital glaucoma.
238763. Glaucoma secondary to spherophakia/ectopia lentis and megalocornea.
3449. Weill-Marchesani syndrome.
PharmGKBiPA164741922.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IR7H. Eukaryota.
ENOG410XSTY. LUCA.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiQ14767.
KOiK08023.
OMAiGHDPKSG.
OrthoDBiEOG091G008S.
PhylomeDBiQ14767.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000119681-MONOMER.
ReactomeiR-HSA-2129379. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSiLTBP2. human.
GeneWikiiLTBP2.
GenomeRNAii4053.
PROiQ14767.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000119681.
CleanExiHS_LTBP2.
HS_LTBP3.
ExpressionAtlasiQ14767. baseline and differential.
GenevisibleiQ14767. HS.

Family and domain databases

Gene3Di3.90.290.10. 5 hits.
InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF07645. EGF_CA. 17 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 20 hits.
SM00179. EGF_CA. 18 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 154 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.