Q14767 (LTBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Latent-transforming growth factor beta-binding protein 2
Short name=LTBP-2

Gene names

Name:	LTBP2
Synonyms:	C14orf141, LTBP3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1821 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play an integral structural role in elastic-fiber architectural organization and/or assembly.
Subunit structure	Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex. Interacts with SDC4. Ref.4 Ref.9
Subcellular location	Secreted By similarity. Note: Localized in nuchal ligament and aorta to the fibrillin-containing, microfibrillar component of elastic fibers By similarity.
Tissue specificity	Expressed in lung, weakly expressed in heart, placenta, liver and skeletal muscle.
Domain	Associates covalently with small latent TGF-beta complex via Repeat B and Repeat C By similarity.
Post-translational modification	Contains hydroxylated asparagine residues By similarity.
Involvement in disease	Primary congenital glaucoma 3D (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. Ref.7 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. Ref.8 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. Ref.10
Sequence similarities	Belongs to the LTBP family. Contains 20 EGF-like domains. Contains 4 TB (TGF-beta binding) domains.
Caution	Ref.1 reported that a complex is formed with TGFB1. Ref.4 has shown that there is no association with TGFB1.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation Dwarfism Glaucoma
Domain	EGF-like domain Repeat Signal
Ligand	Growth factor binding Heparin-binding
PTM	Disulfide bond Glycoprotein Hydroxylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein secretion Traceable author statement Ref.2. Source: ProtInc protein targeting Traceable author statement Ref.1. Source: ProtInc transforming growth factor beta receptor signaling pathway Traceable author statement Ref.2. Source: ProtInc
Cellular_component	extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB proteinaceous extracellular matrix Traceable author statement Ref.1. Source: ProtInc
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro heparin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 35	35	Potential
	Chain	36 – 1821	1786	Latent-transforming growth factor beta-binding protein 2		PRO_0000007643
Regions
	Domain	187 – 219	33	EGF-like 1
	Domain	396 – 428	33	EGF-like 2
	Domain	552 – 604	53	TB 1
	Domain	622 – 662	41	EGF-like 3; calcium-binding Potential
	Domain	672 – 724	53	TB 2
	Domain	844 – 886	43	EGF-like 4
	Domain	887 – 929	43	EGF-like 5; calcium-binding Potential
	Domain	930 – 969	40	EGF-like 6; calcium-binding Potential
	Domain	970 – 1009	40	EGF-like 7; calcium-binding Potential
	Domain	1010 – 1050	41	EGF-like 8; calcium-binding Potential
	Domain	1051 – 1092	42	EGF-like 9; calcium-binding Potential
	Domain	1093 – 1134	42	EGF-like 10; calcium-binding Potential
	Domain	1135 – 1175	41	EGF-like 11; calcium-binding Potential
	Domain	1176 – 1217	42	EGF-like 12; calcium-binding Potential
	Domain	1218 – 1258	41	EGF-like 13; calcium-binding Potential
	Domain	1259 – 1302	44	EGF-like 14; calcium-binding Potential
	Domain	1303 – 1344	42	EGF-like 15; calcium-binding Potential
	Domain	1345 – 1387	43	EGF-like 16; calcium-binding Potential
	Domain	1411 – 1463	53	TB 3
	Domain	1485 – 1527	43	EGF-like 17; calcium-binding Potential
	Domain	1528 – 1567	40	EGF-like 18; calcium-binding Potential
	Domain	1584 – 1636	53	TB 4
	Domain	1733 – 1773	41	EGF-like 19; calcium-binding Potential
	Domain	1774 – 1818	45	EGF-like 20; calcium-binding Potential
	Region	94 – 115	22	Heparin-binding
	Region	232 – 249	18	Heparin-binding
	Region	344 – 354	11	Heparin-binding
	Motif	375 – 377	3	Cell attachment site Potential
	Compositional bias	856 – 1372	517	Cys-rich
Amino acid modifications
	Modified residue	506	1	Phosphoserine By similarity
	Glycosylation	181	1	N-linked (GlcNAc...) Potential
	Glycosylation	343	1	N-linked (GlcNAc...) Potential
	Glycosylation	421	1	N-linked (GlcNAc...) Potential
	Glycosylation	616	1	N-linked (GlcNAc...) Potential
	Glycosylation	811	1	N-linked (GlcNAc...) Potential
	Glycosylation	1170	1	N-linked (GlcNAc...) Potential
	Glycosylation	1309	1	N-linked (GlcNAc...) Potential
	Glycosylation	1430	1	N-linked (GlcNAc...) Potential
	Glycosylation	1568	1	N-linked (GlcNAc...) Potential
	Disulfide bond	191 ↔ 201		By similarity
	Disulfide bond	195 ↔ 207		By similarity
	Disulfide bond	209 ↔ 218		By similarity
	Disulfide bond	400 ↔ 410		By similarity
	Disulfide bond	404 ↔ 416		By similarity
	Disulfide bond	418 ↔ 427		By similarity
	Disulfide bond	626 ↔ 637		By similarity
	Disulfide bond	632 ↔ 646		By similarity
	Disulfide bond	648 ↔ 661		By similarity
	Disulfide bond	848 ↔ 861		By similarity
	Disulfide bond	856 ↔ 870		By similarity
	Disulfide bond	872 ↔ 885		By similarity
	Disulfide bond	891 ↔ 902		By similarity
	Disulfide bond	896 ↔ 911		By similarity
	Disulfide bond	913 ↔ 928		By similarity
	Disulfide bond	934 ↔ 945		By similarity
	Disulfide bond	940 ↔ 954		By similarity
	Disulfide bond	956 ↔ 968		By similarity
	Disulfide bond	974 ↔ 985		By similarity
	Disulfide bond	980 ↔ 994		By similarity
	Disulfide bond	997 ↔ 1008		By similarity
	Disulfide bond	1014 ↔ 1025		By similarity
	Disulfide bond	1020 ↔ 1034		By similarity
	Disulfide bond	1036 ↔ 1049		By similarity
	Disulfide bond	1055 ↔ 1066		By similarity
	Disulfide bond	1061 ↔ 1075		By similarity
	Disulfide bond	1078 ↔ 1091		By similarity
	Disulfide bond	1097 ↔ 1108		By similarity
	Disulfide bond	1103 ↔ 1117		By similarity
	Disulfide bond	1120 ↔ 1133		By similarity
	Disulfide bond	1139 ↔ 1151		By similarity
	Disulfide bond	1146 ↔ 1160		By similarity
	Disulfide bond	1162 ↔ 1174		By similarity
	Disulfide bond	1180 ↔ 1192		By similarity
	Disulfide bond	1186 ↔ 1201		By similarity
	Disulfide bond	1203 ↔ 1216		By similarity
	Disulfide bond	1222 ↔ 1233		By similarity
	Disulfide bond	1228 ↔ 1242		By similarity
	Disulfide bond	1244 ↔ 1257		By similarity
	Disulfide bond	1263 ↔ 1276		By similarity
	Disulfide bond	1271 ↔ 1285		By similarity
	Disulfide bond	1289 ↔ 1301		By similarity
	Disulfide bond	1307 ↔ 1319		By similarity
	Disulfide bond	1313 ↔ 1328		By similarity
	Disulfide bond	1330 ↔ 1343		By similarity
	Disulfide bond	1349 ↔ 1361		By similarity
	Disulfide bond	1356 ↔ 1370		By similarity
	Disulfide bond	1372 ↔ 1386		By similarity
	Disulfide bond	1489 ↔ 1502		By similarity
	Disulfide bond	1497 ↔ 1511		By similarity
	Disulfide bond	1513 ↔ 1526		By similarity
	Disulfide bond	1532 ↔ 1542		By similarity
	Disulfide bond	1537 ↔ 1551		By similarity
	Disulfide bond	1553 ↔ 1566		By similarity
	Disulfide bond	1737 ↔ 1748		By similarity
	Disulfide bond	1743 ↔ 1757		By similarity
	Disulfide bond	1759 ↔ 1772		By similarity
	Disulfide bond	1778 ↔ 1793		By similarity
	Disulfide bond	1788 ↔ 1802		By similarity
	Disulfide bond	1804 ↔ 1817		By similarity
Natural variations
	Natural variant	37	1	R → M. Corresponds to variant rs934996 [ dbSNP | Ensembl ].		VAR_059270
	Natural variant	319	1	P → Q. Corresponds to variant rs2304707 [ dbSNP | Ensembl ].		VAR_055752
	Natural variant	591	1	P → S. Corresponds to variant rs2196862 [ dbSNP | Ensembl ].		VAR_060337
	Natural variant	1177	1	V → M in WMS3. Ref.10		VAR_068647
Experimental info
	Mutagenesis	1449 – 1450	2	DL → EIFP: Gain-of-function. Forms a complex with TGFB1. Ref.4
	Sequence conflict	897	1	K → Q in CAA86030. Ref.1
	Sequence conflict	1443	1	S → T in CAA86030. Ref.1
	Sequence conflict	1615	1	E → K in CAA86030. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q14767 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 3D6952B39885E1A6	FASTA	1,821	195,052
	10 20 30 40 50 60 MRPRTKARSP GRALRNPWRG FLPLTLALFV GAGHAQRDPV GRYEPAGGDA NRLRRPGGSY 70 80 90 100 110 120 PAAAAAKVYS LFREQDAPVA GLQPVERAQP GWGSPRRPTE AEARRPSRAQ QSRRVQPPAQ 130 140 150 160 170 180 TRRSTPLGQQ QPAPRTRAAP ALPRLGTPQR SGAAPPTPPR GRLTGRNVCG GQCCPGWTTA 190 200 210 220 230 240 NSTNHCIKPV CEPPCQNRGS CSRPQLCVCR SGFRGARCEE VIPDEEFDPQ NSRLAPRRWA 250 260 270 280 290 300 ERSPNLRRSS AAGEGTLARA QPPAPQSPPA PQSPPAGTLS GLSQTHPSQQ HVGLSRTVRL 310 320 330 340 350 360 HPTATASSQL SSNALPPGPG LEQRDGTQQA VPLEHPSSPW GLNLTEKIKK IKIVFTPTIC 370 380 390 400 410 420 KQTCARGHCA NSCERGDTTT LYSQGGHGHD PKSGFRIYFC QIPCLNGGRC IGRDECWCPA 430 440 450 460 470 480 NSTGKFCHLP IPQPDREPPG RGSRPRALLE APLKQSTFTL PLSNQLASVN PSLVKVHIHH 490 500 510 520 530 540 PPEASVQIHQ VAQVRGGVEE ALVENSVETR PPPWLPASPG HSLWDSNNIP ARSGEPPRPL 550 560 570 580 590 600 PPAAPRPRGL LGRCYLNTVN GQCANPLLEL TTQEDCCGSV GAFWGVTLCA PCPPRPASPV 610 620 630 640 650 660 IENGQLECPQ GYKRLNLTHC QDINECLTLG LCKDAECVNT RGSYLCTCRP GLMLDPSRSR 670 680 690 700 710 720 CVSDKAISML QGLCYRSLGP GTCTLPLAQR ITKQICCCSR VGKAWGSECE KCPLPGTEAF 730 740 750 760 770 780 REICPAGHGY TYASSDIRLS MRKAEEEELA RPPREQGQRS SGALPGPAER QPLRVVTDTW 790 800 810 820 830 840 LEAGTIPDKG DSQAGQVTTS VTHAPAWVTG NATTPPMPEQ GIAEIQEEQV TPSTDVLVTL 850 860 870 880 890 900 STPGIDRCAA GATNVCGPGT CVNLPDGYRC VCSPGYQLHP SQAYCTDDNE CLRDPCKGKG 910 920 930 940 950 960 RCINRVGSYS CFCYPGYTLA TSGATQECQD INECEQPGVC SGGQCTNTEG SYHCECDQGY 970 980 990 1000 1010 1020 IMVRKGHCQD INECRHPGTC PDGRCVNSPG SYTCLACEEG YRGQSGSCVD VNECLTPGVC 1030 1040 1050 1060 1070 1080 AHGKCTNLEG SFRCSCEQGY EVTSDEKGCQ DVDECASRAS CPTGLCLNTE GSFACSACEN 1090 1100 1110 1120 1130 1140 GYWVNEDGTA CEDLDECAFP GVCPSGVCTN TAGSFSCKDC DGGYRPSPLG DSCEDVDECE 1150 1160 1170 1180 1190 1200 DPQSSCLGGE CKNTVGSYQC LCPQGFQLAN GTVCEDVNEC MGEEHCAPHG ECLNSHGSFF 1210 1220 1230 1240 1250 1260 CLCAPGFVSA EGGTSCQDVD ECATTDPCVG GHCVNTEGSF NCLCETGFQP SPESGECVDI 1270 1280 1290 1300 1310 1320 DECEDYGDPV CGTWKCENSP GSYRCVLGCQ PGFHMAPNGD CIDIDECAND TMCGSHGFCD 1330 1340 1350 1360 1370 1380 NTDGSFRCLC DQGFEISPSG WDCVDVNECE LMLAVCGAAL CENVEGSFLC LCASDLEEYD 1390 1400 1410 1420 1430 1440 AQEGHCRPRG AGGQSMSEAP TGDHAPAPTR MDCYSGQKGH APCSSVLGRN TTQAECCCTQ 1450 1460 1470 1480 1490 1500 GASWGDACDL CPSEDSAEFS EICPSGKGYI PVEGAWTFGQ TMYTDADECV IFGPGLCPNG 1510 1520 1530 1540 1550 1560 RCLNTVPGYV CLCNPGFHYD ASHKKCEDHD ECQDLACENG ECVNTEGSFH CFCSPPLTLD 1570 1580 1590 1600 1610 1620 LSQQRCMNST SSTEDLPDHD IHMDICWKKV TNDVCSEPLR GHRTTYTECC CQDGEAWSQQ 1630 1640 1650 1660 1670 1680 CALCPPRSSE VYAQLCNVAR IEAEREAGVH FRPGYEYGPG PDDLHYSIYG PDGAPFYNYL 1690 1700 1710 1720 1730 1740 GPEDTVPEPA FPNTAGHSAD RTPILESPLQ PSELQPHYVA SHPEPPAGFE GLQAEECGIL 1750 1760 1770 1780 1790 1800 NGCENGRCVR VREGYTCDCF EGFQLDAAHM ACVDVNECDD LNGPAVLCVH GYCENTEGSY 1810 1820 RCHCSPGYVA EAGPPHCTAK E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Null mutations in LTBP2 cause primary congenital glaucoma." Ali M., McKibbin M., Booth A., Parry D.A., Jain P., Riazuddin S.A., Hejtmancik J.F., Khan S.N., Firasat S., Shires M., Gilmour D.F., Towns K., Murphy A.L., Azmanov D., Tournev I., Cherninkova S., Jafri H., Raashid Y. , Toomes C., Craig J., Mackey D.A., Kalaydjieva L., Riazuddin S., Inglehearn C.F. Am. J. Hum. Genet. 84:664-671(2009) [PubMed] [Europe PMC] [Abstract] 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]	"LTBP2 mutations cause Weill-Marchesani and Weill-Marchesani-like syndrome and affect disruptions in the extracellular matrix." Haji-Seyed-Javadi R., Jelodari-Mamaghani S., Paylakhi S.H., Yazdani S., Nilforushan N., Fan J.B., Klotzle B., Mahmoudi M.J., Ebrahimian M.J., Chelich N., Taghiabadi E., Kamyab K., Boileau C., Paisan-Ruiz C., Ronaghi M., Elahi E. Hum. Mutat. 33:1182-1187(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT WMS3 MET-1177.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z37976 mRNA. Translation: CAA86030.1. S82451 mRNA. Translation: AAB37459.1. AC013451 Genomic DNA. Translation: AAF87081.1.
IPI	IPI00292150.
PIR	A55494.
RefSeq	NP_000419.1. NM_000428.2.
UniGene	Hs.512776. Hs.597522.
3D structure databases
ProteinModelPortal	Q14767.
SMR	Q14767. Positions 171-221, 552-736, 856-1624, 1735-1819.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14767. 2 interactions.
MINT	MINT-2806977.
STRING	9606.ENSP00000261978.
PTM databases
PhosphoSite	Q14767.
Polymorphism databases
DMDM	296439311.
Proteomic databases
PaxDb	Q14767.
PRIDE	Q14767.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261978; ENSP00000261978; ENSG00000119681.
GeneID	4053.
KEGG	hsa:4053.
UCSC	uc001xqa.3. human.
Organism-specific databases
CTD	4053.
GeneCards	GC14M074965.
HGNC	HGNC:6715. LTBP2.
HPA	HPA003415.
MIM	251750. phenotype. 602091. gene. 613086. phenotype. 614819. phenotype.
neXtProt	NX_Q14767.
Orphanet	98976. Congenital glaucoma. 238763. Megalocornea - spherophakia - secondary glaucoma.
PharmGKB	PA164741922.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG318792.
HOGENOM	HOG000293153.
HOVERGEN	HBG052370.
InParanoid	Q14767.
KO	K08023.
OMA	GRDECWC.
OrthoDB	EOG46Q6RN.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	Q14767.
Bgee	Q14767.
CleanEx	HS_LTBP2. HS_LTBP3.
Genevestigator	Q14767.
GermOnline	ENSG00000119681. Homo sapiens.
Family and domain databases
Gene3D	3.90.290.10. 5 hits.
InterPro	IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR009030. Growth_fac_rcpt. IPR017878. TB_dom. [Graphical view]
Pfam	PF00008. EGF. 1 hit. PF07645. EGF_CA. 17 hits. PF00683. TB. 4 hits. [Graphical view]
SMART	SM00181. EGF. 4 hits. SM00179. EGF_CA. 16 hits. [Graphical view]
SUPFAM	SSF57581. Fibril-assoc. 4 hits. SSF57184. Grow_fac_recept. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
ChiTaRS	LTBP2. human.
GenomeRNAi	4053.
NextBio	15880.
SOURCE	Search...

Entry information

Entry name

LTBP2_HUMAN

Accession

Primary (citable) accession number: Q14767
Secondary accession number(s): Q99907, Q9NS51

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.