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Q14767 (LTBP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Latent-transforming growth factor beta-binding protein 2

Short name=LTBP-2
Gene names
Name:LTBP2
Synonyms:C14orf141, LTBP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1821 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

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. 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FBLN5Q9UBX52EBI-1546118,EBI-947897

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 18211786Latent-transforming growth factor beta-binding protein 2
PRO_0000007643

Regions

Domain187 – 21933EGF-like 1
Domain396 – 42833EGF-like 2
Domain552 – 60453TB 1
Domain622 – 66241EGF-like 3; calcium-binding Potential
Domain672 – 72453TB 2
Domain844 – 88643EGF-like 4
Domain887 – 92943EGF-like 5; calcium-binding Potential
Domain930 – 96940EGF-like 6; calcium-binding Potential
Domain970 – 100940EGF-like 7; calcium-binding Potential
Domain1010 – 105041EGF-like 8; calcium-binding Potential
Domain1051 – 109242EGF-like 9; calcium-binding Potential
Domain1093 – 113442EGF-like 10; calcium-binding Potential
Domain1135 – 117541EGF-like 11; calcium-binding Potential
Domain1176 – 121742EGF-like 12; calcium-binding Potential
Domain1218 – 125841EGF-like 13; calcium-binding Potential
Domain1259 – 130244EGF-like 14; calcium-binding Potential
Domain1303 – 134442EGF-like 15; calcium-binding Potential
Domain1345 – 138743EGF-like 16; calcium-binding Potential
Domain1411 – 146353TB 3
Domain1485 – 152743EGF-like 17; calcium-binding Potential
Domain1528 – 156740EGF-like 18; calcium-binding Potential
Domain1584 – 163653TB 4
Domain1733 – 177341EGF-like 19; calcium-binding Potential
Domain1774 – 181845EGF-like 20; calcium-binding Potential
Region94 – 11522Heparin-binding
Region232 – 24918Heparin-binding
Region344 – 35411Heparin-binding
Motif375 – 3773Cell attachment site Potential
Compositional bias856 – 1372517Cys-rich

Amino acid modifications

Glycosylation1811N-linked (GlcNAc...) Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Glycosylation4211N-linked (GlcNAc...) Potential
Glycosylation6161N-linked (GlcNAc...) Potential
Glycosylation8111N-linked (GlcNAc...) Potential
Glycosylation11701N-linked (GlcNAc...) Potential
Glycosylation13091N-linked (GlcNAc...) Potential
Glycosylation14301N-linked (GlcNAc...) Potential
Glycosylation15681N-linked (GlcNAc...) Potential
Disulfide bond191 ↔ 201 By similarity
Disulfide bond195 ↔ 207 By similarity
Disulfide bond209 ↔ 218 By similarity
Disulfide bond400 ↔ 410 By similarity
Disulfide bond404 ↔ 416 By similarity
Disulfide bond418 ↔ 427 By similarity
Disulfide bond626 ↔ 637 By similarity
Disulfide bond632 ↔ 646 By similarity
Disulfide bond648 ↔ 661 By similarity
Disulfide bond848 ↔ 861 By similarity
Disulfide bond856 ↔ 870 By similarity
Disulfide bond872 ↔ 885 By similarity
Disulfide bond891 ↔ 902 By similarity
Disulfide bond896 ↔ 911 By similarity
Disulfide bond913 ↔ 928 By similarity
Disulfide bond934 ↔ 945 By similarity
Disulfide bond940 ↔ 954 By similarity
Disulfide bond956 ↔ 968 By similarity
Disulfide bond974 ↔ 985 By similarity
Disulfide bond980 ↔ 994 By similarity
Disulfide bond997 ↔ 1008 By similarity
Disulfide bond1014 ↔ 1025 By similarity
Disulfide bond1020 ↔ 1034 By similarity
Disulfide bond1036 ↔ 1049 By similarity
Disulfide bond1055 ↔ 1066 By similarity
Disulfide bond1061 ↔ 1075 By similarity
Disulfide bond1078 ↔ 1091 By similarity
Disulfide bond1097 ↔ 1108 By similarity
Disulfide bond1103 ↔ 1117 By similarity
Disulfide bond1120 ↔ 1133 By similarity
Disulfide bond1139 ↔ 1151 By similarity
Disulfide bond1146 ↔ 1160 By similarity
Disulfide bond1162 ↔ 1174 By similarity
Disulfide bond1180 ↔ 1192 By similarity
Disulfide bond1186 ↔ 1201 By similarity
Disulfide bond1203 ↔ 1216 By similarity
Disulfide bond1222 ↔ 1233 By similarity
Disulfide bond1228 ↔ 1242 By similarity
Disulfide bond1244 ↔ 1257 By similarity
Disulfide bond1263 ↔ 1276 By similarity
Disulfide bond1271 ↔ 1285 By similarity
Disulfide bond1289 ↔ 1301 By similarity
Disulfide bond1307 ↔ 1319 By similarity
Disulfide bond1313 ↔ 1328 By similarity
Disulfide bond1330 ↔ 1343 By similarity
Disulfide bond1349 ↔ 1361 By similarity
Disulfide bond1356 ↔ 1370 By similarity
Disulfide bond1372 ↔ 1386 By similarity
Disulfide bond1489 ↔ 1502 By similarity
Disulfide bond1497 ↔ 1511 By similarity
Disulfide bond1513 ↔ 1526 By similarity
Disulfide bond1532 ↔ 1542 By similarity
Disulfide bond1537 ↔ 1551 By similarity
Disulfide bond1553 ↔ 1566 By similarity
Disulfide bond1737 ↔ 1748 By similarity
Disulfide bond1743 ↔ 1757 By similarity
Disulfide bond1759 ↔ 1772 By similarity
Disulfide bond1778 ↔ 1793 By similarity
Disulfide bond1788 ↔ 1802 By similarity
Disulfide bond1804 ↔ 1817 By similarity

Natural variations

Natural variant371R → M.
Corresponds to variant rs934996 [ dbSNP | Ensembl ].
VAR_059270
Natural variant3191P → Q.
Corresponds to variant rs2304707 [ dbSNP | Ensembl ].
VAR_055752
Natural variant5911P → S.
Corresponds to variant rs2196862 [ dbSNP | Ensembl ].
VAR_060337
Natural variant11771V → M in WMS3. Ref.10
VAR_068647

Experimental info

Mutagenesis1449 – 14502DL → EIFP: Gain-of-function. Forms a complex with TGFB1. Ref.4
Sequence conflict8971K → Q in CAA86030. Ref.1
Sequence conflict14431S → T in CAA86030. Ref.1
Sequence conflict16151E → K in CAA86030. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q14767 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 3D6952B39885E1A6

FASTA1,821195,052
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
CCDSCCDS9831.1.
PIRA55494.
RefSeqNP_000419.1. NM_000428.2.
UniGeneHs.512776.
Hs.597522.

3D structure databases

ProteinModelPortalQ14767.
SMRQ14767. Positions 171-221, 552-736, 855-1624, 1735-1819.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ14767. 3 interactions.
MINTMINT-2806977.
STRING9606.ENSP00000261978.

PTM databases

PhosphoSiteQ14767.

Polymorphism databases

DMDM296439311.

Proteomic databases

PaxDbQ14767.
PRIDEQ14767.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261978; ENSP00000261978; ENSG00000119681.
GeneID4053.
KEGGhsa:4053.
UCSCuc001xqa.3. human.

Organism-specific databases

CTD4053.
GeneCardsGC14M074965.
GeneReviewsLTBP2.
HGNCHGNC:6715. LTBP2.
HPAHPA003415.
MIM251750. phenotype.
602091. gene.
613086. phenotype.
614819. phenotype.
neXtProtNX_Q14767.
Orphanet98976. Congenital glaucoma.
238763. Glaucoma secondary to spherophakia/ectopia lentis and megalocornea.
3449. Weill-Marchesani syndrome.
PharmGKBPA164741922.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG318792.
HOGENOMHOG000293153.
HOVERGENHBG052370.
InParanoidQ14767.
KOK08023.
OMAYFCQIPC.
OrthoDBEOG7FR7FP.
PhylomeDBQ14767.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ14767.
BgeeQ14767.
CleanExHS_LTBP2.
HS_LTBP3.
GenevestigatorQ14767.

Family and domain databases

Gene3D3.90.290.10. 5 hits.
InterProIPR000742. 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]
PfamPF00008. EGF. 1 hit.
PF07645. EGF_CA. 17 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTSM00181. EGF. 4 hits.
SM00179. EGF_CA. 16 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 5 hits.
SSF57581. SSF57581. 5 hits.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

ChiTaRSLTBP2. human.
GeneWikiLTBP2.
GenomeRNAi4053.
NextBio15880.
PROQ14767.
SOURCESearch...

Entry information

Entry nameLTBP2_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM