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Q14766 (LTBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Latent-transforming growth factor beta-binding protein 1

Short name=LTBP-1
Alternative name(s):
Transforming growth factor beta-1-binding protein 1
Short name=TGF-beta1-BP-1
Gene names
Name:LTBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1721 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in the assembly, secretion and targeting of TGFB1 to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGFB1. May have a structural role in the extra cellular matrix (ECM).

Subunit structure

The large latent complex of TGFB1 from platelets is composed of the TGFB1 molecule non-covalently associated with a disulfide-bonded complex of a dimer of the N-terminal propeptide of the TGFB1 precursor and LTBP1. LTBP1 does not bind directly to active TGFB1. Binds to FBN1 and FBN2. Interacts with ADAMTSL2. Ref.12 Ref.13 Ref.15

Subcellular location

Secreted.

Tissue specificity

Isoform Long is found in fibroblasts.

Domain

Associates covalently with small latent TGF-beta complex via domain TB 3.

Post-translational modification

Contains hydroxylated asparagine residues.

Isoform Short N-terminus is blocked.

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains By similarity.

Two intrachain disulfide bonds from the TB3 domain are rearranged upon TGFB1 binding, and form interchain bonds with TGFB1 propeptide, anchoring it to the extracellular matrix.

Sequence similarities

Belongs to the LTBP family.

Contains 18 EGF-like domains.

Contains 4 TB (TGF-beta binding) domains.

Sequence caution

The sequence BAD92038.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q14766-1)

Also known as: LTBP-1L;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Short (identifier: Q14766-2)

Also known as: LTBP-1S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-326: Missing.
     327-345: EGSFPLRYVQDQVAAPFQL → MDTKLMCLLFFFSLPPLLV
Isoform 3 (identifier: Q14766-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-326: Missing.
     327-345: EGSFPLRYVQDQVAAPFQL → MDTKLMCLLFFFSLPPLLV
     724-776: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q14766-4)

The sequence of this isoform differs from the canonical sequence as follows:
     839-840: PV → PGI
Isoform 5 (identifier: Q14766-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-326: Missing.
     327-345: EGSFPLRYVQDQVAAPFQL → MDTKLMCLLFFFSLPPLLV
     839-840: PV → PGI
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 17211698Latent-transforming growth factor beta-binding protein 1
PRO_0000007635

Regions

Domain187 – 21933EGF-like 1
Domain399 – 43133EGF-like 2
Domain557 – 60953TB 1
Domain626 – 66338EGF-like 3; calcium-binding Potential
Domain677 – 72953TB 2
Domain873 – 91038EGF-like 4; calcium-binding Potential
Domain915 – 95642EGF-like 5; calcium-binding Potential
Domain957 – 99741EGF-like 6; calcium-binding Potential
Domain998 – 103740EGF-like 7; calcium-binding Potential
Domain1038 – 107841EGF-like 8; calcium-binding Potential
Domain1079 – 111941EGF-like 9; calcium-binding Potential
Domain1120 – 116041EGF-like 10; calcium-binding Potential
Domain1161 – 120141EGF-like 11; calcium-binding Potential
Domain1202 – 124342EGF-like 12; calcium-binding Potential
Domain1244 – 128138EGF-like 13; calcium-binding Potential
Domain1286 – 132843EGF-like 14; calcium-binding Potential
Domain1347 – 140155TB 3
Domain1424 – 146643EGF-like 15; calcium-binding Potential
Domain1467 – 150337EGF-like 16; calcium-binding Potential
Domain1524 – 157754TB 4
Domain1621 – 165737EGF-like 17
Domain1662 – 170645EGF-like 18; calcium-binding Potential
Motif1174 – 11763Cell attachment site Potential
Compositional bias100 – 13031Pro-rich

Amino acid modifications

Modified residue9741(3R)-3-hydroxyasparagine
Modified residue11371(3R)-3-hydroxyasparagine
Modified residue15971Phosphoserine Ref.14
Glycosylation3471N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Glycosylation4241N-linked (GlcNAc...) Potential
Glycosylation6201N-linked (GlcNAc...) Potential
Glycosylation11971N-linked (GlcNAc...) Potential
Glycosylation12501N-linked (GlcNAc...) Potential
Glycosylation13661N-linked (GlcNAc...) Ref.11
CAR_000184
Disulfide bond191 ↔ 201 By similarity
Disulfide bond195 ↔ 207 By similarity
Disulfide bond209 ↔ 218 By similarity
Disulfide bond403 ↔ 413 By similarity
Disulfide bond407 ↔ 419 By similarity
Disulfide bond421 ↔ 430 By similarity
Disulfide bond630 ↔ 641 By similarity
Disulfide bond636 ↔ 650 By similarity
Disulfide bond652 ↔ 665 By similarity
Disulfide bond877 ↔ 889 By similarity
Disulfide bond884 ↔ 898 By similarity
Disulfide bond900 ↔ 913 By similarity
Disulfide bond919 ↔ 931 By similarity
Disulfide bond926 ↔ 940 By similarity
Disulfide bond942 ↔ 955 By similarity
Disulfide bond961 ↔ 972 By similarity
Disulfide bond967 ↔ 981 By similarity
Disulfide bond984 ↔ 996 By similarity
Disulfide bond1002 ↔ 1013 By similarity
Disulfide bond1008 ↔ 1022 By similarity
Disulfide bond1025 ↔ 1036 By similarity
Disulfide bond1042 ↔ 1053 By similarity
Disulfide bond1048 ↔ 1062 By similarity
Disulfide bond1064 ↔ 1077 By similarity
Disulfide bond1083 ↔ 1094 By similarity
Disulfide bond1089 ↔ 1103 By similarity
Disulfide bond1105 ↔ 1118 By similarity
Disulfide bond1124 ↔ 1135 By similarity
Disulfide bond1130 ↔ 1144 By similarity
Disulfide bond1146 ↔ 1159 By similarity
Disulfide bond1165 ↔ 1177 By similarity
Disulfide bond1172 ↔ 1186 By similarity
Disulfide bond1188 ↔ 1200 By similarity
Disulfide bond1206 ↔ 1218 By similarity
Disulfide bond1212 ↔ 1227 By similarity
Disulfide bond1229 ↔ 1242 By similarity
Disulfide bond1248 ↔ 1260 By similarity
Disulfide bond1254 ↔ 1269 By similarity
Disulfide bond1349 ↔ 1372 Ref.16
Disulfide bond1359 ↔ 1384Alternate; alternate Ref.16
Disulfide bond1359Interchain (with C-33 in TGFB1); alternate By similarity
Disulfide bond1373 ↔ 1389 Ref.16
Disulfide bond1374 ↔ 1401 Ref.16
Disulfide bond1384Interchain (with C-33 in TGFB1); alternate By similarity
Disulfide bond1471 ↔ 1482 By similarity
Disulfide bond1477 ↔ 1491 By similarity
Disulfide bond1625 ↔ 1636 By similarity
Disulfide bond1631 ↔ 1645 By similarity
Disulfide bond1666 ↔ 1681 By similarity
Disulfide bond1676 ↔ 1690 By similarity
Disulfide bond1692 ↔ 1705 By similarity

Natural variations

Alternative sequence1 – 326326Missing in isoform Short, isoform 3 and isoform 5.
VSP_036963
Alternative sequence327 – 34519EGSFP…APFQL → MDTKLMCLLFFFSLPPLLV in isoform Short, isoform 3 and isoform 5.
VSP_036964
Alternative sequence724 – 77653Missing in isoform 3.
VSP_036965
Alternative sequence839 – 8402PV → PGI in isoform 4 and isoform 5.
VSP_040125

Experimental info

Mutagenesis1385 – 13884EIFP → DL: Loss of binding to TGFB1. Ref.12
Sequence conflict501R → AS in AAA96327. Ref.7
Sequence conflict6911H → Y in AAA61160. Ref.1
Sequence conflict6941S → P in BP291349. Ref.8
Sequence conflict7101Missing in AAA61160. Ref.1
Sequence conflict7101Missing in AAM03124. Ref.2
Sequence conflict7441R → M in BP291349. Ref.8
Sequence conflict792 – 7943PGV → ARS in AAA61160. Ref.1
Sequence conflict792 – 7943PGV → ARS in AAM03124. Ref.2
Sequence conflict8311T → A in AAA61160. Ref.1
Sequence conflict13781V → A in AAA61160. Ref.1
Sequence conflict13781V → A in AAM03124. Ref.2
Sequence conflict13781V → A in BAD92038. Ref.3
Sequence conflict13781V → A in EAX00437. Ref.5
Sequence conflict13781V → A in AAI30290. Ref.6
Sequence conflict16481F → L in AAA61160. Ref.1
Sequence conflict16481F → L in AAM03124. Ref.2
Sequence conflict16611V → F in AAA61160. Ref.1

Secondary structure

................... 1721
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long (LTBP-1L) [UniParc].

Last modified March 2, 2010. Version 4.
Checksum: 432489CAC3023754

FASTA1,721186,796
        10         20         30         40         50         60 
MAGAWLRWGL LLWAGLLASS AHGRLRRITY VVHPGPGLAA GALPLSGPPR SRTFNVALNA 

        70         80         90        100        110        120 
RYSRSSAAAG APSRASPGVP SERTRRTSKP GGAALQGLRP PPPPPPEPAR PAVPGGQLHP 

       130        140        150        160        170        180 
NPGGHPAAAP FTKQGRQVVR SKVPQETQSG GGSRLQVHQK QQLQGVNVCG GRCCHGWSKA 

       190        200        210        220        230        240 
PGSQRCTKPS CVPPCQNGGM CLRPQLCVCK PGTKGKACET IAAQDTSSPV FGGQSPGAAS 

       250        260        270        280        290        300 
SWGPPEQAAK HTSSKKADTL PRVSPVAQMT LTLKPKPSVG LPQQIHSQVT PLSSQSVVIH 

       310        320        330        340        350        360 
HGQTQEYVLK PKYFPAQKGI SGEQSTEGSF PLRYVQDQVA APFQLSNHTG RIKVVFTPSI 

       370        380        390        400        410        420 
CKVTCTKGSC QNSCEKGNTT TLISENGHAA DTLTATNFRV VICHLPCMNG GQCSSRDKCQ 

       430        440        450        460        470        480 
CPPNFTGKLC QIPVHGASVP KLYQHSQQPG KALGTHVIHS THTLPLTVTS QQGVKVKFPP 

       490        500        510        520        530        540 
NIVNIHVKHP PEASVQIHQV SRIDGPTGQK TKEAQPGQSQ VSYQGLPVQK TQTIHSTYSH 

       550        560        570        580        590        600 
QQVIPHVYPV AAKTQLGRCF QETIGSQCGK ALPGLSKQED CCGTVGTSWG FNKCQKCPKK 

       610        620        630        640        650        660 
PSYHGYNQMM ECLPGYKRVN NTFCQDINEC QLQGVCPNGE CLNTMGSYRC TCKIGFGPDP 

       670        680        690        700        710        720 
TFSSCVPDPP VISEEKGPCY RLVSSGRQCM HPLSVHLTKQ LCCCSVGKAW GPHCEKCPLP 

       730        740        750        760        770        780 
GTAAFKEICP GGMGYTVSGV HRRRPIHHHV GKGPVFVKPK NTQPVAKSTH PPPLPAKEEP 

       790        800        810        820        830        840 
VEALTFSREH GPGVAEPEVA TAPPEKEIPS LDQEKTKLEP GQPQLSPGIS TIHLHPQFPV 

       850        860        870        880        890        900 
VIEKTSPPVP VEVAPEASTS SASQVIAPTQ VTEINECTVN PDICGAGHCI NLPVRYTCIC 

       910        920        930        940        950        960 
YEGYRFSEQQ RKCVDIDECT QVQHLCSQGR CENTEGSFLC ICPAGFMASE EGTNCIDVDE 

       970        980        990       1000       1010       1020 
CLRPDVCGEG HCVNTVGAFR CEYCDSGYRM TQRGRCEDID ECLNPSTCPD EQCVNSPGSY 

      1030       1040       1050       1060       1070       1080 
QCVPCTEGFR GWNGQCLDVD ECLEPNVCAN GDCSNLEGSY MCSCHKGYTR TPDHKHCRDI 

      1090       1100       1110       1120       1130       1140 
DECQQGNLCV NGQCKNTEGS FRCTCGQGYQ LSAAKDQCED IDECQHRHLC AHGQCRNTEG 

      1150       1160       1170       1180       1190       1200 
SFQCVCDQGY RASGLGDHCE DINECLEDKS VCQRGDCINT AGSYDCTCPD GFQLDDNKTC 

      1210       1220       1230       1240       1250       1260 
QDINECEHPG LCGPQGECLN TEGSFHCVCQ QGFSISADGR TCEDIDECVN NTVCDSHGFC 

      1270       1280       1290       1300       1310       1320 
DNTAGSFRCL CYQGFQAPQD GQGCVDVNEC ELLSGVCGEA FCENVEGSFL CVCADENQEY 

      1330       1340       1350       1360       1370       1380 
SPMTGQCRSR TSTDLDVDVD QPKEEKKECY YNLNDASLCD NVLAPNVTKQ ECCCTSGVGW 

      1390       1400       1410       1420       1430       1440 
GDNCEIFPCP VLGTAEFTEM CPKGKGFVPA GESSSEAGGE NYKDADECLL FGQEICKNGF 

      1450       1460       1470       1480       1490       1500 
CLNTRPGYEC YCKQGTYYDP VKLQCFDMDE CQDPSSCIDG QCVNTEGSYN CFCTHPMVLD 

      1510       1520       1530       1540       1550       1560 
ASEKRCIRPA ESNEQIEETD VYQDLCWEHL SDEYVCSRPL VGKQTTYTEC CCLYGEAWGM 

      1570       1580       1590       1600       1610       1620 
QCALCPLKDS DDYAQLCNIP VTGRRQPYGR DALVDFSEQY TPEADPYFIQ DRFLNSFEEL 

      1630       1640       1650       1660       1670       1680 
QAEECGILNG CENGRCVRVQ EGYTCDCFDG YHLDTAKMTC VDVNECDELN NRMSLCKNAK 

      1690       1700       1710       1720 
CINTDGSYKC LCLPGYVPSD KPNYCTPLNT ALNLEKDSDL E 

« Hide

Isoform Short (LTBP-1S) [UniParc] [UniParc].

Checksum: 69C41A7EC71FE8D2
Show »

FASTA1,395152,935
Isoform 3 [UniParc].

Checksum: 616E9947D00D3200
Show »

FASTA1,342147,235
Isoform 4 [UniParc].

Checksum: D59CED455F79E348
Show »

FASTA1,722186,867
Isoform 5 [UniParc].

Checksum: 08160DD6EB7DFE97
Show »

FASTA1,396153,006

References

« Hide 'large scale' references
[1]"TGF-beta 1 binding protein: a component of the large latent complex of TGF-beta 1 with multiple repeat sequences."
Kanzaki T., Olofsson A., Moren A., Wernstedt C., Hellman U., Miyazono K., Claesson-Welsh L., Heldin C.-H.
Cell 61:1051-1061(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), PARTIAL PROTEIN SEQUENCE.
Tissue: Fibroblast and Platelet.
[2]"Major alternative spliced-form of LTBP1 mRNA in human glomerular endothelial cell."
Kwak J.H., Shin K.Y., Kim S.I.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
Tissue: Brain.
[7]"Efficient association of an amino-terminally extended form of human latent transforming growth factor-beta binding protein with the extracellular matrix."
Olofsson A., Ichijo H., Moren A., ten Dijke P., Miyazono K., Heldin C.-H.
J. Biol. Chem. 270:31294-31297(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-346.
Tissue: Blood.
[8]Suzuki Y., Yamashita R., Shirota M., Sakakibara Y., Chiba J., Nakai K., Sugano S.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 684-875 (ISOFORMS 4 AND 5).
[9]"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.
[10]"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.
[11]"Hybrid and complex glycans are linked to the conserved N-glycosylation site of the third eight-cysteine domain of LTBP-1 in insect cells."
Rudd P.M., Downing A.K., Cadene M., Harvey D.J., Wormald M.R., Weir I., Dwek R.A., Rifkin D.B., Gleizes P.E.
Biochemistry 39:1596-1603(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-1366.
[12]"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: INTERACTION WITH TGFB1, MUTAGENESIS OF 1385-GLU--PRO-1388.
[13]"Latent transforming growth factor beta-binding protein 1 interacts with fibrillin and is a microfibril-associated protein."
Isogai Z., Ono R.N., Ushiro S., Keene D.R., Chen Y., Mazzieri R., Charbonneau N.L., Reinhardt D.P., Rifkin D.B., Sakai L.Y.
J. Biol. Chem. 278:2750-2757(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FBN1.
[14]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1597, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[15]"ADAMTSL2 mutations in geleophysic dysplasia demonstrate a role for ADAMTS-like proteins in TGF-beta bioavailability regulation."
Le Goff C., Morice-Picard F., Dagoneau N., Wang L.W., Perrot C., Crow Y.J., Bauer F., Flori E., Prost-Squarcioni C., Krakow D., Ge G., Greenspan D.S., Bonnet D., Le Merrer M., Munnich A., Apte S.S., Cormier-Daire V.
Nat. Genet. 40:1119-1123(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADAMTSL2.
[16]"Solution structure of the third TB domain from LTBP1 provides insight into assembly of the large latent complex that sequesters latent TGF-beta."
Lack J., O'Leary J.M., Knott V., Yuan X., Rifkin D.B., Handford P.A., Downing A.K.
J. Mol. Biol. 334:281-291(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1340-1412, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34057 mRNA. Translation: AAA61160.1.
AF489528 mRNA. Translation: AAM03124.1.
AB208801 mRNA. Translation: BAD92038.1. Different initiation.
AC019195 Genomic DNA. Translation: AAY14953.1.
AC019127 Genomic DNA. Translation: AAY24260.1.
AC020594 Genomic DNA. Translation: AAY15036.1.
CH471053 Genomic DNA. Translation: EAX00437.1.
BC130289 mRNA. Translation: AAI30290.1.
L48925 Genomic DNA. Translation: AAA96327.1.
BP291349 mRNA. No translation available.
PIRA35626.
RefSeqNP_000618.3. NM_000627.3.
NP_001159736.1. NM_001166264.1.
NP_001159737.1. NM_001166265.1.
NP_001159738.1. NM_001166266.1.
NP_996826.2. NM_206943.2.
UniGeneHs.619315.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KSQNMR-A1340-1412[»]
ProteinModelPortalQ14766.
SMRQ14766. Positions 550-739, 872-1506, 1622-1706.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110230. 5 interactions.
DIPDIP-50011N.
IntActQ14766. 1 interaction.
MINTMINT-1522113.
STRING9606.ENSP00000346467.

PTM databases

PhosphoSiteQ14766.
UniCarbKBQ14766.

Proteomic databases

PaxDbQ14766.
PRIDEQ14766.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354476; ENSP00000346467; ENSG00000049323. [Q14766-4]
ENST00000390003; ENSP00000374653; ENSG00000049323. [Q14766-5]
ENST00000404525; ENSP00000385359; ENSG00000049323. [Q14766-3]
ENST00000404816; ENSP00000386043; ENSG00000049323. [Q14766-1]
ENST00000407925; ENSP00000384091; ENSG00000049323. [Q14766-2]
GeneID4052.
KEGGhsa:4052.
UCSCuc002rou.3. human. [Q14766-2]
uc002rov.3. human. [Q14766-3]
uc021vft.1. human. [Q14766-1]

Organism-specific databases

CTD4052.
GeneCardsGC02P033172.
HGNCHGNC:6714. LTBP1.
HPACAB025428.
HPA005707.
HPA006221.
MIM150390. gene.
neXtProtNX_Q14766.
PharmGKBPA30477.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG318792.
KOK08023.
OMATQLGRCF.
OrthoDBEOG7FR7FP.
TreeFamTF317514.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ14766.
BgeeQ14766.
CleanExHS_LTBP1.
GenevestigatorQ14766.

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]
PfamPF07645. EGF_CA. 12 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTSM00181. EGF. 5 hits.
SM00179. EGF_CA. 13 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 5 hits.
SSF57581. SSF57581. 4 hits.
PROSITEPS00010. ASX_HYDROXYL. 13 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 11 hits.
PS50026. EGF_3. 14 hits.
PS01187. EGF_CA. 15 hits.
PS51364. TB. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLTBP1. human.
EvolutionaryTraceQ14766.
GeneWikiLTBP1_(gene).
GenomeRNAi4052.
NextBio15874.
PROQ14766.
SOURCESearch...

Entry information

Entry nameLTBP1_HUMAN
AccessionPrimary (citable) accession number: Q14766
Secondary accession number(s): A1L3V1 expand/collapse secondary AC list , P22064, Q53SD8, Q53SF3, Q53SG1, Q59HF7, Q8TD95
Entry history
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 2, 2010
Last modified: March 19, 2014
This is version 134 of the entry and version 4 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM