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Q14766

- LTBP1_HUMAN

UniProt

Q14766 - LTBP1_HUMAN

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Protein

Latent-transforming growth factor beta-binding protein 1

Gene

LTBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. transforming growth factor beta-activated receptor activity Source: UniProtKB
  3. transforming growth factor beta binding Source: UniProt

GO - Biological processi

  1. extracellular matrix organization Source: Reactome
  2. sequestering of TGFbeta in extracellular matrix Source: BHF-UCL
  3. transmembrane receptor protein serine/threonine kinase signaling pathway Source: GOC
Complete GO annotation...

Keywords - Ligandi

Growth factor 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 1
Short name:
LTBP-1
Alternative name(s):
Transforming growth factor beta-1-binding protein 1
Short name:
TGF-beta1-BP-1
Gene namesi
Name:LTBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6714. LTBP1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular matrix Source: UniProt
  2. extracellular region Source: Reactome
  3. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1385 – 13884EIFP → DL: Loss of binding to TGFB1. 1 Publication

Organism-specific databases

PharmGKBiPA30477.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 17211698Latent-transforming growth factor beta-binding protein 1PRO_0000007635Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi191 ↔ 201PROSITE-ProRule annotation
Disulfide bondi195 ↔ 207PROSITE-ProRule annotation
Disulfide bondi209 ↔ 218PROSITE-ProRule annotation
Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi403 ↔ 413PROSITE-ProRule annotation
Disulfide bondi407 ↔ 419PROSITE-ProRule annotation
Disulfide bondi421 ↔ 430PROSITE-ProRule annotation
Glycosylationi424 – 4241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi620 – 6201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi630 ↔ 641PROSITE-ProRule annotation
Disulfide bondi636 ↔ 650PROSITE-ProRule annotation
Disulfide bondi652 ↔ 665PROSITE-ProRule annotation
Disulfide bondi877 ↔ 889PROSITE-ProRule annotation
Disulfide bondi884 ↔ 898PROSITE-ProRule annotation
Disulfide bondi900 ↔ 913PROSITE-ProRule annotation
Disulfide bondi919 ↔ 931PROSITE-ProRule annotation
Disulfide bondi926 ↔ 940PROSITE-ProRule annotation
Disulfide bondi942 ↔ 955PROSITE-ProRule annotation
Disulfide bondi961 ↔ 972PROSITE-ProRule annotation
Disulfide bondi967 ↔ 981PROSITE-ProRule annotation
Modified residuei974 – 9741(3R)-3-hydroxyasparagine1 Publication
Disulfide bondi984 ↔ 996PROSITE-ProRule annotation
Disulfide bondi1002 ↔ 1013PROSITE-ProRule annotation
Disulfide bondi1008 ↔ 1022PROSITE-ProRule annotation
Disulfide bondi1025 ↔ 1036PROSITE-ProRule annotation
Disulfide bondi1042 ↔ 1053PROSITE-ProRule annotation
Disulfide bondi1048 ↔ 1062PROSITE-ProRule annotation
Disulfide bondi1064 ↔ 1077PROSITE-ProRule annotation
Disulfide bondi1083 ↔ 1094PROSITE-ProRule annotation
Disulfide bondi1089 ↔ 1103PROSITE-ProRule annotation
Disulfide bondi1105 ↔ 1118PROSITE-ProRule annotation
Disulfide bondi1124 ↔ 1135PROSITE-ProRule annotation
Disulfide bondi1130 ↔ 1144PROSITE-ProRule annotation
Modified residuei1137 – 11371(3R)-3-hydroxyasparagine1 Publication
Disulfide bondi1146 ↔ 1159PROSITE-ProRule annotation
Disulfide bondi1165 ↔ 1177PROSITE-ProRule annotation
Disulfide bondi1172 ↔ 1186PROSITE-ProRule annotation
Disulfide bondi1188 ↔ 1200PROSITE-ProRule annotation
Glycosylationi1197 – 11971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1206 ↔ 1218PROSITE-ProRule annotation
Disulfide bondi1212 ↔ 1227PROSITE-ProRule annotation
Disulfide bondi1229 ↔ 1242PROSITE-ProRule annotation
Disulfide bondi1248 ↔ 1260PROSITE-ProRule annotation
Glycosylationi1250 – 12501N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1254 ↔ 1269PROSITE-ProRule annotation
Disulfide bondi1349 ↔ 13721 PublicationPROSITE-ProRule annotation
Disulfide bondi1359 ↔ 13841 PublicationPROSITE-ProRule annotation
Disulfide bondi1359 – 1359Interchain (with C-33 in TGFB1); in linked formPROSITE-ProRule annotation
Glycosylationi1366 – 13661N-linked (GlcNAc...)1 PublicationCAR_000184
Disulfide bondi1373 ↔ 13891 PublicationPROSITE-ProRule annotation
Disulfide bondi1374 ↔ 14011 PublicationPROSITE-ProRule annotation
Disulfide bondi1384 – 1384Interchain (with C-33 in TGFB1); in linked formPROSITE-ProRule annotation
Disulfide bondi1471 ↔ 1482PROSITE-ProRule annotation
Disulfide bondi1477 ↔ 1491PROSITE-ProRule annotation
Modified residuei1597 – 15971Phosphoserine1 Publication
Disulfide bondi1625 ↔ 1636PROSITE-ProRule annotation
Disulfide bondi1631 ↔ 1645PROSITE-ProRule annotation
Disulfide bondi1666 ↔ 1681PROSITE-ProRule annotation
Disulfide bondi1676 ↔ 1690PROSITE-ProRule annotation
Disulfide bondi1692 ↔ 1705PROSITE-ProRule annotation

Post-translational modificationi

Contains hydroxylated asparagine residues.1 Publication
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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

MaxQBiQ14766.
PaxDbiQ14766.
PRIDEiQ14766.

PTM databases

PhosphoSiteiQ14766.
UniCarbKBiQ14766.

Expressioni

Tissue specificityi

Isoform Long is found in fibroblasts.

Gene expression databases

BgeeiQ14766.
CleanExiHS_LTBP1.
ExpressionAtlasiQ14766. baseline and differential.
GenevestigatoriQ14766.

Organism-specific databases

HPAiCAB025428.
HPA005707.
HPA006221.

Interactioni

Subunit structurei

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 ADAMTSL2.3 Publications

Protein-protein interaction databases

BioGridi110230. 8 interactions.
DIPiDIP-50011N.
IntActiQ14766. 2 interactions.
MINTiMINT-1522113.
STRINGi9606.ENSP00000346467.

Structurei

Secondary structure

1
1721
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1340 – 13423
Beta strandi1346 – 13538
Turni1355 – 13584
Beta strandi1366 – 13683
Helixi1369 – 13746
Beta strandi1378 – 13825
Beta strandi1385 – 13884
Beta strandi1392 – 13943
Helixi1395 – 14006
Beta strandi1408 – 14103

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KSQNMR-A1340-1412[»]
ProteinModelPortaliQ14766.
SMRiQ14766. Positions 550-739, 872-1506, 1619-1699.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14766.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini187 – 21933EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini399 – 43133EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini557 – 60953TB 1Add
BLAST
Domaini626 – 66338EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini677 – 72953TB 2Add
BLAST
Domaini873 – 91038EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini915 – 95642EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini957 – 99741EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini998 – 103740EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1038 – 107841EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1079 – 111941EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1120 – 116041EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1161 – 120141EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1202 – 124342EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1244 – 128138EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1286 – 132843EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1347 – 140155TB 3Add
BLAST
Domaini1424 – 146643EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1467 – 150337EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1524 – 157754TB 4Add
BLAST
Domaini1621 – 165737EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini1662 – 170645EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1174 – 11763Cell attachment siteSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi100 – 13031Pro-richAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the LTBP family.Curated
Contains 18 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.
InParanoidiQ14766.
KOiK08023.
OMAiKHPPEAS.
OrthoDBiEOG7FR7FP.
PhylomeDBiQ14766.
TreeFamiTF317514.

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]
PfamiPF07645. EGF_CA. 12 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 5 hits.
SM00179. EGF_CA. 13 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 5 hits.
SSF57581. SSF57581. 4 hits.
PROSITEiPS00010. 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]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: Q14766-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAGAWLRWGL LLWAGLLASS AHGRLRRITY VVHPGPGLAA GALPLSGPPR
60 70 80 90 100
SRTFNVALNA RYSRSSAAAG APSRASPGVP SERTRRTSKP GGAALQGLRP
110 120 130 140 150
PPPPPPEPAR PAVPGGQLHP NPGGHPAAAP FTKQGRQVVR SKVPQETQSG
160 170 180 190 200
GGSRLQVHQK QQLQGVNVCG GRCCHGWSKA PGSQRCTKPS CVPPCQNGGM
210 220 230 240 250
CLRPQLCVCK PGTKGKACET IAAQDTSSPV FGGQSPGAAS SWGPPEQAAK
260 270 280 290 300
HTSSKKADTL PRVSPVAQMT LTLKPKPSVG LPQQIHSQVT PLSSQSVVIH
310 320 330 340 350
HGQTQEYVLK PKYFPAQKGI SGEQSTEGSF PLRYVQDQVA APFQLSNHTG
360 370 380 390 400
RIKVVFTPSI CKVTCTKGSC QNSCEKGNTT TLISENGHAA DTLTATNFRV
410 420 430 440 450
VICHLPCMNG GQCSSRDKCQ CPPNFTGKLC QIPVHGASVP KLYQHSQQPG
460 470 480 490 500
KALGTHVIHS THTLPLTVTS QQGVKVKFPP NIVNIHVKHP PEASVQIHQV
510 520 530 540 550
SRIDGPTGQK TKEAQPGQSQ VSYQGLPVQK TQTIHSTYSH QQVIPHVYPV
560 570 580 590 600
AAKTQLGRCF QETIGSQCGK ALPGLSKQED CCGTVGTSWG FNKCQKCPKK
610 620 630 640 650
PSYHGYNQMM ECLPGYKRVN NTFCQDINEC QLQGVCPNGE CLNTMGSYRC
660 670 680 690 700
TCKIGFGPDP TFSSCVPDPP VISEEKGPCY RLVSSGRQCM HPLSVHLTKQ
710 720 730 740 750
LCCCSVGKAW GPHCEKCPLP GTAAFKEICP GGMGYTVSGV HRRRPIHHHV
760 770 780 790 800
GKGPVFVKPK NTQPVAKSTH PPPLPAKEEP VEALTFSREH GPGVAEPEVA
810 820 830 840 850
TAPPEKEIPS LDQEKTKLEP GQPQLSPGIS TIHLHPQFPV VIEKTSPPVP
860 870 880 890 900
VEVAPEASTS SASQVIAPTQ VTEINECTVN PDICGAGHCI NLPVRYTCIC
910 920 930 940 950
YEGYRFSEQQ RKCVDIDECT QVQHLCSQGR CENTEGSFLC ICPAGFMASE
960 970 980 990 1000
EGTNCIDVDE CLRPDVCGEG HCVNTVGAFR CEYCDSGYRM TQRGRCEDID
1010 1020 1030 1040 1050
ECLNPSTCPD EQCVNSPGSY QCVPCTEGFR GWNGQCLDVD ECLEPNVCAN
1060 1070 1080 1090 1100
GDCSNLEGSY MCSCHKGYTR TPDHKHCRDI DECQQGNLCV NGQCKNTEGS
1110 1120 1130 1140 1150
FRCTCGQGYQ LSAAKDQCED IDECQHRHLC AHGQCRNTEG SFQCVCDQGY
1160 1170 1180 1190 1200
RASGLGDHCE DINECLEDKS VCQRGDCINT AGSYDCTCPD GFQLDDNKTC
1210 1220 1230 1240 1250
QDINECEHPG LCGPQGECLN TEGSFHCVCQ QGFSISADGR TCEDIDECVN
1260 1270 1280 1290 1300
NTVCDSHGFC DNTAGSFRCL CYQGFQAPQD GQGCVDVNEC ELLSGVCGEA
1310 1320 1330 1340 1350
FCENVEGSFL CVCADENQEY SPMTGQCRSR TSTDLDVDVD QPKEEKKECY
1360 1370 1380 1390 1400
YNLNDASLCD NVLAPNVTKQ ECCCTSGVGW GDNCEIFPCP VLGTAEFTEM
1410 1420 1430 1440 1450
CPKGKGFVPA GESSSEAGGE NYKDADECLL FGQEICKNGF CLNTRPGYEC
1460 1470 1480 1490 1500
YCKQGTYYDP VKLQCFDMDE CQDPSSCIDG QCVNTEGSYN CFCTHPMVLD
1510 1520 1530 1540 1550
ASEKRCIRPA ESNEQIEETD VYQDLCWEHL SDEYVCSRPL VGKQTTYTEC
1560 1570 1580 1590 1600
CCLYGEAWGM QCALCPLKDS DDYAQLCNIP VTGRRQPYGR DALVDFSEQY
1610 1620 1630 1640 1650
TPEADPYFIQ DRFLNSFEEL QAEECGILNG CENGRCVRVQ EGYTCDCFDG
1660 1670 1680 1690 1700
YHLDTAKMTC VDVNECDELN NRMSLCKNAK CINTDGSYKC LCLPGYVPSD
1710 1720
KPNYCTPLNT ALNLEKDSDL E
Length:1,721
Mass (Da):186,796
Last modified:March 2, 2010 - v4
Checksum:i432489CAC3023754
GO
Isoform Short (identifier: Q14766-2) [UniParc] [UniParc]FASTAAdd to Basket

Also known as: LTBP-1S

The sequence of this isoform differs from the canonical sequence as follows:
     1-326: Missing.
     327-345: EGSFPLRYVQDQVAAPFQL → MDTKLMCLLFFFSLPPLLV

Show »
Length:1,395
Mass (Da):152,935
Checksum:i69C41A7EC71FE8D2
GO
Isoform 3 (identifier: Q14766-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,342
Mass (Da):147,235
Checksum:i616E9947D00D3200
GO
Isoform 4 (identifier: Q14766-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     839-840: PV → PGI

Show »
Length:1,722
Mass (Da):186,867
Checksum:iD59CED455F79E348
GO
Isoform 5 (identifier: Q14766-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,396
Mass (Da):153,006
Checksum:i08160DD6EB7DFE97
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501R → AS in AAA96327. (PubMed:8537398)Curated
Sequence conflicti691 – 6911H → Y in AAA61160. (PubMed:2350783)Curated
Sequence conflicti694 – 6941S → P in BP291349. 1 PublicationCurated
Sequence conflicti710 – 7101Missing in AAA61160. (PubMed:2350783)Curated
Sequence conflicti710 – 7101Missing in AAM03124. 1 PublicationCurated
Sequence conflicti744 – 7441R → M in BP291349. 1 PublicationCurated
Sequence conflicti792 – 7943PGV → ARS in AAA61160. (PubMed:2350783)Curated
Sequence conflicti792 – 7943PGV → ARS in AAM03124. 1 PublicationCurated
Sequence conflicti831 – 8311T → A in AAA61160. (PubMed:2350783)Curated
Sequence conflicti1378 – 13781V → A in AAA61160. (PubMed:2350783)Curated
Sequence conflicti1378 – 13781V → A in AAM03124. 1 PublicationCurated
Sequence conflicti1378 – 13781V → A in BAD92038. 1 PublicationCurated
Sequence conflicti1378 – 13781V → A in EAX00437. 1 PublicationCurated
Sequence conflicti1378 – 13781V → A in AAI30290. (PubMed:15489334)Curated
Sequence conflicti1648 – 16481F → L in AAA61160. (PubMed:2350783)Curated
Sequence conflicti1648 – 16481F → L in AAM03124. 1 PublicationCurated
Sequence conflicti1661 – 16611V → F in AAA61160. (PubMed:2350783)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 326326Missing in isoform Short, isoform 3 and isoform 5. 5 PublicationsVSP_036963Add
BLAST
Alternative sequencei327 – 34519EGSFP…APFQL → MDTKLMCLLFFFSLPPLLV in isoform Short, isoform 3 and isoform 5. 5 PublicationsVSP_036964Add
BLAST
Alternative sequencei724 – 77653Missing in isoform 3. 1 PublicationVSP_036965Add
BLAST
Alternative sequencei839 – 8402PV → PGI in isoform 4 and isoform 5. 1 PublicationVSP_040125

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS33177.2. [Q14766-1]
CCDS33178.2. [Q14766-2]
CCDS54345.1. [Q14766-3]
PIRiA35626.
RefSeqiNP_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.
UniGeneiHs.619315.

Genome annotation databases

EnsembliENST00000404525; ENSP00000385359; ENSG00000049323. [Q14766-3]
ENST00000404816; ENSP00000386043; ENSG00000049323. [Q14766-1]
ENST00000407925; ENSP00000384091; ENSG00000049323. [Q14766-2]
GeneIDi4052.
KEGGihsa:4052.
UCSCiuc002rou.3. human. [Q14766-2]
uc002rov.3. human. [Q14766-3]
uc021vft.1. human. [Q14766-1]

Polymorphism databases

DMDMi290457687.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS33177.2. [Q14766-1 ]
CCDS33178.2. [Q14766-2 ]
CCDS54345.1. [Q14766-3 ]
PIRi A35626.
RefSeqi NP_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.
UniGenei Hs.619315.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KSQ NMR - A 1340-1412 [» ]
ProteinModelPortali Q14766.
SMRi Q14766. Positions 550-739, 872-1506, 1619-1699.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110230. 8 interactions.
DIPi DIP-50011N.
IntActi Q14766. 2 interactions.
MINTi MINT-1522113.
STRINGi 9606.ENSP00000346467.

PTM databases

PhosphoSitei Q14766.
UniCarbKBi Q14766.

Polymorphism databases

DMDMi 290457687.

Proteomic databases

MaxQBi Q14766.
PaxDbi Q14766.
PRIDEi Q14766.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000404525 ; ENSP00000385359 ; ENSG00000049323 . [Q14766-3 ]
ENST00000404816 ; ENSP00000386043 ; ENSG00000049323 . [Q14766-1 ]
ENST00000407925 ; ENSP00000384091 ; ENSG00000049323 . [Q14766-2 ]
GeneIDi 4052.
KEGGi hsa:4052.
UCSCi uc002rou.3. human. [Q14766-2 ]
uc002rov.3. human. [Q14766-3 ]
uc021vft.1. human. [Q14766-1 ]

Organism-specific databases

CTDi 4052.
GeneCardsi GC02P033172.
HGNCi HGNC:6714. LTBP1.
HPAi CAB025428.
HPA005707.
HPA006221.
MIMi 150390. gene.
neXtProti NX_Q14766.
PharmGKBi PA30477.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG318792.
GeneTreei ENSGT00760000118806.
InParanoidi Q14766.
KOi K08023.
OMAi KHPPEAS.
OrthoDBi EOG7FR7FP.
PhylomeDBi Q14766.
TreeFami TF317514.

Enzyme and pathway databases

Reactomei REACT_150331. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSi LTBP1. human.
EvolutionaryTracei Q14766.
GeneWikii LTBP1_(gene).
GenomeRNAii 4052.
NextBioi 15874.
PROi Q14766.
SOURCEi Search...

Gene expression databases

Bgeei Q14766.
CleanExi HS_LTBP1.
ExpressionAtlasi Q14766. baseline and differential.
Genevestigatori Q14766.

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 PF07645. EGF_CA. 12 hits.
PF00683. TB. 4 hits.
[Graphical view ]
SMARTi SM00181. EGF. 5 hits.
SM00179. EGF_CA. 13 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 5 hits.
SSF57581. SSF57581. 4 hits.
PROSITEi PS00010. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, HYDROXYLATION AT ASN-974 AND ASN-1137.
    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.
    , 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. 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. 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.

Entry informationi

Entry nameiLTBP1_HUMAN
AccessioniPrimary (citable) accession number: Q14766
Secondary accession number(s): A1L3V1
, P22064, Q53SD8, Q53SF3, Q53SG1, Q59HF7, Q8TD95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 2, 2010
Last modified: October 29, 2014
This is version 141 of the entry and version 4 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3