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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. protein binding Source: BHF-UCL
  3. transforming growth factor beta binding Source: UniProt
  4. transforming growth factor beta-activated receptor activity Source: UniProtKB
Complete GO annotation...

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 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 17211698Latent-transforming growth factor beta-binding protein 1
PRO_0000007635Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi191 ↔ 201 By similarity
Disulfide bondi195 ↔ 207 By similarity
Disulfide bondi209 ↔ 218 By similarity
Glycosylationi347 – 3471N-linked (GlcNAc...) Reviewed prediction
Glycosylationi378 – 3781N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi403 ↔ 413 By similarity
Disulfide bondi407 ↔ 419 By similarity
Disulfide bondi421 ↔ 430 By similarity
Glycosylationi424 – 4241N-linked (GlcNAc...) Reviewed prediction
Glycosylationi620 – 6201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi630 ↔ 641 By similarity
Disulfide bondi636 ↔ 650 By similarity
Disulfide bondi652 ↔ 665 By similarity
Disulfide bondi877 ↔ 889 By similarity
Disulfide bondi884 ↔ 898 By similarity
Disulfide bondi900 ↔ 913 By similarity
Disulfide bondi919 ↔ 931 By similarity
Disulfide bondi926 ↔ 940 By similarity
Disulfide bondi942 ↔ 955 By similarity
Disulfide bondi961 ↔ 972 By similarity
Disulfide bondi967 ↔ 981 By similarity
Modified residuei974 – 9741(3R)-3-hydroxyasparagine
Disulfide bondi984 ↔ 996 By similarity
Disulfide bondi1002 ↔ 1013 By similarity
Disulfide bondi1008 ↔ 1022 By similarity
Disulfide bondi1025 ↔ 1036 By similarity
Disulfide bondi1042 ↔ 1053 By similarity
Disulfide bondi1048 ↔ 1062 By similarity
Disulfide bondi1064 ↔ 1077 By similarity
Disulfide bondi1083 ↔ 1094 By similarity
Disulfide bondi1089 ↔ 1103 By similarity
Disulfide bondi1105 ↔ 1118 By similarity
Disulfide bondi1124 ↔ 1135 By similarity
Disulfide bondi1130 ↔ 1144 By similarity
Modified residuei1137 – 11371(3R)-3-hydroxyasparagine
Disulfide bondi1146 ↔ 1159 By similarity
Disulfide bondi1165 ↔ 1177 By similarity
Disulfide bondi1172 ↔ 1186 By similarity
Disulfide bondi1188 ↔ 1200 By similarity
Glycosylationi1197 – 11971N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1206 ↔ 1218 By similarity
Disulfide bondi1212 ↔ 1227 By similarity
Disulfide bondi1229 ↔ 1242 By similarity
Disulfide bondi1248 ↔ 1260 By similarity
Glycosylationi1250 – 12501N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1254 ↔ 1269 By similarity
Disulfide bondi1349 ↔ 13721 Publication
Disulfide bondi1359 ↔ 1384
Disulfide bondi1359 – 1359Interchain (with C-33 in TGFB1); in linked form By similarity
Glycosylationi1366 – 13661N-linked (GlcNAc...)1 Publication
CAR_000184
Disulfide bondi1373 ↔ 13891 Publication
Disulfide bondi1374 ↔ 14011 Publication
Disulfide bondi1384 – 1384Interchain (with C-33 in TGFB1); in linked form By similarity
Disulfide bondi1471 ↔ 1482 By similarity
Disulfide bondi1477 ↔ 1491 By similarity
Modified residuei1597 – 15971Phosphoserine1 Publication
Disulfide bondi1625 ↔ 1636 By similarity
Disulfide bondi1631 ↔ 1645 By similarity
Disulfide bondi1666 ↔ 1681 By similarity
Disulfide bondi1676 ↔ 1690 By similarity
Disulfide bondi1692 ↔ 1705 By similarity

Post-translational modificationi

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.

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

ArrayExpressiQ14766.
BgeeiQ14766.
CleanExiHS_LTBP1.
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. 5 interactions.
DIPiDIP-50011N.
IntActiQ14766. 2 interactions.
MINTiMINT-1522113.
STRINGi9606.ENSP00000346467.

Structurei

Secondary structure

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, 1621-1700.

Miscellaneous databases

EvolutionaryTraceiQ14766.

Family & Domainsi

Domains and Repeats

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1174 – 11763Cell attachment site Reviewed prediction

Compositional bias

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

Domaini

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

Sequence similaritiesi

Belongs to the LTBP family.
Contains 18 EGF-like domains.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG318792.
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

MAGAWLRWGL LLWAGLLASS AHGRLRRITY VVHPGPGLAA GALPLSGPPR     50
SRTFNVALNA RYSRSSAAAG APSRASPGVP SERTRRTSKP GGAALQGLRP 100
PPPPPPEPAR PAVPGGQLHP NPGGHPAAAP FTKQGRQVVR SKVPQETQSG 150
GGSRLQVHQK QQLQGVNVCG GRCCHGWSKA PGSQRCTKPS CVPPCQNGGM 200
CLRPQLCVCK PGTKGKACET IAAQDTSSPV FGGQSPGAAS SWGPPEQAAK 250
HTSSKKADTL PRVSPVAQMT LTLKPKPSVG LPQQIHSQVT PLSSQSVVIH 300
HGQTQEYVLK PKYFPAQKGI SGEQSTEGSF PLRYVQDQVA APFQLSNHTG 350
RIKVVFTPSI CKVTCTKGSC QNSCEKGNTT TLISENGHAA DTLTATNFRV 400
VICHLPCMNG GQCSSRDKCQ CPPNFTGKLC QIPVHGASVP KLYQHSQQPG 450
KALGTHVIHS THTLPLTVTS QQGVKVKFPP NIVNIHVKHP PEASVQIHQV 500
SRIDGPTGQK TKEAQPGQSQ VSYQGLPVQK TQTIHSTYSH QQVIPHVYPV 550
AAKTQLGRCF QETIGSQCGK ALPGLSKQED CCGTVGTSWG FNKCQKCPKK 600
PSYHGYNQMM ECLPGYKRVN NTFCQDINEC QLQGVCPNGE CLNTMGSYRC 650
TCKIGFGPDP TFSSCVPDPP VISEEKGPCY RLVSSGRQCM HPLSVHLTKQ 700
LCCCSVGKAW GPHCEKCPLP GTAAFKEICP GGMGYTVSGV HRRRPIHHHV 750
GKGPVFVKPK NTQPVAKSTH PPPLPAKEEP VEALTFSREH GPGVAEPEVA 800
TAPPEKEIPS LDQEKTKLEP GQPQLSPGIS TIHLHPQFPV VIEKTSPPVP 850
VEVAPEASTS SASQVIAPTQ VTEINECTVN PDICGAGHCI NLPVRYTCIC 900
YEGYRFSEQQ RKCVDIDECT QVQHLCSQGR CENTEGSFLC ICPAGFMASE 950
EGTNCIDVDE CLRPDVCGEG HCVNTVGAFR CEYCDSGYRM TQRGRCEDID 1000
ECLNPSTCPD EQCVNSPGSY QCVPCTEGFR GWNGQCLDVD ECLEPNVCAN 1050
GDCSNLEGSY MCSCHKGYTR TPDHKHCRDI DECQQGNLCV NGQCKNTEGS 1100
FRCTCGQGYQ LSAAKDQCED IDECQHRHLC AHGQCRNTEG SFQCVCDQGY 1150
RASGLGDHCE DINECLEDKS VCQRGDCINT AGSYDCTCPD GFQLDDNKTC 1200
QDINECEHPG LCGPQGECLN TEGSFHCVCQ QGFSISADGR TCEDIDECVN 1250
NTVCDSHGFC DNTAGSFRCL CYQGFQAPQD GQGCVDVNEC ELLSGVCGEA 1300
FCENVEGSFL CVCADENQEY SPMTGQCRSR TSTDLDVDVD QPKEEKKECY 1350
YNLNDASLCD NVLAPNVTKQ ECCCTSGVGW GDNCEIFPCP VLGTAEFTEM 1400
CPKGKGFVPA GESSSEAGGE NYKDADECLL FGQEICKNGF CLNTRPGYEC 1450
YCKQGTYYDP VKLQCFDMDE CQDPSSCIDG QCVNTEGSYN CFCTHPMVLD 1500
ASEKRCIRPA ESNEQIEETD VYQDLCWEHL SDEYVCSRPL VGKQTTYTEC 1550
CCLYGEAWGM QCALCPLKDS DDYAQLCNIP VTGRRQPYGR DALVDFSEQY 1600
TPEADPYFIQ DRFLNSFEEL QAEECGILNG CENGRCVRVQ EGYTCDCFDG 1650
YHLDTAKMTC VDVNECDELN NRMSLCKNAK CINTDGSYKC LCLPGYVPSD 1700
KPNYCTPLNT ALNLEKDSDL E 1721
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 326326Missing in isoform Short, isoform 3 and isoform 5.
VSP_036963Add
BLAST
Alternative sequencei327 – 34519EGSFP…APFQL → MDTKLMCLLFFFSLPPLLV in isoform Short, isoform 3 and isoform 5.
VSP_036964Add
BLAST
Alternative sequencei724 – 77653Missing in isoform 3.
VSP_036965Add
BLAST
Alternative sequencei839 – 8402PV → PGI in isoform 4 and isoform 5.
VSP_040125

Sequence conflict

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

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

EnsembliENST00000354476; ENSP00000346467; ENSG00000049323. [Q14766-4]
ENST00000390003; ENSP00000374653; ENSG00000049323. [Q14766-5]
ENST00000404525; 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, 1621-1700.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110230. 5 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 ENST00000354476 ; ENSP00000346467 ; ENSG00000049323 . [Q14766-4 ]
ENST00000390003 ; ENSP00000374653 ; ENSG00000049323 . [Q14766-5 ]
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.
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

ArrayExpressi Q14766.
Bgeei Q14766.
CleanExi HS_LTBP1.
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: September 3, 2014
This is version 139 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

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