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Protein

Latent-transforming growth factor beta-binding protein 1

Gene

Ltbp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • aorta development Source: MGI
  • coronary vasculature development Source: MGI
  • transforming growth factor beta receptor signaling pathway Source: MGI
  • ventricular septum development Source: MGI
Complete GO annotation...

Keywords - Ligandi

Growth factor binding

Enzyme and pathway databases

ReactomeiR-MMU-2129379. 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
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:109151. Ltbp1.

Subcellular locationi

  • Secreted By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 17121689Latent-transforming growth factor beta-binding protein 1PRO_0000007637Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi185 ↔ 195PROSITE-ProRule annotation
Disulfide bondi189 ↔ 201PROSITE-ProRule annotation
Disulfide bondi203 ↔ 212PROSITE-ProRule annotation
Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence analysis
Glycosylationi370 – 3701N-linked (GlcNAc...)Sequence analysis
Disulfide bondi395 ↔ 405PROSITE-ProRule annotation
Disulfide bondi399 ↔ 411PROSITE-ProRule annotation
Disulfide bondi413 ↔ 422PROSITE-ProRule annotation
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence analysis
Glycosylationi612 – 6121N-linked (GlcNAc...)Sequence analysis
Disulfide bondi622 ↔ 633PROSITE-ProRule annotation
Disulfide bondi628 ↔ 642PROSITE-ProRule annotation
Disulfide bondi644 ↔ 657PROSITE-ProRule annotation
Disulfide bondi869 ↔ 881PROSITE-ProRule annotation
Disulfide bondi876 ↔ 890PROSITE-ProRule annotation
Disulfide bondi892 ↔ 905PROSITE-ProRule annotation
Disulfide bondi911 ↔ 923PROSITE-ProRule annotation
Disulfide bondi918 ↔ 932PROSITE-ProRule annotation
Disulfide bondi934 ↔ 947PROSITE-ProRule annotation
Disulfide bondi953 ↔ 964PROSITE-ProRule annotation
Disulfide bondi959 ↔ 973PROSITE-ProRule annotation
Modified residuei966 – 9661(3R)-3-hydroxyasparagineBy similarity
Disulfide bondi976 ↔ 988PROSITE-ProRule annotation
Disulfide bondi994 ↔ 1005PROSITE-ProRule annotation
Disulfide bondi1000 ↔ 1014PROSITE-ProRule annotation
Disulfide bondi1017 ↔ 1028PROSITE-ProRule annotation
Disulfide bondi1034 ↔ 1045PROSITE-ProRule annotation
Disulfide bondi1040 ↔ 1054PROSITE-ProRule annotation
Glycosylationi1042 – 10421N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1056 ↔ 1069PROSITE-ProRule annotation
Disulfide bondi1075 ↔ 1086PROSITE-ProRule annotation
Disulfide bondi1081 ↔ 1095PROSITE-ProRule annotation
Disulfide bondi1097 ↔ 1110PROSITE-ProRule annotation
Disulfide bondi1116 ↔ 1127PROSITE-ProRule annotation
Disulfide bondi1122 ↔ 1136PROSITE-ProRule annotation
Modified residuei1129 – 11291(3R)-3-hydroxyasparagineBy similarity
Disulfide bondi1138 ↔ 1151PROSITE-ProRule annotation
Disulfide bondi1157 ↔ 1169PROSITE-ProRule annotation
Disulfide bondi1164 ↔ 1178PROSITE-ProRule annotation
Disulfide bondi1180 ↔ 1192PROSITE-ProRule annotation
Disulfide bondi1198 ↔ 1210PROSITE-ProRule annotation
Disulfide bondi1204 ↔ 1219PROSITE-ProRule annotation
Disulfide bondi1221 ↔ 1234PROSITE-ProRule annotation
Disulfide bondi1240 ↔ 1252PROSITE-ProRule annotation
Glycosylationi1242 – 12421N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1246 ↔ 1261PROSITE-ProRule annotation
Disulfide bondi1263 ↔ 1276PROSITE-ProRule annotation
Disulfide bondi1282 ↔ 1294PROSITE-ProRule annotation
Disulfide bondi1289 ↔ 1303PROSITE-ProRule annotation
Disulfide bondi1305 ↔ 1319PROSITE-ProRule annotation
Disulfide bondi1340 ↔ 1363PROSITE-ProRule annotation
Disulfide bondi1350 ↔ 1375PROSITE-ProRule annotation
Disulfide bondi1350 – 1350Interchain (with C-33 in TGFB1); in linked formPROSITE-ProRule annotation
Glycosylationi1357 – 13571N-linked (GlcNAc...)By similarity
Disulfide bondi1364 ↔ 1380PROSITE-ProRule annotation
Disulfide bondi1365 ↔ 1392PROSITE-ProRule annotation
Disulfide bondi1375 – 1375Interchain (with C-33 in TGFB1); in linked formPROSITE-ProRule annotation
Modified residuei1405 – 14051PhosphoserineBy similarity
Disulfide bondi1419 ↔ 1432PROSITE-ProRule annotation
Disulfide bondi1427 ↔ 1441PROSITE-ProRule annotation
Disulfide bondi1443 ↔ 1456PROSITE-ProRule annotation
Disulfide bondi1462 ↔ 1473PROSITE-ProRule annotation
Disulfide bondi1468 ↔ 1482PROSITE-ProRule annotation
Disulfide bondi1484 ↔ 1497PROSITE-ProRule annotation
Modified residuei1588 – 15881PhosphoserineBy similarity
Modified residuei1607 – 16071PhosphoserineCombined sources
Disulfide bondi1616 ↔ 1627PROSITE-ProRule annotation
Disulfide bondi1622 ↔ 1636PROSITE-ProRule annotation
Disulfide bondi1638 ↔ 1651PROSITE-ProRule annotation
Disulfide bondi1657 ↔ 1672PROSITE-ProRule annotation
Disulfide bondi1667 ↔ 1681PROSITE-ProRule annotation
Disulfide bondi1683 ↔ 1696PROSITE-ProRule annotation

Post-translational modificationi

Contains hydroxylated asparagine residues.By similarity
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.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

MaxQBiQ8CG19.
PaxDbiQ8CG19.
PRIDEiQ8CG19.

PTM databases

PhosphoSiteiQ8CG19.

Expressioni

Gene expression databases

BgeeiQ8CG19.
ExpressionAtlasiQ8CG19. baseline and differential.
GenevisibleiQ8CG19. MM.

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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi234589. 1 interaction.
IntActiQ8CG19. 1 interaction.
MINTiMINT-1751360.
STRINGi10090.ENSMUSP00000001927.

Structurei

3D structure databases

ProteinModelPortaliQ8CG19.
SMRiQ8CG19. Positions 542-731, 864-1497, 1622-1688.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini181 – 21333EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini391 – 42333EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini549 – 60153TB 1Add
BLAST
Domaini618 – 65841EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini669 – 72153TB 2Add
BLAST
Domaini865 – 90642EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini907 – 94842EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini949 – 98941EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini990 – 102940EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1030 – 107041EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1071 – 111141EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1112 – 115241EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1153 – 119341EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1194 – 123542EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1236 – 127742EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1278 – 132043EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1338 – 139255TB 3Add
BLAST
Domaini1415 – 145743EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1458 – 149841EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1515 – 156854TB 4Add
BLAST
Domaini1612 – 165241EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini1653 – 169745EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi96 – 12429Pro-richAdd
BLAST

Domaini

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

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

eggNOGiKOG1217. Eukaryota.
ENOG410Z7XK. LUCA.
GeneTreeiENSGT00760000118806.
InParanoidiQ8CG19.
KOiK19559.
OMAiTQLGRCF.
OrthoDBiEOG7FR7FP.
PhylomeDBiQ8CG19.
TreeFamiTF317514.

Family and domain databases

Gene3Di3.90.290.10. 5 hits.
InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PfamiPF07645. EGF_CA. 15 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 18 hits.
SM00179. EGF_CA. 16 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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q8CG19-1) [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 LLWAGLLAWS AHGRVRRITY VVRPGPGLPA GALPLAGPPR
60 70 80 90 100
TFNVALDARY SRSSTAASSR ALAGPPAERT RRTSQPGGAA LPGLRSPLPP
110 120 130 140 150
EPARPGGPSR QLHSKAGAQT AVTRFAKHGR QVVRSQVQQD AQSAGGSRLQ
160 170 180 190 200
VQQKQQLQGI NVCGGQCCHG WSKPPGSQRC TKPSCVPPCQ NGGMCLRPQL
210 220 230 240 250
CVCKPGSKGK ACEITAAQDT MPPAFGGQNP GSSWAPLEQA AKHTSTKKAD
260 270 280 290 300
TLPRVSPVAQ MTLTLKPKPS MGLSQQIHPQ VAPLSSQNVM IRHGQTQEYL
310 320 330 340 350
LKPKYFPAPK VVSAEQSTEG SFSLRYGQEQ GTAPFQVSNH TGRIKVVFTP
360 370 380 390 400
SICKVTCTKG NCQNSCQKGN TTTLISENGH AADTLTATNF RVVICHLPCM
410 420 430 440 450
NGGQCSSRDK CQCPPNFTGK LCQIPVLGAS MPKLYQHAQQ QGKALGSHVI
460 470 480 490 500
HSTHTLPLTM TSQQGVKVKF PPNIVNIHVK HPPEASVQIH QVSRIDSPGG
510 520 530 540 550
QKVKEAQPGQ SQVSYQGLPV QKTQTVHSTY SHQQLIPHVY PVAAKTQLGR
560 570 580 590 600
CFQETIGSQC GKALPGLSKQ EDCCGTVGTS WGFNKCQKCP KKQSYHGYTQ
610 620 630 640 650
MMECLQGYKR VNNTFCQDIN ECQLQGVCPN GECLNTMGSY RCSCKMGFGP
660 670 680 690 700
DPTFSSCVPD PPVISEEKGP CYRLVSPGRH CMHPLSVHLT KQICCCSVGK
710 720 730 740 750
AWGPHCEKCP LPGTAAFKEI CPGGMGYTVS GVHRRRPIHQ HIGKEAVYVK
760 770 780 790 800
PKNTQPVAKS THPPPLPAKE EPVEALTSSW EHGPRGAEPE VVTAPPEKEI
810 820 830 840 850
PSLDQEKTRL EPGQPQLSPG VSTIHLHPQF PVVVEKTSPP VPVEVAPEAS
860 870 880 890 900
TSSASQVIAP TQVTEINECT VNPDICGAGH CINLPVRYTC ICYEGYKFSE
910 920 930 940 950
QLRKCVDIDE CAQVRHLCSQ GRCENTEGSF LCVCPAGFMA SEEGTNCIDV
960 970 980 990 1000
DECLRPDMCR DGRCINTAGA FRCEYCDSGY RMSRRGYCED IDECLKPSTC
1010 1020 1030 1040 1050
PEEQCVNTPG SYQCVPCTEG FRGWNGQCLD VDECLQPKVC TNGSCTNLEG
1060 1070 1080 1090 1100
SYMCSCHRGY SPTPDHRHCQ DIDECQQGNL CMNGQCRNTD GSFRCTCGQG
1110 1120 1130 1140 1150
YQLSAAKDQC EDIDECEHHH LCSHGQCRNT EGSFQCVCNQ GYRASVLGDH
1160 1170 1180 1190 1200
CEDINECLED SSVCQGGDCI NTAGSYDCTC PDGFQLNDNK GCQDINECAQ
1210 1220 1230 1240 1250
PGLCGSHGEC LNTQGSFHCV CEQGFSISAD GRTCEDIDEC VNNTVCDSHG
1260 1270 1280 1290 1300
FCDNTAGSFR CLCYQGFQAP QDGQGCVDVN ECELLSGVCG EAFCENVEGS
1310 1320 1330 1340 1350
FLCVCADENQ EYSPMTGQCR SRVTEDSGVD RQPREEKKEC YYNLNDASLC
1360 1370 1380 1390 1400
DNVLAPNVTK QECCCTSGAG WGDNCEIFPC PVQGTAEFTE MCPRGKGLVP
1410 1420 1430 1440 1450
AGESSYDTGG ENYKDADECL LFGEEICKNG YCLNTQPGYE CYCKQGTYYD
1460 1470 1480 1490 1500
PVKLQCFDMD ECQDPNSCID GQCVNTEGSY NCFCTHPMVL DASEKRCVQP
1510 1520 1530 1540 1550
TESNEQIEET DVYQDLCWEH LSEEYVCSRP LVGKQTTYTE CCCLYGEAWG
1560 1570 1580 1590 1600
MQCALCPMKD SDDYAQLCNI PVTGRRRPYG RDALVDFSEQ YGPETDPYFI
1610 1620 1630 1640 1650
QDRFLNSFEE LQAEECGILN GCENGRCVRV QEGYTCDCFD GYHLDMAKMT
1660 1670 1680 1690 1700
CVDVNECSEL NNRMSLCKNA KCINTEGSYK CLCLPGYIPS DKPNYCTPLN
1710
SALNLDKESD LE
Length:1,712
Mass (Da):186,717
Last modified:May 5, 2009 - v2
Checksum:iDB0564112F1F7843
GO
Isoform Short (identifier: Q8CG19-2) [UniParc] [UniParc]FASTAAdd to basket

Also known as: LTBP-1S

The sequence of this isoform differs from the canonical sequence as follows:
     1-318: Missing.
     319-336: EGSFSLRYGQEQGTAPFQ → MDTKLMCLLFFLCLPLLL

Show »
Length:1,394
Mass (Da):153,185
Checksum:i0D10BF1FB3B4A85A
GO
Isoform 3 (identifier: Q8CG19-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-318: Missing.
     319-336: EGSFSLRYGQEQGTAPFQ → MDTKLMCLLFFLCLPLLL
     716-768: Missing.

Note: No experimental confirmation available.
Show »
Length:1,341
Mass (Da):147,418
Checksum:iFB1930C28738FDE5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti313 – 3131S → F in AAN77250 (PubMed:12711388).Curated
Sequence conflicti506 – 5061A → T in AAN77250 (PubMed:12711388).Curated
Sequence conflicti506 – 5061A → T in AAN77251 (PubMed:12711388).Curated
Sequence conflicti506 – 5061A → T in AAC33307 (Ref. 3) Curated
Sequence conflicti559 – 5591Q → QQ in AAN77250 (PubMed:12711388).Curated
Sequence conflicti559 – 5591Q → QQ in AAC33307 (Ref. 3) Curated
Sequence conflicti1033 – 10331E → K in AAC33307 (Ref. 3) Curated
Sequence conflicti1111 – 11111E → G in BAC34222 (PubMed:16141072).Curated
Sequence conflicti1216 – 12161S → F in BAC34222 (PubMed:16141072).Curated
Sequence conflicti1631 – 16311Q → H in AAN77250 (PubMed:12711388).Curated
Sequence conflicti1631 – 16311Q → H in AAN77251 (PubMed:12711388).Curated
Sequence conflicti1659 – 16591E → G in BAC34222 (PubMed:16141072).Curated
Sequence conflicti1712 – 17121E → N in AAC33307 (Ref. 3) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 318318Missing in isoform Short and isoform 3. 1 PublicationVSP_036968Add
BLAST
Alternative sequencei319 – 33618EGSFS…TAPFQ → MDTKLMCLLFFLCLPLLL in isoform Short and isoform 3. 1 PublicationVSP_036969Add
BLAST
Alternative sequencei716 – 76853Missing in isoform 3. CuratedVSP_036970Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF346465
, AF346434, AF346435, AF346436, AF346437, AF346438, AF346439, AF346440, AF346441, AF346442, AF346443, AF346444, AF346445, AF346446, AF346447, AF346448, AF346449, AF346450, AF346451, AF346452, AF346453, AF346454, AF346455, AF346456, AF346457, AF346458, AF346459, AF346460, AF346461, AF346462, AF346463, AF346464 Genomic DNA. Translation: AAN77250.1.
AF346465
, AF346438, AF346439, AF346440, AF346441, AF346442, AF346443, AF346444, AF346445, AF346446, AF346447, AF346448, AF346449, AF346450, AF346451, AF346452, AF346453, AF346454, AF346455, AF346456, AF346457, AF346458, AF346459, AF346460, AF346461, AF346462, AF346463, AF346464 Genomic DNA. Translation: AAN77251.1.
AY143161 Genomic DNA. Translation: AAN38831.1.
AF022889 mRNA. Translation: AAC33307.1.
CT033758
, AC118018, AC126550, AC154178, AC154491 Genomic DNA. Translation: CAM24102.1.
CT033758, AC118018, AC154491 Genomic DNA. Translation: CAM24104.1.
CT033758, AC118018, AC154491 Genomic DNA. Translation: CAM24103.1.
BC094612 mRNA. Translation: AAH94612.1.
AK050380 mRNA. Translation: BAC34222.1.
AK080024 mRNA. Translation: BAC37808.1.
CCDSiCCDS28973.1. [Q8CG19-1]
CCDS37694.1. [Q8CG19-2]
RefSeqiNP_064303.2. NM_019919.3. [Q8CG19-1]
NP_996841.1. NM_206958.2. [Q8CG19-2]
XP_006524418.1. XM_006524355.2. [Q8CG19-3]
UniGeneiMm.269747.

Genome annotation databases

EnsembliENSMUST00000001927; ENSMUSP00000001927; ENSMUSG00000001870. [Q8CG19-1]
ENSMUST00000112514; ENSMUSP00000108133; ENSMUSG00000001870. [Q8CG19-3]
ENSMUST00000112516; ENSMUSP00000108135; ENSMUSG00000001870. [Q8CG19-2]
GeneIDi268977.
KEGGimmu:268977.
UCSCiuc008dom.2. mouse. [Q8CG19-1]
uc008doo.2. mouse. [Q8CG19-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF346465
, AF346434, AF346435, AF346436, AF346437, AF346438, AF346439, AF346440, AF346441, AF346442, AF346443, AF346444, AF346445, AF346446, AF346447, AF346448, AF346449, AF346450, AF346451, AF346452, AF346453, AF346454, AF346455, AF346456, AF346457, AF346458, AF346459, AF346460, AF346461, AF346462, AF346463, AF346464 Genomic DNA. Translation: AAN77250.1.
AF346465
, AF346438, AF346439, AF346440, AF346441, AF346442, AF346443, AF346444, AF346445, AF346446, AF346447, AF346448, AF346449, AF346450, AF346451, AF346452, AF346453, AF346454, AF346455, AF346456, AF346457, AF346458, AF346459, AF346460, AF346461, AF346462, AF346463, AF346464 Genomic DNA. Translation: AAN77251.1.
AY143161 Genomic DNA. Translation: AAN38831.1.
AF022889 mRNA. Translation: AAC33307.1.
CT033758
, AC118018, AC126550, AC154178, AC154491 Genomic DNA. Translation: CAM24102.1.
CT033758, AC118018, AC154491 Genomic DNA. Translation: CAM24104.1.
CT033758, AC118018, AC154491 Genomic DNA. Translation: CAM24103.1.
BC094612 mRNA. Translation: AAH94612.1.
AK050380 mRNA. Translation: BAC34222.1.
AK080024 mRNA. Translation: BAC37808.1.
CCDSiCCDS28973.1. [Q8CG19-1]
CCDS37694.1. [Q8CG19-2]
RefSeqiNP_064303.2. NM_019919.3. [Q8CG19-1]
NP_996841.1. NM_206958.2. [Q8CG19-2]
XP_006524418.1. XM_006524355.2. [Q8CG19-3]
UniGeneiMm.269747.

3D structure databases

ProteinModelPortaliQ8CG19.
SMRiQ8CG19. Positions 542-731, 864-1497, 1622-1688.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234589. 1 interaction.
IntActiQ8CG19. 1 interaction.
MINTiMINT-1751360.
STRINGi10090.ENSMUSP00000001927.

PTM databases

PhosphoSiteiQ8CG19.

Proteomic databases

MaxQBiQ8CG19.
PaxDbiQ8CG19.
PRIDEiQ8CG19.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001927; ENSMUSP00000001927; ENSMUSG00000001870. [Q8CG19-1]
ENSMUST00000112514; ENSMUSP00000108133; ENSMUSG00000001870. [Q8CG19-3]
ENSMUST00000112516; ENSMUSP00000108135; ENSMUSG00000001870. [Q8CG19-2]
GeneIDi268977.
KEGGimmu:268977.
UCSCiuc008dom.2. mouse. [Q8CG19-1]
uc008doo.2. mouse. [Q8CG19-2]

Organism-specific databases

CTDi4052.
MGIiMGI:109151. Ltbp1.

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
ENOG410Z7XK. LUCA.
GeneTreeiENSGT00760000118806.
InParanoidiQ8CG19.
KOiK19559.
OMAiTQLGRCF.
OrthoDBiEOG7FR7FP.
PhylomeDBiQ8CG19.
TreeFamiTF317514.

Enzyme and pathway databases

ReactomeiR-MMU-2129379. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSiLtbp1. mouse.
NextBioi392619.
PROiQ8CG19.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CG19.
ExpressionAtlasiQ8CG19. baseline and differential.
GenevisibleiQ8CG19. MM.

Family and domain databases

Gene3Di3.90.290.10. 5 hits.
InterProiIPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PfamiPF07645. EGF_CA. 15 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 18 hits.
SM00179. EGF_CA. 16 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the mouse Ltbp-1 gene reveals tissue specific expression of alternatively spliced forms."
    Noguera I., Obata H., Gualandris A., Cowin P., Rifkin D.B.
    Gene 308:31-41(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS LONG AND SHORT).
  2. "The murine latent transforming growth factor-beta binding protein (Ltbp-1) is alternatively spliced, and maps to a region syntenic to human chromosome 2p21-22."
    Weiskirchen R., Moser M., Guenther K., Weiskirchen S., Gressner A.M.
    Gene 308:43-52(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    Strain: 129/SvJImported.
  3. Noguera I., Cowin P., Rifkin D.B.
    Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
    Strain: BALB/cJ.
    Tissue: Heart.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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).
    Strain: C57BL/6J.
    Tissue: Brain.
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1111-1712.
    Strain: C57BL/6J.
    Tissue: Aorta, Liver and Vein.
  7. "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.
  8. "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.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1607, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung.

Entry informationi

Entry nameiLTBP1_MOUSE
AccessioniPrimary (citable) accession number: Q8CG19
Secondary accession number(s): B1B1D9
, B1B1E1, O88349, Q505C9, Q8BNW7, Q8C7F5, Q8CG18, Q8CIR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 5, 2009
Last modified: May 11, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.