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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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 23Sequence analysisAdd BLAST23
ChainiPRO_000000763724 – 1712Latent-transforming growth factor beta-binding protein 1Add BLAST1689

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi185 ↔ 195PROSITE-ProRule annotation
Disulfide bondi189 ↔ 201PROSITE-ProRule annotation
Disulfide bondi203 ↔ 212PROSITE-ProRule annotation
Glycosylationi339N-linked (GlcNAc...)Sequence analysis1
Glycosylationi370N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi395 ↔ 405PROSITE-ProRule annotation
Disulfide bondi399 ↔ 411PROSITE-ProRule annotation
Disulfide bondi413 ↔ 422PROSITE-ProRule annotation
Glycosylationi416N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi551 ↔ 573PROSITE-ProRule annotation
Disulfide bondi560 ↔ 586PROSITE-ProRule annotation
Disulfide bondi574 ↔ 589PROSITE-ProRule annotation
Glycosylationi612N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi622 ↔ 633PROSITE-ProRule annotation
Disulfide bondi628 ↔ 642PROSITE-ProRule annotation
Disulfide bondi644 ↔ 657PROSITE-ProRule annotation
Disulfide bondi671 ↔ 694PROSITE-ProRule annotation
Disulfide bondi681 ↔ 706PROSITE-ProRule annotation
Disulfide bondi695 ↔ 709PROSITE-ProRule annotation
Disulfide bondi696 ↔ 721PROSITE-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(3R)-3-hydroxyasparagineBy similarity1
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
Glycosylationi1042N-linked (GlcNAc...)Sequence analysis1
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(3R)-3-hydroxyasparagineBy similarity1
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
Glycosylationi1242N-linked (GlcNAc...)Sequence analysis1
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 bondi1350Interchain (with C-33 in TGFB1); in linked formPROSITE-ProRule annotation
Glycosylationi1357N-linked (GlcNAc...)By similarity1
Disulfide bondi1364 ↔ 1380PROSITE-ProRule annotation
Disulfide bondi1365 ↔ 1392PROSITE-ProRule annotation
Disulfide bondi1375Interchain (with C-33 in TGFB1); in linked formPROSITE-ProRule annotation
Modified residuei1405PhosphoserineBy similarity1
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
Disulfide bondi1517 ↔ 1541PROSITE-ProRule annotation
Disulfide bondi1527 ↔ 1553PROSITE-ProRule annotation
Disulfide bondi1542 ↔ 1556PROSITE-ProRule annotation
Disulfide bondi1543 ↔ 1568PROSITE-ProRule annotation
Modified residuei1588PhosphoserineBy similarity1
Modified residuei1607PhosphoserineCombined sources1
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

PaxDbiQ8CG19.
PeptideAtlasiQ8CG19.
PRIDEiQ8CG19.

PTM databases

iPTMnetiQ8CG19.
PhosphoSitePlusiQ8CG19.

Expressioni

Gene expression databases

BgeeiENSMUSG00000001870.
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. Interacts with FBN2. Interacts with ADAMTSL2. Interacts (via C-terminal domain) with FBN1 (via N-terminal domain).By similarity

GO - Molecular functioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ8CG19.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini181 – 213EGF-like 1PROSITE-ProRule annotationAdd BLAST33
Domaini391 – 423EGF-like 2PROSITE-ProRule annotationAdd BLAST33
Domaini549 – 601TB 1PROSITE-ProRule annotationAdd BLAST53
Domaini618 – 658EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini669 – 721TB 2PROSITE-ProRule annotationAdd BLAST53
Domaini865 – 906EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini907 – 948EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini949 – 989EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini990 – 1029EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Domaini1030 – 1070EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1071 – 1111EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1112 – 1152EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1153 – 1193EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1194 – 1235EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1236 – 1277EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST42
Domaini1278 – 1320EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1338 – 1392TB 3PROSITE-ProRule annotationAdd BLAST55
Domaini1415 – 1457EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST43
Domaini1458 – 1498EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Domaini1515 – 1568TB 4PROSITE-ProRule annotationAdd BLAST54
Domaini1612 – 1652EGF-like 17PROSITE-ProRule annotationAdd BLAST41
Domaini1653 – 1697EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd BLAST45

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1498 – 1712C-terminal domainBy similarityAdd BLAST215

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi96 – 124Pro-richAdd BLAST29

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.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
ENOG410Z7XK. LUCA.
GeneTreeiENSGT00760000118806.
InParanoidiQ8CG19.
KOiK19559.
OMAiTQLGRCF.
OrthoDBiEOG091G008S.
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)DescriptionActionsGraphical viewLength
Sequence conflicti313S → F in AAN77250 (PubMed:12711388).Curated1
Sequence conflicti506A → T in AAN77250 (PubMed:12711388).Curated1
Sequence conflicti506A → T in AAN77251 (PubMed:12711388).Curated1
Sequence conflicti506A → T in AAC33307 (Ref. 3) Curated1
Sequence conflicti559Q → QQ in AAN77250 (PubMed:12711388).Curated1
Sequence conflicti559Q → QQ in AAC33307 (Ref. 3) Curated1
Sequence conflicti1033E → K in AAC33307 (Ref. 3) Curated1
Sequence conflicti1111E → G in BAC34222 (PubMed:16141072).Curated1
Sequence conflicti1216S → F in BAC34222 (PubMed:16141072).Curated1
Sequence conflicti1631Q → H in AAN77250 (PubMed:12711388).Curated1
Sequence conflicti1631Q → H in AAN77251 (PubMed:12711388).Curated1
Sequence conflicti1659E → G in BAC34222 (PubMed:16141072).Curated1
Sequence conflicti1712E → N in AAC33307 (Ref. 3) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0369681 – 318Missing in isoform Short and isoform 3. 1 PublicationAdd BLAST318
Alternative sequenceiVSP_036969319 – 336EGSFS…TAPFQ → MDTKLMCLLFFLCLPLLL in isoform Short and isoform 3. 1 PublicationAdd BLAST18
Alternative sequenceiVSP_036970716 – 768Missing in isoform 3. CuratedAdd BLAST53

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_019919.4. [Q8CG19-1]
NP_996841.1. NM_206958.3. [Q8CG19-2]
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_019919.4. [Q8CG19-1]
NP_996841.1. NM_206958.3. [Q8CG19-2]
UniGeneiMm.269747.

3D structure databases

ProteinModelPortaliQ8CG19.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ8CG19.
PhosphoSitePlusiQ8CG19.

Proteomic databases

PaxDbiQ8CG19.
PeptideAtlasiQ8CG19.
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.
OrthoDBiEOG091G008S.
PhylomeDBiQ8CG19.
TreeFamiTF317514.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiLtbp1. mouse.
PROiQ8CG19.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000001870.
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...

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: November 30, 2016
This is version 139 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.