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Q9NS15

- LTBP3_HUMAN

UniProt

Q9NS15 - LTBP3_HUMAN

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Protein

Latent-transforming growth factor beta-binding protein 3

Gene

LTBP3

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 binding Source: UniProt

GO - Biological processi

  1. bone morphogenesis Source: Ensembl
  2. bone remodeling Source: Ensembl
  3. extracellular matrix organization Source: Reactome
  4. lung saccule development Source: Ensembl
  5. negative regulation of bone mineralization Source: Ensembl
  6. negative regulation of chondrocyte differentiation Source: Ensembl
  7. positive regulation of bone resorption Source: Ensembl
  8. positive regulation of mesenchymal stem cell differentiation Source: UniProt
  9. positive regulation of mesenchymal stem cell proliferation Source: UniProt
  10. transforming growth factor beta activation Source: UniProt
  11. transforming growth factor beta receptor signaling pathway Source: Ensembl
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 3
Short name:
LTBP-3
Gene namesi
Name:LTBP3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:6716. LTBP3.

Subcellular locationi

Secreted By similarity
Note: Secretion occurs after coexpression with TGFB1 and requires complexing with 'Cys-33' of the TGFB1 propeptide.By similarity

GO - Cellular componenti

  1. extracellular matrix Source: UniProt
  2. extracellular region Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Tooth agenesis selective 6 (STHAG6) [MIM:613097]: A form of selective tooth agenesis, a common anomaly characterized by the congenital absence of one or more teeth. Selective tooth agenesis without associated systemic disorders has sometimes been divided into 2 types: oligodontia, defined as agenesis of 6 or more permanent teeth, and hypodontia, defined as agenesis of less than 6 teeth. The number in both cases does not include absence of third molars (wisdom teeth). In tooth agenesis selective type 6, alveolar bone is absent where the teeth are missing. Some individuals have short stature.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Organism-specific databases

MIMi613097. phenotype.
Orphaneti2227. Hypodontia.
99798. Oligodontia.
PharmGKBiPA30479.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4343Sequence AnalysisAdd
BLAST
Chaini44 – 13031260Latent-transforming growth factor beta-binding protein 3PRO_0000007646Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi113 ↔ 123PROSITE-ProRule annotation
Disulfide bondi117 ↔ 129PROSITE-ProRule annotation
Disulfide bondi131 ↔ 140PROSITE-ProRule annotation
Glycosylationi349 – 3491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi359 ↔ 370PROSITE-ProRule annotation
Disulfide bondi365 ↔ 379PROSITE-ProRule annotation
Disulfide bondi381 ↔ 394PROSITE-ProRule annotation
Disulfide bondi578 ↔ 590PROSITE-ProRule annotation
Disulfide bondi585 ↔ 599PROSITE-ProRule annotation
Disulfide bondi601 ↔ 614PROSITE-ProRule annotation
Disulfide bondi620 ↔ 632PROSITE-ProRule annotation
Disulfide bondi625 ↔ 641PROSITE-ProRule annotation
Disulfide bondi643 ↔ 658PROSITE-ProRule annotation
Disulfide bondi664 ↔ 676PROSITE-ProRule annotation
Disulfide bondi670 ↔ 685PROSITE-ProRule annotation
Disulfide bondi687 ↔ 701PROSITE-ProRule annotation
Disulfide bondi748 ↔ 759PROSITE-ProRule annotation
Disulfide bondi754 ↔ 768PROSITE-ProRule annotation
Disulfide bondi770 ↔ 783PROSITE-ProRule annotation
Disulfide bondi789 ↔ 800PROSITE-ProRule annotation
Disulfide bondi795 ↔ 809PROSITE-ProRule annotation
Disulfide bondi811 ↔ 824PROSITE-ProRule annotation
Disulfide bondi830 ↔ 841PROSITE-ProRule annotation
Disulfide bondi836 ↔ 850PROSITE-ProRule annotation
Glycosylationi845 – 8451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi852 ↔ 864PROSITE-ProRule annotation
Disulfide bondi870 ↔ 883PROSITE-ProRule annotation
Disulfide bondi877 ↔ 892PROSITE-ProRule annotation
Disulfide bondi894 ↔ 907PROSITE-ProRule annotation
Glycosylationi936 – 9361N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi997 ↔ 1010PROSITE-ProRule annotation
Disulfide bondi1005 ↔ 1019PROSITE-ProRule annotation
Disulfide bondi1021 ↔ 1034PROSITE-ProRule annotation
Disulfide bondi1040 ↔ 1051PROSITE-ProRule annotation
Disulfide bondi1046 ↔ 1060PROSITE-ProRule annotation
Disulfide bondi1062 ↔ 1075PROSITE-ProRule annotation
Disulfide bondi1086 ↔ 1097PROSITE-ProRule annotation
Disulfide bondi1092 ↔ 1106PROSITE-ProRule annotation
Disulfide bondi1108 ↔ 1121PROSITE-ProRule annotation
Disulfide bondi1258 ↔ 1273PROSITE-ProRule annotation
Disulfide bondi1268 ↔ 1282PROSITE-ProRule annotation
Glycosylationi1275 – 12751N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1284 ↔ 1297PROSITE-ProRule annotation

Post-translational modificationi

Contains hydroxylated asparagine residues.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

Proteomic databases

MaxQBiQ9NS15.
PaxDbiQ9NS15.
PRIDEiQ9NS15.

PTM databases

PhosphoSiteiQ9NS15.

Expressioni

Tissue specificityi

Isoform 2 is expressed prominently in heart, skeletal muscle, prostate, testis, small intestine and ovary. Isoform 1 is strongly expressed in pancreas and liver.

Gene expression databases

BgeeiQ9NS15.
CleanExiHS_LTBP3.
ExpressionAtlasiQ9NS15. baseline and differential.
GenevestigatoriQ9NS15.

Interactioni

Subunit structurei

Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex.

Protein-protein interaction databases

BioGridi110232. 8 interactions.
IntActiQ9NS15. 6 interactions.
MINTiMINT-1184940.
STRINGi9606.ENSP00000301873.

Structurei

3D structure databases

ProteinModelPortaliQ9NS15.
SMRiQ9NS15. Positions 296-461, 573-1116, 1234-1297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini109 – 14133EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini277 – 33155TB 1Add
BLAST
Domaini355 – 39541EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini403 – 45553TB 2Add
BLAST
Domaini574 – 61542EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini616 – 65944EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini660 – 70243EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini744 – 78441EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini785 – 82541EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini826 – 86540EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini866 – 90843EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini917 – 97155TB 3Add
BLAST
Domaini993 – 103543EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1036 – 107641EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1082 – 112241EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1136 – 118651TB 4Add
BLAST
Domaini1254 – 129845EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 167165Gly-richAdd
BLAST
Compositional biasi578 – 894317Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the LTBP family.Curated
Contains 13 EGF-like domains.PROSITE-ProRule annotation
Contains 4 TB (TGF-beta binding) domains.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG261244.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiQ9NS15.
KOiK08023.
OMAiEGPPAQH.
PhylomeDBiQ9NS15.
TreeFamiTF317514.

Family and domain databases

Gene3Di3.90.290.10. 5 hits.
InterProiIPR026823. cEGF.
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]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 10 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 3 hits.
SM00179. EGF_CA. 12 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 4 hits.
SSF57581. SSF57581. 4 hits.
PROSITEiPS00010. ASX_HYDROXYL. 11 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 13 hits.
PS01187. EGF_CA. 12 hits.
PS51364. TB. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NS15-1) [UniParc]FASTAAdd to Basket

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
MPGPRGAAGG LAPEMRGAGA AGLLALLLLL LLLLLGLGGR VEGGPAGERG
60 70 80 90 100
AGGGGALARE RFKVVFAPVI CKRTCLKGQC RDSCQQGSNM TLIGENGHST
110 120 130 140 150
DTLTGSGFRV VVCPLPCMNG GQCSSRNQCL CPPDFTGRFC QVPAGGAGGG
160 170 180 190 200
TGGSGPGLSR TGALSTGALP PLAPEGDSVA SKHAIYAVQV IADPPGPGEG
210 220 230 240 250
PPAQHAAFLV PLGPGQISAE VQAPPPVVNV RVHHPPEASV QVHRIESSNA
260 270 280 290 300
ESAAPSQHLL PHPKPSHPRP PTQKPLGRCF QDTLPKQPCG SNPLPGLTKQ
310 320 330 340 350
EDCCGSIGTA WGQSKCHKCP QLQYTGVQKP GPVRGEVGAD CPQGYKRLNS
360 370 380 390 400
THCQDINECA MPGVCRHGDC LNNPGSYRCV CPPGHSLGPS RTQCIADKPE
410 420 430 440 450
EKSLCFRLVS PEHQCQHPLT TRLTRQLCCC SVGKAWGARC QRCPTDGTAA
460 470 480 490 500
FKEICPAGKG YHILTSHQTL TIQGESDFSL FLHPDGPPKP QQLPESPSQA
510 520 530 540 550
PPPEDTEEER GVTTDSPVSE ERSVQQSHPT ATTTPARPYP ELISRPSPPT
560 570 580 590 600
MRWFLPDLPP SRSAVEIAPT QVTETDECRL NQNICGHGEC VPGPPDYSCH
610 620 630 640 650
CNPGYRSHPQ HRYCVDVNEC EAEPCGPGRG ICMNTGGSYN CHCNRGYRLH
660 670 680 690 700
VGAGGRSCVD LNECAKPHLC GDGGFCINFP GHYKCNCYPG YRLKASRPPV
710 720 730 740 750
CEDIDECRDP SSCPDGKCEN KPGSFKCIAC QPGYRSQGGG ACRDVNECAE
760 770 780 790 800
GSPCSPGWCE NLPGSFRCTC AQGYAPAPDG RSCLDVDECE AGDVCDNGIC
810 820 830 840 850
SNTPGSFQCQ CLSGYHLSRD RSHCEDIDEC DFPAACIGGD CINTNGSYRC
860 870 880 890 900
LCPQGHRLVG GRKCQDIDEC SQDPSLCLPH GACKNLQGSY VCVCDEGFTP
910 920 930 940 950
TQDQHGCEEV EQPHHKKECY LNFDDTVFCD SVLATNVTQQ ECCCSLGAGW
960 970 980 990 1000
GDHCEIYPCP VYSSAEFHSL CPDGKGYTQD NNIVNYGIPA HRDIDECMLF
1010 1020 1030 1040 1050
GSEICKEGKC VNTQPGYECY CKQGFYYDGN LLECVDVDEC LDESNCRNGV
1060 1070 1080 1090 1100
CENTRGGYRC ACTPPAEYSP AQRQCLSPEE MDVDECQDPA ACRPGRCVNL
1110 1120 1130 1140 1150
PGSYRCECRP PWVPGPSGRD CQLPESPAER APERRDVCWS QRGEDGMCAG
1160 1170 1180 1190 1200
PLAGPALTFD DCCCRQGRGW GAQCRPCPPR GAGSHCPTSQ SESNSFWDTS
1210 1220 1230 1240 1250
PLLLGKPPRD EDSSEEDSDE CRCVSGRCVP RPGGAVCECP GGFQLDASRA
1260 1270 1280 1290 1300
RCVDIDECRE LNQRGLLCKS ERCVNTSGSF RCVCKAGFAR SRPHGACVPQ

RRR
Length:1,303
Mass (Da):139,359
Last modified:October 17, 2006 - v4
Checksum:i3BC6B1EE19198414
GO
Isoform 2 (identifier: Q9NS15-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1082-1128: Missing.

Show »
Length:1,256
Mass (Da):134,292
Checksum:i1D930E5D208601E2
GO

Sequence cautioni

The sequence BAB15767.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351Missing in BAB15767. 1 PublicationCurated
Sequence conflicti477 – 4771D → H in AAB64201. (PubMed:9620332)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1082 – 112847Missing in isoform 2. 1 PublicationVSP_009241Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF135960 mRNA. Translation: AAF62352.3.
AK024477 mRNA. Translation: BAB15767.1. Different initiation.
AF011407 mRNA. Translation: AAB64201.1.
BC008761 mRNA. Translation: AAH08761.2.
AL117551 mRNA. Translation: CAB55988.1.
CCDSiCCDS44647.1. [Q9NS15-1]
CCDS8103.1. [Q9NS15-2]
PIRiT17298.
RefSeqiNP_001123616.1. NM_001130144.2. [Q9NS15-1]
NP_001157738.1. NM_001164266.1.
NP_066548.2. NM_021070.4. [Q9NS15-2]
UniGeneiHs.289019.

Genome annotation databases

EnsembliENST00000301873; ENSP00000301873; ENSG00000168056. [Q9NS15-1]
ENST00000322147; ENSP00000326647; ENSG00000168056. [Q9NS15-2]
GeneIDi4054.
KEGGihsa:4054.
UCSCiuc001oei.3. human. [Q9NS15-2]
uc001oej.3. human. [Q9NS15-1]

Polymorphism databases

DMDMi116242623.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF135960 mRNA. Translation: AAF62352.3 .
AK024477 mRNA. Translation: BAB15767.1 . Different initiation.
AF011407 mRNA. Translation: AAB64201.1 .
BC008761 mRNA. Translation: AAH08761.2 .
AL117551 mRNA. Translation: CAB55988.1 .
CCDSi CCDS44647.1. [Q9NS15-1 ]
CCDS8103.1. [Q9NS15-2 ]
PIRi T17298.
RefSeqi NP_001123616.1. NM_001130144.2. [Q9NS15-1 ]
NP_001157738.1. NM_001164266.1.
NP_066548.2. NM_021070.4. [Q9NS15-2 ]
UniGenei Hs.289019.

3D structure databases

ProteinModelPortali Q9NS15.
SMRi Q9NS15. Positions 296-461, 573-1116, 1234-1297.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110232. 8 interactions.
IntActi Q9NS15. 6 interactions.
MINTi MINT-1184940.
STRINGi 9606.ENSP00000301873.

PTM databases

PhosphoSitei Q9NS15.

Polymorphism databases

DMDMi 116242623.

Proteomic databases

MaxQBi Q9NS15.
PaxDbi Q9NS15.
PRIDEi Q9NS15.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301873 ; ENSP00000301873 ; ENSG00000168056 . [Q9NS15-1 ]
ENST00000322147 ; ENSP00000326647 ; ENSG00000168056 . [Q9NS15-2 ]
GeneIDi 4054.
KEGGi hsa:4054.
UCSCi uc001oei.3. human. [Q9NS15-2 ]
uc001oej.3. human. [Q9NS15-1 ]

Organism-specific databases

CTDi 4054.
GeneCardsi GC11M065306.
HGNCi HGNC:6716. LTBP3.
MIMi 602090. gene.
613097. phenotype.
neXtProti NX_Q9NS15.
Orphaneti 2227. Hypodontia.
99798. Oligodontia.
PharmGKBi PA30479.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG261244.
GeneTreei ENSGT00760000118806.
HOGENOMi HOG000293153.
HOVERGENi HBG052370.
InParanoidi Q9NS15.
KOi K08023.
OMAi EGPPAQH.
PhylomeDBi Q9NS15.
TreeFami TF317514.

Enzyme and pathway databases

Reactomei REACT_150331. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSi LTBP3. human.
GeneWikii LTBP3.
GenomeRNAii 4054.
NextBioi 15884.
PROi Q9NS15.
SOURCEi Search...

Gene expression databases

Bgeei Q9NS15.
CleanExi HS_LTBP3.
ExpressionAtlasi Q9NS15. baseline and differential.
Genevestigatori Q9NS15.

Family and domain databases

Gene3Di 3.90.290.10. 5 hits.
InterProi IPR026823. cEGF.
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 PF12662. cEGF. 1 hit.
PF07645. EGF_CA. 10 hits.
PF00683. TB. 4 hits.
[Graphical view ]
SMARTi SM00181. EGF. 3 hits.
SM00179. EGF_CA. 12 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 4 hits.
SSF57581. SSF57581. 4 hits.
PROSITEi PS00010. ASX_HYDROXYL. 11 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 13 hits.
PS01187. EGF_CA. 12 hits.
PS51364. TB. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Secretion of human latent TGF-beta-binding protein-3 (LTBP-3) is dependent on co-expression of TGF-beta."
    Penttinen C., Saharinen J., Weikkolainen K., Hyytiainen M., Keski-Oja J.
    J. Cell Sci. 115:3457-3468(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION (ISOFORM 2).
  2. "The nucleotide sequence of a long cDNA clone isolated from human spleen."
    Ohara O., Nagase T., Kikuno R., Okumura K.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Spleen.
  3. "Analysis of the expression pattern of the latent transforming growth factor beta binding protein isoforms in normal and diseased human liver reveals a new splice variant missing the proteinase-sensitive hinge region."
    Michel K., Roth S., Trautwein C., Gong W., Flemming P., Gressner A.M.
    Hepatology 27:1592-1599(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 394-573.
    Tissue: Liver.
  4. "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] OF 514-1303 (ISOFORM 2).
    Tissue: Colon.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 793-1303.
    Tissue: Uterus.
  6. "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.
  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. "Oligodontia is caused by mutation in LTBP3, the gene encoding latent TGF-beta binding protein 3."
    Noor A., Windpassinger C., Vitcu I., Orlic M., Rafiq M.A., Khalid M., Malik M.N., Ayub M., Alman B., Vincent J.B.
    Am. J. Hum. Genet. 84:519-523(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN STHAG6.

Entry informationi

Entry nameiLTBP3_HUMAN
AccessioniPrimary (citable) accession number: Q9NS15
Secondary accession number(s): O15107
, Q96HB9, Q9H7K2, Q9UFN4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 17, 2006
Last modified: November 26, 2014
This is version 130 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3