LTBP1
entrez
4052
canonical
uniprot
Q14766
canonical
ensembl
ENSG00000049323
resolver
ensp
ENSP00000384091
resolver
ensp
ENSP00000385359
resolver
ensp
ENSP00000386043
resolver
ensp
ENSP00000393057
resolver
ensp
ENSP00000562736
resolver
ensp
ENSP00000562737
resolver
ensp
ENSP00000562738
resolver
ensp
ENSP00000599219
resolver
ensp
ENSP00000599220
resolver
ensp
ENSP00000599225
resolver
ensp
ENSP00000599226
resolver
ensp
ENSP00000599227
resolver
ensp
ENSP00000599229
resolver
ensp
ENSP00000624881
resolver
ensp
ENSP00000624882
resolver
ensp
ENSP00000624883
resolver
enst
ENST00000418533
resolver
genesymbol
LTBP1
resolver
hgnc
HGNC:6714
resolver
uniprot
A1L3V1
resolver
uniprot
B7ZLY3
resolver
uniprot
E7EV71
resolver
uniprot
P22064
resolver
uniprot
Q53SD8
resolver
uniprot
Q53SF3
resolver
uniprot
Q53SG1
resolver
uniprot
Q59HF7
resolver
uniprot
Q8TD95
resolver
uniprot_entry
B7ZLY3_HUMAN
resolver
uniprot_entry
E7EV71_HUMAN
resolver
uniprot_entry
LTBP1_HUMAN
resolver
uniprot_sec
A1L3V1
resolver
uniprot_sec
P22064
resolver
uniprot_sec
Q53SD8
resolver
uniprot_sec
Q53SF3
resolver
uniprot_sec
Q53SG1
resolver
uniprot_sec
Q59HF7
resolver
uniprot_sec
Q8TD95
resolver
amino_acid_sequence
MAGAWLRWGLLLWAGLLASSAHGRLRRITYVVHPGPGLAAGALPLSGPPRSRTFNVALNARYSRSSAAAGAPSRASPGVPSERTRRTSKPGGAALQGLRPPPPPPPEPARPAVPGGQLHPNPGGHPAAAPFTKQGRQVVRSKVPQETQSGGGSRLQVHQKQQLQGVNVCGGRCCHGWSKAPGSQRCTKPSCVPPCQNGGMCLRPQLCVCKPGTKGKACETIAAQDTSSPVFGGQSPGAASSWGPPEQAAKHTSSKKADTLPRVSPVAQMTLTLKPKPSVGLPQQIHSQVTPLSSQSVVIHHGQTQEYVLKPKYFPAQKGISGEQSTEGSFPLRYVQDQVAAPFQLSNHTGRIKVVFTPSICKVTCTKGSCQNSCEKGNTTTLISENGHAADTLTATNFRVVICHLPCMNGGQCSSRDKCQCPPNFTGKLCQIPVHGASVPKLYQHSQQPGKALGTHVIHSTHTLPLTVTSQQGVKVKFPPNIVNIHVKHPPEASVQIHQVSRIDGPTGQKTKEAQPGQSQVSYQGLPVQKTQTIHSTYSHQQVIPHVYPVAAKTQLGRCFQETIGSQCGKALPGLSKQEDCCGTVGTSWGFNKCQKCPKKPSYHGYNQMMECLPGYKRVNNTFCQDINECQLQGVCPNGECLNTMGSYRCTCKIGFGPDPTFSSCVPDPPVISEEKGPCYRLVSSGRQCMHPLSVHLTKQLCCCSVGKAWGPHCEKCPLPGTAAFKEICPGGMGYTVSGVHRRRPIHHHVGKGPVFVKPKNTQPVAKSTHPPPLPAKEEPVEALTFSREHGPGVAEPEVATAPPEKEIPSLDQEKTKLEPGQPQLSPGISTIHLHPQFPVVIEKTSPPVPVEVAPEASTSSASQVIAPTQVTEINECTVNPDICGAGHCINLPVRYTCICYEGYRFSEQQRKCVDIDECTQVQHLCSQGRCENTEGSFLCICPAGFMASEEGTNCIDVDECLRPDVCGEGHCVNTVGAFRCEYCDSGYRMTQRGRCEDIDECLNPSTCPDEQCVNSPGSYQCVPCTEGFRGWNGQCLDVDECLEPNVCANGDCSNLEGSYMCSCHKGYTRTPDHKHCRDIDECQQGNLCVNGQCKNTEGSFRCTCGQGYQLSAAKDQCEDIDECQHRHLCAHGQCRNTEGSFQCVCDQGYRASGLGDHCEDINECLEDKSVCQRGDCINTAGSYDCTCPDGFQLDDNKTCQDINECEHPGLCGPQGECLNTEGSFHCVCQQGFSISADGRTCEDIDECVNNTVCDSHGFCDNTAGSFRCLCYQGFQAPQDGQGCVDVNECELLSGVCGEAFCENVEGSFLCVCADENQEYSPMTGQCRSRTSTDLDVDVDQPKEEKKECYYNLNDASLCDNVLAPNVTKQECCCTSGVGWGDNCEIFPCPVLGTAEFTEMCPKGKGFVPAGESSSEAGGENYKDADECLLFGQEICKNGFCLNTRPGYECYCKQGTYYDPVKLQCFDMDECQDPSSCIDGQCVNTEGSYNCFCTHPMVLDASEKRCIRPAESNEQIEETDVYQDLCWEHLSDEYVCSRPLVGKQTTYTECCCLYGEAWGMQCALCPLKDSDDYAQLCNIPVTGRRQPYGRDALVDFSEQYTPEADPYFIQDRFLNSFEELQAEECGILNGCENGRCVRVQEGYTCDCFDGYHLDTAKMTCVDVNECDELNNRMSLCKNAKCINTDGSYKCLCLPGYVPSDKPNYCTPLNTALNLEKDSDLE
uniprot
proteins
disease_involvement
DISEASE: Cutis laxa, autosomal recessive, 2E (ARCL2E) [MIM:619451]: A form of cutis laxa, a disorder characterized by an excessive congenital skin wrinkling, a large fontanelle with delayed closure, a typical facial appearance with downslanting palpebral fissures, and a general connective tissue weakness. ARCL2E patients present with cutis laxa, inguinal hernia, craniofacial dysmorphology, variable heart defects, and prominent skeletal features including craniosynostosis, short stature, brachydactyly, and syndactyly. {ECO:0000269|PubMed:33991472}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Key regulator of transforming growth factor beta (TGFB1, TGFB2 and TGFB3) that controls TGF-beta activation by maintaining it in a latent state during storage in extracellular space (PubMed:2022183, PubMed:8617200, PubMed:8939931). Associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGF-beta, and regulates integrin-dependent activation of TGF-beta (PubMed:15184403, PubMed:8617200, PubMed:8939931). Outcompeted by LRRC32/GARP for binding to LAP regulatory chain of TGF-beta (PubMed:22278742). {ECO:0000269|PubMed:15184403, ECO:0000269|PubMed:2022183, ECO:0000269|PubMed:22278742, ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931}.
uniprot
proteins
mass_dalton
186796
uniprot
proteins
mutagenesis
MUTAGEN 1348; /note="E->A: Abolishes interaction with the Latency-associated peptide chain (LAP) regulatory chain of TGFB1; when associated with 1382-A--A-1385."; /evidence="ECO:0000269|PubMed:15567420"; MUTAGEN 1366; /note="N->A,Q: Abolishes N-glycosylation at this site without affecting ability to interact with the Latency-associated peptide chain (LAP) regulatory chain of TGFB1."; /evidence="ECO:0000269|PubMed:8617200, ECO:0000269|PubMed:8939931"; MUTAGEN 1382..1385; /note="DNCE->ANCA: Abolishes interaction with the Latency-associated peptide chain (LAP) regulatory chain of TGFB1; when associated with A-1348."; /evidence="ECO:0000269|PubMed:15567420"; MUTAGEN 1385..1388; /note="EIFP->DL: Loss of binding to TGFB1."; /evidence="ECO:0000269|PubMed:10930463
uniprot
proteins
post_translational_modification
PTM: Contains hydroxylated asparagine residues. {ECO:0000269|PubMed:2350783}.; PTM: Isoform Short N-terminus is blocked. {ECO:0000269|PubMed:2350783}.; PTM: 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. {ECO:0000269|PubMed:14607119}.; PTM: O-glycosylated on serine residues by POGLUT2 and POGLUT3. {ECO:0000269|PubMed:34411563}.
uniprot
proteins
protein_family
LTBP family
uniprot
proteins
pubmed
10677208
uniprot
proteins
pubmed
10743502
uniprot
proteins
pubmed
10930463
uniprot
proteins
pubmed
11104663
uniprot
proteins
pubmed
12429738
uniprot
proteins
pubmed
14607119
uniprot
proteins
pubmed
15184403
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15567420
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16157329
uniprot
proteins
pubmed
17293099
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18677313
uniprot
proteins
pubmed
2022183
uniprot
proteins
pubmed
22278742
uniprot
proteins
pubmed
2350783
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26091039
uniprot
proteins
pubmed
27339457
uniprot
proteins
pubmed
33991472
uniprot
proteins
pubmed
34411563
uniprot
proteins
pubmed
38237698
uniprot
proteins
pubmed
8537398
uniprot
proteins
pubmed
8617200
uniprot
proteins
pubmed
8939931
uniprot
proteins
sequence_length
1721
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16157329}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:16157329, ECO:0000269|PubMed:8617200}.
uniprot
proteins