Reviewed, UniProtKB/Swiss-Prot Q14766 (LTBP1_HUMAN)

Names and origin

Protein names

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 names

Name:

LTBP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1721 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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).
Subunit structure	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. Ref.10 Ref.11 Ref.13
Subcellular location	Secreted.
Tissue specificity	The long isoform is found in fibroblasts.
Domain	Associates covalently with small latent TGF-beta complex via domain TB 3.
Post-translational modification	Contains hydroxylated asparagine residues. The N-terminus is blocked (isoform Short). The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains By similarity.
Sequence similarities	Belongs to the LTBP family. Contains 18 EGF-like domains. Contains 4 TB (TGF-beta binding) domains.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Alternative splicing
Domain	EGF-like domain Repeat Signal
Ligand	Growth factor binding
PTM	Disulfide bond Glycoprotein Hydroxylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA proteinaceous extracellular matrix Ref.7 Non-traceable author statement. Source: UniProtKB
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro growth factor binding Inferred from electronic annotation. Source: UniProtKB-KW transforming growth factor beta receptor activity Ref.7 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: Q14766-1)

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.

Isoform Short (identifier: Q14766-2)

Also known as: LTBP-1S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-326: Missing.
     327-345: EGSFPLRYVQDQVAAPFQL → MDTKLMCLLFFFSLPPLLV

Isoform 3 (identifier: Q14766-3)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Potential

Chain

24 – 1721

1698

Latent-transforming growth factor beta-binding protein 1

PRO_0000007635

Regions

Domain

187 – 219

33

EGF-like 1

Domain

399 – 431

33

EGF-like 2

Domain

557 – 609

53

TB 1

Domain

626 – 663

38

EGF-like 3; calcium-binding Potential

Domain

677 – 729

53

TB 2

Domain

873 – 910

38

EGF-like 4; calcium-binding Potential

Domain

915 – 956

42

EGF-like 5; calcium-binding Potential

Domain

957 – 997

41

EGF-like 6; calcium-binding Potential

Domain

998 – 1037

40

EGF-like 7; calcium-binding Potential

Domain

1038 – 1078

41

EGF-like 8; calcium-binding Potential

Domain

1079 – 1119

41

EGF-like 9; calcium-binding Potential

Domain

1120 – 1160

41

EGF-like 10; calcium-binding Potential

Domain

1161 – 1201

41

EGF-like 11; calcium-binding Potential

Domain

1202 – 1243

42

EGF-like 12; calcium-binding Potential

Domain

1244 – 1281

38

EGF-like 13; calcium-binding Potential

Domain

1286 – 1328

43

EGF-like 14; calcium-binding Potential

Domain

1347 – 1401

55

TB 3

Domain

1424 – 1466

43

EGF-like 15; calcium-binding Potential

Domain

1467 – 1503

37

EGF-like 16; calcium-binding Potential

Domain

1524 – 1577

54

TB 4

Domain

1621 – 1657

37

EGF-like 17

Domain

1662 – 1706

45

EGF-like 18; calcium-binding Potential

Motif

1174 – 1176

3

Cell attachment site Potential

Compositional bias

100 – 130

31

Pro-rich

Amino acid modifications

Modified residue

974

1

(3R)-3-hydroxyasparagine

Modified residue

1137

1

(3R)-3-hydroxyasparagine

Modified residue

1597

1

Phosphoserine Ref.12

Modified residue

1600

1

Phosphotyrosine Ref.12

Modified residue

1601

1

Phosphothreonine Ref.12

Glycosylation

347

1

N-linked (GlcNAc...) Potential

Glycosylation

378

1

N-linked (GlcNAc...) Potential

Glycosylation

424

1

N-linked (GlcNAc...) Potential

Glycosylation

620

1

N-linked (GlcNAc...) Potential

Glycosylation

1197

1

N-linked (GlcNAc...) Potential

Glycosylation

1250

1

N-linked (GlcNAc...) Potential

Glycosylation

1366

1

N-linked (GlcNAc...) Ref.14

CAR_000184

Disulfide bond

191 ↔ 201

By similarity

Disulfide bond

195 ↔ 207

By similarity

Disulfide bond

209 ↔ 218

By similarity

Disulfide bond

403 ↔ 413

By similarity

Disulfide bond

407 ↔ 419

By similarity

Disulfide bond

421 ↔ 430

By similarity

Disulfide bond

630 ↔ 641

By similarity

Disulfide bond

636 ↔ 650

By similarity

Disulfide bond

652 ↔ 665

By similarity

Disulfide bond

877 ↔ 889

By similarity

Disulfide bond

884 ↔ 898

By similarity

Disulfide bond

900 ↔ 913

By similarity

Disulfide bond

919 ↔ 931

By similarity

Disulfide bond

926 ↔ 940

By similarity

Disulfide bond

942 ↔ 955

By similarity

Disulfide bond

961 ↔ 972

By similarity

Disulfide bond

967 ↔ 981

By similarity

Disulfide bond

984 ↔ 996

By similarity

Disulfide bond

1002 ↔ 1013

By similarity

Disulfide bond

1008 ↔ 1022

By similarity

Disulfide bond

1025 ↔ 1036

By similarity

Disulfide bond

1042 ↔ 1053

By similarity

Disulfide bond

1048 ↔ 1062

By similarity

Disulfide bond

1064 ↔ 1077

By similarity

Disulfide bond

1083 ↔ 1094

By similarity

Disulfide bond

1089 ↔ 1103

By similarity

Disulfide bond

1105 ↔ 1118

By similarity

Disulfide bond

1124 ↔ 1135

By similarity

Disulfide bond

1130 ↔ 1144

By similarity

Disulfide bond

1146 ↔ 1159

By similarity

Disulfide bond

1165 ↔ 1177

By similarity

Disulfide bond

1172 ↔ 1186

By similarity

Disulfide bond

1188 ↔ 1200

By similarity

Disulfide bond

1206 ↔ 1218

By similarity

Disulfide bond

1212 ↔ 1227

By similarity

Disulfide bond

1229 ↔ 1242

By similarity

Disulfide bond

1248 ↔ 1260

By similarity

Disulfide bond

1254 ↔ 1269

By similarity

Disulfide bond

1349 ↔ 1372

Ref.15

Disulfide bond

1359 ↔ 1384

Ref.15

Disulfide bond

1373 ↔ 1389

Ref.15

Disulfide bond

1374 ↔ 1401

Ref.15

Disulfide bond

1471 ↔ 1482

By similarity

Disulfide bond

1477 ↔ 1491

By similarity

Disulfide bond

1625 ↔ 1636

By similarity

Disulfide bond

1631 ↔ 1645

By similarity

Disulfide bond

1666 ↔ 1681

By similarity

Disulfide bond

1676 ↔ 1690

By similarity

Disulfide bond

1692 ↔ 1705

By similarity

Natural variations

Alternative sequence

1 – 326

326

Missing in isoform Short and isoform 3.

VSP_036963

Alternative sequence

327 – 345

19

EGSFP…APFQL → MDTKLMCLLFFFSLPPLLV in isoform Short and isoform 3.

VSP_036964

Alternative sequence

724 – 776

53

Missing in isoform 3.

VSP_036965

Experimental info

Mutagenesis

1385 – 1388

4

EIFP → DL: Loss of binding to TGFB1. Ref.10

Sequence conflict

50

1

R → AS in AAA96327. Ref.7

Sequence conflict

691

1

H → Y in AAA61160. Ref.1

Sequence conflict

710

1

Missing in AAA61160. Ref.1

Sequence conflict

710

1

Missing in AAM03124. Ref.2

Sequence conflict

792 – 794

3

PGV → ARS in AAA61160. Ref.1

Sequence conflict

792 – 794

3

PGV → ARS in AAM03124. Ref.2

Sequence conflict

831

1

T → A in AAA61160. Ref.1

Sequence conflict

1378

1

A → V in AAY24260. Ref.4

Sequence conflict

1648

1

F → L in AAA61160. Ref.1

Sequence conflict

1648

1

F → L in AAM03124. Ref.2

Sequence conflict

1661

1

V → F in AAA61160. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1721

Helix Strand Turn

Details...

Beta strand

1340 – 1342

3

Beta strand

1346 – 1353

8

Turn

1355 – 1358

4

Beta strand

1366 – 1368

3

Helix

1369 – 1374

6

Beta strand

1378 – 1382

5

Beta strand

1385 – 1388

4

Beta strand

1392 – 1394

3

Helix

1395 – 1400

6

Beta strand

1408 – 1410

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long (LTBP-1L) [UniParc]. Last modified May 5, 2009. Version 3. Checksum: 2355712F64CC9DDB	FASTA	1,721	186,768
	10 20 30 40 50 60 MAGAWLRWGL LLWAGLLASS AHGRLRRITY VVHPGPGLAA GALPLSGPPR SRTFNVALNA 70 80 90 100 110 120 RYSRSSAAAG APSRASPGVP SERTRRTSKP GGAALQGLRP PPPPPPEPAR PAVPGGQLHP 130 140 150 160 170 180 NPGGHPAAAP FTKQGRQVVR SKVPQETQSG GGSRLQVHQK QQLQGVNVCG GRCCHGWSKA 190 200 210 220 230 240 PGSQRCTKPS CVPPCQNGGM CLRPQLCVCK PGTKGKACET IAAQDTSSPV FGGQSPGAAS 250 260 270 280 290 300 SWGPPEQAAK HTSSKKADTL PRVSPVAQMT LTLKPKPSVG LPQQIHSQVT PLSSQSVVIH 310 320 330 340 350 360 HGQTQEYVLK PKYFPAQKGI SGEQSTEGSF PLRYVQDQVA APFQLSNHTG RIKVVFTPSI 370 380 390 400 410 420 CKVTCTKGSC QNSCEKGNTT TLISENGHAA DTLTATNFRV VICHLPCMNG GQCSSRDKCQ 430 440 450 460 470 480 CPPNFTGKLC QIPVHGASVP KLYQHSQQPG KALGTHVIHS THTLPLTVTS QQGVKVKFPP 490 500 510 520 530 540 NIVNIHVKHP PEASVQIHQV SRIDGPTGQK TKEAQPGQSQ VSYQGLPVQK TQTIHSTYSH 550 560 570 580 590 600 QQVIPHVYPV AAKTQLGRCF QETIGSQCGK ALPGLSKQED CCGTVGTSWG FNKCQKCPKK 610 620 630 640 650 660 PSYHGYNQMM ECLPGYKRVN NTFCQDINEC QLQGVCPNGE CLNTMGSYRC TCKIGFGPDP 670 680 690 700 710 720 TFSSCVPDPP VISEEKGPCY RLVSSGRQCM HPLSVHLTKQ LCCCSVGKAW GPHCEKCPLP 730 740 750 760 770 780 GTAAFKEICP GGMGYTVSGV HRRRPIHHHV GKGPVFVKPK NTQPVAKSTH PPPLPAKEEP 790 800 810 820 830 840 VEALTFSREH GPGVAEPEVA TAPPEKEIPS LDQEKTKLEP GQPQLSPGIS TIHLHPQFPV 850 860 870 880 890 900 VIEKTSPPVP VEVAPEASTS SASQVIAPTQ VTEINECTVN PDICGAGHCI NLPVRYTCIC 910 920 930 940 950 960 YEGYRFSEQQ RKCVDIDECT QVQHLCSQGR CENTEGSFLC ICPAGFMASE EGTNCIDVDE 970 980 990 1000 1010 1020 CLRPDVCGEG HCVNTVGAFR CEYCDSGYRM TQRGRCEDID ECLNPSTCPD EQCVNSPGSY 1030 1040 1050 1060 1070 1080 QCVPCTEGFR GWNGQCLDVD ECLEPNVCAN GDCSNLEGSY MCSCHKGYTR TPDHKHCRDI 1090 1100 1110 1120 1130 1140 DECQQGNLCV NGQCKNTEGS FRCTCGQGYQ LSAAKDQCED IDECQHRHLC AHGQCRNTEG 1150 1160 1170 1180 1190 1200 SFQCVCDQGY RASGLGDHCE DINECLEDKS VCQRGDCINT AGSYDCTCPD GFQLDDNKTC 1210 1220 1230 1240 1250 1260 QDINECEHPG LCGPQGECLN TEGSFHCVCQ QGFSISADGR TCEDIDECVN NTVCDSHGFC 1270 1280 1290 1300 1310 1320 DNTAGSFRCL CYQGFQAPQD GQGCVDVNEC ELLSGVCGEA FCENVEGSFL CVCADENQEY 1330 1340 1350 1360 1370 1380 SPMTGQCRSR TSTDLDVDVD QPKEEKKECY YNLNDASLCD NVLAPNVTKQ ECCCTSGAGW 1390 1400 1410 1420 1430 1440 GDNCEIFPCP VLGTAEFTEM CPKGKGFVPA GESSSEAGGE NYKDADECLL FGQEICKNGF 1450 1460 1470 1480 1490 1500 CLNTRPGYEC YCKQGTYYDP VKLQCFDMDE CQDPSSCIDG QCVNTEGSYN CFCTHPMVLD 1510 1520 1530 1540 1550 1560 ASEKRCIRPA ESNEQIEETD VYQDLCWEHL SDEYVCSRPL VGKQTTYTEC CCLYGEAWGM 1570 1580 1590 1600 1610 1620 QCALCPLKDS DDYAQLCNIP VTGRRQPYGR DALVDFSEQY TPEADPYFIQ DRFLNSFEEL 1630 1640 1650 1660 1670 1680 QAEECGILNG CENGRCVRVQ EGYTCDCFDG YHLDTAKMTC VDVNECDELN NRMSLCKNAK 1690 1700 1710 1720 CINTDGSYKC LCLPGYVPSD KPNYCTPLNT ALNLEKDSDL E
	Isoform Short (LTBP-1S) [UniParc] [UniParc]. Checksum: 09B5E29B60D1425D	FASTA	1,395	152,907
	10 20 30 40 50 60 MDTKLMCLLF FFSLPPLLVS NHTGRIKVVF TPSICKVTCT KGSCQNSCEK GNTTTLISEN 70 80 90 100 110 120 GHAADTLTAT NFRVVICHLP CMNGGQCSSR DKCQCPPNFT GKLCQIPVHG ASVPKLYQHS 130 140 150 160 170 180 QQPGKALGTH VIHSTHTLPL TVTSQQGVKV KFPPNIVNIH VKHPPEASVQ IHQVSRIDGP 190 200 210 220 230 240 TGQKTKEAQP GQSQVSYQGL PVQKTQTIHS TYSHQQVIPH VYPVAAKTQL GRCFQETIGS 250 260 270 280 290 300 QCGKALPGLS KQEDCCGTVG TSWGFNKCQK CPKKPSYHGY NQMMECLPGY KRVNNTFCQD 310 320 330 340 350 360 INECQLQGVC PNGECLNTMG SYRCTCKIGF GPDPTFSSCV PDPPVISEEK GPCYRLVSSG 370 380 390 400 410 420 RQCMHPLSVH LTKQLCCCSV GKAWGPHCEK CPLPGTAAFK EICPGGMGYT VSGVHRRRPI 430 440 450 460 470 480 HHHVGKGPVF VKPKNTQPVA KSTHPPPLPA KEEPVEALTF SREHGPGVAE PEVATAPPEK 490 500 510 520 530 540 EIPSLDQEKT KLEPGQPQLS PGISTIHLHP QFPVVIEKTS PPVPVEVAPE ASTSSASQVI 550 560 570 580 590 600 APTQVTEINE CTVNPDICGA GHCINLPVRY TCICYEGYRF SEQQRKCVDI DECTQVQHLC 610 620 630 640 650 660 SQGRCENTEG SFLCICPAGF MASEEGTNCI DVDECLRPDV CGEGHCVNTV GAFRCEYCDS 670 680 690 700 710 720 GYRMTQRGRC EDIDECLNPS TCPDEQCVNS PGSYQCVPCT EGFRGWNGQC LDVDECLEPN 730 740 750 760 770 780 VCANGDCSNL EGSYMCSCHK GYTRTPDHKH CRDIDECQQG NLCVNGQCKN TEGSFRCTCG 790 800 810 820 830 840 QGYQLSAAKD QCEDIDECQH RHLCAHGQCR NTEGSFQCVC DQGYRASGLG DHCEDINECL 850 860 870 880 890 900 EDKSVCQRGD CINTAGSYDC TCPDGFQLDD NKTCQDINEC EHPGLCGPQG ECLNTEGSFH 910 920 930 940 950 960 CVCQQGFSIS ADGRTCEDID ECVNNTVCDS HGFCDNTAGS FRCLCYQGFQ APQDGQGCVD 970 980 990 1000 1010 1020 VNECELLSGV CGEAFCENVE GSFLCVCADE NQEYSPMTGQ CRSRTSTDLD VDVDQPKEEK 1030 1040 1050 1060 1070 1080 KECYYNLNDA SLCDNVLAPN VTKQECCCTS GAGWGDNCEI FPCPVLGTAE FTEMCPKGKG 1090 1100 1110 1120 1130 1140 FVPAGESSSE AGGENYKDAD ECLLFGQEIC KNGFCLNTRP GYECYCKQGT YYDPVKLQCF 1150 1160 1170 1180 1190 1200 DMDECQDPSS CIDGQCVNTE GSYNCFCTHP MVLDASEKRC IRPAESNEQI EETDVYQDLC 1210 1220 1230 1240 1250 1260 WEHLSDEYVC SRPLVGKQTT YTECCCLYGE AWGMQCALCP LKDSDDYAQL CNIPVTGRRQ 1270 1280 1290 1300 1310 1320 PYGRDALVDF SEQYTPEADP YFIQDRFLNS FEELQAEECG ILNGCENGRC VRVQEGYTCD 1330 1340 1350 1360 1370 1380 CFDGYHLDTA KMTCVDVNEC DELNNRMSLC KNAKCINTDG SYKCLCLPGY VPSDKPNYCT 1390 PLNTALNLEK DSDLE
	Isoform 3. Checksum: 011F61A277C3988F	FASTA	1,342	147,207
	10 20 30 40 50 60 MDTKLMCLLF FFSLPPLLVS NHTGRIKVVF TPSICKVTCT KGSCQNSCEK GNTTTLISEN 70 80 90 100 110 120 GHAADTLTAT NFRVVICHLP CMNGGQCSSR DKCQCPPNFT GKLCQIPVHG ASVPKLYQHS 130 140 150 160 170 180 QQPGKALGTH VIHSTHTLPL TVTSQQGVKV KFPPNIVNIH VKHPPEASVQ IHQVSRIDGP 190 200 210 220 230 240 TGQKTKEAQP GQSQVSYQGL PVQKTQTIHS TYSHQQVIPH VYPVAAKTQL GRCFQETIGS 250 260 270 280 290 300 QCGKALPGLS KQEDCCGTVG TSWGFNKCQK CPKKPSYHGY NQMMECLPGY KRVNNTFCQD 310 320 330 340 350 360 INECQLQGVC PNGECLNTMG SYRCTCKIGF GPDPTFSSCV PDPPVISEEK GPCYRLVSSG 370 380 390 400 410 420 RQCMHPLSVH LTKQLCCCSV GKAWGPHCEK CPLPGTAKEE PVEALTFSRE HGPGVAEPEV 430 440 450 460 470 480 ATAPPEKEIP SLDQEKTKLE PGQPQLSPGI STIHLHPQFP VVIEKTSPPV PVEVAPEAST 490 500 510 520 530 540 SSASQVIAPT QVTEINECTV NPDICGAGHC INLPVRYTCI CYEGYRFSEQ QRKCVDIDEC 550 560 570 580 590 600 TQVQHLCSQG RCENTEGSFL CICPAGFMAS EEGTNCIDVD ECLRPDVCGE GHCVNTVGAF 610 620 630 640 650 660 RCEYCDSGYR MTQRGRCEDI DECLNPSTCP DEQCVNSPGS YQCVPCTEGF RGWNGQCLDV 670 680 690 700 710 720 DECLEPNVCA NGDCSNLEGS YMCSCHKGYT RTPDHKHCRD IDECQQGNLC VNGQCKNTEG 730 740 750 760 770 780 SFRCTCGQGY QLSAAKDQCE DIDECQHRHL CAHGQCRNTE GSFQCVCDQG YRASGLGDHC 790 800 810 820 830 840 EDINECLEDK SVCQRGDCIN TAGSYDCTCP DGFQLDDNKT CQDINECEHP GLCGPQGECL 850 860 870 880 890 900 NTEGSFHCVC QQGFSISADG RTCEDIDECV NNTVCDSHGF CDNTAGSFRC LCYQGFQAPQ 910 920 930 940 950 960 DGQGCVDVNE CELLSGVCGE AFCENVEGSF LCVCADENQE YSPMTGQCRS RTSTDLDVDV 970 980 990 1000 1010 1020 DQPKEEKKEC YYNLNDASLC DNVLAPNVTK QECCCTSGAG WGDNCEIFPC PVLGTAEFTE 1030 1040 1050 1060 1070 1080 MCPKGKGFVP AGESSSEAGG ENYKDADECL LFGQEICKNG FCLNTRPGYE CYCKQGTYYD 1090 1100 1110 1120 1130 1140 PVKLQCFDMD ECQDPSSCID GQCVNTEGSY NCFCTHPMVL DASEKRCIRP AESNEQIEET 1150 1160 1170 1180 1190 1200 DVYQDLCWEH LSDEYVCSRP LVGKQTTYTE CCCLYGEAWG MQCALCPLKD SDDYAQLCNI 1210 1220 1230 1240 1250 1260 PVTGRRQPYG RDALVDFSEQ YTPEADPYFI QDRFLNSFEE LQAEECGILN GCENGRCVRV 1270 1280 1290 1300 1310 1320 QEGYTCDCFD GYHLDTAKMT CVDVNECDEL NNRMSLCKNA KCINTDGSYK CLCLPGYVPS 1330 1340 DKPNYCTPLN TALNLEKDSD LE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2350783] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), PARTIAL PROTEIN SEQUENCE. 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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 8537398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-346. Tissue: Blood.
[8]	"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: 10743502] [Abstract] Cited for: REVIEW.
[9]	"The latent transforming growth factor beta binding protein (LTBP) family." Oklu R., Hesketh R. Biochem. J. 352:601-610(2000) [PubMed: 11104663] [Abstract] Cited for: REVIEW.
[10]	"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: 10930463] [Abstract] Cited for: INTERACTION WITH TGFB1, MUTAGENESIS OF 1385-GLU--PRO-1388.
[11]	"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: 12429738] [Abstract] Cited for: INTERACTION WITH FBN1.
[12]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1597; TYR-1600 AND THR-1601, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"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: 18677313] [Abstract] Cited for: INTERACTION WITH ADAMTSL2.
[14]	"Identification of N-glycosylation sites on secreted proteins of human hepatocellular carcinoma cells with a complementary proteomics approach." Cao J., Shen C., Wang H., Shen H., Chen Y., Nie A., Yan G., Lu H., Liu Y., Yang P. J. Proteome Res. 8:662-672(2009) [PubMed: 19196183] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1366, MASS SPECTROMETRY.
[15]	"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: 14607119] [Abstract] Cited for: STRUCTURE BY NMR OF 1340-1412, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00220249.

PIR

A35626.

RefSeq

NP_000618.2.
NP_996826.1.

UniGene

Hs.713533

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KSQ	NMR	-	A	1340-1412	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14766. 1 interaction.

PTM databases

GlycoSuiteDB

P22064.

PhosphoSite

Q14766.

Genome annotation databases

Ensembl

ENSG00000049323. Homo sapiens. [Contig view]

GeneID

4052.

Organism-specific databases

GeneCards

GC02P033084.

H-InvDB

HIX0029849.

HGNC

HGNC:6714. LTBP1.

HPA

HPA005707.
HPA006221.

MIM

150390. gene.

PharmGKB

PA30477.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q14766.

Gene expression databases

ArrayExpress

Q14766.

Bgee

Q14766.

CleanEx

HS_LTBP1.

GermOnline

ENSG00000049323. Homo sapiens.

Family and domain databases

InterPro

IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_CS.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR013091. EGF_Ca_bd_2.
IPR018097. EGF_Ca_bd_CS.
IPR002212. Fibril-assoc.
IPR017878. TFG_b-bd.
[Graphical view]

Gene3D

G3DSA:3.90.290.10. Fibril-assoc. 3 hits.

Pfam

PF00008. EGF. 5 hits.
PF07645. EGF_CA. 11 hits.
PF00683. TB. 4 hits.
[Graphical view]

SMART

SM00181. EGF. 5 hits.
SM00179. EGF_CA. 13 hits.
[Graphical view]

PROSITE

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]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

LTBP1_HUMAN

Accession

Primary (citable) accession number: Q14766
Secondary accession number(s): A1L3V1 , P22064, Q53SD8, Q53SF3, Q53SG1, Q59HF7, Q8TD95

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	May 5, 2009
Last modified:	June 16, 2009
This is version 90 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)