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Protein

Latent-transforming growth factor beta-binding protein 2

Gene

Ltbp2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May play an integral structural role in elastic-fiber architectural organization and/or assembly. May be involved in the assembly, secretion and targeting of TGF- beta to sites at which it is stored and/or activated. May play critical roles in controlling and directing the activity of TGF-beta. May have a structural role in the extra cellular matrix (ECM).

GO - Molecular functioni

GO - Biological processi

  • extracellular fibril organization Source: MGI
Complete GO annotation...

Keywords - Ligandi

Growth factor binding, Heparin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Latent-transforming growth factor beta-binding protein 2
Short name:
LTBP-2
Gene namesi
Name:Ltbp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:99502. Ltbp2.

Subcellular locationi

  • Secreted By similarity

  • Note: Localized in nuchal ligament and aorta to the fibrillin-containing, microfibrillar component of elastic fibers.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535By similarityAdd
BLAST
Chaini36 – 18131778Latent-transforming growth factor beta-binding protein 2PRO_0000007644Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi175 – 1751N-linked (GlcNAc...)Sequence analysis
Disulfide bondi185 ↔ 195PROSITE-ProRule annotation
Disulfide bondi189 ↔ 201PROSITE-ProRule annotation
Disulfide bondi203 ↔ 212PROSITE-ProRule annotation
Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence analysis
Disulfide bondi385 ↔ 395PROSITE-ProRule annotation
Disulfide bondi389 ↔ 401PROSITE-ProRule annotation
Disulfide bondi403 ↔ 412PROSITE-ProRule annotation
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence analysis
Modified residuei491 – 4911PhosphoserineCombined sources
Disulfide bondi538 ↔ 560PROSITE-ProRule annotation
Disulfide bondi547 ↔ 573PROSITE-ProRule annotation
Disulfide bondi561 ↔ 576PROSITE-ProRule annotation
Glycosylationi603 – 6031N-linked (GlcNAc...)Sequence analysis
Disulfide bondi613 ↔ 624PROSITE-ProRule annotation
Disulfide bondi619 ↔ 633PROSITE-ProRule annotation
Disulfide bondi635 ↔ 648PROSITE-ProRule annotation
Disulfide bondi661 ↔ 683PROSITE-ProRule annotation
Disulfide bondi670 ↔ 696PROSITE-ProRule annotation
Disulfide bondi684 ↔ 699PROSITE-ProRule annotation
Disulfide bondi685 ↔ 711PROSITE-ProRule annotation
Disulfide bondi839 ↔ 852PROSITE-ProRule annotation
Disulfide bondi847 ↔ 861PROSITE-ProRule annotation
Disulfide bondi863 ↔ 876PROSITE-ProRule annotation
Disulfide bondi882 ↔ 893PROSITE-ProRule annotation
Disulfide bondi887 ↔ 902PROSITE-ProRule annotation
Disulfide bondi904 ↔ 919PROSITE-ProRule annotation
Disulfide bondi925 ↔ 936PROSITE-ProRule annotation
Disulfide bondi931 ↔ 945PROSITE-ProRule annotation
Disulfide bondi947 ↔ 959PROSITE-ProRule annotation
Disulfide bondi965 ↔ 976PROSITE-ProRule annotation
Disulfide bondi971 ↔ 985PROSITE-ProRule annotation
Disulfide bondi988 ↔ 999PROSITE-ProRule annotation
Disulfide bondi1005 ↔ 1016PROSITE-ProRule annotation
Disulfide bondi1011 ↔ 1025PROSITE-ProRule annotation
Disulfide bondi1027 ↔ 1040PROSITE-ProRule annotation
Disulfide bondi1046 ↔ 1057PROSITE-ProRule annotation
Disulfide bondi1052 ↔ 1066PROSITE-ProRule annotation
Disulfide bondi1069 ↔ 1082PROSITE-ProRule annotation
Disulfide bondi1088 ↔ 1099PROSITE-ProRule annotation
Disulfide bondi1094 ↔ 1108PROSITE-ProRule annotation
Disulfide bondi1111 ↔ 1124PROSITE-ProRule annotation
Disulfide bondi1130 ↔ 1142PROSITE-ProRule annotation
Disulfide bondi1137 ↔ 1151PROSITE-ProRule annotation
Disulfide bondi1153 ↔ 1165PROSITE-ProRule annotation
Glycosylationi1161 – 11611N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1171 ↔ 1183PROSITE-ProRule annotation
Disulfide bondi1177 ↔ 1192PROSITE-ProRule annotation
Disulfide bondi1194 ↔ 1207PROSITE-ProRule annotation
Disulfide bondi1213 ↔ 1224PROSITE-ProRule annotation
Disulfide bondi1219 ↔ 1233PROSITE-ProRule annotation
Disulfide bondi1235 ↔ 1249PROSITE-ProRule annotation
Disulfide bondi1255 ↔ 1268PROSITE-ProRule annotation
Disulfide bondi1263 ↔ 1277PROSITE-ProRule annotation
Disulfide bondi1281 ↔ 1293PROSITE-ProRule annotation
Disulfide bondi1299 ↔ 1311PROSITE-ProRule annotation
Glycosylationi1301 – 13011N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1305 ↔ 1320PROSITE-ProRule annotation
Disulfide bondi1322 ↔ 1335PROSITE-ProRule annotation
Disulfide bondi1341 ↔ 1353PROSITE-ProRule annotation
Disulfide bondi1348 ↔ 1362PROSITE-ProRule annotation
Disulfide bondi1364 ↔ 1378PROSITE-ProRule annotation
Disulfide bondi1405 ↔ 1428PROSITE-ProRule annotation
Disulfide bondi1415 ↔ 1440PROSITE-ProRule annotation
Glycosylationi1422 – 14221N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1429 ↔ 1443PROSITE-ProRule annotation
Disulfide bondi1430 ↔ 1455PROSITE-ProRule annotation
Disulfide bondi1481 ↔ 1494PROSITE-ProRule annotation
Disulfide bondi1489 ↔ 1503PROSITE-ProRule annotation
Disulfide bondi1505 ↔ 1518PROSITE-ProRule annotation
Disulfide bondi1524 ↔ 1534PROSITE-ProRule annotation
Disulfide bondi1529 ↔ 1543PROSITE-ProRule annotation
Disulfide bondi1545 ↔ 1558PROSITE-ProRule annotation
Glycosylationi1560 – 15601N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1578 ↔ 1601PROSITE-ProRule annotation
Disulfide bondi1587 ↔ 1613PROSITE-ProRule annotation
Disulfide bondi1602 ↔ 1616PROSITE-ProRule annotation
Disulfide bondi1603 ↔ 1628PROSITE-ProRule annotation
Disulfide bondi1729 ↔ 1740PROSITE-ProRule annotation
Disulfide bondi1735 ↔ 1749PROSITE-ProRule annotation
Disulfide bondi1751 ↔ 1764PROSITE-ProRule annotation
Disulfide bondi1770 ↔ 1785PROSITE-ProRule annotation
Disulfide bondi1780 ↔ 1794PROSITE-ProRule annotation
Disulfide bondi1796 ↔ 1809PROSITE-ProRule annotation

Post-translational modificationi

Contains hydroxylated asparagine residues.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein

Proteomic databases

MaxQBiO08999.
PaxDbiO08999.
PRIDEiO08999.

PTM databases

iPTMnetiO08999.
PhosphoSiteiO08999.

Expressioni

Tissue specificityi

Expressed in the anterior chamber of the eye.1 Publication

Interactioni

Subunit structurei

Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex. Interacts with SDC4 (By similarity).By similarity

Protein-protein interaction databases

IntActiO08999. 2 interactions.
MINTiMINT-4100636.
STRINGi10090.ENSMUSP00000105883.

Structurei

3D structure databases

ProteinModelPortaliO08999.
SMRiO08999. Positions 146-215, 536-717, 847-1558, 1727-1811.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini181 – 21333EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini381 – 41333EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini536 – 58853TB 1PROSITE-ProRule annotationAdd
BLAST
Domaini609 – 64941EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini659 – 71153TB 2PROSITE-ProRule annotationAdd
BLAST
Domaini835 – 87743EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini878 – 92043EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini921 – 96040EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini961 – 100040EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1001 – 104141EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1042 – 108342EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1084 – 112542EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1126 – 116641EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1167 – 120842EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1209 – 125042EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1251 – 129444EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1295 – 133642EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1337 – 137943EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1403 – 145553TB 3PROSITE-ProRule annotationAdd
BLAST
Domaini1477 – 151943EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1520 – 155940EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1576 – 162853TB 4PROSITE-ProRule annotationAdd
BLAST
Domaini1725 – 176541EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1766 – 181045EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 11522Heparin-bindingBy similarityAdd
BLAST
Regioni226 – 24318Heparin-bindingBy similarityAdd
BLAST
Regioni329 – 33911Heparin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi847 – 1364518Cys-richAdd
BLAST

Domaini

Associates covalently with small latent TGF-beta complex via Repeat B and Repeat C.

Sequence similaritiesi

Belongs to the LTBP family.Curated
Contains 20 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

eggNOGiENOG410KD9U. Eukaryota.
ENOG410XSTY. LUCA.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiO08999.
KOiK08023.
PhylomeDBiO08999.

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]
PfamiPF00008. EGF. 1 hit.
PF07645. EGF_CA. 16 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 20 hits.
SM00179. EGF_CA. 18 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 7 hits.
SSF57581. SSF57581. 4 hits.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00010. ASX_HYDROXYL. 12 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 10 hits.
PS50026. EGF_3. 15 hits.
PS01187. EGF_CA. 16 hits.
PS51364. TB. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O08999-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRAPTTARCS GCIQRVRWRG FLPLVLAVLM GTSHAQRDSI GRYEPASRDA
60 70 80 90 100
NRLWHPVGSH PAAAAAKVYS LFREPDAPVP GLSPSEWNQP AQGNPGWLAE
110 120 130 140 150
AEARRPPRTQ QLRRVQPPVQ TRRSHPRGQQ QIAARAAPSV ARLETPQRPA
160 170 180 190 200
AARRGRLTGR NVCGGQCCPG WTTSNSTNHC IKPVCQPPCQ NRGSCSRPQV
210 220 230 240 250
CICRSGFRGA RCEEVIPEEE FDPQNARPVP RRSVERAPGP HRSSEARGSL
260 270 280 290 300
VTRIQPLVPP PSPPPSRRLS QPWPLQQHSG PSRTVRRYPA TGANGQLMSN
310 320 330 340 350
ALPSGLELRD SSPQAAHVNH LSPPWGLNLT EKIKKIKVVF TPTICKQTCA
360 370 380 390 400
RGRCANSCEK GDTTTLYSQG GHGHDPKSGF RIYFCQIPCL NGGRCIGRDE
410 420 430 440 450
CWCPANSTGK FCHLPVPQPD REPAGRGSRH RTLLEGPLKQ STFTLPLSNQ
460 470 480 490 500
LASVNPSLVK VQIHHPPEAS VQIHQVARVR GELDPVLEDN SVETRASHRP
510 520 530 540 550
HGNLGHSPWA SNSIPARAGE APRPPPVLSR HYGLLGQCYL STVNGQCANP
560 570 580 590 600
LGSLTSQEDC CGSVGTFWGV TSCAPCPPRQ EGPAFPVIEN GQLECPQGYK
610 620 630 640 650
RLNLSHCQDI NECLTLGLCK DSECVNTRGS YLCTCRPGLM LDPSRSRCVS
660 670 680 690 700
DKAVSMQQGL CYRSLGSGTC TLPLVHRITK QICCCSRVGK AWGSTCEQCP
710 720 730 740 750
LPGTEAFREI CPAGHGYTYS SSDIRLSMRK AEEEELASPL REQTEQSTAP
760 770 780 790 800
PPGQAERQPL RAATATWIEA ETLPDKGDSR AVQITTSAPH LPARVPGDAT
810 820 830 840 850
GRPAPSLPGQ GIPESPAEEQ VIPSSDVLVT HSPPDFDPCF AGASNICGPG
860 870 880 890 900
TCVSLPNGYR CVCSPGYQLH PSQDYCTDDN ECMRNPCEGR GRCVNSVGSY
910 920 930 940 950
SCLCYPGYTL VTLGDTQECQ DIDECEQPGV CSGGRCSNTE GSYHCECDRG
960 970 980 990 1000
YIMVRKGHCQ DINECRHPGT CPDGRCVNSP GSYTCLACEE GYVGQSGSCV
1010 1020 1030 1040 1050
DVNECLTPGI CTHGRCINME GSFRCSCEPG YEVTPDKKGC RDVDECASRA
1060 1070 1080 1090 1100
SCPTGLCLNT EGSFTCSACQ SGYWVNEDGT ACEDLDECAF PGVCPTGVCT
1110 1120 1130 1140 1150
NTVGSFSCKD CDQGYRPNPL GNRCEDVDEC EGPQSSCRGG ECKNTEGSYQ
1160 1170 1180 1190 1200
CLCHQGFQLV NGTMCEDVNE CVGEEHCAPH GECLNSLGSF FCLCAPGFAS
1210 1220 1230 1240 1250
AEGGTRCQDV DECAATDPCP GGHCVNTEGS FSCLCETASF QPSPDSGECL
1260 1270 1280 1290 1300
DIDECEDRED PVCGAWRCEN SPGSYRCILD CQPGFYVAPN GDCIDIDECA
1310 1320 1330 1340 1350
NDTVCGNHGF CDNTDGSFRC LCDQGFETSP SGWECVDVNE CELMMAVCGD
1360 1370 1380 1390 1400
ALCENVEGSF LCLCASDLEE YDAEEGHCRP RVAGAQRIPE VRTEDQAPSL
1410 1420 1430 1440 1450
IRMECYSEHN GGPPCSQILG QNSTQAECCC TQGARWGKAC APCPSEDSVE
1460 1470 1480 1490 1500
FSQLCPSGQG YIPVEGAWTF GQTMYTDADE CVLFGPALCQ NGRCSNIVPG
1510 1520 1530 1540 1550
YICLCNPGYH YDASSRKCQD HNECQDLACE NGECVNQEGS FHCLCNPPLT
1560 1570 1580 1590 1600
LDLSGQRCVN TTSSTEDFPD HDIHMDICWK KVTNDVCSQP LRGHHTTYTE
1610 1620 1630 1640 1650
CCCQDGEAWS QQCALCPPRS SEVYAQLCNV ARIEAERGAG IHFRPGYEYG
1660 1670 1680 1690 1700
PGLDDLPENL YGPDGAPFYN YLGPEDTAPE PPFSNPASQP GDNTPVLEPP
1710 1720 1730 1740 1750
LQPSELQPHY LASHSEPPAS FEGLQAEECG ILNGCENGRC VRVREGYTCD
1760 1770 1780 1790 1800
CFEGFQLDAP TLACVDVNEC EDLNGPARLC AHGHCENTEG SYRCHCSPGY
1810
VAEPGPPHCA AKE
Length:1,813
Mass (Da):195,829
Last modified:January 16, 2004 - v2
Checksum:iD993DF6489AA27D5
GO

Sequence cautioni

The sequence AAB61611.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC35229.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141Q → R in BAC35229 (PubMed:16141072).Curated
Sequence conflicti74 – 741E → G in BAC35229 (PubMed:16141072).Curated
Sequence conflicti97 – 971W → R in BAC35229 (PubMed:16141072).Curated
Sequence conflicti498 – 4981H → R in BAC35229 (PubMed:16141072).Curated
Sequence conflicti553 – 5531S → E in BAC35229 (PubMed:16141072).Curated
Sequence conflicti580 – 5823Missing in BAC35229 (PubMed:16141072).Curated
Sequence conflicti778 – 7781D → L in BAC35229 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004874 mRNA. Translation: AAB61611.1. Different initiation.
AK052980 mRNA. Translation: BAC35229.1. Different initiation.
RefSeqiNP_038617.3. NM_013589.3.
UniGeneiMm.3900.

Genome annotation databases

GeneIDi16997.
KEGGimmu:16997.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF004874 mRNA. Translation: AAB61611.1. Different initiation.
AK052980 mRNA. Translation: BAC35229.1. Different initiation.
RefSeqiNP_038617.3. NM_013589.3.
UniGeneiMm.3900.

3D structure databases

ProteinModelPortaliO08999.
SMRiO08999. Positions 146-215, 536-717, 847-1558, 1727-1811.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08999. 2 interactions.
MINTiMINT-4100636.
STRINGi10090.ENSMUSP00000105883.

PTM databases

iPTMnetiO08999.
PhosphoSiteiO08999.

Proteomic databases

MaxQBiO08999.
PaxDbiO08999.
PRIDEiO08999.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi16997.
KEGGimmu:16997.

Organism-specific databases

CTDi4053.
MGIiMGI:99502. Ltbp2.

Phylogenomic databases

eggNOGiENOG410KD9U. Eukaryota.
ENOG410XSTY. LUCA.
HOGENOMiHOG000293153.
HOVERGENiHBG052370.
InParanoidiO08999.
KOiK08023.
PhylomeDBiO08999.

Miscellaneous databases

ChiTaRSiLtbp2. mouse.
PROiO08999.
SOURCEiSearch...

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]
PfamiPF00008. EGF. 1 hit.
PF07645. EGF_CA. 16 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTiSM00181. EGF. 20 hits.
SM00179. EGF_CA. 18 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 7 hits.
SSF57581. SSF57581. 4 hits.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00010. ASX_HYDROXYL. 12 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 10 hits.
PS50026. EGF_3. 15 hits.
PS01187. EGF_CA. 16 hits.
PS51364. TB. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "8-cysteine TGF-BP structural motifs are the site of covalent binding between mouse LTBP-3, LTBP-2, and latent TGF-beta 1."
    Yin W., Fang J., Smiley E., Bonadio J.
    Biochim. Biophys. Acta 1383:340-350(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TGFB1.
  2. "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 1-778.
    Strain: C57BL/6J.
    Tissue: Head.
  3. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 205-211, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  4. "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.
  5. "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.
  6. Cited for: TISSUE SPECIFICITY.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung and Spleen.

Entry informationi

Entry nameiLTBP2_MOUSE
AccessioniPrimary (citable) accession number: O08999
Secondary accession number(s): Q8C6W9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: January 16, 2004
Last modified: July 6, 2016
This is version 137 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, Direct protein sequencing, 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.