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Reviewed, UniProtKB/Swiss-Prot Q8CG19 (LTBP1_MOUSE)

Last modified July 7, 2009. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length1712 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Secreted By similarity. UniProtKB Q14766

Domain

Associates covalently with small latent TGF-beta complex via domain TB 3 By similarity.

Post-translational modification

Contains hydroxylated asparagine residues By similarity. UniProtKB P22064

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.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q8CG19-1)

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: Q8CG19-2)

Also known as: LTBP-1S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-318: Missing.
     319-336: EGSFSLRYGQEQGTAPFQ → MDTKLMCLLFFLCLPLLL
Isoform 3 (identifier: Q8CG19-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 17121689Latent-transforming growth factor beta-binding protein 1
PRO_0000007637

Regions

Domain181 – 21333EGF-like 1
Domain391 – 42333EGF-like 2
Domain549 – 60153TB 1
Domain618 – 65841EGF-like 3; calcium-binding Potential
Domain669 – 72153TB 2
Domain865 – 90642EGF-like 4; calcium-binding Potential
Domain907 – 94842EGF-like 5; calcium-binding Potential
Domain949 – 98941EGF-like 6; calcium-binding Potential
Domain990 – 102940EGF-like 7; calcium-binding Potential
Domain1030 – 107041EGF-like 8; calcium-binding Potential
Domain1071 – 111141EGF-like 9; calcium-binding Potential
Domain1112 – 115241EGF-like 10; calcium-binding Potential
Domain1153 – 119341EGF-like 11; calcium-binding Potential
Domain1194 – 123542EGF-like 12; calcium-binding Potential
Domain1236 – 127742EGF-like 13; calcium-binding Potential
Domain1278 – 132043EGF-like 14; calcium-binding Potential
Domain1338 – 139255TB 3
Domain1415 – 145743EGF-like 15; calcium-binding Potential
Domain1458 – 149841EGF-like 16; calcium-binding Potential
Domain1515 – 156854TB 4
Domain1612 – 165241EGF-like 17
Domain1653 – 169745EGF-like 18; calcium-binding Potential
Compositional bias96 – 12429Pro-rich

Amino acid modifications

Modified residue9661(3R)-3-hydroxyasparagine By similarity
Modified residue11291(3R)-3-hydroxyasparagine By similarity
Modified residue15881Phosphoserine By similarity
Modified residue15911Phosphotyrosine By similarity
Glycosylation3391N-linked (GlcNAc...) Potential
Glycosylation3701N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Potential
Glycosylation6121N-linked (GlcNAc...) Potential
Glycosylation10421N-linked (GlcNAc...) Potential
Glycosylation12421N-linked (GlcNAc...) Potential
Glycosylation13571N-linked (GlcNAc...) By similarity
Disulfide bond185 ↔ 195 By similarity
Disulfide bond189 ↔ 201 By similarity
Disulfide bond203 ↔ 212 By similarity
Disulfide bond395 ↔ 405 By similarity
Disulfide bond399 ↔ 411 By similarity
Disulfide bond413 ↔ 422 By similarity
Disulfide bond622 ↔ 633 By similarity
Disulfide bond628 ↔ 642 By similarity
Disulfide bond644 ↔ 657 By similarity
Disulfide bond869 ↔ 881 By similarity
Disulfide bond876 ↔ 890 By similarity
Disulfide bond892 ↔ 905 By similarity
Disulfide bond911 ↔ 923 By similarity
Disulfide bond918 ↔ 932 By similarity
Disulfide bond934 ↔ 947 By similarity
Disulfide bond953 ↔ 964 By similarity
Disulfide bond959 ↔ 973 By similarity
Disulfide bond976 ↔ 988 By similarity
Disulfide bond994 ↔ 1005 By similarity
Disulfide bond1000 ↔ 1014 By similarity
Disulfide bond1017 ↔ 1028 By similarity
Disulfide bond1034 ↔ 1045 By similarity
Disulfide bond1040 ↔ 1054 By similarity
Disulfide bond1056 ↔ 1069 By similarity
Disulfide bond1075 ↔ 1086 By similarity
Disulfide bond1081 ↔ 1095 By similarity
Disulfide bond1097 ↔ 1110 By similarity
Disulfide bond1116 ↔ 1127 By similarity
Disulfide bond1122 ↔ 1136 By similarity
Disulfide bond1138 ↔ 1151 By similarity
Disulfide bond1157 ↔ 1169 By similarity
Disulfide bond1164 ↔ 1178 By similarity
Disulfide bond1180 ↔ 1192 By similarity
Disulfide bond1198 ↔ 1210 By similarity
Disulfide bond1204 ↔ 1219 By similarity
Disulfide bond1221 ↔ 1234 By similarity
Disulfide bond1240 ↔ 1252 By similarity
Disulfide bond1246 ↔ 1261 By similarity
Disulfide bond1263 ↔ 1276 By similarity
Disulfide bond1282 ↔ 1294 By similarity
Disulfide bond1289 ↔ 1303 By similarity
Disulfide bond1305 ↔ 1319 By similarity
Disulfide bond1340 ↔ 1363 By similarity
Disulfide bond1350 ↔ 1375 By similarity
Disulfide bond1364 ↔ 1380 By similarity
Disulfide bond1365 ↔ 1392 By similarity
Disulfide bond1419 ↔ 1432 By similarity
Disulfide bond1427 ↔ 1441 By similarity
Disulfide bond1443 ↔ 1456 By similarity
Disulfide bond1462 ↔ 1473 By similarity
Disulfide bond1468 ↔ 1482 By similarity
Disulfide bond1484 ↔ 1497 By similarity
Disulfide bond1616 ↔ 1627 By similarity
Disulfide bond1622 ↔ 1636 By similarity
Disulfide bond1638 ↔ 1651 By similarity
Disulfide bond1657 ↔ 1672 By similarity
Disulfide bond1667 ↔ 1681 By similarity
Disulfide bond1683 ↔ 1696 By similarity

Natural variations

Alternative sequence1 – 318318Missing in isoform Short and isoform 3.
VSP_036968
Alternative sequence319 – 33618EGSFS…TAPFQ → MDTKLMCLLFFLCLPLLL in isoform Short and isoform 3.
VSP_036969
Alternative sequence716 – 76853Missing in isoform 3.
VSP_036970

Experimental info

Sequence conflict3131S → F in AAN77250. Ref.1
Sequence conflict5061A → T in AAN77250. Ref.1
Sequence conflict5061A → T in AAN77251. Ref.1
Sequence conflict5061A → T in AAC33307. Ref.3
Sequence conflict5591Q → QQ in AAN77250. Ref.1
Sequence conflict5591Q → QQ in AAC33307. Ref.3
Sequence conflict10331E → K in AAC33307. Ref.3
Sequence conflict11111E → G in BAC34222. Ref.6
Sequence conflict12161S → F in BAC34222. Ref.6
Sequence conflict16311Q → H in AAN77250. Ref.1
Sequence conflict16311Q → H in AAN77251. Ref.1
Sequence conflict16591E → G in BAC34222. Ref.6
Sequence conflict17121E → N in AAC33307. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform Long (LTBP-1L) [UniParc].

Last modified May 5, 2009. Version 2.
Checksum: DB0564112F1F7843

FASTA1,712186,717
        10         20         30         40         50         60 
MAGAWLRWGL LLWAGLLAWS AHGRVRRITY VVRPGPGLPA GALPLAGPPR TFNVALDARY 

        70         80         90        100        110        120 
SRSSTAASSR ALAGPPAERT RRTSQPGGAA LPGLRSPLPP EPARPGGPSR QLHSKAGAQT 

       130        140        150        160        170        180 
AVTRFAKHGR QVVRSQVQQD AQSAGGSRLQ VQQKQQLQGI NVCGGQCCHG WSKPPGSQRC 

       190        200        210        220        230        240 
TKPSCVPPCQ NGGMCLRPQL CVCKPGSKGK ACEITAAQDT MPPAFGGQNP GSSWAPLEQA 

       250        260        270        280        290        300 
AKHTSTKKAD TLPRVSPVAQ MTLTLKPKPS MGLSQQIHPQ VAPLSSQNVM IRHGQTQEYL 

       310        320        330        340        350        360 
LKPKYFPAPK VVSAEQSTEG SFSLRYGQEQ GTAPFQVSNH TGRIKVVFTP SICKVTCTKG 

       370        380        390        400        410        420 
NCQNSCQKGN TTTLISENGH AADTLTATNF RVVICHLPCM NGGQCSSRDK CQCPPNFTGK 

       430        440        450        460        470        480 
LCQIPVLGAS MPKLYQHAQQ QGKALGSHVI HSTHTLPLTM TSQQGVKVKF PPNIVNIHVK 

       490        500        510        520        530        540 
HPPEASVQIH QVSRIDSPGG QKVKEAQPGQ SQVSYQGLPV QKTQTVHSTY SHQQLIPHVY 

       550        560        570        580        590        600 
PVAAKTQLGR CFQETIGSQC GKALPGLSKQ EDCCGTVGTS WGFNKCQKCP KKQSYHGYTQ 

       610        620        630        640        650        660 
MMECLQGYKR VNNTFCQDIN ECQLQGVCPN GECLNTMGSY RCSCKMGFGP DPTFSSCVPD 

       670        680        690        700        710        720 
PPVISEEKGP CYRLVSPGRH CMHPLSVHLT KQICCCSVGK AWGPHCEKCP LPGTAAFKEI 

       730        740        750        760        770        780 
CPGGMGYTVS GVHRRRPIHQ HIGKEAVYVK PKNTQPVAKS THPPPLPAKE EPVEALTSSW 

       790        800        810        820        830        840 
EHGPRGAEPE VVTAPPEKEI PSLDQEKTRL EPGQPQLSPG VSTIHLHPQF PVVVEKTSPP 

       850        860        870        880        890        900 
VPVEVAPEAS TSSASQVIAP TQVTEINECT VNPDICGAGH CINLPVRYTC ICYEGYKFSE 

       910        920        930        940        950        960 
QLRKCVDIDE CAQVRHLCSQ GRCENTEGSF LCVCPAGFMA SEEGTNCIDV DECLRPDMCR 

       970        980        990       1000       1010       1020 
DGRCINTAGA FRCEYCDSGY RMSRRGYCED IDECLKPSTC PEEQCVNTPG SYQCVPCTEG 

      1030       1040       1050       1060       1070       1080 
FRGWNGQCLD VDECLQPKVC TNGSCTNLEG SYMCSCHRGY SPTPDHRHCQ DIDECQQGNL 

      1090       1100       1110       1120       1130       1140 
CMNGQCRNTD GSFRCTCGQG YQLSAAKDQC EDIDECEHHH LCSHGQCRNT EGSFQCVCNQ 

      1150       1160       1170       1180       1190       1200 
GYRASVLGDH CEDINECLED SSVCQGGDCI NTAGSYDCTC PDGFQLNDNK GCQDINECAQ 

      1210       1220       1230       1240       1250       1260 
PGLCGSHGEC LNTQGSFHCV CEQGFSISAD GRTCEDIDEC VNNTVCDSHG FCDNTAGSFR 

      1270       1280       1290       1300       1310       1320 
CLCYQGFQAP QDGQGCVDVN ECELLSGVCG EAFCENVEGS FLCVCADENQ EYSPMTGQCR 

      1330       1340       1350       1360       1370       1380 
SRVTEDSGVD RQPREEKKEC YYNLNDASLC DNVLAPNVTK QECCCTSGAG WGDNCEIFPC 

      1390       1400       1410       1420       1430       1440 
PVQGTAEFTE MCPRGKGLVP AGESSYDTGG ENYKDADECL LFGEEICKNG YCLNTQPGYE 

      1450       1460       1470       1480       1490       1500 
CYCKQGTYYD PVKLQCFDMD ECQDPNSCID GQCVNTEGSY NCFCTHPMVL DASEKRCVQP 

      1510       1520       1530       1540       1550       1560 
TESNEQIEET DVYQDLCWEH LSEEYVCSRP LVGKQTTYTE CCCLYGEAWG MQCALCPMKD 

      1570       1580       1590       1600       1610       1620 
SDDYAQLCNI PVTGRRRPYG RDALVDFSEQ YGPETDPYFI QDRFLNSFEE LQAEECGILN 

      1630       1640       1650       1660       1670       1680 
GCENGRCVRV QEGYTCDCFD GYHLDMAKMT CVDVNECSEL NNRMSLCKNA KCINTEGSYK 

      1690       1700       1710 
CLCLPGYIPS DKPNYCTPLN SALNLDKESD LE 

« Hide

Isoform Short (LTBP-1S) [UniParc] [UniParc].

Checksum: 0D10BF1FB3B4A85A
Show »

FASTA1,394153,185
Isoform 3.

Checksum: FB1930C28738FDE5
Show »

FASTA1,341147,418

References

« Hide 'large scale' references
[1]"Molecular cloning of the mouse Ltbp-1 gene reveals tissue specific expression of alternatively spliced forms."
Noguera I., Obata H., Gualandris A., Cowin P., Rifkin D.B.
Gene 308:31-41(2003) [PubMed: 12711388] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS LONG AND SHORT).
[2]"The murine latent transforming growth factor-beta binding protein (Ltbp-1) is alternatively spliced, and maps to a region syntenic to human chromosome 2p21-22."
Weiskirchen R., Moser M., Guenther K., Weiskirchen S., Gressner A.M.
Gene 308:43-52(2003) [PubMed: 12711389] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
Strain: 129/SvJ.
[3]Noguera I., Cowin P., Rifkin D.B.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Strain: BALB/c.
Tissue: Heart.
[4]The mouse genome sequencing consortium
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"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).
Strain: C57BL/6.
Tissue: Brain.
[6]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1111-1712.
Strain: C57BL/6J.
Tissue: Aorta, Liver and Vein.
[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: 10743502] [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: 11104663] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF346465 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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.
IPIIPI00352982.
IPI00828560.
IPI00830551.
RefSeqNP_064303.2.
NP_996841.1.
UniGeneMm.269747

3D structure databases

HSSPHSSP built from PDB template 1BF9 based on UniProtKB P08709.
SMRQ8CG19. Positions 1333-1404.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8CG19. 1 interaction.

PTM databases

PhosphoSiteQ8CG19.

Proteomic databases

PRIDEQ8CG19.

Genome annotation databases

EnsemblENSMUSG00000001870. Mus musculus. [Contig view]
GeneID268977.

Organism-specific databases

MGIMGI:109151. Ltbp1.

Phylogenomic databases

HOGENOMQ8CG19.
HOVERGENQ8CG19.

Gene expression databases

ArrayExpressQ8CG19.
BgeeQ8CG19.
GermOnlineENSMUSG00000001870. Mus musculus.

Family and domain databases

InterProIPR006209. 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.
IPR013111. EGF_extracell.
IPR002212. Fibril-assoc.
IPR017878. TFG_b-bd.
[Graphical view]
Gene3DG3DSA:3.90.290.10. Fibril-assoc. 3 hits.
PfamPF00008. EGF. 4 hits.
PF07974. EGF_2. 1 hit.
PF07645. EGF_CA. 11 hits.
PF00683. TB. 4 hits.
[Graphical view]
SMARTSM00181. EGF. 5 hits.
SM00179. EGF_CA. 13 hits.
[Graphical view]
PROSITEPS00010. 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]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameLTBP1_MOUSE
AccessionPrimary (citable) accession number: Q8CG19
Secondary accession number(s): B1B1D9 expand/collapse secondary AC list , B1B1E1, O88349, Q505C9, Q8BNW7, Q8C7F5, Q8CG18, Q8CIR0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2003
Last sequence update: May 5, 2009
Last modified: July 7, 2009
This is version 68 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents