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Q8N2S1 (LTBP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Latent-transforming growth factor beta-binding protein 4

Short name=LTBP-4
Gene names
Name:LTBP4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1624 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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) By similarity.

Subunit structure

Forms part of the large latent transforming growth factor beta precursor complex; removal is essential for activation of complex. Interacts with LTBP1 and TGFB1. Binds to FBN1 By similarity. Ref.2

Subcellular location

Secretedextracellular spaceextracellular matrix Ref.2 Ref.5.

Tissue specificity

Highly expressed in heart, skeletal muscle, pancreas, uterus, and small intestine. Weakly expressed in placenta and lung. Ref.1 Ref.2

Developmental stage

Very low expression in fetal brain, liver, heart, spleen and thymus. Ref.2

Post-translational modification

Contains hydroxylated asparagine residues By similarity.

Involvement in disease

Urban-Rifkin-Davis syndrome (URDS) [MIM:613177]: A syndrome characterized by disrupted pulmonary, gastrointestinal, urinary, musculoskeletal, craniofacial and dermal development. Clinical features include cutis laxa, mild cardiovascular lesions, respiratory distress with cystic and atelectatic changes in the lungs, and diverticulosis, tortuosity and stenosis at various levels of the intestinal tract. Craniofacial features include microretrognathia, flat midface, receding forehead and wide fontanelles.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Sequence similarities

Belongs to the LTBP family.

Contains 16 EGF-like domains.

Contains 4 TB (TGF-beta binding) domains.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainEGF-like domain
Repeat
Signal
   LigandGrowth factor binding
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processextracellular matrix organization

Traceable author statement. Source: Reactome

growth hormone secretion

Traceable author statement Ref.2. Source: UniProtKB

multicellular organismal development

Traceable author statement Ref.2. Source: UniProtKB

protein folding

Traceable author statement Ref.2. Source: UniProtKB

regulation of cell differentiation

Traceable author statement Ref.2. Source: UniProtKB

regulation of cell growth

Traceable author statement Ref.2. Source: UniProtKB

regulation of proteolysis

Inferred from direct assay Ref.2. Source: UniProtKB

regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement Ref.2. Source: UniProtKB

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular matrix

Inferred from direct assay Ref.5. Source: UniProt

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

proteinaceous extracellular matrix

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functioncalcium ion binding

Non-traceable author statement Ref.2. Source: UniProtKB

glycosaminoglycan binding

Non-traceable author statement Ref.2. Source: UniProtKB

integrin binding

Non-traceable author statement Ref.2. Source: UniProtKB

transforming growth factor beta binding

Inferred from direct assay Ref.2. Source: UniProtKB

transforming growth factor beta-activated receptor activity

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATXN7O152652EBI-947718,EBI-708350
CACNA1AO005552EBI-947718,EBI-766279

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N2S1-1)

Also known as: LTBP-4L;

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 2 (identifier: Q8N2S1-2)

Also known as: LTBP-4S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-67: Missing.
     68-151: RAFCRVRSCQ...QRAPAGKAPV → MAGGVRLLWV...APGGPGFRAF
Isoform 3 (identifier: Q8N2S1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: MPRPGTSGRR...QTSRRSRCIR → MGDVKALLFVVAARARRLGGAAASESLAVSE
Isoform 4 (identifier: Q8N2S1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-902: Missing.
     903-919: CTCAPGYRPGPRGASCL → MLGGAGGGPGLRTPCPA
     1007-1092: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 16241597Latent-transforming growth factor beta-binding protein 4
PRO_0000310964

Regions

Domain149 – 18133EGF-like 1
Domain287 – 33953TB 1
Domain357 – 39741EGF-like 2; calcium-binding Potential
Domain407 – 45953TB 2
Domain545 – 58642EGF-like 3
Domain587 – 62842EGF-like 4; calcium-binding Potential
Domain629 – 67042EGF-like 5; calcium-binding Potential
Domain671 – 70838EGF-like 6; calcium-binding Potential
Domain710 – 75142EGF-like 7; calcium-binding Potential
Domain752 – 79342EGF-like 8; calcium-binding Potential
Domain834 – 87744EGF-like 9; calcium-binding Potential
Domain878 – 91942EGF-like 10; calcium-binding Potential
Domain920 – 96041EGF-like 11; calcium-binding Potential
Domain1049 – 109042EGF-like 12; calcium-binding Potential
Domain1181 – 123555TB 3
Domain1253 – 129543EGF-like 13; calcium-binding Potential
Domain1296 – 133742EGF-like 14; calcium-binding Potential
Domain1349 – 140254TB 4
Domain1533 – 157341EGF-like 15
Domain1574 – 161845EGF-like 16
Compositional bias478 – 56588Pro-rich
Compositional bias549 – 1118570Cys-rich
Compositional bias1119 – 117557Pro-rich
Compositional bias1407 – 149286Pro-rich

Amino acid modifications

Glycosylation3521N-linked (GlcNAc...) Potential
Glycosylation4251N-linked (GlcNAc...) Potential
Glycosylation10551N-linked (GlcNAc...) Potential
Glycosylation12001N-linked (GlcNAc...) Potential
Glycosylation13391N-linked (GlcNAc...) Potential
Disulfide bond153 ↔ 163 By similarity
Disulfide bond157 ↔ 169 By similarity
Disulfide bond171 ↔ 180 By similarity
Disulfide bond361 ↔ 372 By similarity
Disulfide bond367 ↔ 381 By similarity
Disulfide bond383 ↔ 396 By similarity
Disulfide bond549 ↔ 561 By similarity
Disulfide bond556 ↔ 570 By similarity
Disulfide bond572 ↔ 585 By similarity
Disulfide bond591 ↔ 603 By similarity
Disulfide bond598 ↔ 612 By similarity
Disulfide bond614 ↔ 627 By similarity
Disulfide bond633 ↔ 645 By similarity
Disulfide bond640 ↔ 654 By similarity
Disulfide bond656 ↔ 669 By similarity
Disulfide bond675 ↔ 687 By similarity
Disulfide bond682 ↔ 696 By similarity
Disulfide bond698 ↔ 707 By similarity
Disulfide bond714 ↔ 726 By similarity
Disulfide bond721 ↔ 735 By similarity
Disulfide bond737 ↔ 750 By similarity
Disulfide bond756 ↔ 768 By similarity
Disulfide bond763 ↔ 777 By similarity
Disulfide bond779 ↔ 792 By similarity
Disulfide bond838 ↔ 851 By similarity
Disulfide bond845 ↔ 860 By similarity
Disulfide bond862 ↔ 876 By similarity
Disulfide bond882 ↔ 894 By similarity
Disulfide bond888 ↔ 903 By similarity
Disulfide bond905 ↔ 918 By similarity
Disulfide bond924 ↔ 935 By similarity
Disulfide bond930 ↔ 944 By similarity
Disulfide bond946 ↔ 959 By similarity
Disulfide bond1053 ↔ 1065 By similarity
Disulfide bond1059 ↔ 1074 By similarity
Disulfide bond1076 ↔ 1089 By similarity
Disulfide bond1257 ↔ 1270 By similarity
Disulfide bond1265 ↔ 1279 By similarity
Disulfide bond1281 ↔ 1294 By similarity
Disulfide bond1300 ↔ 1312 By similarity
Disulfide bond1307 ↔ 1321 By similarity
Disulfide bond1323 ↔ 1336 By similarity
Disulfide bond1537 ↔ 1548 By similarity
Disulfide bond1543 ↔ 1557 By similarity
Disulfide bond1559 ↔ 1572 By similarity
Disulfide bond1578 ↔ 1593 By similarity
Disulfide bond1588 ↔ 1602 By similarity
Disulfide bond1604 ↔ 1617 By similarity

Natural variations

Alternative sequence1 – 902902Missing in isoform 4.
VSP_029362
Alternative sequence1 – 6868MPRPG…SRCIR → MGDVKALLFVVAARARRLGG AAASESLAVSE in isoform 3.
VSP_029363
Alternative sequence1 – 6767Missing in isoform 2.
VSP_029364
Alternative sequence68 – 15184RAFCR…GKAPV → MAGGVRLLWVSLLVLLAQLG PQPGLGRLGERLRVRFTPVV CGLRCVHGPTGSRCTPTCAP RNATSVDSGAPGGAAPGGPG FRAF in isoform 2.
VSP_029365
Alternative sequence903 – 91917CTCAP…GASCL → MLGGAGGGPGLRTPCPA in isoform 4.
VSP_029366
Alternative sequence1007 – 109286Missing in isoform 4.
VSP_029367
Natural variant1941V → I. Ref.2
Corresponds to variant rs2303729 [ dbSNP | Ensembl ].
VAR_037119
Natural variant3111C → G in URDS. Ref.6
VAR_064153
Natural variant6351R → G.
Corresponds to variant rs33937741 [ dbSNP | Ensembl ].
VAR_037120
Natural variant6791P → A.
Corresponds to variant rs34299942 [ dbSNP | Ensembl ].
VAR_037121
Natural variant7871T → A. Ref.2
Corresponds to variant rs1131620 [ dbSNP | Ensembl ].
VAR_037122
Natural variant8201T → A. Ref.2
Corresponds to variant rs1051303 [ dbSNP | Ensembl ].
VAR_037123
Natural variant11411T → M. Ref.1 Ref.2
Corresponds to variant rs10880 [ dbSNP | Ensembl ].
VAR_037124

Experimental info

Sequence conflict1701L → F in CAA73944. Ref.1
Sequence conflict3461T → A in BAC11024. Ref.3
Sequence conflict5261L → F in AAC39879. Ref.2
Sequence conflict5261L → F in AAC39880. Ref.2
Sequence conflict6861A → G in CAA73944. Ref.1
Sequence conflict9741G → R in BAC11024. Ref.3
Sequence conflict11391A → V in CAA73944. Ref.1
Sequence conflict11421F → S in CAA73944. Ref.1
Sequence conflict11511A → V in CAA73944. Ref.1
Sequence conflict11651P → S in CAA73944. Ref.1
Sequence conflict1169 – 11702ST → RK in CAA73944. Ref.1
Sequence conflict11731Q → K in CAA73944. Ref.1
Sequence conflict11801R → C in CAA73944. Ref.1
Sequence conflict14021C → R in BAC11024. Ref.3
Sequence conflict15121P → S in BAC11024. Ref.3
Sequence conflict15461G → D in CAA73944. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LTBP-4L) [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 75682D1F6E40657A

FASTA1,624173,435
        10         20         30         40         50         60 
MPRPGTSGRR PLLLVLLLPL FAAATSAASP SPSPSQVVEV PGVPSRPASV AVCRCCPGQT 

        70         80         90        100        110        120 
SRRSRCIRAF CRVRSCQPKK CAGPQRCLNP VPAVPSPSPS VRKRQVSLNW QPLTLQEARA 

       130        140        150        160        170        180 
LLKRRRPRGP GGRGLLRRRP PQRAPAGKAP VLCPLICHNG GVCVKPDRCL CPPDFAGKFC 

       190        200        210        220        230        240 
QLHSSGARPP APAVPGLTRS VYTMPLANHR DDEHGVASMV SVHVEHPQEA SVVVHQVERV 

       250        260        270        280        290        300 
SGPWEEADAE AVARAEAAAR AEAAAPYTVL AQSAPREDGY SDASGFGYCF RELRGGECAS 

       310        320        330        340        350        360 
PLPGLRTQEV CCRGAGLAWG VHDCQLCSER LGNSERVSAP DGPCPTGFER VNGSCEDVDE 

       370        380        390        400        410        420 
CATGGRCQHG ECANTRGGYT CVCPDGFLLD SSRSSCISQH VISEAKGPCF RVLRDGGCSL 

       430        440        450        460        470        480 
PILRNITKQI CCCSRVGKAW GRGCQLCPPF GSEGFREICP AGPGYHYSAS DLRYNTRPLG 

       490        500        510        520        530        540 
QEPPRVSLSQ PRTLPATSRP SAGFLPTHRL EPRPEPRPDP RPGPELPLPS IPAWTGPEIP 

       550        560        570        580        590        600 
ESGPSSGMCQ RNPQVCGPGR CISRPSGYTC ACDSGFRLSP QGTRCIDVDE CRRVPPPCAP 

       610        620        630        640        650        660 
GRCENSPGSF RCVCGPGFRA GPRAAECLDV DECHRVPPPC DLGRCENTPG SFLCVCPAGY 

       670        680        690        700        710        720 
QAAPHGASCQ DVDECTQSPG LCGRGACKNL PGSFRCVCPA GFRGSACEED VDECAQEPPP 

       730        740        750        760        770        780 
CGPGRCDNTA GSFHCACPAG FRSRGPGAPC QDVDECARSP PPCTYGRCEN TEGSFQCVCP 

       790        800        810        820        830        840 
MGFQPNTAGS ECEDVDECEN HLACPGQECV NSPGSFQCRT CPSGHHLHRG RCTDVDECSS 

       850        860        870        880        890        900 
GAPPCGPHGH CTNTEGSFRC SCAPGYRAPS GRPGPCADVN ECLEGDFCFP HGECLNTDGS 

       910        920        930        940        950        960 
FACTCAPGYR PGPRGASCLD VDECSEEDLC QSGICTNTDG SFECICPPGH RAGPDLASCL 

       970        980        990       1000       1010       1020 
DVDECRERGP ALCGSQRCEN SPGSYRCVRD CDPGYHAGPE GTCDDVDECQ EYGPEICGAQ 

      1030       1040       1050       1060       1070       1080 
RCENTPGSYR CTPACDPGYQ PTPGGGCQDV DECRNRSFCG AHAVCQNLPG SFQCLCDQGY 

      1090       1100       1110       1120       1130       1140 
EGARDGRHCV DVNECETLQG VCGAALCENV EGSFLCVCPN SPEEFDPMTG RCVPPRTSAG 

      1150       1160       1170       1180       1190       1200 
TFPGSQPQAP ASPVLPARPP PPPLPRRPST PRQGPVGSGR RECYFDTAAP DACDNILARN 

      1210       1220       1230       1240       1250       1260 
VTWQECCCTV GEGWGSGCRI QQCPGTETAE YQSLCPHGRG YLAPSGDLSL RRDVDECQLF 

      1270       1280       1290       1300       1310       1320 
RDQVCKSGVC VNTAPGYSCY CSNGYYYHTQ RLECIDNDEC ADEEPACEGG RCVNTVGSYH 

      1330       1340       1350       1360       1370       1380 
CTCEPPLVLD GSQRRCVSNE SQSLDDNLGV CWQEVGADLV CSHPRLDRQA TYTECCCLYG 

      1390       1400       1410       1420       1430       1440 
EAWGMDCALC PAQDSDDFEA LCNVLRPPAY SPPRPGGFGL PYEYGPDLGP PYQGLPYGPE 

      1450       1460       1470       1480       1490       1500 
LYPPPALPYD PYPPPPGPFA RREAPYGAPR FDMPDFEDDG GPYGESEAPA PPGPGTRWPY 

      1510       1520       1530       1540       1550       1560 
RSRDTRRSFP EPEEPPEGGS YAGSLAEPYE ELEAEECGIL DGCTNGRCVR VPEGFTCRCF 

      1570       1580       1590       1600       1610       1620 
DGYRLDMTRM ACVDINECDE AEAASPLCVN ARCLNTDGSF RCICRPGFAP THQPHHCAPA 


RPRA 

« Hide

Isoform 2 (LTBP-4S) [UniParc].

Checksum: 3F2995909633F6D0
Show »

FASTA1,557165,742
Isoform 3 [UniParc].

Checksum: D7675F3B239B3D39
Show »

FASTA1,587169,484
Isoform 4 [UniParc].

Checksum: 0CAA11F48CB0C133
Show »

FASTA63668,525

References

« Hide 'large scale' references
[1]"Sequence and expression of a novel member (LTBP-4) of the family of latent transforming growth factor-beta binding proteins."
Giltay R., Kostka G., Timpl R.
FEBS Lett. 411:164-168(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, VARIANT MET-1141.
[2]"Identification and characterization of a new latent transforming growth factor-beta-binding protein, LTBP-4."
Saharinen J., Taipale J., Monni O., Keski-Oja J.
J. Biol. Chem. 273:18459-18469(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH LTBP1 AND TGFB1, VARIANTS ILE-194; ALA-787; ALA-820 AND MET-1141.
Tissue: Heart.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Embryo.
[4]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Sequential deposition of latent TGF-beta binding proteins (LTBPs) during formation of the extracellular matrix in human lung fibroblasts."
Koli K., Hyytieainen M., Ryynanen M.J., Keski-Oja J.
Exp. Cell Res. 310:370-382(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"Mutations in LTBP4 cause a syndrome of impaired pulmonary, gastrointestinal, genitourinary, musculoskeletal, and dermal development."
Urban Z., Hucthagowder V., Schuermann N., Todorovic V., Zilberberg L., Choi J., Sens C., Brown C.W., Clark R.D., Holland K.E., Marble M., Sakai L.Y., Dabovic B., Rifkin D.B., Davis E.C.
Am. J. Hum. Genet. 85:593-605(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT URDS GLY-311.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13622 mRNA. Translation: CAA73944.1.
AF051344 mRNA. Translation: AAC39879.2.
AF051345 mRNA. Translation: AAC39880.2.
AK074499 mRNA. Translation: BAC11024.1.
AC010412 Genomic DNA. No translation available.
RefSeqNP_001036009.1. NM_001042544.1.
NP_001036010.1. NM_001042545.1.
NP_003564.2. NM_003573.2.
UniGeneHs.466766.

3D structure databases

ProteinModelPortalQ8N2S1.
SMRQ8N2S1. Positions 287-465, 545-1119, 1161-1387, 1511-1621.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114009. 14 interactions.
IntActQ8N2S1. 31 interactions.
MINTMINT-2794871.
STRING9606.ENSP00000311905.

PTM databases

PhosphoSiteQ8N2S1.

Polymorphism databases

DMDM160410003.

Proteomic databases

PaxDbQ8N2S1.
PRIDEQ8N2S1.

Protocols and materials databases

DNASU8425.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308370; ENSP00000311905; ENSG00000090006.
GeneID8425.
KEGGhsa:8425.
UCSCuc002oog.1. human. [Q8N2S1-3]
uc002ooh.1. human. [Q8N2S1-1]
uc002ooi.1. human. [Q8N2S1-2]
uc002ooj.1. human. [Q8N2S1-4]

Organism-specific databases

CTD8425.
GeneCardsGC19P041099.
HGNCHGNC:6717. LTBP4.
HPACAB015194.
MIM604710. gene.
613177. phenotype.
neXtProtNX_Q8N2S1.
Orphanet221145. Cutis laxa with severe pulmonary, gastrointestinal and urinary anomalies.
98896. Duchenne muscular dystrophy.
PharmGKBPA30480.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG261153.
HOGENOMHOG000293153.
HOVERGENHBG052370.
InParanoidQ8N2S1.
KOK08023.
PhylomeDBQ8N2S1.
TreeFamTF317514.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ8N2S1.
BgeeQ8N2S1.
CleanExHS_LTBP4.
GenevestigatorQ8N2S1.

Family and domain databases

Gene3D3.90.290.10. 5 hits.
InterProIPR026823. 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]
PfamPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 15 hits.
PF00683. TB. 3 hits.
[Graphical view]
SMARTSM00181. EGF. 4 hits.
SM00179. EGF_CA. 16 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 6 hits.
SSF57581. SSF57581. 4 hits.
PROSITEPS00010. ASX_HYDROXYL. 14 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 12 hits.
PS50026. EGF_3. 15 hits.
PS01187. EGF_CA. 17 hits.
PS51364. TB. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLTBP4. human.
GenomeRNAi8425.
NextBio31524.
PROQ8N2S1.
SOURCESearch...

Entry information

Entry nameLTBP4_HUMAN
AccessionPrimary (citable) accession number: Q8N2S1
Secondary accession number(s): O00508, O75412, O75413
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM