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Q06828 (FMOD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibromodulin

Short name=FM
Alternative name(s):
Collagen-binding 59 kDa protein
Keratan sulfate proteoglycan fibromodulin
Short name=KSPG fibromodulin
Gene names
Name:FMOD
Synonyms:FM, SLRR2E
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Affects the rate of fibrils formation. May have a primary role in collagen fibrillogenesis By similarity.

Subunit structure

Binds to type I and type II collagen By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrix.

Post-translational modification

Binds keratan sulfate chains.

Sequence similarities

Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class II subfamily.

Contains 11 LRR (leucine-rich) repeats.

Contains 1 LRRNT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 376358Fibromodulin
PRO_0000032739

Regions

Domain67 – 10539LRRNT
Repeat106 – 12722LRR 1
Repeat130 – 15122LRR 2
Repeat156 – 17621LRR 3
Repeat177 – 19822LRR 4
Repeat201 – 22222LRR 5
Repeat224 – 24522LRR 6
Repeat246 – 26621LRR 7
Repeat269 – 28921LRR 8
Repeat294 – 31522LRR 9
Repeat316 – 33520LRR 10
Repeat344 – 36522LRR 11
Compositional bias76 – 9217Cys-rich

Sites

Site631Not sulfated
Site651Not sulfated

Amino acid modifications

Modified residue191Pyrrolidone carboxylic acid
Modified residue201Sulfotyrosine Ref.7
Modified residue381Sulfotyrosine Probable
Modified residue391Sulfotyrosine Probable
Modified residue451Sulfotyrosine Probable
Modified residue471Sulfotyrosine Probable
Modified residue531Sulfotyrosine Ref.7
Modified residue551Sulfotyrosine Ref.7
Glycosylation1271N-linked (GlcNAc...) (keratan sulfate) By similarity
Glycosylation1661N-linked (GlcNAc...) (keratan sulfate) By similarity
Glycosylation2011N-linked (GlcNAc...) (keratan sulfate) By similarity
Glycosylation2911N-linked (GlcNAc...) (keratan sulfate) By similarity
Glycosylation3411N-linked (GlcNAc...) Potential
Disulfide bond334 ↔ 367 By similarity

Experimental info

Sequence conflict41T → A in CAA53233. Ref.2
Sequence conflict871P → L in CAA53233. Ref.2
Sequence conflict2101N → D in CAA53233. Ref.2
Sequence conflict2261I → Y in CAA51418. Ref.1
Sequence conflict3441K → Q in CAA51418. Ref.1
Sequence conflict3481L → V in CAA51418. Ref.1
Sequence conflict3481L → V in CAA53233. Ref.2
Sequence conflict3551I → M in CAA51418. Ref.1
Sequence conflict3631D → E in CAA51418. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q06828 [UniParc].

Last modified February 10, 2009. Version 2.
Checksum: DC19D5E6724AB004

FASTA37643,179
        10         20         30         40         50         60 
MQWTSLLLLA GLFSLSQAQY EDDPHWWFHY LRSQQSTYYD PYDPYPYETY EPYPYGVDEG 

        70         80         90        100        110        120 
PAYTYGSPSP PDPRDCPQEC DCPPNFPTAM YCDNRNLKYL PFVPSRMKYV YFQNNQITSI 

       130        140        150        160        170        180 
QEGVFDNATG LLWIALHGNQ ITSDKVGRKV FSKLRHLERL YLDHNNLTRM PGPLPRSLRE 

       190        200        210        220        230        240 
LHLDHNQISR VPNNALEGLE NLTALYLQHN EIQEVGSSMR GLRSLILLDL SYNHLRKVPD 

       250        260        270        280        290        300 
GLPSALEQLY MEHNNVYTVP DSYFRGAPKL LYVRLSHNSL TNNGLASNTF NSSSLLELDL 

       310        320        330        340        350        360 
SYNQLQKIPP VNTNLENLYL QGNRINEFSI SSFCTVVDVV NFSKLQVLRL DGNEIKRSAM 

       370 
PADAPLCLRL ASLIEI 

« Hide

References

« Hide 'large scale' references
[1]"Structure and deduced amino acid sequence of the human fibromodulin gene."
Antonsson P., Heinegaard D., Oldberg A.
Biochim. Biophys. Acta 1174:204-206(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta."
Hildebrand A., Romaris M., Rasmussen L.M., Heinegard D., Twardzik D.R., Border W.A., Ruoslahti E.
Biochem. J. 302:527-534(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Tissue: Placenta.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [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. expand/collapse author list , 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 (JUL-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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"Identification of tyrosine sulfation in extracellular leucine-rich repeat proteins using mass spectrometry."
Onnerfjord P., Heathfield T.F., Heinegaard D.
J. Biol. Chem. 279:26-33(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION AT TYR-20; TYR-38; TYR-39; TYR-45; TYR-47; TYR-53 AND TYR-55, LACK OF SULFATION AT TYR-63 AND TYR-65, PYROGLUTAMATE FORMATION AT GLN-19, MASS SPECTROMETRY.
[8]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-201.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X72913 Genomic DNA. Translation: CAA51418.1.
X75546 mRNA. Translation: CAA53233.1.
AK291632 mRNA. Translation: BAF84321.1.
AL359837 Genomic DNA. Translation: CAH73821.1.
CH471067 Genomic DNA. Translation: EAW91477.1.
BC035281 mRNA. Translation: AAH35281.1.
PIRS55275.
RefSeqNP_002014.2. NM_002023.4.
UniGeneHs.519168.

3D structure databases

ProteinModelPortalQ06828.
SMRQ06828. Positions 73-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108618. 2 interactions.
IntActQ06828. 2 interactions.
MINTMINT-7005481.
STRING9606.ENSP00000347041.

Polymorphism databases

DMDM223590208.

Proteomic databases

PaxDbQ06828.
PRIDEQ06828.

Protocols and materials databases

DNASU2331.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354955; ENSP00000347041; ENSG00000122176.
GeneID2331.
KEGGhsa:2331.
UCSCuc001gzr.3. human.

Organism-specific databases

CTD2331.
GeneCardsGC01M203311.
H-InvDBHIX0028648.
HGNCHGNC:3774. FMOD.
MIM600245. gene.
neXtProtNX_Q06828.
PharmGKBPA28190.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000234447.
HOVERGENHBG108061.
InParanoidQ06828.
KOK08121.
OMADEDPHWW.
OrthoDBEOG741Z2B.
PhylomeDBQ06828.
TreeFamTF334562.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ06828.
BgeeQ06828.
CleanExHS_FMOD.
GenevestigatorQ06828.

Family and domain databases

InterProIPR027215. Fibromodulin.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PANTHERPTHR24371:SF11. PTHR24371:SF11. 1 hit.
PfamPF01462. LRRNT. 1 hit.
[Graphical view]
SMARTSM00369. LRR_TYP. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 10 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiFMOD_(gene).
GenomeRNAi2331.
NextBio9461.
PMAP-CutDBQ8IV47.
PROQ06828.
SOURCESearch...

Entry information

Entry nameFMOD_HUMAN
AccessionPrimary (citable) accession number: Q06828
Secondary accession number(s): Q15331, Q8IV47
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 10, 2009
Last modified: March 19, 2014
This is version 124 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 chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM