Q06828 (FMOD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	376 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	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	Secreted › extracellular space › extracellular 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.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Domain	Leucine-rich repeat Repeat Signal
PTM	Disulfide bond Glycoprotein Proteoglycan Pyrrolidone carboxylic acid Sulfation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Traceable author statement. Source: Reactome keratan sulfate biosynthetic process Traceable author statement. Source: Reactome keratan sulfate catabolic process Traceable author statement. Source: Reactome transforming growth factor beta receptor complex assembly Traceable author statement Ref.2. Source: ProtInc
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL lysosomal lumen Traceable author statement. Source: Reactome proteinaceous extracellular matrix Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	By similarity
	Chain	19 – 376	358	Fibromodulin		PRO_0000032739
Regions
	Domain	67 – 105	39	LRRNT
	Repeat	106 – 127	22	LRR 1
	Repeat	130 – 151	22	LRR 2
	Repeat	156 – 176	21	LRR 3
	Repeat	177 – 198	22	LRR 4
	Repeat	201 – 222	22	LRR 5
	Repeat	224 – 245	22	LRR 6
	Repeat	246 – 266	21	LRR 7
	Repeat	269 – 289	21	LRR 8
	Repeat	294 – 315	22	LRR 9
	Repeat	316 – 335	20	LRR 10
	Repeat	344 – 365	22	LRR 11
	Compositional bias	76 – 92	17	Cys-rich
Sites
	Site	63	1	Not sulfated
	Site	65	1	Not sulfated
Amino acid modifications
	Modified residue	19	1	Pyrrolidone carboxylic acid
	Modified residue	20	1	Sulfotyrosine Ref.7
	Modified residue	38	1	Sulfotyrosine Probable
	Modified residue	39	1	Sulfotyrosine Probable
	Modified residue	45	1	Sulfotyrosine Probable
	Modified residue	47	1	Sulfotyrosine Probable
	Modified residue	53	1	Sulfotyrosine Ref.7
	Modified residue	55	1	Sulfotyrosine Ref.7
	Glycosylation	127	1	N-linked (GlcNAc...) (keratan sulfate) By similarity
	Glycosylation	166	1	N-linked (GlcNAc...) (keratan sulfate) By similarity
	Glycosylation	201	1	N-linked (GlcNAc...) (keratan sulfate) By similarity
	Glycosylation	291	1	N-linked (GlcNAc...) (keratan sulfate) By similarity
	Glycosylation	341	1	N-linked (GlcNAc...) Potential
	Disulfide bond	334 ↔ 367		By similarity
Experimental info
	Sequence conflict	4	1	T → A in CAA53233. Ref.2
	Sequence conflict	87	1	P → L in CAA53233. Ref.2
	Sequence conflict	210	1	N → D in CAA53233. Ref.2
	Sequence conflict	226	1	I → Y in CAA51418. Ref.1
	Sequence conflict	344	1	K → Q in CAA51418. Ref.1
	Sequence conflict	348	1	L → V in CAA51418. Ref.1
	Sequence conflict	348	1	L → V in CAA53233. Ref.2
	Sequence conflict	355	1	I → M in CAA51418. Ref.1
	Sequence conflict	363	1	D → E in CAA51418. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q06828 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: DC19D5E6724AB004	FASTA	376	43,179
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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.
IPI	IPI00000860.
PIR	S55275.
RefSeq	NP_002014.2. NM_002023.3.
UniGene	Hs.519168.
3D structure databases
ProteinModelPortal	Q06828.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q06828. 1 interaction.
MINT	MINT-7005481.
STRING	9606.ENSP00000347041.
Polymorphism databases
DMDM	223590208.
Proteomic databases
PaxDb	Q06828.
PRIDE	Q06828.
Protocols and materials databases
DNASU	2331.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000354955; ENSP00000347041; ENSG00000122176.
GeneID	2331.
KEGG	hsa:2331.
UCSC	uc001gzr.3. human.
Organism-specific databases
CTD	2331.
GeneCards	GC01M203311.
H-InvDB	HIX0028648.
HGNC	HGNC:3774. FMOD.
MIM	600245. gene.
neXtProt	NX_Q06828.
PharmGKB	PA28190.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG4886.
HOGENOM	HOG000234447.
HOVERGEN	HBG108061.
InParanoid	Q06828.
KO	K08121.
OMA	AQYDEDP.
OrthoDB	EOG4CJVHR.
PhylomeDB	Q06828.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_116125. Disease.
Gene expression databases
ArrayExpress	Q06828.
Bgee	Q06828.
CleanEx	HS_FMOD.
Genevestigator	Q06828.
GermOnline	ENSG00000122176. Homo sapiens.
Family and domain databases
InterPro	IPR027215. Fibromodulin. IPR001611. Leu-rich_rpt. IPR003591. Leu-rich_rpt_typical-subtyp. IPR000372. LRR-contain_N. [Graphical view]
PANTHER	PTHR24371:SF11. PTHR24371:SF11. 1 hit.
Pfam	PF01462. LRRNT. 1 hit. [Graphical view]
SMART	SM00369. LRR_TYP. 1 hit. SM00013. LRRNT. 1 hit. [Graphical view]
PROSITE	PS51450. LRR. 10 hits. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	2331.
NextBio	9461.
PMAP-CutDB	Q8IV47.
SOURCE	Search...

Entry information

Entry name

FMOD_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.