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Q06828

- FMOD_HUMAN

UniProt

Q06828 - FMOD_HUMAN

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Protein
Fibromodulin
Gene
FMOD, FM, SLRR2E
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei63 – 631Not sulfated
Sitei65 – 651Not sulfated

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. extracellular matrix organization Source: Reactome
  3. glycosaminoglycan metabolic process Source: Reactome
  4. keratan sulfate biosynthetic process Source: Reactome
  5. keratan sulfate catabolic process Source: Reactome
  6. keratan sulfate metabolic process Source: Reactome
  7. small molecule metabolic process Source: Reactome
  8. transforming growth factor beta receptor complex assembly Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_121120. Keratan sulfate biosynthesis.
REACT_121313. Keratan sulfate degradation.
REACT_163906. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibromodulin
Short name:
FM
Alternative name(s):
Collagen-binding 59 kDa protein
Keratan sulfate proteoglycan fibromodulin
Short name:
KSPG fibromodulin
Gene namesi
Name:FMOD
Synonyms:FM, SLRR2E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3774. FMOD.

Subcellular locationi

GO - Cellular componenti

  1. Golgi lumen Source: Reactome
  2. extracellular region Source: Reactome
  3. extracellular space Source: BHF-UCL
  4. lysosomal lumen Source: Reactome
  5. proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28190.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 By similarity
Add
BLAST
Chaini19 – 376358Fibromodulin
PRO_0000032739Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Pyrrolidone carboxylic acid
Modified residuei20 – 201Sulfotyrosine1 Publication
Modified residuei38 – 381Sulfotyrosine Inferred
Modified residuei39 – 391Sulfotyrosine Inferred
Modified residuei45 – 451Sulfotyrosine Inferred
Modified residuei47 – 471Sulfotyrosine Inferred
Modified residuei53 – 531Sulfotyrosine1 Publication
Modified residuei55 – 551Sulfotyrosine1 Publication
Glycosylationi127 – 1271N-linked (GlcNAc...) (keratan sulfate) By similarity
Glycosylationi166 – 1661N-linked (GlcNAc...) (keratan sulfate) By similarity
Glycosylationi201 – 2011N-linked (GlcNAc...) (keratan sulfate) By similarity
Glycosylationi291 – 2911N-linked (GlcNAc...) (keratan sulfate) By similarity
Disulfide bondi334 ↔ 367 By similarity
Glycosylationi341 – 3411N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

Binds keratan sulfate chains.

Keywords - PTMi

Disulfide bond, Glycoprotein, Proteoglycan, Pyrrolidone carboxylic acid, Sulfation

Proteomic databases

PaxDbiQ06828.
PRIDEiQ06828.

Miscellaneous databases

PMAP-CutDBQ8IV47.

Expressioni

Gene expression databases

ArrayExpressiQ06828.
BgeeiQ06828.
CleanExiHS_FMOD.
GenevestigatoriQ06828.

Interactioni

Subunit structurei

Binds to type I and type II collagen By similarity.

Protein-protein interaction databases

BioGridi108618. 2 interactions.
IntActiQ06828. 2 interactions.
MINTiMINT-7005481.
STRINGi9606.ENSP00000347041.

Structurei

3D structure databases

ProteinModelPortaliQ06828.
SMRiQ06828. Positions 73-369.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 10539LRRNT
Add
BLAST
Repeati106 – 12722LRR 1
Add
BLAST
Repeati130 – 15122LRR 2
Add
BLAST
Repeati156 – 17621LRR 3
Add
BLAST
Repeati177 – 19822LRR 4
Add
BLAST
Repeati201 – 22222LRR 5
Add
BLAST
Repeati224 – 24522LRR 6
Add
BLAST
Repeati246 – 26621LRR 7
Add
BLAST
Repeati269 – 28921LRR 8
Add
BLAST
Repeati294 – 31522LRR 9
Add
BLAST
Repeati316 – 33520LRR 10
Add
BLAST
Repeati344 – 36522LRR 11
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi76 – 9217Cys-rich
Add
BLAST

Sequence similaritiesi

Contains 1 LRRNT domain.

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiCOG4886.
HOGENOMiHOG000234447.
HOVERGENiHBG108061.
InParanoidiQ06828.
KOiK08121.
OMAiDEDPHWW.
OrthoDBiEOG741Z2B.
PhylomeDBiQ06828.
TreeFamiTF334562.

Family and domain databases

InterProiIPR027215. Fibromodulin.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view]
PANTHERiPTHR24371:SF11. PTHR24371:SF11. 1 hit.
PfamiPF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 10 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q06828-1 [UniParc]FASTAAdd to Basket

« Hide

MQWTSLLLLA GLFSLSQAQY EDDPHWWFHY LRSQQSTYYD PYDPYPYETY    50
EPYPYGVDEG PAYTYGSPSP PDPRDCPQEC DCPPNFPTAM YCDNRNLKYL 100
PFVPSRMKYV YFQNNQITSI QEGVFDNATG LLWIALHGNQ ITSDKVGRKV 150
FSKLRHLERL YLDHNNLTRM PGPLPRSLRE LHLDHNQISR VPNNALEGLE 200
NLTALYLQHN EIQEVGSSMR GLRSLILLDL SYNHLRKVPD GLPSALEQLY 250
MEHNNVYTVP DSYFRGAPKL LYVRLSHNSL TNNGLASNTF NSSSLLELDL 300
SYNQLQKIPP VNTNLENLYL QGNRINEFSI SSFCTVVDVV NFSKLQVLRL 350
DGNEIKRSAM PADAPLCLRL ASLIEI 376
Length:376
Mass (Da):43,179
Last modified:February 10, 2009 - v2
Checksum:iDC19D5E6724AB004
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41T → A in CAA53233. 1 Publication
Sequence conflicti87 – 871P → L in CAA53233. 1 Publication
Sequence conflicti210 – 2101N → D in CAA53233. 1 Publication
Sequence conflicti226 – 2261I → Y in CAA51418. 1 Publication
Sequence conflicti344 – 3441K → Q in CAA51418. 1 Publication
Sequence conflicti348 – 3481L → V in CAA51418. 1 Publication
Sequence conflicti348 – 3481L → V in CAA53233. 1 Publication
Sequence conflicti355 – 3551I → M in CAA51418. 1 Publication
Sequence conflicti363 – 3631D → E in CAA51418. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS30976.1.
PIRiS55275.
RefSeqiNP_002014.2. NM_002023.4.
UniGeneiHs.519168.

Genome annotation databases

EnsembliENST00000354955; ENSP00000347041; ENSG00000122176.
GeneIDi2331.
KEGGihsa:2331.
UCSCiuc001gzr.3. human.

Polymorphism databases

DMDMi223590208.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS30976.1.
PIRi S55275.
RefSeqi NP_002014.2. NM_002023.4.
UniGenei Hs.519168.

3D structure databases

ProteinModelPortali Q06828.
SMRi Q06828. Positions 73-369.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108618. 2 interactions.
IntActi Q06828. 2 interactions.
MINTi MINT-7005481.
STRINGi 9606.ENSP00000347041.

Polymorphism databases

DMDMi 223590208.

Proteomic databases

PaxDbi Q06828.
PRIDEi Q06828.

Protocols and materials databases

DNASUi 2331.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000354955 ; ENSP00000347041 ; ENSG00000122176 .
GeneIDi 2331.
KEGGi hsa:2331.
UCSCi uc001gzr.3. human.

Organism-specific databases

CTDi 2331.
GeneCardsi GC01M203311.
H-InvDB HIX0028648.
HGNCi HGNC:3774. FMOD.
MIMi 600245. gene.
neXtProti NX_Q06828.
PharmGKBi PA28190.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4886.
HOGENOMi HOG000234447.
HOVERGENi HBG108061.
InParanoidi Q06828.
KOi K08121.
OMAi DEDPHWW.
OrthoDBi EOG741Z2B.
PhylomeDBi Q06828.
TreeFami TF334562.

Enzyme and pathway databases

Reactomei REACT_121120. Keratan sulfate biosynthesis.
REACT_121313. Keratan sulfate degradation.
REACT_163906. ECM proteoglycans.

Miscellaneous databases

GeneWikii FMOD_(gene).
GenomeRNAii 2331.
NextBioi 9461.
PMAP-CutDB Q8IV47.
PROi Q06828.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q06828.
Bgeei Q06828.
CleanExi HS_FMOD.
Genevestigatori Q06828.

Family and domain databases

InterProi IPR027215. Fibromodulin.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000372. LRR-contain_N.
[Graphical view ]
PANTHERi PTHR24371:SF11. PTHR24371:SF11. 1 hit.
Pfami PF13855. LRR_8. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view ]
SMARTi SM00369. LRR_TYP. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view ]
PROSITEi PS51450. LRR. 10 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY 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.

Entry informationi

Entry nameiFMOD_HUMAN
AccessioniPrimary (citable) accession number: Q06828
Secondary accession number(s): Q15331, Q8IV47
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 10, 2009
Last modified: September 3, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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