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Q06828

- FMOD_HUMAN

UniProt

Q06828 - FMOD_HUMAN

Protein

Fibromodulin

Gene

FMOD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (10 Feb 2009)
      Previous versions | rss
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    Functioni

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

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

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28190.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818By similarityAdd
    BLAST
    Chaini19 – 376358FibromodulinPRO_0000032739Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei19 – 191Pyrrolidone carboxylic acid1 Publication
    Modified residuei20 – 201Sulfotyrosine1 Publication
    Modified residuei38 – 381Sulfotyrosine1 Publication
    Modified residuei39 – 391Sulfotyrosine1 Publication
    Modified residuei45 – 451Sulfotyrosine1 Publication
    Modified residuei47 – 471Sulfotyrosine1 Publication
    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 ↔ 367By similarity
    Glycosylationi341 – 3411N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Binds keratan sulfate chains.1 Publication

    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. 3 interactions.
    MINTiMINT-7005481.
    STRINGi9606.ENSP00000347041.

    Structurei

    3D structure databases

    ProteinModelPortaliQ06828.
    SMRiQ06828. Positions 73-369.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Compositional bias

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

    Sequence similaritiesi

    Contains 11 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRNT domain.Curated

    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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41T → A in CAA53233. (PubMed:8093006)Curated
    Sequence conflicti87 – 871P → L in CAA53233. (PubMed:8093006)Curated
    Sequence conflicti210 – 2101N → D in CAA53233. (PubMed:8093006)Curated
    Sequence conflicti226 – 2261I → Y in CAA51418. (PubMed:8357838)Curated
    Sequence conflicti344 – 3441K → Q in CAA51418. (PubMed:8357838)Curated
    Sequence conflicti348 – 3481L → V in CAA51418. (PubMed:8357838)Curated
    Sequence conflicti348 – 3481L → V in CAA53233. (PubMed:8093006)Curated
    Sequence conflicti355 – 3551I → M in CAA51418. (PubMed:8357838)Curated
    Sequence conflicti363 – 3631D → E in CAA51418. (PubMed:8357838)Curated

    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...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108618. 2 interactions.
    IntActi Q06828. 3 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

    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: October 1, 2014
    This is version 130 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