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Protein

Fibromodulin

Gene

FMOD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

Enzyme and pathway databases

ReactomeiR-HSA-2022854 Keratan sulfate biosynthesis
R-HSA-2022857 Keratan sulfate degradation
R-HSA-3000178 ECM proteoglycans
R-HSA-3656225 Defective CHST6 causes MCDC1
R-HSA-3656243 Defective ST3GAL3 causes MCT12 and EIEE15
R-HSA-3656244 Defective B4GALT1 causes B4GALT1-CDG (CDG-2d)

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000122176.10
HGNCiHGNC:3774 FMOD
MIMi600245 gene
neXtProtiNX_Q06828

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi2331
OpenTargetsiENSG00000122176
PharmGKBiPA28190

Polymorphism and mutation databases

DMDMi223590208

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18By similarityAdd BLAST18
ChainiPRO_000003273919 – 376FibromodulinAdd BLAST358

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19Pyrrolidone carboxylic acid1 Publication1
Modified residuei20Sulfotyrosine1 Publication1
Modified residuei38Sulfotyrosine1 Publication1
Modified residuei39Sulfotyrosine1 Publication1
Modified residuei45Sulfotyrosine1 Publication1
Modified residuei47Sulfotyrosine1 Publication1
Modified residuei53Sulfotyrosine1 Publication1
Modified residuei55Sulfotyrosine1 Publication1
Glycosylationi127N-linked (GlcNAc...) (keratan sulfate) asparagineBy similarity1
Glycosylationi166N-linked (GlcNAc...) (keratan sulfate) asparagineBy similarity1
Glycosylationi201N-linked (GlcNAc...) (keratan sulfate) asparagineBy similarity1
Glycosylationi291N-linked (GlcNAc...) (keratan sulfate) asparagineBy similarity1
Disulfide bondi334 ↔ 367By similarity
Glycosylationi341N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Binds keratan sulfate chains.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei63Not sulfated1 Publication1
Sitei65Not sulfated1 Publication1

Keywords - PTMi

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

Proteomic databases

EPDiQ06828
PaxDbiQ06828
PeptideAtlasiQ06828
PRIDEiQ06828

PTM databases

PhosphoSitePlusiQ06828

Miscellaneous databases

PMAP-CutDBiQ8IV47

Expressioni

Gene expression databases

BgeeiENSG00000122176
CleanExiHS_FMOD
ExpressionAtlasiQ06828 baseline and differential
GenevisibleiQ06828 HS

Interactioni

Subunit structurei

Binds to type I and type II collagen.By similarity

Protein-protein interaction databases

BioGridi108618, 10 interactors
IntActiQ06828, 3 interactors
MINTiQ06828
STRINGi9606.ENSP00000347041

Structurei

Secondary structure

1376
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi89 – 91Combined sources3
Beta strandi108 – 111Combined sources4
Turni122 – 125Combined sources4
Beta strandi133 – 135Combined sources3
Helixi143 – 145Combined sources3
Turni148 – 153Combined sources6
Beta strandi159 – 161Combined sources3
Beta strandi164 – 166Combined sources3
Beta strandi179 – 182Combined sources4
Turni193 – 198Combined sources6
Beta strandi204 – 206Combined sources3
Turni216 – 221Combined sources6
Beta strandi227 – 229Combined sources3
Beta strandi248 – 250Combined sources3
Turni261 – 266Combined sources6
Beta strandi272 – 274Combined sources3
Helixi282 – 284Combined sources3
Turni287 – 290Combined sources4
Beta strandi297 – 299Combined sources3
Beta strandi317 – 319Combined sources3
Helixi330 – 332Combined sources3
Beta strandi338 – 340Combined sources3
Beta strandi347 – 349Combined sources3
Beta strandi352 – 354Combined sources3
Helixi357 – 359Combined sources3
Helixi364 – 366Combined sources3
Beta strandi373 – 375Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5MX0X-ray2.21A/B18-376[»]
ProteinModelPortaliQ06828
SMRiQ06828
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini67 – 105LRRNTAdd BLAST39
Repeati106 – 127LRR 1Add BLAST22
Repeati130 – 151LRR 2Add BLAST22
Repeati156 – 176LRR 3Add BLAST21
Repeati177 – 198LRR 4Add BLAST22
Repeati201 – 222LRR 5Add BLAST22
Repeati224 – 245LRR 6Add BLAST22
Repeati246 – 266LRR 7Add BLAST21
Repeati269 – 289LRR 8Add BLAST21
Repeati294 – 315LRR 9Add BLAST22
Repeati316 – 335LRR 10Add BLAST20
Repeati344 – 365LRR 11Add BLAST22

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi76 – 92Cys-richAdd BLAST17

Sequence similaritiesi

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal

Phylogenomic databases

eggNOGiKOG0619 Eukaryota
COG4886 LUCA
GeneTreeiENSGT00760000118969
HOGENOMiHOG000234447
HOVERGENiHBG108061
InParanoidiQ06828
KOiK08121
OMAiDEDPHWW
OrthoDBiEOG091G0A3V
PhylomeDBiQ06828
TreeFamiTF334562

Family and domain databases

Gene3Di3.80.10.10, 3 hits
InterProiView protein in InterPro
IPR027215 Fibromodulin
IPR001611 Leu-rich_rpt
IPR003591 Leu-rich_rpt_typical-subtyp
IPR032675 LRR_dom_sf
IPR000372 LRRNT
PANTHERiPTHR24373:SF127 PTHR24373:SF127, 1 hit
PfamiView protein in Pfam
PF13855 LRR_8, 3 hits
PF01462 LRRNT, 1 hit
SMARTiView protein in SMART
SM00369 LRR_TYP, 8 hits
SM00013 LRRNT, 1 hit
PROSITEiView protein in PROSITE
PS51450 LRR, 10 hits

Sequencei

Sequence statusi: Complete.

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

Q06828-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQWTSLLLLA GLFSLSQAQY EDDPHWWFHY LRSQQSTYYD PYDPYPYETY
60 70 80 90 100
EPYPYGVDEG PAYTYGSPSP PDPRDCPQEC DCPPNFPTAM YCDNRNLKYL
110 120 130 140 150
PFVPSRMKYV YFQNNQITSI QEGVFDNATG LLWIALHGNQ ITSDKVGRKV
160 170 180 190 200
FSKLRHLERL YLDHNNLTRM PGPLPRSLRE LHLDHNQISR VPNNALEGLE
210 220 230 240 250
NLTALYLQHN EIQEVGSSMR GLRSLILLDL SYNHLRKVPD GLPSALEQLY
260 270 280 290 300
MEHNNVYTVP DSYFRGAPKL LYVRLSHNSL TNNGLASNTF NSSSLLELDL
310 320 330 340 350
SYNQLQKIPP VNTNLENLYL QGNRINEFSI SSFCTVVDVV NFSKLQVLRL
360 370
DGNEIKRSAM PADAPLCLRL ASLIEI
Length:376
Mass (Da):43,179
Last modified:February 10, 2009 - v2
Checksum:iDC19D5E6724AB004
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4T → A in CAA53233 (PubMed:8093006).Curated1
Sequence conflicti87P → L in CAA53233 (PubMed:8093006).Curated1
Sequence conflicti210N → D in CAA53233 (PubMed:8093006).Curated1
Sequence conflicti226I → Y in CAA51418 (PubMed:8357838).Curated1
Sequence conflicti344K → Q in CAA51418 (PubMed:8357838).Curated1
Sequence conflicti348L → V in CAA51418 (PubMed:8357838).Curated1
Sequence conflicti348L → V in CAA53233 (PubMed:8093006).Curated1
Sequence conflicti355I → M in CAA51418 (PubMed:8357838).Curated1
Sequence conflicti363D → E in CAA51418 (PubMed:8357838).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72913 Genomic DNA Translation: CAA51418.1
X75546 mRNA Translation: CAA53233.1
AK291632 mRNA Translation: BAF84321.1
AL359837 Genomic DNA No translation available.
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.5 human

Similar proteinsi

Entry informationi

Entry nameiFMOD_HUMAN
AccessioniPrimary (citable) accession number: Q06828
Secondary accession number(s): Q15331, Q8IV47
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 10, 2009
Last modified: February 28, 2018
This is version 164 of the entry and version 2 of the sequence. See 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

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health