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Protein

Ficolin-2

Gene

FCN2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Enhances phagocytosis of S.typhimurium by neutrophils, suggesting an opsonic effect via the collagen region.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi249 – 2491CalciumCombined sources1 Publication
Metal bindingi251 – 2511CalciumCombined sources1 Publication
Metal bindingi253 – 2531Calcium; via carbonyl oxygenCombined sources1 Publication
Metal bindingi255 – 2551Calcium; via carbonyl oxygenCombined sources1 Publication

GO - Molecular functioni

  • antigen binding Source: UniProtKB
  • calcium-dependent protein binding Source: UniProtKB
  • mannan binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • proteoglycan binding Source: UniProtKB

GO - Biological processi

  • complement activation Source: Reactome
  • complement activation, lectin pathway Source: UniProtKB
  • defense response to Gram-negative bacterium Source: UniProtKB
  • defense response to Gram-positive bacterium Source: UniProtKB
  • innate immune response Source: Reactome
  • opsonization Source: UniProtKB
  • recognition of apoptotic cell Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Complement activation lectin pathway, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-166662. Lectin pathway of complement activation.
R-HSA-166663. Initial triggering of complement.
R-HSA-2855086. Ficolins bind to repetitive carbohydrate structures on the target cell surface.

Names & Taxonomyi

Protein namesi
Recommended name:
Ficolin-2
Alternative name(s):
37 kDa elastin-binding protein
Collagen/fibrinogen domain-containing protein 2
EBP-37
Ficolin-B
Ficolin-beta
Hucolin
L-ficolin
Serum lectin p35
Gene namesi
Name:FCN2
Synonyms:FCNL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:3624. FCN2.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • collagen trimer Source: UniProtKB-KW
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28070.

Polymorphism and mutation databases

BioMutaiFCN2.
DMDMi166214934.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence analysisAdd
BLAST
Chaini26 – 313288Ficolin-2PRO_0000009139Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei77 – 771Hydroxyproline1 Publication
Modified residuei80 – 801Hydroxyproline1 Publication
Modified residuei86 – 861Hydroxyproline1 Publication
Disulfide bondi98 ↔ 126By similarity
Disulfide bondi105 ↔ 133Combined sources1 Publication
Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence analysis1 Publication
Disulfide bondi257 ↔ 270Combined sources1 Publication
Glycosylationi300 – 3001N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

PaxDbiQ15485.
PRIDEiQ15485.

Expressioni

Tissue specificityi

Expressed by the liver and secreted in plasma.

Gene expression databases

BgeeiQ15485.
CleanExiHS_FCN2.
GenevisibleiQ15485. HS.

Interactioni

Subunit structurei

Homotrimer (PubMed:17215869). Interacts with elastin. Interacts with MASP1 and MASP2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LRP1Q079542EBI-7468784,EBI-1046087

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • proteoglycan binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108514. 3 interactions.
IntActiQ15485. 3 interactions.
MINTiMINT-5223224.
STRINGi9606.ENSP00000291744.

Structurei

Secondary structure

1
313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni98 – 1003Combined sources
Helixi105 – 1106Combined sources
Beta strandi115 – 1228Combined sources
Beta strandi124 – 1263Combined sources
Beta strandi128 – 1347Combined sources
Helixi137 – 1393Combined sources
Beta strandi142 – 15110Combined sources
Helixi159 – 1646Combined sources
Beta strandi166 – 1683Combined sources
Helixi177 – 1826Combined sources
Beta strandi185 – 1873Combined sources
Beta strandi191 – 1966Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi202 – 2087Combined sources
Beta strandi210 – 2123Combined sources
Turni215 – 2195Combined sources
Beta strandi221 – 2233Combined sources
Beta strandi226 – 2283Combined sources
Helixi236 – 2383Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi251 – 2555Combined sources
Helixi258 – 2614Combined sources
Beta strandi263 – 2653Combined sources
Beta strandi268 – 2703Combined sources
Beta strandi272 – 2743Combined sources
Beta strandi285 – 2884Combined sources
Beta strandi290 – 2934Combined sources
Turni294 – 2974Combined sources
Beta strandi299 – 3024Combined sources
Beta strandi304 – 3107Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J0GX-ray2.85A/B/C/D/E/F97-313[»]
2J0HX-ray2.85A/B/C/D/E/F97-313[»]
2J0YX-ray2.35A/B/C/D/E/F97-313[»]
2J1GX-ray1.95A/B/C/D/E/F97-313[»]
2J2PX-ray2.80A/B/C/D/E/F97-313[»]
2J3FX-ray2.80A/B/C/D/E/F95-313[»]
2J3GX-ray2.50A/B/C/D/E/F97-313[»]
2J3OX-ray2.65A/B/C/D/E/F95-313[»]
2J3UX-ray2.15A/B/C/D/E/F97-313[»]
2J61X-ray2.70A/B97-313[»]
4NYTX-ray2.25A/B/C97-313[»]
4R9JX-ray2.10A/B/G97-313[»]
4R9TX-ray2.25A/B/C97-313[»]
ProteinModelPortaliQ15485.
SMRiQ15485. Positions 97-313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15485.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini51 – 9242Collagen-likeAdd
BLAST
Domaini96 – 313218Fibrinogen C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni241 – 2422Carbohydrate binding1 Publication

Domaini

The fibrinogen-like domain (FBG) contains calcium-binding sites that may be involved in carbohydrate binding.1 Publication

Sequence similaritiesi

Belongs to the ficolin lectin family.Curated
Contains 1 collagen-like domain.Curated
Contains 1 fibrinogen C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000037127.
HOVERGENiHBG001644.
InParanoidiQ15485.
KOiK10104.
OMAiNTGNCAV.
OrthoDBiEOG7X9G60.
PhylomeDBiQ15485.
TreeFamiTF329953.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR008160. Collagen.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamiPF01391. Collagen. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15485-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MELDRAVGVL GAATLLLSFL GMAWALQAAD TCPEVKMVGL EGSDKLTILR
60 70 80 90 100
GCPGLPGAPG PKGEAGTNGK RGERGPPGPP GKAGPPGPNG APGEPQPCLT
110 120 130 140 150
GPRTCKDLLD RGHFLSGWHT IYLPDCRPLT VLCDMDTDGG GWTVFQRRVD
160 170 180 190 200
GSVDFYRDWA TYKQGFGSRL GEFWLGNDNI HALTAQGTSE LRVDLVDFED
210 220 230 240 250
NYQFAKYRSF KVADEAEKYN LVLGAFVEGS AGDSLTFHNN QSFSTKDQDN
260 270 280 290 300
DLNTGNCAVM FQGAWWYKNC HVSNLNGRYL RGTHGSFANG INWKSGKGYN
310
YSYKVSEMKV RPA
Length:313
Mass (Da):34,001
Last modified:January 15, 2008 - v2
Checksum:iD363029846CCB3C9
GO
Isoform 2 (identifier: Q15485-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     34-71: Missing.

Note: No experimental confirmation available.
Show »
Length:275
Mass (Da):30,228
Checksum:i033A008F64CFA4C0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611P → D in BAA08352 (PubMed:8884275).Curated
Sequence conflicti61 – 611P → D in ABB01005 (PubMed:8576206).Curated
Sequence conflicti98 – 981C → A AA sequence (PubMed:8586615).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti80 – 801P → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036342
Natural varianti113 – 1131H → Y.1 Publication
Corresponds to variant rs17549179 [ dbSNP | Ensembl ].
VAR_049072
Natural varianti117 – 1171G → S.
Corresponds to variant rs12684476 [ dbSNP | Ensembl ].
VAR_049073
Natural varianti236 – 2361T → M.
Corresponds to variant rs17549193 [ dbSNP | Ensembl ].
VAR_049074
Natural varianti258 – 2581A → S.
Corresponds to variant rs7851696 [ dbSNP | Ensembl ].
VAR_049075

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei34 – 7138Missing in isoform 2. CuratedVSP_030027Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63160 Genomic DNA. Translation: BAA09636.1.
D49353 mRNA. Translation: BAA08352.1.
DQ217935 Genomic DNA. Translation: ABB01005.1.
AK290843 mRNA. Translation: BAF83532.1.
AL603650 Genomic DNA. Translation: CAI39861.1.
CH471090 Genomic DNA. Translation: EAW88133.1.
CH471090 Genomic DNA. Translation: EAW88135.1.
BC069572 mRNA. Translation: AAH69572.1.
BC069825 mRNA. Translation: AAH69825.1.
CCDSiCCDS6983.1. [Q15485-1]
PIRiPH0263.
S68005.
RefSeqiNP_004099.2. NM_004108.2. [Q15485-1]
NP_056652.1. NM_015837.2. [Q15485-2]
UniGeneiHs.54517.

Genome annotation databases

EnsembliENST00000291744; ENSP00000291744; ENSG00000160339. [Q15485-1]
ENST00000350339; ENSP00000291741; ENSG00000160339. [Q15485-2]
GeneIDi2220.
KEGGihsa:2220.
UCSCiuc004cfg.1. human. [Q15485-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63160 Genomic DNA. Translation: BAA09636.1.
D49353 mRNA. Translation: BAA08352.1.
DQ217935 Genomic DNA. Translation: ABB01005.1.
AK290843 mRNA. Translation: BAF83532.1.
AL603650 Genomic DNA. Translation: CAI39861.1.
CH471090 Genomic DNA. Translation: EAW88133.1.
CH471090 Genomic DNA. Translation: EAW88135.1.
BC069572 mRNA. Translation: AAH69572.1.
BC069825 mRNA. Translation: AAH69825.1.
CCDSiCCDS6983.1. [Q15485-1]
PIRiPH0263.
S68005.
RefSeqiNP_004099.2. NM_004108.2. [Q15485-1]
NP_056652.1. NM_015837.2. [Q15485-2]
UniGeneiHs.54517.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J0GX-ray2.85A/B/C/D/E/F97-313[»]
2J0HX-ray2.85A/B/C/D/E/F97-313[»]
2J0YX-ray2.35A/B/C/D/E/F97-313[»]
2J1GX-ray1.95A/B/C/D/E/F97-313[»]
2J2PX-ray2.80A/B/C/D/E/F97-313[»]
2J3FX-ray2.80A/B/C/D/E/F95-313[»]
2J3GX-ray2.50A/B/C/D/E/F97-313[»]
2J3OX-ray2.65A/B/C/D/E/F95-313[»]
2J3UX-ray2.15A/B/C/D/E/F97-313[»]
2J61X-ray2.70A/B97-313[»]
4NYTX-ray2.25A/B/C97-313[»]
4R9JX-ray2.10A/B/G97-313[»]
4R9TX-ray2.25A/B/C97-313[»]
ProteinModelPortaliQ15485.
SMRiQ15485. Positions 97-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108514. 3 interactions.
IntActiQ15485. 3 interactions.
MINTiMINT-5223224.
STRINGi9606.ENSP00000291744.

Polymorphism and mutation databases

BioMutaiFCN2.
DMDMi166214934.

Proteomic databases

PaxDbiQ15485.
PRIDEiQ15485.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000291744; ENSP00000291744; ENSG00000160339. [Q15485-1]
ENST00000350339; ENSP00000291741; ENSG00000160339. [Q15485-2]
GeneIDi2220.
KEGGihsa:2220.
UCSCiuc004cfg.1. human. [Q15485-1]

Organism-specific databases

CTDi2220.
GeneCardsiFCN2.
HGNCiHGNC:3624. FCN2.
MIMi601624. gene.
neXtProtiNX_Q15485.
PharmGKBiPA28070.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
GeneTreeiENSGT00830000128240.
HOGENOMiHOG000037127.
HOVERGENiHBG001644.
InParanoidiQ15485.
KOiK10104.
OMAiNTGNCAV.
OrthoDBiEOG7X9G60.
PhylomeDBiQ15485.
TreeFamiTF329953.

Enzyme and pathway databases

ReactomeiR-HSA-166662. Lectin pathway of complement activation.
R-HSA-166663. Initial triggering of complement.
R-HSA-2855086. Ficolins bind to repetitive carbohydrate structures on the target cell surface.

Miscellaneous databases

EvolutionaryTraceiQ15485.
GeneWikiiFCN2.
GenomeRNAii2220.
NextBioi9005.
PROiQ15485.
SOURCEiSearch...

Gene expression databases

BgeeiQ15485.
CleanExiHS_FCN2.
GenevisibleiQ15485. HS.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR008160. Collagen.
IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamiPF01391. Collagen. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view]
SMARTiSM00186. FBG. 1 hit.
[Graphical view]
SUPFAMiSSF56496. SSF56496. 1 hit.
PROSITEiPS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of the human lectin P35 gene and its related gene."
    Endo Y., Sato Y., Matsushita M., Fujita T.
    Genomics 36:515-521(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin."
    Matsushita M., Endo Y., Taira S., Sato Y., Fujita T., Ichikawa N., Nakata M., Mizuochi T.
    J. Biol. Chem. 271:2448-2454(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "Genetic variation in immune response genes."
    Tan J., Ong R., Hibberd M.L., Seielstad M.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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] (ISOFORM 1), VARIANT TYR-113.
    Tissue: Liver.
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
  8. "Hucolin, a new corticosteroid-binding protein from human plasma with structural similarities to ficolins, transforming growth factor-beta 1-binding proteins."
    Edgar P.F.
    FEBS Lett. 375:159-161(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 26-50 (ISOFORM 1).
    Tissue: Plasma.
  9. "EBP-37, a new elastin-binding protein in human plasma: structural similarity to ficolins, transforming growth factor-beta 1-binding proteins."
    Harumiya S., Omori A., Sugiura T., Fukumoto Y., Tachikawa H., Fujimoto D.
    J. Biochem. 117:1029-1035(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 65-99; 191-198 AND 218-228 (ISOFORM 1), SUBUNIT, HYDROXYLATION AT PRO-77; PRO-80 AND PRO-86.
    Tissue: Plasma.
  10. "Complement-activating complex of ficolin and mannose-binding lectin-associated serine protease."
    Matsushita M., Endo Y., Fujita T.
    J. Immunol. 164:2281-2284(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MASP1 AND MASP2.
  11. "Structural insights into the innate immune recognition specificities of L- and H-ficolins."
    Garlatti V., Belloy N., Martin L., Lacroix M., Matsushita M., Endo Y., Fujita T., Fontecilla-Camps J.C., Arlaud G.J., Thielens N.M., Gaboriaud C.
    EMBO J. 26:623-633(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 97-313 IN COMPLEXES WITH CALCIUM AND FUCOSE, FUNCTION, SUBUNIT, DOMAIN, DISULFIDE BOND, GLYCOSYLATION AT ASN-240.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-80.

Entry informationi

Entry nameiFCN2_HUMAN
AccessioniPrimary (citable) accession number: Q15485
Secondary accession number(s): A6NFG7
, A8K478, Q6IS69, Q7M4P4, Q9UC57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 15, 2008
Last modified: May 11, 2016
This is version 148 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.