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O00602

- FCN1_HUMAN

UniProt

O00602 - FCN1_HUMAN

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Protein

Ficolin-1

Gene
FCN1, FCNM
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Complement-activating lectin and pattern recognition receptor. Binds GlcNAc. Binds preferentially to 9-O-acetylated 2-6-linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi262 – 2621Calcium
Metal bindingi264 – 2641Calcium
Metal bindingi266 – 2661Calcium; via carbonyl oxygen
Metal bindingi268 – 2681Calcium; via carbonyl oxygen
Sitei300 – 3001Mediates specificity for sialic acids
Sitei312 – 3121Mediates specificity for sialic acids

GO - Molecular functioni

  1. antigen binding Source: ProtInc
  2. calcium ion binding Source: ProtInc
  3. carbohydrate binding Source: ProtInc
  4. protein binding Source: IntAct

GO - Biological processi

  1. complement activation Source: Reactome
  2. complement activation, lectin pathway Source: Reactome
  3. innate immune response Source: Reactome
  4. opsonization Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_163810. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
REACT_7964. Lectin pathway of complement activation.
REACT_8024. Initial triggering of complement.

Names & Taxonomyi

Protein namesi
Recommended name:
Ficolin-1
Alternative name(s):
Collagen/fibrinogen domain-containing protein 1
Ficolin-A
Ficolin-alpha
M-ficolin
Gene namesi
Name:FCN1
Synonyms:FCNM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:3623. FCN1.

Subcellular locationi

Secreted
Note: Found on the monocyte and granulocyte surface.1 Publication

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi250 – 2501G → F: Inhibits binding to the 9-O-acetylated sialic acid derivatives. 1 Publication
Mutagenesisi285 – 2851A → V: Inhibits binding to the 9-O-acetylated sialic acid derivatives. 1 Publication
Mutagenesisi300 – 3001Y → F: Abolishes interaction with all sialic acid-containing glycans. 1 Publication

Organism-specific databases

PharmGKBiPA28069.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Chaini30 – 326297Ficolin-1PRO_0000009136Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi111 ↔ 1393 Publications
Disulfide bondi118 ↔ 1463 Publications
Disulfide bondi270 ↔ 2833 Publications
Glycosylationi305 – 3051N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO00602.
PeptideAtlasiO00602.
PRIDEiO00602.

Expressioni

Tissue specificityi

Peripheral blood leukocytes, monocytes and granulocytes. Also detected in spleen, lung, and thymus, may be due to the presence of tissue macrophages or trapped blood in these tissues. Not detected on lymphocytes.1 Publication

Gene expression databases

ArrayExpressiO00602.
BgeeiO00602.
CleanExiHS_FCN1.
GenevestigatoriO00602.

Organism-specific databases

HPAiCAB016760.
HPA000685.
HPA001295.

Interactioni

Subunit structurei

Homotrimer. Interacts with elastin.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CRP-1Q2TS393EBI-5282479,EBI-7468648From a different organism.

Protein-protein interaction databases

BioGridi108513. 2 interactions.
IntActiO00602. 1 interaction.
MINTiMINT-5223276.
STRINGi9606.ENSP00000360871.

Structurei

Secondary structure

1
326
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni111 – 1133
Helixi118 – 1236
Beta strandi130 – 1356
Beta strandi141 – 1477
Helixi150 – 1523
Beta strandi155 – 16410
Helixi172 – 1776
Beta strandi179 – 1813
Helixi190 – 1989
Beta strandi202 – 2098
Beta strandi215 – 2217
Beta strandi223 – 2253
Helixi228 – 2303
Beta strandi234 – 2363
Beta strandi239 – 2413
Helixi249 – 2513
Beta strandi264 – 2685
Helixi270 – 2734
Beta strandi281 – 2833
Beta strandi285 – 2873
Beta strandi298 – 3014
Beta strandi303 – 3064
Turni307 – 3093
Beta strandi312 – 3154
Beta strandi317 – 3259

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D39X-ray1.90A/B/C115-326[»]
2JHHX-ray1.70C/F109-326[»]
2JHIX-ray1.80F109-326[»]
2JHKX-ray1.75F109-326[»]
2JHLX-ray1.75F109-326[»]
2JHMX-ray1.52F109-326[»]
2WNPX-ray1.21F110-326[»]
ProteinModelPortaliO00602.
SMRiO00602. Positions 110-326.

Miscellaneous databases

EvolutionaryTraceiO00602.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 9339Collagen-likeAdd
BLAST
Domaini109 – 326218Fibrinogen C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni115 – 15440A domain; contributes to trimerizationAdd
BLAST
Regioni155 – 24389B domain; contributes to trimerizationAdd
BLAST
Regioni282 – 2843Carbohydrate-binding
Regioni317 – 32610P domain

Domaini

The Fibrinogen C-terminal domain mediates calcium-dependent binding to carbohydrates and tethering to the cell surface in monocytes and granulocytes. The domain undergoes a conformational switch at pH under 6.2, and looses its carbohydrate-binding ability.

Sequence similaritiesi

Belongs to the ficolin lectin family.

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG249945.
HOGENOMiHOG000037127.
HOVERGENiHBG001644.
KOiK10104.
OMAiNFFSTKD.
OrthoDBiEOG7X9G60.
PhylomeDBiO00602.
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]

Sequencei

Sequence statusi: Complete.

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

O00602-1 [UniParc]FASTAAdd to Basket

« Hide

MELSGATMAR GLAVLLVLFL HIKNLPAQAA DTCPEVKVVG LEGSDKLTIL    50
RGCPGLPGAP GPKGEAGVIG ERGERGLPGA PGKAGPVGPK GDRGEKGMRG 100
EKGDAGQSQS CATGPRNCKD LLDRGYFLSG WHTIYLPDCR PLTVLCDMDT 150
DGGGWTVFQR RMDGSVDFYR DWAAYKQGFG SQLGEFWLGN DNIHALTAQG 200
SSELRVDLVD FEGNHQFAKY KSFKVADEAE KYKLVLGAFV GGSAGNSLTG 250
HNNNFFSTKD QDNDVSSSNC AEKFQGAWWY ADCHASNLNG LYLMGPHESY 300
ANGINWSAAK GYKYSYKVSE MKVRPA 326
Length:326
Mass (Da):35,078
Last modified:May 2, 2002 - v2
Checksum:i184D24B371B251AB
GO

Sequence cautioni

The sequence BAA12120.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti93 – 931R → Q.
Corresponds to variant rs56345770 [ dbSNP | Ensembl ].
VAR_061172
Natural varianti126 – 1261Y → H.
Corresponds to variant rs17549179 [ dbSNP | Ensembl ].
VAR_024450
Natural varianti175 – 1751Y → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036341

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331T → N in AAB50706. 1 Publication
Sequence conflicti287 – 2871N → S in AAB50706. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S80990 mRNA. Translation: AAB50706.1.
AK314867 mRNA. Translation: BAG37382.1.
AL353611 Genomic DNA. Translation: CAH73911.1.
CH471090 Genomic DNA. Translation: EAW88137.1.
BC020635 mRNA. Translation: AAH20635.1.
D83920 mRNA. Translation: BAA12120.1. Different initiation.
CCDSiCCDS6985.1.
PIRiS61517.
RefSeqiNP_001994.2. NM_002003.3.
UniGeneiHs.440898.

Genome annotation databases

EnsembliENST00000371806; ENSP00000360871; ENSG00000085265.
GeneIDi2219.
KEGGihsa:2219.
UCSCiuc004cfi.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S80990 mRNA. Translation: AAB50706.1 .
AK314867 mRNA. Translation: BAG37382.1 .
AL353611 Genomic DNA. Translation: CAH73911.1 .
CH471090 Genomic DNA. Translation: EAW88137.1 .
BC020635 mRNA. Translation: AAH20635.1 .
D83920 mRNA. Translation: BAA12120.1 . Different initiation.
CCDSi CCDS6985.1.
PIRi S61517.
RefSeqi NP_001994.2. NM_002003.3.
UniGenei Hs.440898.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2D39 X-ray 1.90 A/B/C 115-326 [» ]
2JHH X-ray 1.70 C/F 109-326 [» ]
2JHI X-ray 1.80 F 109-326 [» ]
2JHK X-ray 1.75 F 109-326 [» ]
2JHL X-ray 1.75 F 109-326 [» ]
2JHM X-ray 1.52 F 109-326 [» ]
2WNP X-ray 1.21 F 110-326 [» ]
ProteinModelPortali O00602.
SMRi O00602. Positions 110-326.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108513. 2 interactions.
IntActi O00602. 1 interaction.
MINTi MINT-5223276.
STRINGi 9606.ENSP00000360871.

Proteomic databases

PaxDbi O00602.
PeptideAtlasi O00602.
PRIDEi O00602.

Protocols and materials databases

DNASUi 2219.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371806 ; ENSP00000360871 ; ENSG00000085265 .
GeneIDi 2219.
KEGGi hsa:2219.
UCSCi uc004cfi.3. human.

Organism-specific databases

CTDi 2219.
GeneCardsi GC09M137801.
HGNCi HGNC:3623. FCN1.
HPAi CAB016760.
HPA000685.
HPA001295.
MIMi 601252. gene.
neXtProti NX_O00602.
PharmGKBi PA28069.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG249945.
HOGENOMi HOG000037127.
HOVERGENi HBG001644.
KOi K10104.
OMAi NFFSTKD.
OrthoDBi EOG7X9G60.
PhylomeDBi O00602.
TreeFami TF329953.

Enzyme and pathway databases

Reactomei REACT_163810. Ficolins bind to repetitive carbohydrate structures on the target cell surface.
REACT_7964. Lectin pathway of complement activation.
REACT_8024. Initial triggering of complement.

Miscellaneous databases

EvolutionaryTracei O00602.
GeneWikii FCN1.
GenomeRNAii 2219.
NextBioi 9001.
PROi O00602.
SOURCEi Search...

Gene expression databases

ArrayExpressi O00602.
Bgeei O00602.
CleanExi HS_FCN1.
Genevestigatori O00602.

Family and domain databases

Gene3Di 3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProi IPR008160. 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 ]
Pfami PF01391. Collagen. 1 hit.
PF00147. Fibrinogen_C. 1 hit.
[Graphical view ]
SMARTi SM00186. FBG. 1 hit.
[Graphical view ]
SUPFAMi SSF56496. SSF56496. 1 hit.
PROSITEi PS00514. FIBRINOGEN_C_1. 1 hit.
PS51406. FIBRINOGEN_C_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9."
    Lu J., Tay P.N., Kon O.L., Reid K.B.
    Biochem. J. 313:473-478(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Uterus.
  2. "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].
  3. "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].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Lung.
  6. "Characterization of ficolins as novel elastin-binding proteins and molecular cloning of human ficolin-1."
    Harumiya S., Takeda K., Sugiura T., Fukumoto Y., Tachikawa H., Miyazono K., Fujimoto D., Ichijo H.
    J. Biochem. 120:745-751(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-326.
    Tissue: Uterus.
  7. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-44.
  8. "Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain."
    Honore C., Rorvig S., Hummelshoj T., Skjoedt M.O., Borregaard N., Garred P.
    J. Leukoc. Biol. 88:145-158(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  9. "Trivalent recognition unit of innate immunity system: crystal structure of trimeric human M-ficolin fibrinogen-like domain."
    Tanio M., Kondo S., Sugio S., Kohno T.
    J. Biol. Chem. 282:3889-3895(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 115-326, SUBUNIT, DISULFIDE BONDS, CALCIUM-BINDING SITES, PH-DEPENDENCY.
  10. "Structural basis for innate immune sensing by M-ficolin and its control by a pH-dependent conformational switch."
    Garlatti V., Martin L., Gout E., Reiser J.B., Fujita T., Arlaud G.J., Thielens N.M., Gaboriaud C.
    J. Biol. Chem. 282:35814-35820(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 109-326 IN COMPLEX WITH CARBOHYDRATE, DISULFIDE BONDS, CALCIUM-BINDING SITES, PH-DEPENDENCY.
  11. "Carbohydrate recognition properties of human ficolins: glycan array screening reveals the sialic acid binding specificity of M-ficolin."
    Gout E., Garlatti V., Smith D.F., Lacroix M., Dumestre-Perard C., Lunardi T., Martin L., Cesbron J.Y., Arlaud G.J., Gaboriaud C., Thielens N.M.
    J. Biol. Chem. 285:6612-6622(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.21 ANGSTROMS) OF 110-326, DISULFIDE BONDS, FUNCTION, SUBUNIT, SUBSTRATE SPECIFICITY, CALCIUM-BINDING SITES, MUTAGENESIS OF GLY-250; ALA-285 AND TYR-300.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-175.

Entry informationi

Entry nameiFCN1_HUMAN
AccessioniPrimary (citable) accession number: O00602
Secondary accession number(s): Q5VYV5, Q92596
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 2, 2002
Last modified: September 3, 2014
This is version 132 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

External Data

Dasty 3

Similar proteinsi