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P02671

- FIBA_HUMAN

UniProt

P02671 - FIBA_HUMAN

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Protein
Fibrinogen alpha chain
Gene
FGA
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei35 – 362Cleavage; by thrombin; to release fibrinopeptide A
Sitei100 – 1012Cleavage; by plasmin; to break down fibrin clots
Sitei121 – 1222Cleavage; by hementin; to prevent blood coagulation
Sitei123 – 1242Cleavage; by plasmin; to break down fibrin clots

GO - Molecular functioni

  1. protein binding Source: UniProtKB
  2. structural molecule activity Source: BHF-UCL

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. blood coagulation, common pathway Source: BHF-UCL
  3. cell-matrix adhesion Source: BHF-UCL
  4. cellular protein complex assembly Source: BHF-UCL
  5. extracellular matrix organization Source: Reactome
  6. negative regulation of blood coagulation, common pathway Source: BHF-UCL
  7. negative regulation of endothelial cell apoptotic process Source: BHF-UCL
  8. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
  9. platelet activation Source: Reactome
  10. platelet aggregation Source: BHF-UCL
  11. platelet degranulation Source: Reactome
  12. positive regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  13. positive regulation of exocytosis Source: BHF-UCL
  14. positive regulation of heterotypic cell-cell adhesion Source: BHF-UCL
  15. positive regulation of peptide hormone secretion Source: BHF-UCL
  16. positive regulation of protein secretion Source: BHF-UCL
  17. positive regulation of substrate adhesion-dependent cell spreading Source: BHF-UCL
  18. positive regulation of vasoconstriction Source: BHF-UCL
  19. protein polymerization Source: BHF-UCL
  20. response to calcium ion Source: BHF-UCL
  21. signal transduction Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Enzyme and pathway databases

ReactomeiREACT_13552. Integrin cell surface interactions.
REACT_1439. Common Pathway.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_75925. Amyloids.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrinogen alpha chain
Cleaved into the following 2 chains:
Gene namesi
Name:FGA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:3661. FGA.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. cell cortex Source: Ensembl
  3. cell surface Source: BHF-UCL
  4. external side of plasma membrane Source: BHF-UCL
  5. extracellular region Source: UniProtKB
  6. extracellular space Source: BHF-UCL
  7. extracellular vesicular exosome Source: UniProt
  8. fibrinogen complex Source: BHF-UCL
  9. plasma membrane Source: Reactome
  10. platelet alpha granule Source: BHF-UCL
  11. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Secreted

Pathology & Biotechi

Involvement in diseasei

Congenital afibrinogenemia (CAFBN) [MIM:202400]: Rare autosomal recessive disorder is characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen.
Note: The disease is caused by mutations affecting the gene represented in this entry. The majority of cases of afibrinogenemia are due to truncating mutations. Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias.
Amyloidosis 8 (AMYL8) [MIM:105200]: A hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti545 – 5451E → V in AMYL8.
VAR_010731
Natural varianti573 – 5731R → L in AMYL8. 1 Publication
VAR_010732

Keywords - Diseasei

Amyloidosis, Disease mutation

Organism-specific databases

MIMi105200. phenotype.
134820. gene+phenotype.
202400. phenotype.
Orphaneti98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
93562. Familial renal amyloidosis due to fibrinogen A alpha-chain variant.
PharmGKBiPA429.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19193 Publications
Add
BLAST
Peptidei20 – 3516Fibrinopeptide A1 Publication
PRO_0000009021Add
BLAST
Chaini36 – 866831Fibrinogen alpha chain
PRO_0000009022Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei22 – 221Phosphoserine1 Publication
Disulfide bondi47 – 47Interchain2 Publications
Disulfide bondi55 – 55Interchain (with C-95 in beta chain)2 Publications
Disulfide bondi64 – 64Interchain (with C-49 in gamma chain)2 Publications
Disulfide bondi68 – 68Interchain (with C-106 in beta chain)2 Publications
Disulfide bondi180 – 180Interchain (with C-165 in gamma chain)2 Publications
Disulfide bondi184 – 184Interchain (with C-223 in beta chain)2 Publications
Glycosylationi320 – 3201O-linked (GalNAc...)1 Publication
Cross-linki322 – 322Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-41 in alpha-2-antiplasmin)
Cross-linki347 – 347Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Glycosylationi351 – 3511O-linked (GalNAc...)1 Publication
Cross-linki385 – 385Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)
Modified residuei412 – 4121Phosphothreonine1 Publication
Glycosylationi453 – 4531N-linked (GlcNAc...); in variant Caracas-2
Disulfide bondi461 ↔ 4912 Publications
Cross-linki527 – 527Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Reviewed prediction
Cross-linki558 – 558Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Reviewed prediction
Modified residuei565 – 56514-hydroxyproline; by P4HA11 Publication
Cross-linki575 – 575Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Reviewed prediction
Cross-linki581 – 581Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Reviewed prediction
Cross-linki599 – 599Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-?) Reviewed prediction
Modified residuei609 – 6091Phosphoserine1 Publication
Glycosylationi686 – 6861N-linked (GlcNAc...)2 Publications

Post-translational modificationi

The alpha chain is not glycosylated.1 Publication
Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.
About one-third of the alpha chains in the molecules in blood were found to be phosphorylated.1 Publication
Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
Phosphorylation sites are present in the extracellular medium.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Isopeptide bond, Phosphoprotein

Proteomic databases

MaxQBiP02671.
PaxDbiP02671.
PeptideAtlasiP02671.
PRIDEiP02671.

2D gel databases

OGPiP02671.
SWISS-2DPAGEP02671.

PTM databases

PhosphoSiteiP02671.

Miscellaneous databases

PMAP-CutDBP02671.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

ArrayExpressiP02671.
BgeeiP02671.
CleanExiHS_FGA.
GenevestigatoriP02671.

Organism-specific databases

HPAiCAB016776.
HPA051370.

Interactioni

Subunit structurei

Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain.1 Publication

Protein-protein interaction databases

BioGridi108534. 20 interactions.
DIPiDIP-29643N.
IntActiP02671. 12 interactions.
MINTiMINT-1033042.
STRINGi9606.ENSP00000306361.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni27 – 315
Beta strandi57 – 604
Beta strandi63 – 653
Helixi67 – 9226
Helixi94 – 11118
Helixi116 – 12914
Turni133 – 1353
Turni139 – 1413
Helixi142 – 17837
Turni179 – 1835
Beta strandi184 – 1863
Helixi195 – 20915
Beta strandi337 – 3437
Beta strandi673 – 6819
Helixi689 – 6946
Helixi711 – 7188
Beta strandi723 – 7297
Beta strandi735 – 74410
Turni747 – 7515
Beta strandi753 – 76210
Turni765 – 7684
Turni771 – 7733
Helixi775 – 7784
Beta strandi793 – 7975
Helixi799 – 8035
Beta strandi810 – 8123
Beta strandi814 – 8163
Beta strandi823 – 8264
Helixi829 – 8313
Beta strandi840 – 8434
Helixi844 – 8474
Beta strandi854 – 8618

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BBRX-ray2.30F/G/I26-35[»]
1DM4X-ray2.50C26-35[»]
1FZAX-ray2.90A/D130-216[»]
1FZBX-ray2.90A/D130-216[»]
1FZCX-ray2.30A/D130-216[»]
1FZDX-ray2.10A/B/C/D/E/F/G/H666-866[»]
1FZEX-ray3.00A/D130-216[»]
1FZFX-ray2.70A/D130-216[»]
1FZGX-ray2.50A/D130-216[»]
1LT9X-ray2.80A/D145-210[»]
1LTJX-ray2.80A/D145-210[»]
1N86X-ray3.20A/D130-216[»]
1N8EX-ray4.50A/D130-218[»]
1RE3X-ray2.45A/D145-210[»]
1RE4X-ray2.70A/D145-210[»]
1RF0X-ray2.81A/D145-210[»]
1RF1X-ray2.53A/D145-210[»]
1YCPX-ray2.50F/N20-42[»]
2A45X-ray3.65G/J36-92[»]
2FFDX-ray2.89A/D145-210[»]
2H43X-ray2.70A/D130-216[»]
2HLOX-ray2.60A/D130-216[»]
2HODX-ray2.90A/D/G/J130-216[»]
2HPCX-ray2.90A/D/G/J130-216[»]
2OYHX-ray2.40A/D145-210[»]
2OYIX-ray2.70A/D145-210[»]
2Q9IX-ray2.80A/D130-216[»]
2XNXX-ray3.30A/D/G/J130-216[»]
2XNYX-ray7.50A/D130-216[»]
2Z4EX-ray2.70A/D130-216[»]
3AT0X-ray2.50B332-347[»]
3BVHX-ray2.60A/D148-209[»]
3E1IX-ray2.30A/D130-216[»]
3GHGX-ray2.90A/D/G/J20-581[»]
3H32X-ray3.60A/D20-216[»]
3HUSX-ray3.04A/D145-210[»]
4F27X-ray1.92Q336-347[»]
ProteinModelPortaliP02671.
SMRiP02671. Positions 46-231, 411-524, 596-866.

Miscellaneous databases

EvolutionaryTraceiP02671.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini623 – 864242Fibrinogen C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni36 – 383Alpha-chain polymerization, binding distal domain of another fibrin gamma chain

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili68 – 631564 By similarity
Add
BLAST

Domaini

A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiNOG114889.
HOGENOMiHOG000285947.
HOVERGENiHBG005668.
InParanoidiP02671.
KOiK03903.
OMAiYKCPSGC.
OrthoDBiEOG7X9G60.
PhylomeDBiP02671.
TreeFamiTF351984.

Family and domain databases

Gene3Di3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProiIPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR012290. Fibrinogen_a/b/g_coil_dom.
IPR021996. Fibrinogen_aC.
IPR020837. Fibrinogen_CS.
[Graphical view]
PfamiPF08702. Fib_alpha. 1 hit.
PF12160. Fibrinogen_aC. 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. Align

Isoform 1 (identifier: P02671-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha-E

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

MFSMRIVCLV LSVVGTAWTA DSGEGDFLAE GGGVRGPRVV ERHQSACKDS    50
DWPFCSDEDW NYKCPSGCRM KGLIDEVNQD FTNRINKLKN SLFEYQKNNK 100
DSHSLTTNIM EILRGDFSSA NNRDNTYNRV SEDLRSRIEV LKRKVIEKVQ 150
HIQLLQKNVR AQLVDMKRLE VDIDIKIRSC RGSCSRALAR EVDLKDYEDQ 200
QKQLEQVIAK DLLPSRDRQH LPLIKMKPVP DLVPGNFKSQ LQKVPPEWKA 250
LTDMPQMRME LERPGGNEIT RGGSTSYGTG SETESPRNPS SAGSWNSGSS 300
GPGSTGNRNP GSSGTGGTAT WKPGSSGPGS TGSWNSGSSG TGSTGNQNPG 350
SPRPGSTGTW NPGSSERGSA GHWTSESSVS GSTGQWHSES GSFRPDSPGS 400
GNARPNNPDW GTFEEVSGNV SPGTRREYHT EKLVTSKGDK ELRTGKEKVT 450
SGSTTTTRRS CSKTVTKTVI GPDGHKEVTK EVVTSEDGSD CPEAMDLGTL 500
SGIGTLDGFR HRHPDEAAFF DTASTGKTFP GFFSPMLGEF VSETESRGSE 550
SGIFTNTKES SSHHPGIAEF PSRGKSSSYS KQFTSSTSYN RGDSTFESKS 600
YKMADEAGSE ADHEGTHSTK RGHAKSRPVR DCDDVLQTHP SGTQSGIFNI 650
KLPGSSKIFS VYCDQETSLG GWLLIQQRMD GSLNFNRTWQ DYKRGFGSLN 700
DEGEGEFWLG NDYLHLLTQR GSVLRVELED WAGNEAYAEY HFRVGSEAEG 750
YALQVSSYEG TAGDALIEGS VEEGAEYTSH NNMQFSTFDR DADQWEENCA 800
EVYGGGWWYN NCQAANLNGI YYPGGSYDPR NNSPYEIENG VVWVSFRGAD 850
YSLRAVRMKI RPLVTQ 866
Length:866
Mass (Da):94,973
Last modified:October 1, 1996 - v2
Checksum:iEA73A81204D8AEC4
GO
Isoform 2 (identifier: P02671-2) [UniParc]FASTAAdd to Basket

Also known as: Alpha

The sequence of this isoform differs from the canonical sequence as follows:
     631-644: DCDDVLQTHPSGTQ → GIHTSPLGKPSLSP
     645-866: Missing.

Show »
Length:644
Mass (Da):69,757
Checksum:iB9035F3DD864572A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61I → V.1 Publication
Corresponds to variant rs2070025 [ dbSNP | Ensembl ].
VAR_011609
Natural varianti26 – 261D → N in Lille-1.
VAR_002390
Natural varianti31 – 311G → V in Rouen-1.
VAR_002391
Natural varianti35 – 351R → C.
VAR_002392
Natural varianti35 – 351R → H.1 Publication
VAR_002393
Natural varianti37 – 371P → L in Kyoto-2. 1 Publication
VAR_002394
Natural varianti38 – 381R → G in Aarhus-1.
VAR_002397
Natural varianti38 – 381R → N in Munich-1; requires 2 nucleotide substitutions.
VAR_002395
Natural varianti38 – 381R → S in Detroit-1.
VAR_002396
Natural varianti39 – 391V → D in Canterbury. 1 Publication
VAR_010730
Natural varianti66 – 661S → T.
VAR_002398
Natural varianti160 – 1601R → S in Lima. 1 Publication
VAR_002399
Natural varianti331 – 3311T → A.3 Publications
Corresponds to variant rs6050 [ dbSNP | Ensembl ].
VAR_011610
Natural varianti446 – 4461K → E.1 Publication
Corresponds to variant rs6052 [ dbSNP | Ensembl ].
VAR_014168
Natural varianti453 – 4531S → N in Caracas-2. 1 Publication
VAR_002400
Natural varianti456 – 4561T → A.1 Publication
Corresponds to variant rs2070031 [ dbSNP | Ensembl ].
VAR_011611
Natural varianti545 – 5451E → V in AMYL8.
VAR_010731
Natural varianti573 – 5731R → C in Dusart/Paris-5. 1 Publication
VAR_002401
Natural varianti573 – 5731R → L in AMYL8. 1 Publication
VAR_010732

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei631 – 64414DCDDV…PSGTQ → GIHTSPLGKPSLSP in isoform 2.
VSP_001531Add
BLAST
Alternative sequencei645 – 866222Missing in isoform 2.
VSP_001532Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti177 – 1771I → V in BAF83248. 1 Publication
Sequence conflicti184 – 1841C → W in AAA52426. 1 Publication
Sequence conflicti215 – 2162SR → RS AA sequence 1 Publication
Sequence conflicti299 – 2991S → G AA sequence 1 Publication
Sequence conflicti304 – 3041S → G AA sequence 1 Publication
Sequence conflicti317 – 3182GT → SG AA sequence 1 Publication
Isoform 2 (identifier: P02671-2)
Sequence conflicti640 – 6445PSLSP → LPCPPRLS in AAK31372. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64982 Genomic DNA. Translation: AAA17056.1.
M64982 Genomic DNA. Translation: AAA17055.1.
M58569 Transcribed RNA. Translation: AAC97142.1.
M58569 Transcribed RNA. Translation: AAC97143.1.
AF361104 Genomic DNA. Translation: AAK31372.1.
AF361104 Genomic DNA. Translation: AAK31373.1.
AK290559 mRNA. Translation: BAF83248.1.
CH471056 Genomic DNA. Translation: EAX04925.1.
CH471056 Genomic DNA. Translation: EAX04926.1.
CH471056 Genomic DNA. Translation: EAX04927.1.
CH471056 Genomic DNA. Translation: EAX04928.1.
BC098280 mRNA. Translation: AAH98280.1.
BC099706 mRNA. Translation: AAH99706.1.
BC099720 mRNA. Translation: AAH99720.1.
BC101935 mRNA. Translation: AAI01936.1.
J00128 mRNA. Translation: AAA52427.1.
J00127 mRNA. Translation: AAA52426.1.
K02272 mRNA. Translation: AAA52428.1.
M26878 mRNA. Translation: AAA52444.1.
CCDSiCCDS3787.1. [P02671-1]
CCDS47152.1. [P02671-2]
PIRiA93956. FGHUA.
D44234.
RefSeqiNP_000499.1. NM_000508.3. [P02671-1]
NP_068657.1. NM_021871.2. [P02671-2]
UniGeneiHs.351593.

Genome annotation databases

EnsembliENST00000302053; ENSP00000306361; ENSG00000171560. [P02671-1]
ENST00000403106; ENSP00000385981; ENSG00000171560. [P02671-2]
GeneIDi2243.
KEGGihsa:2243.
UCSCiuc003iod.1. human. [P02671-1]
uc003ioe.1. human. [P02671-2]

Polymorphism databases

DMDMi1706799.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Fibrinogen entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64982 Genomic DNA. Translation: AAA17056.1 .
M64982 Genomic DNA. Translation: AAA17055.1 .
M58569 Transcribed RNA. Translation: AAC97142.1 .
M58569 Transcribed RNA. Translation: AAC97143.1 .
AF361104 Genomic DNA. Translation: AAK31372.1 .
AF361104 Genomic DNA. Translation: AAK31373.1 .
AK290559 mRNA. Translation: BAF83248.1 .
CH471056 Genomic DNA. Translation: EAX04925.1 .
CH471056 Genomic DNA. Translation: EAX04926.1 .
CH471056 Genomic DNA. Translation: EAX04927.1 .
CH471056 Genomic DNA. Translation: EAX04928.1 .
BC098280 mRNA. Translation: AAH98280.1 .
BC099706 mRNA. Translation: AAH99706.1 .
BC099720 mRNA. Translation: AAH99720.1 .
BC101935 mRNA. Translation: AAI01936.1 .
J00128 mRNA. Translation: AAA52427.1 .
J00127 mRNA. Translation: AAA52426.1 .
K02272 mRNA. Translation: AAA52428.1 .
M26878 mRNA. Translation: AAA52444.1 .
CCDSi CCDS3787.1. [P02671-1 ]
CCDS47152.1. [P02671-2 ]
PIRi A93956. FGHUA.
D44234.
RefSeqi NP_000499.1. NM_000508.3. [P02671-1 ]
NP_068657.1. NM_021871.2. [P02671-2 ]
UniGenei Hs.351593.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BBR X-ray 2.30 F/G/I 26-35 [» ]
1DM4 X-ray 2.50 C 26-35 [» ]
1FZA X-ray 2.90 A/D 130-216 [» ]
1FZB X-ray 2.90 A/D 130-216 [» ]
1FZC X-ray 2.30 A/D 130-216 [» ]
1FZD X-ray 2.10 A/B/C/D/E/F/G/H 666-866 [» ]
1FZE X-ray 3.00 A/D 130-216 [» ]
1FZF X-ray 2.70 A/D 130-216 [» ]
1FZG X-ray 2.50 A/D 130-216 [» ]
1LT9 X-ray 2.80 A/D 145-210 [» ]
1LTJ X-ray 2.80 A/D 145-210 [» ]
1N86 X-ray 3.20 A/D 130-216 [» ]
1N8E X-ray 4.50 A/D 130-218 [» ]
1RE3 X-ray 2.45 A/D 145-210 [» ]
1RE4 X-ray 2.70 A/D 145-210 [» ]
1RF0 X-ray 2.81 A/D 145-210 [» ]
1RF1 X-ray 2.53 A/D 145-210 [» ]
1YCP X-ray 2.50 F/N 20-42 [» ]
2A45 X-ray 3.65 G/J 36-92 [» ]
2FFD X-ray 2.89 A/D 145-210 [» ]
2H43 X-ray 2.70 A/D 130-216 [» ]
2HLO X-ray 2.60 A/D 130-216 [» ]
2HOD X-ray 2.90 A/D/G/J 130-216 [» ]
2HPC X-ray 2.90 A/D/G/J 130-216 [» ]
2OYH X-ray 2.40 A/D 145-210 [» ]
2OYI X-ray 2.70 A/D 145-210 [» ]
2Q9I X-ray 2.80 A/D 130-216 [» ]
2XNX X-ray 3.30 A/D/G/J 130-216 [» ]
2XNY X-ray 7.50 A/D 130-216 [» ]
2Z4E X-ray 2.70 A/D 130-216 [» ]
3AT0 X-ray 2.50 B 332-347 [» ]
3BVH X-ray 2.60 A/D 148-209 [» ]
3E1I X-ray 2.30 A/D 130-216 [» ]
3GHG X-ray 2.90 A/D/G/J 20-581 [» ]
3H32 X-ray 3.60 A/D 20-216 [» ]
3HUS X-ray 3.04 A/D 145-210 [» ]
4F27 X-ray 1.92 Q 336-347 [» ]
ProteinModelPortali P02671.
SMRi P02671. Positions 46-231, 411-524, 596-866.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108534. 20 interactions.
DIPi DIP-29643N.
IntActi P02671. 12 interactions.
MINTi MINT-1033042.
STRINGi 9606.ENSP00000306361.

Chemistry

BindingDBi P02671.
ChEMBLi CHEMBL2364709.
DrugBanki DB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00364. Sucralfate.
DB00031. Tenecteplase.

PTM databases

PhosphoSitei P02671.

Polymorphism databases

DMDMi 1706799.

2D gel databases

OGPi P02671.
SWISS-2DPAGE P02671.

Proteomic databases

MaxQBi P02671.
PaxDbi P02671.
PeptideAtlasi P02671.
PRIDEi P02671.

Protocols and materials databases

DNASUi 2243.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000302053 ; ENSP00000306361 ; ENSG00000171560 . [P02671-1 ]
ENST00000403106 ; ENSP00000385981 ; ENSG00000171560 . [P02671-2 ]
GeneIDi 2243.
KEGGi hsa:2243.
UCSCi uc003iod.1. human. [P02671-1 ]
uc003ioe.1. human. [P02671-2 ]

Organism-specific databases

CTDi 2243.
GeneCardsi GC04M155504.
HGNCi HGNC:3661. FGA.
HPAi CAB016776.
HPA051370.
MIMi 105200. phenotype.
134820. gene+phenotype.
202400. phenotype.
neXtProti NX_P02671.
Orphaneti 98880. Familial afibrinogenemia.
98881. Familial dysfibrinogenemia.
248408. Familial hypodysfibrinogenemia.
101041. Familial hypofibrinogenemia.
93562. Familial renal amyloidosis due to fibrinogen A alpha-chain variant.
PharmGKBi PA429.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG114889.
HOGENOMi HOG000285947.
HOVERGENi HBG005668.
InParanoidi P02671.
KOi K03903.
OMAi YKCPSGC.
OrthoDBi EOG7X9G60.
PhylomeDBi P02671.
TreeFami TF351984.

Enzyme and pathway databases

Reactomei REACT_13552. Integrin cell surface interactions.
REACT_1439. Common Pathway.
REACT_15381. p130Cas linkage to MAPK signaling for integrins.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_75925. Amyloids.

Miscellaneous databases

ChiTaRSi FGA. human.
EvolutionaryTracei P02671.
GeneWikii Fibrinogen_alpha_chain.
GenomeRNAii 2243.
NextBioi 35464018.
PMAP-CutDB P02671.
PROi P02671.
SOURCEi Search...

Gene expression databases

ArrayExpressi P02671.
Bgeei P02671.
CleanExi HS_FGA.
Genevestigatori P02671.

Family and domain databases

Gene3Di 3.90.215.10. 1 hit.
4.10.530.10. 1 hit.
InterProi IPR014716. Fibrinogen_a/b/g_C_1.
IPR014715. Fibrinogen_a/b/g_C_2.
IPR002181. Fibrinogen_a/b/g_C_dom.
IPR012290. Fibrinogen_a/b/g_coil_dom.
IPR021996. Fibrinogen_aC.
IPR020837. Fibrinogen_CS.
[Graphical view ]
Pfami PF08702. Fib_alpha. 1 hit.
PF12160. Fibrinogen_aC. 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. "Carboxy-terminal-extended variant of the human fibrinogen alpha subunit: a novel exon conferring marked homology to beta and gamma subunits."
    Fu Y., Weissbach L., Plant P.W., Oddoux C., Cao Y., Liang T.J., Roy S.N., Redman C.M., Grieninger G.
    Biochemistry 31:11968-11972(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
  2. "Fibrinogen DNA and protein sequences."
    Chung D.W., Grieninger G.
    (In) Ebert R.F. (eds.); Index of variant human fibrinogens, pp.13-24, CRC Press, Boca Raton (1994)
    Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
  3. SeattleSNPs variation discovery resource
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-6; ALA-331 AND ALA-456.
  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 2), VARIANT ALA-331.
    Tissue: Heart.
  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] (ISOFORM 2).
  7. "Nucleotide sequences of the three genes coding for human fibrinogen."
    Chung D.W., Harris J.E., Davie E.W.
    Adv. Exp. Med. Biol. 281:39-48(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-655 (ISOFORM 1).
    Tissue: Liver.
  8. "Partial mRNA sequences for human A alpha, B beta, and gamma fibrinogen chains: evolutionary and functional implications."
    Kant J.A., Lord S.T., Crabtree G.R.
    Proc. Natl. Acad. Sci. U.S.A. 80:3953-3957(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  9. "Characterization of a complementary deoxyribonucleic acid coding for the alpha chain of human fibrinogen."
    Rixon M.W., Chan W.-Y., Davie E.W., Chung D.W.
    Biochemistry 22:3237-3244(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-629.
  10. "Human fibrinogen: sequence, sulfur bridges, glycosylation and some structural variants."
    Henschen A., Lottspeich F., Southan C., Topfer-Petersen E.
    (In) Peeters H. (eds.); Protides of the biological fluids, Proc. 28th colloquium, pp.51-56, Pergamon Press, Oxford (1980)
    Cited for: PROTEIN SEQUENCE OF 20-629.
  11. "Amino acid sequence studies on the alpha chain of human fibrinogen. Overlapping sequences providing the complete sequence."
    Watt K.W.K., Cottrell B.A., Strong D.D., Doolittle R.F.
    Biochemistry 18:5410-5416(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 20-629, DISULFIDE BONDS.
  12. "Isolation and characterisation of cDNA clones for the A alpha- and gamma-chains of human fibrinogen."
    Imam A.M.A., Eaton M.A.W., Williamson R., Humphries S.
    Nucleic Acids Res. 11:7427-7434(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 110-156.
  13. Cited for: NUCLEOTIDE SEQUENCE OF 605-644 (ISOFORM 2).
  14. "Studies on fibrinopeptides from primates."
    Blombaeck B., Blombaeck M., Grondahl N.J., Guthrie C., Hinton M.
    Acta Chem. Scand. 19:1788-1789(1965)
    Cited for: PROTEIN SEQUENCE OF 20-35.
  15. "Amino acid sequence studies on the alpha chain of human fibrinogen. Exact location of cross-linking acceptor sites."
    Cottrell B.A., Strong D.D., Watt K.W.K., Doolittle R.F.
    Biochemistry 18:5405-5410(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING ACCEPTOR SITES.
  16. "Localization of the alpha-chain cross-link acceptor sites of human fibrin."
    Fretto L.J., Ferguson E.W., Steinman H.M., McKee P.A.
    J. Biol. Chem. 253:2184-2195(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING ACCEPTOR SITES.
  17. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-686.
    Tissue: Plasma.
  18. "Disulfide bridges in NH2-terminal part of human fibrinogen."
    Blombaeck B., Hessel B., Hogg D.
    Thromb. Res. 8:639-658(1976) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  19. "Fibrinogen and fibrin."
    Doolittle R.F.
    Annu. Rev. Biochem. 53:195-229(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, ELECTRON MICROSCOPY, POLYMERIZATION, LIGANDS.
  20. "Cross-linking site in fibrinogen for alpha 2-plasmin inhibitor."
    Kimura S., Aoki N.
    J. Biol. Chem. 261:15591-15595(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING SITE FOR ALPHA-2-PLASMIN INHIBITOR.
  21. Cited for: PHOSPHORYLATION.
  22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-412 AND SER-609, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  24. Cited for: HYDROXYLATION AT PRO-565.
  25. "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-686.
    Tissue: Liver.
  26. "A unique proteolytic fragment of human fibrinogen containing the A alpha COOH-terminal domain of the native molecule."
    Kirschbaum N.E., Budzynski A.Z.
    J. Biol. Chem. 265:13669-13676(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY HEMENTIN AND PLASMIN.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Glycoproteomic analysis of human fibrinogen reveals novel regions of O-glycosylation."
    Zauner G., Hoffmann M., Rapp E., Koeleman C.A., Dragan I., Deelder A.M., Wuhrer M., Hensbergen P.J.
    J. Proteome Res. 11:5804-5814(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-320 AND SER-351.
  29. "The structure of residues 7-16 of the A alpha-chain of human fibrinogen bound to bovine thrombin at 2.3-A resolution."
    Martin P.D., Robertson W., Turk D., Huber R., Bode W., Edwards B.F.P.
    J. Biol. Chem. 267:7911-7920(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-39.
  30. "Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin."
    Spraggon G., Everse S.J., Doolittle R.F.
    Nature 389:455-462(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 130-216.
  31. "Crystal structure of fragment double-D from human fibrin with two different bound ligands."
    Everse S.J., Spraggon G., Veerapandian L., Riley M., Doolittle R.F.
    Biochemistry 37:8637-8642(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 130-216.
  32. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 670-866.
  33. "Conformational changes in fragments D and double-D from human fibrin(ogen) upon binding the peptide ligand Gly-His-Arg-Pro-amide."
    Everse S.J., Spraggon G., Veerapandian L., Doolittle R.F.
    Biochemistry 38:2941-2946(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 130-216.
  34. "Fibrinogen Kyoto II, a new congenitally abnormal molecule, characterized by the replacement of A alpha proline-18 by leucine."
    Yoshida N., Okuma M., Hirata H., Matsuda M., Yamazumi K., Asakura S.
    Blood 78:149-153(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT KYOTO-2 LEU-37.
  35. "Fibrinogen Lima: a homozygous dysfibrinogen with an A alpha-arginine-141 to serine substitution associated with extra N-glycosylation at A alpha-asparagine-139. Impaired fibrin gel formation but normal fibrin-facilitated plasminogen activation catalyzed by tissue-type plasminogen activator."
    Maekawa H., Yamazumi K., Muramatsu S., Kaneko M., Hirata H., Takahashi N., Arocha-Pinango C.L., Rodriguez S., Nagy H., Perez-Requejo J.L., Matsuda M.
    J. Clin. Invest. 90:67-76(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LIMA SER-160.
  36. "An A alpha Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation."
    Maekawa H., Yamazumi K., Muramatsu S., Kaneko M., Hirata H., Takahashi N., de Bosch N.B., Carvajal Z., Ojeda A., Arocha-Pinango C.L., Matsuda M.
    J. Biol. Chem. 266:11575-11581(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CARACAS-2 ASN-453.
  37. "Molecular basis for fibrinogen Dusart (A alpha 554 Arg-->Cys) and its association with abnormal fibrin polymerization and thrombophilia."
    Koopman J., Haverkate F., Grimbergen J., Lord S.T., Mosesson M.W., Diorio J.P., Siebenlist K.S., Legrand C., Soria J., Soria C., Caen J.P.
    J. Clin. Invest. 91:1637-1643(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DUSART/PARIS-5 CYS-573.
  38. "Hereditary renal amyloidosis associated with a mutant fibrinogen alpha-chain."
    Benson M.D., Liepnieks J., Uemichi T., Wheeler G., Correa R.
    Nat. Genet. 3:252-255(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT AMYL8 LEU-573.
  39. "Fibrinogen Osaka IV: a congenital dysfibrinogenemia found in a patient originally reported in relation to surgery, now defined to have an A alpha arginine-16 to histidine substitution."
    Yamazumi K., Terukina S., Matsuda M., Kanbayashi J., Sakon M., Tsujinaka T.
    Surg. Today 23:45-50(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT OSAKA IV HIS-35.
  40. "Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A-alpha 20 Val-to-Asp)."
    Brennan S.O., Hammonds B., George P.M.
    J. Clin. Invest. 96:2854-2858(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CANTERBURY ASP-39.
  41. Cited for: VARIANTS ALA-331 AND GLU-446.

Entry informationi

Entry nameiFIBA_HUMAN
AccessioniPrimary (citable) accession number: P02671
Secondary accession number(s): A8K3E4
, D3DP14, D3DP15, Q4QQH7, Q9BX62, Q9UCH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 189 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 4
    Human chromosome 4: 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

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