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Protein

Coagulation factor IX

Gene

F9

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca2+ ions, phospholipids, and factor VIIIa.By similarity

Catalytic activityi

Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi41 – 411Calcium 2By similarity
Metal bindingi46 – 461Calcium 1; via 4-carboxyglutamateBy similarity
Metal bindingi46 – 461Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi47 – 471Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi47 – 471Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi54 – 541Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity
Metal bindingi56 – 561Calcium 1; via 4-carboxyglutamateBy similarity
Metal bindingi56 – 561Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi56 – 561Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi59 – 591Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity
Metal bindingi60 – 601Calcium 1; via 4-carboxyglutamateBy similarity
Metal bindingi65 – 651Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity
Metal bindingi66 – 661Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi66 – 661Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi69 – 691Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi69 – 691Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity
Metal bindingi69 – 691Calcium 5; via 4-carboxyglutamateBy similarity
Metal bindingi75 – 751Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity
Metal bindingi79 – 791Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity
Metal bindingi86 – 861Calcium 7By similarity
Metal bindingi87 – 871Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi89 – 891Calcium 7By similarity
Metal bindingi103 – 1031Calcium 7By similarity
Metal bindingi104 – 1041Calcium 7; via carbonyl oxygenBy similarity
Active sitei268 – 2681Charge relay systemBy similarity
Metal bindingi282 – 2821Calcium 8By similarity
Metal bindingi284 – 2841Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi287 – 2871Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi289 – 2891Calcium 8By similarity
Metal bindingi292 – 2921Calcium 8By similarity
Active sitei316 – 3161Charge relay systemBy similarity
Active sitei412 – 4121Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

  • blood coagulation Source: RGD
  • proteolysis Source: UniProtKB
  • zymogen activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-RNO-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-RNO-159740. Gamma-carboxylation of protein precursors.
R-RNO-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-RNO-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Protein family/group databases

MEROPSiS01.214.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor IX (EC:3.4.21.22By similarity)
Alternative name(s):
Christmas factor
Cleaved into the following 2 chains:
Gene namesi
Name:F9
Synonyms:Cf9
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi2589. F9.

Subcellular locationi

  • Secreted By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Propeptidei22 – 3918By similarityPRO_0000433111Add
BLAST
Chaini40 – 462423Coagulation factor IXPRO_0000088685Add
BLAST
Chaini40 – 185146Coagulation factor IXa light chainPRO_0000433112Add
BLAST
Propeptidei186 – 22742Activation peptideBy similarityPRO_0000433113Add
BLAST
Chaini228 – 462235Coagulation factor IXa heavy chainPRO_0000433114Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 4614-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei56 – 5614-carboxyglutamatePROSITE-ProRule annotationBy similarity
Disulfide bondi57 ↔ 62By similarity
Modified residuei59 – 5914-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei65 – 6514-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei69 – 6914-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotationBy similarity
Modified residuei75 – 7514-carboxyglutamatePROSITE-ProRule annotationBy similarity
Glycosylationi78 – 781O-linked (GalNAc...)By similarity
Modified residuei79 – 7914-carboxyglutamatePROSITE-ProRule annotationBy similarity
Disulfide bondi90 ↔ 101By similarity
Glycosylationi92 – 921O-linked (Glc...); alternateBy similarity
Glycosylationi92 – 921O-linked (Xyl...); alternateBy similarity
Disulfide bondi95 ↔ 110By similarity
Modified residuei103 – 1031(3R)-3-hydroxyaspartateBy similarity
Modified residuei107 – 1071PhosphoserineBy similarity
Disulfide bondi112 ↔ 121By similarity
Disulfide bondi127 ↔ 138By similarity
Disulfide bondi134 ↔ 148By similarity
Disulfide bondi150 ↔ 163By similarity
Disulfide bondi171 ↔ 336Interchain (between light and heavy chains)By similarity
Modified residuei195 – 1951SulfotyrosineBy similarity
Modified residuei198 – 1981PhosphoserineBy similarity
Modified residuei199 – 1991Phosphothreonine; alternateBy similarity
Glycosylationi199 – 1991O-linked (GalNAc...); alternateBy similarity
Glycosylationi208 – 2081N-linked (GlcNAc...)Sequence analysis
Glycosylationi214 – 2141N-linked (GlcNAc...)Sequence analysis
Glycosylationi216 – 2161O-linked (GalNAc...)By similarity
Glycosylationi226 – 2261O-linked (GalNAc...)By similarity
Disulfide bondi253 ↔ 269By similarity
Glycosylationi307 – 3071N-linked (GlcNAc...)Sequence analysis
Disulfide bondi383 ↔ 397By similarity
Disulfide bondi408 ↔ 436By similarity

Post-translational modificationi

Activated by factor XIa, which excises the activation peptide. The propeptide can also be removed by snake venom protease.By similarity
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.By similarity
Predominantly O-glucosylated at Ser-92 by POGLUT1 in vitro.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei185 – 1862Cleavage; by factor XIaBy similarity
Sitei227 – 2282Cleavage; by factor XIaBy similarity

Keywords - PTMi

Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

PaxDbiP16296.
PeptideAtlasiP16296.
PRIDEiP16296.

Interactioni

Subunit structurei

Heterodimer of a light chain and a heavy chain; disulfide-linked. Interacts with SERPINC1.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004559.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 8647GlaPROSITE-ProRule annotationAdd
BLAST
Domaini86 – 12237EGF-like; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini228 – 460233Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Domaini

Calcium binds to the gamma-carboxyglutamic acid (Gla) residues in the Gla domain. Calcium can also bind, with stronger affinity, to another site beyond the Gla domain. Under physiological ion concentrations, Ca2+ is displaced by Mg2+ from some of the gammaglutamate residues in the N-terminal Gla domain. This leads to a subtle conformation change that may affect the interaction with its binding protein.By similarity

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOVERGENiHBG013304.
InParanoidiP16296.
KOiK01321.
OMAiMKGKYGI.
OrthoDBiEOG75B84T.
TreeFamiTF327329.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P16296-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADAPGLIPI FLLGYLLSTE CAVFLDRENA TKILTRPKRY NSGKLEEFVQ
60 70 80 90 100
GNLERECIEE RCSFEEAREV FENTEKTTEF WKQYVDGDQC ESNPCLNGGI
110 120 130 140 150
CKDDINSYEC WCQAGFEGRN CELDATCSIK NGRCKQFCKN SPDNKIICSC
160 170 180 190 200
TEGYQLAEDQ KSCEPAVPFP CGRVSVAYNS KKITRAETVF SNTDYGNSTE
210 220 230 240 250
LILDDITNST ILDNLTENSE PINDFTRVVG GENAKPGQIP WQVILNGEIE
260 270 280 290 300
AFCGGAIINE KWIVTAAHCL KPGDKIEVVA GEHNIDEKED TEQRRNVIRT
310 320 330 340 350
IPHHQYNATI NKYSHDIALL ELDKPLILNS YVTPICVANK EYTNIFLKFG
360 370 380 390 400
SGYVSGWGKV FNKGRQASIL QYLRVPLVDR ATCLRSTKFS IYNNMFCAGY
410 420 430 440 450
REGGKDSCEG DSGGPHVTEV EGTSFLTGII SWGEECAMKG KYGIYTKVSR
460
YVNWIKEKTK LT
Length:462
Mass (Da):51,808
Last modified:May 27, 2015 - v2
Checksum:i6C50A44A8F0945EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06108743 Genomic DNA. No translation available.
AABR06108744 Genomic DNA. No translation available.
AABR06108745 Genomic DNA. No translation available.
AABR06108746 Genomic DNA. No translation available.
CH474019 Genomic DNA. Translation: EDL86171.1.
M26247 mRNA. Translation: AAA41162.1.
PIRiI84621.
RefSeqiNP_113728.1. NM_031540.1.
UniGeneiRn.37599.

Genome annotation databases

EnsembliENSRNOT00000004559; ENSRNOP00000004559; ENSRNOG00000003430.
GeneIDi24946.
KEGGirno:24946.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06108743 Genomic DNA. No translation available.
AABR06108744 Genomic DNA. No translation available.
AABR06108745 Genomic DNA. No translation available.
AABR06108746 Genomic DNA. No translation available.
CH474019 Genomic DNA. Translation: EDL86171.1.
M26247 mRNA. Translation: AAA41162.1.
PIRiI84621.
RefSeqiNP_113728.1. NM_031540.1.
UniGeneiRn.37599.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000004559.

Protein family/group databases

MEROPSiS01.214.

Proteomic databases

PaxDbiP16296.
PeptideAtlasiP16296.
PRIDEiP16296.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000004559; ENSRNOP00000004559; ENSRNOG00000003430.
GeneIDi24946.
KEGGirno:24946.

Organism-specific databases

CTDi2158.
RGDi2589. F9.

Phylogenomic databases

eggNOGiENOG410IGPV. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOVERGENiHBG013304.
InParanoidiP16296.
KOiK01321.
OMAiMKGKYGI.
OrthoDBiEOG75B84T.
TreeFamiTF327329.

Enzyme and pathway databases

ReactomeiR-RNO-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-RNO-140837. Intrinsic Pathway of Fibrin Clot Formation.
R-RNO-159740. Gamma-carboxylation of protein precursors.
R-RNO-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-RNO-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Miscellaneous databases

PROiP16296.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "Direct sequencing of the activation peptide and the catalytic domain of the factor IX gene in six species."
    Sarkar G., Koeberl D.D., Sommer S.S.
    Genomics 6:133-143(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 173-454.

Entry informationi

Entry nameiFA9_RAT
AccessioniPrimary (citable) accession number: P16296
Secondary accession number(s): F1M1M6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 27, 2015
Last modified: July 6, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.