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Protein

Coagulation factor IX

Gene

F9

Organism
Mus musculus (Mouse)
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 bindingi47 – 471Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi48 – 481Calcium 2By similarity
Metal bindingi53 – 531Calcium 1; via 4-carboxyglutamateBy similarity
Metal bindingi53 – 531Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi54 – 541Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi54 – 541Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi61 – 611Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity
Metal bindingi63 – 631Calcium 1; via 4-carboxyglutamateBy similarity
Metal bindingi63 – 631Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi63 – 631Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi66 – 661Calcium 4 or magnesium 1; via 4-carboxyglutamateBy similarity
Metal bindingi67 – 671Calcium 1; via 4-carboxyglutamateBy similarity
Metal bindingi72 – 721Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity
Metal bindingi73 – 731Calcium 2; via 4-carboxyglutamateBy similarity
Metal bindingi73 – 731Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi76 – 761Calcium 3; via 4-carboxyglutamateBy similarity
Metal bindingi76 – 761Calcium 5 or magnesium 2; via 4-carboxyglutamateBy similarity
Metal bindingi82 – 821Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity
Metal bindingi86 – 861Calcium 6 or magnesium 3; via 4-carboxyglutamateBy similarity
Metal bindingi93 – 931Calcium 7By similarity
Metal bindingi94 – 941Calcium 7; via carbonyl oxygenBy similarity
Metal bindingi96 – 961Calcium 7By similarity
Metal bindingi110 – 1101Calcium 7By similarity
Metal bindingi111 – 1111Calcium 7; via carbonyl oxygenBy similarity
Sitei192 – 1932Cleavage; by factor XIaBy similarity
Sitei236 – 2372Cleavage; by factor XIaBy similarity
Active sitei277 – 2771Charge relay systemBy similarity
Metal bindingi291 – 2911Calcium 8By similarity
Metal bindingi293 – 2931Calcium 8; via carbonyl oxygenBy similarity
Metal bindingi298 – 2981Calcium 8By similarity
Metal bindingi301 – 3011Calcium 8By similarity
Active sitei325 – 3251Charge relay systemBy similarity
Active sitei421 – 4211Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

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

ReactomeiREACT_281620. Gamma-carboxylation of protein precursors.
REACT_325479. Extrinsic Pathway of Fibrin Clot Formation.
REACT_340184. Intrinsic Pathway of Fibrin Clot Formation.
REACT_351509. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_352087. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:88384. 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 – 2828Sequence AnalysisAdd
BLAST
Propeptidei29 – 4618By similarityPRO_0000027760Add
BLAST
Chaini47 – 471425Coagulation factor IXPRO_0000027761Add
BLAST
Chaini47 – 192146Coagulation factor IXa light chainPRO_0000027762Add
BLAST
Propeptidei193 – 23644Activation peptideBy similarityPRO_0000027763Add
BLAST
Chaini237 – 471235Coagulation factor IXa heavy chainPRO_0000027764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 5314-carboxyglutamatePROSITE-ProRule annotation
Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotation
Modified residuei61 – 6114-carboxyglutamatePROSITE-ProRule annotation
Modified residuei63 – 6314-carboxyglutamatePROSITE-ProRule annotation
Disulfide bondi64 ↔ 69By similarity
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation
Modified residuei67 – 6714-carboxyglutamatePROSITE-ProRule annotation
Modified residuei72 – 7214-carboxyglutamatePROSITE-ProRule annotation
Modified residuei73 – 7314-carboxyglutamatePROSITE-ProRule annotation
Modified residuei76 – 7614-carboxyglutamatePROSITE-ProRule annotation
Modified residuei79 – 7914-carboxyglutamatePROSITE-ProRule annotation
Modified residuei82 – 8214-carboxyglutamatePROSITE-ProRule annotation
Glycosylationi85 – 851O-linked (GalNAc...)By similarity
Modified residuei86 – 8614-carboxyglutamatePROSITE-ProRule annotation
Disulfide bondi97 ↔ 108By similarity
Glycosylationi99 – 991O-linked (Glc...); alternateBy similarity
Glycosylationi99 – 991O-linked (Xyl...); alternateBy similarity
Disulfide bondi102 ↔ 117By similarity
Modified residuei110 – 1101(3R)-3-hydroxyaspartateBy similarity
Modified residuei114 – 1141PhosphoserineBy similarity
Disulfide bondi119 ↔ 128By similarity
Disulfide bondi134 ↔ 145By similarity
Disulfide bondi141 ↔ 155By similarity
Disulfide bondi157 ↔ 170By similarity
Disulfide bondi178 ↔ 345Interchain (between light and heavy chains)By similarity
Modified residuei202 – 2021SulfotyrosineBy similarity
Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence Analysis
Modified residuei205 – 2051PhosphoserineBy similarity
Modified residuei206 – 2061PhosphothreonineBy similarity
Glycosylationi206 – 2061O-linked (GalNAc...)By similarity
Glycosylationi223 – 2231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi225 – 2251O-linked (GalNAc...)By similarity
Glycosylationi235 – 2351O-linked (GalNAc...)By similarity
Disulfide bondi262 ↔ 278By similarity
Disulfide bondi392 ↔ 406By similarity
Disulfide bondi417 ↔ 445By 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-99 by POGLUT1 in vitro.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

MaxQBiP16294.
PaxDbiP16294.
PRIDEiP16294.

PTM databases

PhosphoSiteiP16294.

Expressioni

Tissue specificityi

Detected in liver.1 Publication

Gene expression databases

BgeeiP16294.
CleanExiMM_F9.
ExpressionAtlasiP16294. baseline and differential.
GenevisibleiP16294. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033477.

Structurei

3D structure databases

ProteinModelPortaliP16294.
SMRiP16294. Positions 47-192, 237-470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 9246GlaPROSITE-ProRule annotationAdd
BLAST
Domaini93 – 12937EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini130 – 17142EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini237 – 469233Peptidase 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, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP16294.
KOiK01321.
OMAiMKGKYGI.
OrthoDBiEOG75B84T.
PhylomeDBiP16294.
TreeFamiTF327329.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[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. 1 hit.
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.

P16294-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKHLNTVMAE SPALITIFLL GYLLSTECAV FLDRENATKI LTRPKRYNSG
60 70 80 90 100
KLEEFVRGNL ERECIEERCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN
110 120 130 140 150
PCLNGGICKD DISSYECWCQ VGFEGRNCEL DATCNIKNGR CKQFCKNSPD
160 170 180 190 200
NKVICSCTEG YQLAEDQKSC EPTVPFPCGR ASISYSSKKI TRAETVFSNM
210 220 230 240 250
DYENSTEAVF IQDDITDGAI LNNVTESSES LNDFTRVVGG ENAKPGQIPW
260 270 280 290 300
QVILNGEIEA FCGGAIINEK WIVTAAHCLK PGDKIEVVAG EYNIDKKEDT
310 320 330 340 350
EQRRNVIRTI PHHQYNATIN KYSHDIALLE LDKPLILNSY VTPICVANRE
360 370 380 390 400
YTNIFLKFGS GYVSGWGKVF NKGRQASILQ YLRVPLVDRA TCLRSTTFTI
410 420 430 440 450
YNNMFCAGYR EGGKDSCEGD SGGPHVTEVE GTSFLTGIIS WGEECAMKGK
460 470
YGIYTKVSRY VNWIKEKTKL T
Length:471
Mass (Da):52,978
Last modified:January 9, 2007 - v3
Checksum:i05E08E86622397E2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti375 – 3751Q → H in AAA37629 (PubMed:2323576).Curated
Sequence conflicti400 – 4001I → T in AAA37629 (PubMed:2323576).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK149372 mRNA. Translation: BAE28840.1.
M23109 mRNA. Translation: AAA37629.1.
M26236 mRNA. Translation: AAA37630.1.
CCDSiCCDS30158.1.
PIRiJQ0419.
RefSeqiNP_001292726.1. NM_001305797.1.
NP_032005.1. NM_007979.2.
UniGeneiMm.391283.

Genome annotation databases

EnsembliENSMUST00000033477; ENSMUSP00000033477; ENSMUSG00000031138.
GeneIDi14071.
KEGGimmu:14071.
UCSCiuc009thw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK149372 mRNA. Translation: BAE28840.1.
M23109 mRNA. Translation: AAA37629.1.
M26236 mRNA. Translation: AAA37630.1.
CCDSiCCDS30158.1.
PIRiJQ0419.
RefSeqiNP_001292726.1. NM_001305797.1.
NP_032005.1. NM_007979.2.
UniGeneiMm.391283.

3D structure databases

ProteinModelPortaliP16294.
SMRiP16294. Positions 47-192, 237-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033477.

Protein family/group databases

MEROPSiS01.214.

PTM databases

PhosphoSiteiP16294.

Proteomic databases

MaxQBiP16294.
PaxDbiP16294.
PRIDEiP16294.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033477; ENSMUSP00000033477; ENSMUSG00000031138.
GeneIDi14071.
KEGGimmu:14071.
UCSCiuc009thw.2. mouse.

Organism-specific databases

CTDi2158.
MGIiMGI:88384. F9.

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP16294.
KOiK01321.
OMAiMKGKYGI.
OrthoDBiEOG75B84T.
PhylomeDBiP16294.
TreeFamiTF327329.

Enzyme and pathway databases

ReactomeiREACT_281620. Gamma-carboxylation of protein precursors.
REACT_325479. Extrinsic Pathway of Fibrin Clot Formation.
REACT_340184. Intrinsic Pathway of Fibrin Clot Formation.
REACT_351509. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_352087. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Miscellaneous databases

NextBioi285068.
PROiP16294.
SOURCEiSearch...

Gene expression databases

BgeeiP16294.
CleanExiMM_F9.
ExpressionAtlasiP16294. baseline and differential.
GenevisibleiP16294. MM.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[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. 1 hit.
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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "Deduced amino acid sequence of mouse blood-coagulation factor IX."
    Wu S.-M., Stafford D.W., Ware J.
    Gene 86:275-278(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-471, TISSUE SPECIFICITY.
  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 180-463.

Entry informationi

Entry nameiFA9_MOUSE
AccessioniPrimary (citable) accession number: P16294
Secondary accession number(s): Q3UES1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 9, 2007
Last modified: July 22, 2015
This is version 173 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.