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P09760

- FER_RAT

UniProt

P09760 - FER_RAT

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Protein

Tyrosine-protein kinase Fer

Gene

Fer

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

Functioni

Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this clearly depends on cell type and stimulus (By similarity). Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission.By similarity1 Publication

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei592 – 5921ATPPROSITE-ProRule annotation
Active sitei685 – 6851Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi570 – 5789ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. actin binding Source: RGD
  2. ATP binding Source: UniProtKB-KW
  3. cadherin binding Source: RGD
  4. cell adhesion molecule binding Source: RGD
  5. cytoskeletal protein binding Source: RGD
  6. epidermal growth factor receptor binding Source: UniProtKB
  7. gamma-catenin binding Source: RGD
  8. lipid binding Source: UniProtKB
  9. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
  10. protein kinase binding Source: RGD
  11. Rab GTPase binding Source: RGD

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. cell-cell adhesion mediated by cadherin Source: UniProtKB
  3. cell proliferation Source: Ensembl
  4. cellular response to insulin stimulus Source: UniProtKB
  5. cellular response to macrophage colony-stimulating factor stimulus Source: Ensembl
  6. cellular response to reactive oxygen species Source: UniProtKB
  7. chemotaxis Source: Ensembl
  8. cytokine-mediated signaling pathway Source: UniProtKB
  9. diapedesis Source: UniProtKB
  10. extracellular matrix-cell signaling Source: UniProtKB
  11. Fc-epsilon receptor signaling pathway Source: UniProtKB
  12. insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: UniProtKB
  13. interleukin-6-mediated signaling pathway Source: Ensembl
  14. Kit signaling pathway Source: UniProtKB
  15. microtubule cytoskeleton organization Source: UniProtKB
  16. mitotic cell cycle Source: Ensembl
  17. negative regulation of mast cell activation involved in immune response Source: UniProtKB
  18. peptidyl-tyrosine phosphorylation Source: UniProtKB
  19. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  20. positive regulation of actin filament polymerization Source: UniProtKB
  21. positive regulation of cell migration Source: UniProtKB
  22. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
  23. protein autophosphorylation Source: Ensembl
  24. regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  25. regulation of fibroblast migration Source: Ensembl
  26. regulation of lamellipodium assembly Source: UniProtKB
  27. regulation of protein phosphorylation Source: UniProtKB
  28. response to lipopolysaccharide Source: UniProtKB
  29. response to platelet-derived growth factor Source: UniProtKB
  30. substrate adhesion-dependent cell spreading Source: UniProtKB
  31. tyrosine phosphorylation of Stat3 protein Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Ligandi

ATP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_195025. Signaling by SCF-KIT.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase Fer (EC:2.7.10.2)
Alternative name(s):
Proto-oncogene c-Fer
Tyrosine-protein kinase FLK
p94-Fer
Gene namesi
Name:Fer
Synonyms:Fert2, Flk
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 9

Organism-specific databases

RGDi1306273. Fer.

Subcellular locationi

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projection By similarity. Cell junction By similarity. Membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Nucleus By similarity. Cytoplasmcell cortex By similarity
Note: Associated with the chromatin. Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts (By similarity).By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. cell junction Source: UniProtKB-KW
  3. cytoplasm Source: UniProtKB
  4. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  5. lamellipodium Source: Ensembl
  6. microtubule cytoskeleton Source: Ensembl
  7. nuclear chromatin Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 823823Tyrosine-protein kinase FerPRO_0000088093Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei402 – 4021PhosphotyrosineBy similarity
Modified residuei434 – 4341PhosphoserineBy similarity
Modified residuei616 – 6161Phosphotyrosine; by autocatalysisBy similarity
Modified residuei715 – 7151Phosphotyrosine; by autocatalysisBy similarity

Post-translational modificationi

Autophosphorylated.By similarity
Polyubiquitinated; this leads to proteasomal degradation.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP09760.
PRIDEiP09760.

PTM databases

PhosphoSiteiP09760.

Expressioni

Gene expression databases

ExpressionAtlasiP09760. baseline.
GenevestigatoriP09760.

Interactioni

Subunit structurei

Homotrimer. Interacts with IRS1, JAK1, NRP1, PIK3R1, PLEC and TMF1. Interacts with PPP1CA and regulates its phosphorylation at 'Thr-320'. Interacts with CTNND1, EGFR, FLT3, PECAM1, PDGFR and STAT3. Interacts (via SH2 domain) with CTTN. Interacts with HSP90; this stabilizes phosphorylated FER and protects FER against proteasomal degradation. Component of a complex that contains at least FER, CTTN and PTK2/FAK1 (By similarity). Interacts with ARHGDIA.By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021758.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5858FCHPROSITE-ProRule annotationAdd
BLAST
Domaini461 – 55191SH2PROSITE-ProRule annotationAdd
BLAST
Domaini564 – 815252Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 300300Important for interaction with membranes containing phosphoinositidesBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili123 – 18563Sequence AnalysisAdd
BLAST
Coiled coili301 – 38282Sequence AnalysisAdd
BLAST

Domaini

The coiled coil domains mediate homooligomerization and are required for location at microtubules.By similarity
The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes.By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily.PROSITE-ProRule annotation
Contains 1 FCH domain.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH2 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000233858.
HOVERGENiHBG001540.
InParanoidiP09760.
KOiK08889.
OMAiFVDNLYR.
OrthoDBiEOG708VXW.
TreeFamiTF315363.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR001060. FCH_dom.
IPR028539. Fer.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR016250. Tyr-prot_kinase_Fes/Fps.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERiPTHR24418:SF227. PTHR24418:SF227. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
PIRSFiPIRSF000632. TyrPK_fps. 1 hit.
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00055. FCH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50133. FCH. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P09760-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC
60 70 80 90 100
NQVDKDSTVQ VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL
110 120 130 140 150
TMMIKDKQQV KKSYVGIHQQ IEAEMIKVTK TELEKLKSSY RQLIKEMNSA
160 170 180 190 200
KEKYKEALAK GKETEKAKER CDKATMKLHM LHNQYVLALK GAQLHQSQYY
210 220 230 240 250
DTTLPLLLDS VQKMQEEMIK ALKGIFDEYS EITSLVTEEI VNVHKEIQMS
260 270 280 290 300
VDQIDPSTEY NDFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL
310 320 330 340 350
TADSLQVMLK TLAEELTQTQ QMLLHKEAAV LELEKRIEES SETCAKKSDI
360 370 380 390 400
VLLLGQKQAL EELKQSVQQL RCTEAKCAAQ KELLEQKVQE NDGKEPPPVV
410 420 430 440 450
NYEEDARSVT SMERKERLSK FESIRHSIAG IIKSPKSVLG SSTQLSDVIS
460 470 480 490 500
VGEKPLAEHD WYHGAIPRIE AQELLKQQGD FLVRESHGKP GEYVLSVYSD
510 520 530 540 550
GQRRHFIIQF VDNLYRFEGT GFSNIPQLID HHFNTKQVIT KKSGVVLLNP
560 570 580 590 600
IPKDKKWVLN HEDVSLGELL GKGNFGEVYK GTLKDKTPVA VKTCKEDLPQ
610 620 630 640 650
ELKIKFLQEA KILKQYDHPN IVKLIGVCTQ RQPVYIIMEL VPGGDFLSFL
660 670 680 690 700
RKRKDELKLK QLVRFSLDVA AGMLYLEGKN CIHRDLAARN CLVGENNTLK
710 720 730 740 750
ISDFGMSRQE DGGVYSSSGL KQIPIKWTAP EALNYGRYSS ESDVWSFGIL
760 770 780 790 800
LWETFSLGVC PYPGMTNQQA REQVERGYRM SAPQNCPEEI FTIMMKCWDY
810 820
KPENRPKFSD LHKELTAIKK KIT
Length:823
Mass (Da):94,314
Last modified:September 21, 2011 - v2
Checksum:iCA4F31E375F747DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti501 – 5011G → R in CAA31778. (PubMed:2485255)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13412 mRNA. Translation: CAA31778.1.
PIRiS04328.
RefSeqiXP_006245662.1. XM_006245600.2.
XP_008765589.1. XM_008767367.1.
XP_008765591.1. XM_008767369.1.
XP_008765592.1. XM_008767370.1.
UniGeneiRn.102629.

Genome annotation databases

EnsembliENSRNOT00000021758; ENSRNOP00000021758; ENSRNOG00000015898.
GeneIDi301737.
KEGGirno:301737.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13412 mRNA. Translation: CAA31778.1 .
PIRi S04328.
RefSeqi XP_006245662.1. XM_006245600.2.
XP_008765589.1. XM_008767367.1.
XP_008765591.1. XM_008767369.1.
XP_008765592.1. XM_008767370.1.
UniGenei Rn.102629.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000021758.

PTM databases

PhosphoSitei P09760.

Proteomic databases

PaxDbi P09760.
PRIDEi P09760.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000021758 ; ENSRNOP00000021758 ; ENSRNOG00000015898 .
GeneIDi 301737.
KEGGi rno:301737.

Organism-specific databases

CTDi 2241.
RGDi 1306273. Fer.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119011.
HOGENOMi HOG000233858.
HOVERGENi HBG001540.
InParanoidi P09760.
KOi K08889.
OMAi FVDNLYR.
OrthoDBi EOG708VXW.
TreeFami TF315363.

Enzyme and pathway databases

Reactomei REACT_195025. Signaling by SCF-KIT.

Miscellaneous databases

PROi P09760.

Gene expression databases

ExpressionAtlasi P09760. baseline.
Genevestigatori P09760.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR001060. FCH_dom.
IPR028539. Fer.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR016250. Tyr-prot_kinase_Fes/Fps.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view ]
PANTHERi PTHR24418:SF227. PTHR24418:SF227. 1 hit.
Pfami PF00611. FCH. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000632. TyrPK_fps. 1 hit.
PRINTSi PR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00055. FCH. 1 hit.
SM00252. SH2. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS50133. FCH. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "Novel protein-tyrosine kinase cDNAs related to fps/fes and eph cloned using anti-phosphotyrosine antibody."
    Letwin K., Yee S.P., Pawson T.
    Oncogene 3:621-627(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 501-823.
    Strain: Wistar.
    Tissue: Brain.
  3. "Synapses are regulated by the cytoplasmic tyrosine kinase Fer in a pathway mediated by p120catenin, Fer, SHP-2, and beta-catenin."
    Lee S.H., Peng I.F., Ng Y.G., Yanagisawa M., Bamji S.X., Elia L.P., Balsamo J., Lilien J., Anastasiadis P.Z., Ullian E.M., Reichardt L.F.
    J. Cell Biol. 183:893-908(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SYNAPSE ORGANIZATION AND SYNAPTIC TRANSMISSION.
  4. "The Fer tyrosine kinase regulates interactions of Rho GDP-Dissociation Inhibitor alpha with the small GTPase Rac."
    Fei F., Kweon S.M., Haataja L., De Sepulveda P., Groffen J., Heisterkamp N.
    BMC Biochem. 11:48-48(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGDIA.

Entry informationi

Entry nameiFER_RAT
AccessioniPrimary (citable) accession number: P09760
Secondary accession number(s): F1MA12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: September 21, 2011
Last modified: November 26, 2014
This is version 135 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3