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Q99P84

- PLCE1_RAT

UniProt

Q99P84 - PLCE1_RAT

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Protein

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1

Gene

Plce1

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

Functioni

The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. PLCE1 is a bifunctional enzyme which also regulates small GTPases of the Ras superfamily through its Ras guanine-exchange factor (RasGEF) activity. As an effector of heterotrimeric and small G-protein, it may play a role in cell survival, cell growth, actin organization and T-cell activation.3 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.1 Publication

Cofactori

Ca2+1 Publication

Enzyme regulationi

Activated by the heterotrimeric G-protein subunits GNA12, GNA13 and GNB1-GNG2. Activated by HRAS, RAP1A, RHOA, RHOB, RHOC, RRAS and RRAS2. Activated by the G(s)-coupled GPCRs ADRB2, PTGER1 and CHRM3 through cyclic-AMP formation and RAP2B activation. Inhibited by G(i)-coupled GPCRs.5 Publications

Kineticsi

  1. KM=6.0 µM for PtdIns(4,5)P21 Publication

Vmax=10 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1388 – 13881PROSITE-ProRule annotation
Active sitei1433 – 14331PROSITE-ProRule annotation

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. enzyme binding Source: UniProtKB
  3. guanyl-nucleotide exchange factor activity Source: UniProtKB-KW
  4. phosphatidylinositol phospholipase C activity Source: UniProtKB
  5. phospholipase C activity Source: UniProtKB
  6. Ras GTPase binding Source: RGD
  7. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. activation of MAPK activity Source: UniProtKB
  2. G-protein coupled receptor signaling pathway Source: RGD
  3. lipid catabolic process Source: UniProtKB-KW
  4. phospholipase C-activating G-protein coupled receptor signaling pathway Source: UniProtKB
  5. Ras protein signal transduction Source: RGD
  6. regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  7. regulation of protein kinase activity Source: UniProtKB
  8. regulation of Ras protein signal transduction Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor, Hydrolase, Transducer

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.4.11. 5301.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1 (EC:3.1.4.11)
Alternative name(s):
Phosphoinositide phospholipase C-epsilon-1
Phospholipase C-epsilon-1
Short name:
PLC-epsilon-1
Gene namesi
Name:Plce1
Synonyms:Plce
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi69424. Plce1.

Subcellular locationi

Cytoplasmcytosol By similarity. Cell membrane By similarity. Golgi apparatus membrane By similarity
Note: Recruited to plasma membrane by activated HRAS and RAP2. Recruited to perinuclear membrane by activated RAP1A. Associates with Golgi membranes (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: RGD
  2. cytosol Source: UniProtKB
  3. Golgi apparatus Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2150 – 21501K → A: Inhibits binding to HRAS by 59% and phospholipase stimulation by HRAS by 51%. Inhibits binding to HRAS by 97% and phospholipase stimulation by HRAS by 86%; when associated with A-2152. 1 Publication
Mutagenesisi2150 – 21501K → E: Inhibits binding to HRAS by 99% and phospholipase stimulation by HRAS by 94%. Inhibits binding to HRAS by 97% and phospholipase stimulation by HRAS by 94%; when associated with E-2152. 1 Publication
Mutagenesisi2152 – 21521K → A: Inhibits binding to HRAS by 19% and phospholipase stimulation by HRAS by 30%. Inhibits binding to HRAS by 97% and phospholipase stimulation by HRAS by 86%; when associated with A-2150. 1 Publication
Mutagenesisi2152 – 21521K → E: Inhibits binding to HRAS by 67% and phospholipase stimulation by HRAS by 47%. Inhibits binding to HRAS by 97% and phospholipase stimulation by HRAS by 94%; when associated with E-2150. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 228122811-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1PRO_0000256240Add
BLAST

Proteomic databases

PaxDbiQ99P84.
PRIDEiQ99P84.

PTM databases

PhosphoSiteiQ99P84.

Expressioni

Tissue specificityi

Ubiquitously expressed. Detected in glomerular podocytes (at protein level).2 Publications

Gene expression databases

GenevestigatoriQ99P84.

Interactioni

Subunit structurei

Interacts with GTP-bound HRAS, RAP1A and probably with RAP2A, RAP2B and RRAS. Interacts with RHOA. Interacts with IQGAP1 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ99P84. 1 interaction.
STRINGi10116.ENSRNOP00000019771.

Structurei

3D structure databases

ProteinModelPortaliQ99P84.
SMRiQ99P84. Positions 1985-2093, 2110-2225.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini528 – 781254Ras-GEFPROSITE-ProRule annotationAdd
BLAST
Domaini1373 – 1521149PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST
Domaini1709 – 1825117PI-PLC Y-boxPROSITE-ProRule annotationAdd
BLAST
Domaini1835 – 1935101C2PROSITE-ProRule annotationAdd
BLAST
Domaini1991 – 2093103Ras-associating 1PROSITE-ProRule annotationAdd
BLAST
Domaini2114 – 2217104Ras-associating 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1667 – 174377Required for activation by RHOA, RHOB, GNA12, GNA13 and G-beta gammaAdd
BLAST

Domaini

The Ras-associating domain 1 is degenerated and may not bind HRAS (By similarity). The Ras-associating domain 2 mediates interaction with GTP-bound HRAS, RAP1A and probably RAP2A and RAP2B and recruitment of HRAS to the cell membrane.By similarity
The Ras-GEF domain has a GEF activity towards HRAS and RAP1A. Mediates activation of the mitogen-activated protein kinase pathway (By similarity).By similarity

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation
Contains 1 PI-PLC Y-box domain.PROSITE-ProRule annotation
Contains 2 Ras-associating domains.PROSITE-ProRule annotation
Contains 1 Ras-GEF domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG149692.
HOGENOMiHOG000090225.
HOVERGENiHBG059220.
InParanoidiQ99P84.
KOiK05860.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.840.10. 2 hits.
2.60.40.150. 1 hit.
3.20.20.190. 3 hits.
InterProiIPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
IPR028398. PLC-epsilon1.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
IPR000159. Ras-assoc.
IPR023578. Ras_GEF_dom.
IPR001895. RASGEF_cat_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view]
PANTHERiPTHR10336. PTHR10336. 1 hit.
PTHR10336:SF6. PTHR10336:SF6. 1 hit.
PfamiPF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF00788. RA. 1 hit.
PF00617. RasGEF. 1 hit.
[Graphical view]
PRINTSiPR00390. PHPHLIPASEC.
SMARTiSM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00314. RA. 1 hit.
SM00147. RasGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48366. SSF48366. 2 hits.
SSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 3 hits.
SSF54236. SSF54236. 2 hits.
PROSITEiPS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99P84-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTSEEMAASF LIPVPQRKVA SAQSVAEERG EKVSEAGIPK TRAGRQGGLT
60 70 80 90 100
PRTISQRNEP EEESPRTDFS QVFSIARGEL DSDENHNERC WEENVPGSTK
110 120 130 140 150
NHAVNCNSLL QSHQHALPPS QLCEVCDSVT EEHLCLQPGI PSPLERKVFP
160 170 180 190 200
GIELEMEDSP MDVSPLGNQP GIMESSGPHS DRNMAVFHFH YAGDRTMPGA
210 220 230 240 250
FHTLSEKFIL DDCANCVTLP GGQQNKNYMA YTCKLVELTR TCGSKNGQLK
260 270 280 290 300
CDHCTSLRDE YLCFESSCRK AEALSSGGGF CEDGFTHGPS AKTFLNPLEE
310 320 330 340 350
FSDNCEDVDD IFKGKKERST LLVRRFCKND REVKKSVYTG TRAIVRTLPS
360 370 380 390 400
GHIGLAAWSY VDQKKAGLMW PCGNGMRPLS TVDVRQSGRQ RLSEAQWCLI
410 420 430 440 450
YSAVRREETE DTVGSLLHCS TQLPTPDTAH GRIGDGPCLK QCVRDSECEY
460 470 480 490 500
RATLQRTSIA QYITGSLLEA TTSLGARSSL LSSFGGSTGR IMLKERQPGT
510 520 530 540 550
SMANSSPVPS SSAGISKELI DLQPLIQFPE EVASILTEQE QNIYRRVLPM
560 570 580 590 600
DYLCFLTRDL SSPECQRSLP RLKACISESI LMSQSGEHNA LEDLVMRFNE
610 620 630 640 650
VSSWVTWLIL TAGSMEEKRE VFSYLVHVAK CCWNMGNYNA VMEFLAGLRS
660 670 680 690 700
RKVLKMWQFM DQSDIETMRS LKDAMAQHES SVEYKKVVTR ALHIPGCKVV
710 720 730 740 750
PFCGVFLKEL CEVLDGASGL LKLCPRYSSQ EEALEFVADY SGQDNFLQRV
760 770 780 790 800
GQNGLKNPEK ELTVNSIFQI IRSCSRSLET EDEESASEGS GSRKNSLKDK
810 820 830 840 850
TRWQFIIGDL LDSDNDIFEK SKECDPHGSE ESQKAFDHGT ELIPWYVLSI
860 870 880 890 900
QADVHQFLLQ GATVIHYDQD THLSARCFLQ LQPDNSTLTW MKPPTASPAG
910 920 930 940 950
ARLKLGVLSN VAEPGKFPSL GNAGVSGLVE GILDLFSVKA VYMGHPGIDI
960 970 980 990 1000
HTVCVQNKLS SMLLSETGVT LLYGLQTTDN RLLHFVAPKH TAKMLFSGLL
1010 1020 1030 1040 1050
ELTTAVRKIR KFPDQRQQWL RKQYVSFYQE DGRYEGPTLA HAVELFGGRR
1060 1070 1080 1090 1100
WSTRNPSPGM SAKNAEKPNM QRNNTLGIST TKKKKKMLMR GESGEVTDDE
1110 1120 1130 1140 1150
MATRKAKMYR ECRSRSGSDP QEANEQEDSE ANVITNPPNP LHSRRAYSLT
1160 1170 1180 1190 1200
TAGSPNLATG MSSPISAWSS SSWHGRIKGG MKGFQSFMVS DSNMSFIEFV
1210 1220 1230 1240 1250
ELFKSFSIRS RKDLKDIFDI YSVPCNRSAS ESTPLYTNLT IEENTNDLQP
1260 1270 1280 1290 1300
DLDLLTRNVS DLGLFMKSKQ QLSDNQRQIS DAIAAASIVT NGTGIESTSL
1310 1320 1330 1340 1350
GIFGVGILQL NDFLVNCQGE HCTYDEILSI IQKFEPNISM CHQGLLSFEG
1360 1370 1380 1390 1400
FARFLMDKDN FASKNDESRE NKKDLQLPLS YYYIESSHNT YLTGHQLKGE
1410 1420 1430 1440 1450
SSVELYSQVL LQGCRSIELD CWDGDDGMPI IYHGHTLTTK IPFKEVVEAI
1460 1470 1480 1490 1500
DRSAFITSDL PIIISIENHC SLPQQRKMAE IFKSVFGEKL VAKFLFETDF
1510 1520 1530 1540 1550
SDDPMLPSPD QLRRKVLLKN KKLKAHQTPV DILKQKAHQL ASMQTQAFTG
1560 1570 1580 1590 1600
GNANPPPASN EEEEDEEDEY DYDYESLSDD NILEDRPENK SCADKLQFEY
1610 1620 1630 1640 1650
NEEVPKRIKK ADNSSGNKGK VYDMELGEEF YLPQNKKESR QIAPELSDLV
1660 1670 1680 1690 1700
IYCQAVKFPG LSTLNSSGSG RGKERKSRKS IFGNNPGRMS PGETASFNRT
1710 1720 1730 1740 1750
SGKSSCEGIR QIWEEPPLSP NTSLSAIIRT PKCYHISSLN ENAAKRLCRR
1760 1770 1780 1790 1800
YSQKLIQHTA CQLLRTYPAA TRIDSSNPNP LMFWLHGIQL VALNYQTDDL
1810 1820 1830 1840 1850
PLHLNAAMFE ANGGCGYVLK PPVLWDKSCP MYQKFSPLER DLDAMDPATY
1860 1870 1880 1890 1900
SLTIISGQNV CPSNSTGSPC IEVDVLGMPL DSCHFRTKPI HRNTLNPMWN
1910 1920 1930 1940 1950
EQFLFRVHFE DLVFLRFAVV ENNSSAITAQ RIIPLKALKR GYRHLQLRNL
1960 1970 1980 1990 2000
HNEILEISSL FINSRRMEDN PSGSTRPASL MFNTEERKCS QTHKVTVHGV
2010 2020 2030 2040 2050
PGPEPFAVFT INEGTKAKQL LQQILAVDQD TKLTAADYFL MEEKHFISKE
2060 2070 2080 2090 2100
KNECRKQPFQ RAVGPEEDIV QILNSWFPEE GYVGRIVLKP QQETLEEKNI
2110 2120 2130 2140 2150
VHDDREVILS SEEESFFVQV HDVSPEQPRT VIKAPRVSTA QDVIQQTLCK
2160 2170 2180 2190 2200
AKYSYSILNN PNPCDYVLLE EVMKDAPNKK SSTPKSSQRI LLDQECVFQA
2210 2220 2230 2240 2250
QSKWKGAGKF ILKLKEQVQA SREDKRRGIS FASELKKLTK STKQTRGLTS
2260 2270 2280
PPQLVASESV QSKEEKPMGA LASGDTAGYQ S
Length:2,281
Mass (Da):255,393
Last modified:June 1, 2001 - v1
Checksum:i7409A739B61F69EF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF323615 mRNA. Translation: AAK06775.1.
RefSeqiNP_446210.1. NM_053758.2.
UniGeneiRn.64650.

Genome annotation databases

GeneIDi114633.
KEGGirno:114633.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF323615 mRNA. Translation: AAK06775.1 .
RefSeqi NP_446210.1. NM_053758.2.
UniGenei Rn.64650.

3D structure databases

ProteinModelPortali Q99P84.
SMRi Q99P84. Positions 1985-2093, 2110-2225.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q99P84. 1 interaction.
STRINGi 10116.ENSRNOP00000019771.

PTM databases

PhosphoSitei Q99P84.

Proteomic databases

PaxDbi Q99P84.
PRIDEi Q99P84.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 114633.
KEGGi rno:114633.

Organism-specific databases

CTDi 51196.
RGDi 69424. Plce1.

Phylogenomic databases

eggNOGi NOG149692.
HOGENOMi HOG000090225.
HOVERGENi HBG059220.
InParanoidi Q99P84.
KOi K05860.

Enzyme and pathway databases

BRENDAi 3.1.4.11. 5301.

Miscellaneous databases

NextBioi 618799.
PROi Q99P84.

Gene expression databases

Genevestigatori Q99P84.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.10.840.10. 2 hits.
2.60.40.150. 1 hit.
3.20.20.190. 3 hits.
InterProi IPR000008. C2_dom.
IPR011992. EF-hand-dom_pair.
IPR001192. PI-PLC_fam.
IPR028398. PLC-epsilon1.
IPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR015359. PLipase_C_EF-hand-like.
IPR000909. PLipase_C_PInositol-sp_X_dom.
IPR001711. PLipase_C_Pinositol-sp_Y.
IPR000159. Ras-assoc.
IPR023578. Ras_GEF_dom.
IPR001895. RASGEF_cat_dom.
IPR029071. Ubiquitin-rel_dom.
[Graphical view ]
PANTHERi PTHR10336. PTHR10336. 1 hit.
PTHR10336:SF6. PTHR10336:SF6. 1 hit.
Pfami PF00168. C2. 1 hit.
PF09279. EF-hand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
PF00788. RA. 1 hit.
PF00617. RasGEF. 1 hit.
[Graphical view ]
PRINTSi PR00390. PHPHLIPASEC.
SMARTi SM00239. C2. 1 hit.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
SM00314. RA. 1 hit.
SM00147. RasGEF. 1 hit.
[Graphical view ]
SUPFAMi SSF48366. SSF48366. 2 hits.
SSF49562. SSF49562. 1 hit.
SSF51695. SSF51695. 3 hits.
SSF54236. SSF54236. 2 hits.
PROSITEi PS50004. C2. 1 hit.
PS50007. PIPLC_X_DOMAIN. 1 hit.
PS50008. PIPLC_Y_DOMAIN. 1 hit.
PS50200. RA. 1 hit.
PS50009. RASGEF_CAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Phospholipase C(epsilon): a novel Ras effector."
    Kelley G.G., Reks S.E., Ondrako J.M., Smrcka A.V.
    EMBO J. 20:743-754(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, CATALYTIC ACTIVITY, ENZYME REGULATION, COFACTOR, INTERACTION WITH HRAS AND RAP1A, MUTAGENESIS OF LYS-2150 AND LYS-2152.
    Tissue: Heart.
  2. "Activation of phospholipase C-epsilon by heterotrimeric G protein betagamma-subunits."
    Wing M.R., Houston D., Kelley G.G., Der C.J., Siderovski D.P., Harden T.K.
    J. Biol. Chem. 276:48257-48261(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  3. "Involvement of phosphatidylinositol 3-kinase, but not RalGDS, in TC21/R-Ras2-mediated transformation."
    Murphy G.A., Graham S.M., Morita S., Reks S.E., Rogers-Graham K., Vojtek A., Kelley G.G., Der C.J.
    J. Biol. Chem. 277:9966-9975(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  4. "Direct activation of phospholipase C-epsilon by Rho."
    Wing M.R., Snyder J.T., Sondek J., Harden T.K.
    J. Biol. Chem. 278:41253-41258(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH RHOA.
  5. Cited for: FUNCTION.
  6. "RhoA activates purified phospholipase C-epsilon by a guanine nucleotide-dependent mechanism."
    Seifert J.P., Wing M.R., Snyder J.T., Gershburg S., Sondek J., Harden T.K.
    J. Biol. Chem. 279:47992-47997(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  7. "G-protein-coupled receptor agonists activate endogenous phospholipase Cepsilon and phospholipase Cbeta3 in a temporally distinct manner."
    Kelley G.G., Kaproth-Joslin K.A., Reks S.E., Smrcka A.V., Wojcikiewicz R.J.H.
    J. Biol. Chem. 281:2639-2648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH IQGAP1.

Entry informationi

Entry nameiPLCE1_RAT
AccessioniPrimary (citable) accession number: Q99P84
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2001
Last modified: November 26, 2014
This is version 103 of the entry and version 1 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