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Q04631

- FNTA_RAT

UniProt

Q04631 - FNTA_RAT

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Protein

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

Gene

Fnta

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

Functioni

Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation.4 Publications

Catalytic activityi

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.

Enzyme regulationi

Activated by the AGRIN-induced phosphorylation which is mediated by MUSK.By similarity

GO - Molecular functioni

  1. CAAX-protein geranylgeranyltransferase activity Source: UniProtKB-EC
  2. protein farnesyltransferase activity Source: RGD
  3. protein geranylgeranyltransferase activity Source: UniProtKB

GO - Biological processi

  1. negative regulation of apoptotic process Source: RGD
  2. negative regulation of nitric-oxide synthase biosynthetic process Source: RGD
  3. positive regulation of cell cycle Source: RGD
  4. positive regulation of cell proliferation Source: RGD
  5. positive regulation of nitric-oxide synthase biosynthetic process Source: RGD
  6. protein farnesylation Source: UniProtKB
  7. protein geranylgeranylation Source: UniProtKB
  8. response to cytokine Source: RGD
  9. response to inorganic substance Source: RGD
  10. response to organic cyclic compound Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Enzyme and pathway databases

SABIO-RKQ04631.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (EC:2.5.1.58, EC:2.5.1.59)
Alternative name(s):
CAAX farnesyltransferase subunit alpha
FTase-alpha
Ras proteins prenyltransferase subunit alpha
Type I protein geranyl-geranyltransferase subunit alpha
Short name:
GGTase-I-alpha
Gene namesi
Name:Fnta
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2625. Fnta.

Subcellular locationi

GO - Cellular componenti

  1. CAAX-protein geranylgeranyltransferase complex Source: RGD
  2. cytoplasm Source: RGD
  3. protein farnesyltransferase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 377376Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaPRO_0000119748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Post-translational modificationi

Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN stimulation and results in the activation of FNTA By similarity.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ04631.
PRIDEiQ04631.

PTM databases

PhosphoSiteiQ04631.

Expressioni

Gene expression databases

GenevestigatoriQ04631.

Interactioni

Subunit structurei

Interacts with MUSK; the interaction is direct and mediates AGRIN-induced phosphorylation of FNTA By similarity. Heterodimer of FNTA and FNTB (farnesyltransferase). Heterodimer of FNTA and PGGT1B (geranylgeranyltransferase).By similarity16 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FntbQ0229314EBI-602447,EBI-602454
KRASP01116-22EBI-602447,EBI-367427From a different organism.
Pggt1bP536105EBI-602447,EBI-602610

Protein-protein interaction databases

DIPiDIP-6131N.
IntActiQ04631. 8 interactions.
MINTiMINT-121907.
STRINGi10116.ENSRNOP00000019594.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi58 – 603
Helixi66 – 683
Helixi70 – 723
Beta strandi73 – 753
Beta strandi87 – 904
Helixi94 – 10916
Helixi114 – 12613
Helixi131 – 14313
Helixi148 – 16114
Helixi166 – 17914
Turni182 – 1843
Helixi185 – 19511
Helixi200 – 21314
Helixi216 – 2183
Helixi219 – 22911
Turni230 – 2323
Helixi234 – 24613
Beta strandi250 – 2523
Helixi253 – 26917
Beta strandi270 – 2723
Helixi274 – 28411
Turni285 – 2873
Helixi289 – 2913
Helixi293 – 3008
Helixi303 – 3064
Helixi309 – 32416
Helixi330 – 34617
Turni347 – 3493
Helixi350 – 3523
Helixi353 – 36715
Turni369 – 3724

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8DX-ray2.00A1-377[»]
1D8EX-ray3.00A1-377[»]
1FPPX-ray2.75A1-377[»]
1FT1X-ray2.25A1-377[»]
1FT2X-ray3.40A55-369[»]
1FTImodel-A55-369[»]
1HZ7model-A116-247[»]
1JCRX-ray2.00A1-377[»]
1JCSX-ray2.20A1-377[»]
1KZOX-ray2.20A1-377[»]
1KZPX-ray2.10A1-377[»]
1KZRmodel-A55-377[»]
1N4PX-ray2.65A/C/E/G/I/K1-377[»]
1N4QX-ray2.40A/C/E/G/I/K1-377[»]
1N4RX-ray2.80A/C/E/G/I/K1-377[»]
1N4SX-ray2.60A/C/E/G/I/K1-377[»]
1N94X-ray3.50A55-369[»]
1N95X-ray2.30A55-369[»]
1N9AX-ray3.20A55-369[»]
1NI1X-ray2.30A55-369[»]
1NL4X-ray2.70A55-366[»]
1O1RX-ray2.30A1-377[»]
1O1SX-ray2.30A1-377[»]
1O1TX-ray2.10A1-377[»]
1O5MX-ray2.30A1-377[»]
1QBQX-ray2.40A45-377[»]
1QE2model-A116-247[»]
1S64X-ray2.55A/C/E/G/I/K1-377[»]
1SA5X-ray2.60A1-377[»]
1TN7X-ray2.30A1-377[»]
1TN8X-ray2.25A1-377[»]
1TNBX-ray2.85A/C/E/G/I/K1-377[»]
1TNOX-ray2.70A/C/E/G/I/K1-377[»]
1TNUX-ray2.70A/C/E/G/I/K1-377[»]
1TNYX-ray2.70A/C/E/G/I/K1-377[»]
1TNZX-ray2.90A/C/E/G/I/K1-377[»]
1X81X-ray3.50A55-369[»]
2BEDX-ray2.70A54-366[»]
2FTImodel-A55-369[»]
2R2LX-ray2.23A54-368[»]
2ZIRX-ray2.40A1-377[»]
2ZISX-ray2.60A1-377[»]
3DPYX-ray2.70A1-377[»]
3E30X-ray2.45A1-377[»]
3E32X-ray2.45A1-377[»]
3E33X-ray1.90A1-377[»]
3E34X-ray2.05A1-377[»]
3EU5X-ray2.80A1-377[»]
3EUVX-ray2.75A1-377[»]
3FTImodel-A55-369[»]
3KSLX-ray2.05A1-377[»]
3KSQX-ray2.10A1-377[»]
4GTMX-ray2.20A1-377[»]
4GTOX-ray2.15A1-377[»]
4GTPX-ray2.75A1-377[»]
4GTQX-ray2.60A1-377[»]
4GTRX-ray2.20A1-377[»]
ProteinModelPortaliQ04631.
SMRiQ04631. Positions 55-377.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ04631.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati112 – 14635PFTA 1Add
BLAST
Repeati147 – 18135PFTA 2Add
BLAST
Repeati182 – 21433PFTA 3Add
BLAST
Repeati215 – 24935PFTA 4Add
BLAST
Repeati255 – 28935PFTA 5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi22 – 309Pro-rich

Sequence similaritiesi

Contains 5 PFTA repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5536.
HOGENOMiHOG000188957.
HOVERGENiHBG004498.
InParanoidiQ04631.
KOiK05955.
PhylomeDBiQ04631.

Family and domain databases

InterProiIPR002088. Prenyl_trans_a.
[Graphical view]
PfamiPF01239. PPTA. 5 hits.
[Graphical view]
PROSITEiPS51147. PFTA. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q04631-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAATEGVGES APGGEPGQPE QPPPPPPPPP AQQPQEEEMA AEAGEAAASP
60 70 80 90 100
MDDGFLSLDS PTYVLYRDRA EWADIDPVPQ NDGPSPVVQI IYSEKFRDVY
110 120 130 140 150
DYFRAVLQRD ERSERAFKLT RDAIELNAAN YTVWHFRRVL LRSLQKDLQE
160 170 180 190 200
EMNYIIAIIE EQPKNYQVWH HRRVLVEWLK DPSQELEFIA DILNQDAKNY
210 220 230 240 250
HAWQHRQWVI QEFRLWDNEL QYVDQLLKED VRNNSVWNQR HFVISNTTGY
260 270 280 290 300
SDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS RYPNLLNQLL
310 320 330 340 350
DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT
360 370
IRKEYWRYIG RSLQSKHSRE SDIPASV
Length:377
Mass (Da):44,049
Last modified:October 1, 1993 - v1
Checksum:iDFFFECC1B88BC080
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M81225 mRNA. Translation: AAA41833.1.
PIRiA41625.
RefSeqiNP_036979.1. NM_012847.1.
UniGeneiRn.5990.

Genome annotation databases

GeneIDi25318.
KEGGirno:25318.
UCSCiRGD:2625. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M81225 mRNA. Translation: AAA41833.1 .
PIRi A41625.
RefSeqi NP_036979.1. NM_012847.1.
UniGenei Rn.5990.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D8D X-ray 2.00 A 1-377 [» ]
1D8E X-ray 3.00 A 1-377 [» ]
1FPP X-ray 2.75 A 1-377 [» ]
1FT1 X-ray 2.25 A 1-377 [» ]
1FT2 X-ray 3.40 A 55-369 [» ]
1FTI model - A 55-369 [» ]
1HZ7 model - A 116-247 [» ]
1JCR X-ray 2.00 A 1-377 [» ]
1JCS X-ray 2.20 A 1-377 [» ]
1KZO X-ray 2.20 A 1-377 [» ]
1KZP X-ray 2.10 A 1-377 [» ]
1KZR model - A 55-377 [» ]
1N4P X-ray 2.65 A/C/E/G/I/K 1-377 [» ]
1N4Q X-ray 2.40 A/C/E/G/I/K 1-377 [» ]
1N4R X-ray 2.80 A/C/E/G/I/K 1-377 [» ]
1N4S X-ray 2.60 A/C/E/G/I/K 1-377 [» ]
1N94 X-ray 3.50 A 55-369 [» ]
1N95 X-ray 2.30 A 55-369 [» ]
1N9A X-ray 3.20 A 55-369 [» ]
1NI1 X-ray 2.30 A 55-369 [» ]
1NL4 X-ray 2.70 A 55-366 [» ]
1O1R X-ray 2.30 A 1-377 [» ]
1O1S X-ray 2.30 A 1-377 [» ]
1O1T X-ray 2.10 A 1-377 [» ]
1O5M X-ray 2.30 A 1-377 [» ]
1QBQ X-ray 2.40 A 45-377 [» ]
1QE2 model - A 116-247 [» ]
1S64 X-ray 2.55 A/C/E/G/I/K 1-377 [» ]
1SA5 X-ray 2.60 A 1-377 [» ]
1TN7 X-ray 2.30 A 1-377 [» ]
1TN8 X-ray 2.25 A 1-377 [» ]
1TNB X-ray 2.85 A/C/E/G/I/K 1-377 [» ]
1TNO X-ray 2.70 A/C/E/G/I/K 1-377 [» ]
1TNU X-ray 2.70 A/C/E/G/I/K 1-377 [» ]
1TNY X-ray 2.70 A/C/E/G/I/K 1-377 [» ]
1TNZ X-ray 2.90 A/C/E/G/I/K 1-377 [» ]
1X81 X-ray 3.50 A 55-369 [» ]
2BED X-ray 2.70 A 54-366 [» ]
2FTI model - A 55-369 [» ]
2R2L X-ray 2.23 A 54-368 [» ]
2ZIR X-ray 2.40 A 1-377 [» ]
2ZIS X-ray 2.60 A 1-377 [» ]
3DPY X-ray 2.70 A 1-377 [» ]
3E30 X-ray 2.45 A 1-377 [» ]
3E32 X-ray 2.45 A 1-377 [» ]
3E33 X-ray 1.90 A 1-377 [» ]
3E34 X-ray 2.05 A 1-377 [» ]
3EU5 X-ray 2.80 A 1-377 [» ]
3EUV X-ray 2.75 A 1-377 [» ]
3FTI model - A 55-369 [» ]
3KSL X-ray 2.05 A 1-377 [» ]
3KSQ X-ray 2.10 A 1-377 [» ]
4GTM X-ray 2.20 A 1-377 [» ]
4GTO X-ray 2.15 A 1-377 [» ]
4GTP X-ray 2.75 A 1-377 [» ]
4GTQ X-ray 2.60 A 1-377 [» ]
4GTR X-ray 2.20 A 1-377 [» ]
ProteinModelPortali Q04631.
SMRi Q04631. Positions 55-377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6131N.
IntActi Q04631. 8 interactions.
MINTi MINT-121907.
STRINGi 10116.ENSRNOP00000019594.

Chemistry

BindingDBi Q04631.
ChEMBLi CHEMBL2095197.

PTM databases

PhosphoSitei Q04631.

Proteomic databases

PaxDbi Q04631.
PRIDEi Q04631.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 25318.
KEGGi rno:25318.
UCSCi RGD:2625. rat.

Organism-specific databases

CTDi 2339.
RGDi 2625. Fnta.

Phylogenomic databases

eggNOGi COG5536.
HOGENOMi HOG000188957.
HOVERGENi HBG004498.
InParanoidi Q04631.
KOi K05955.
PhylomeDBi Q04631.

Enzyme and pathway databases

SABIO-RK Q04631.

Miscellaneous databases

EvolutionaryTracei Q04631.
NextBioi 606153.
PROi Q04631.

Gene expression databases

Genevestigatori Q04631.

Family and domain databases

InterProi IPR002088. Prenyl_trans_a.
[Graphical view ]
Pfami PF01239. PPTA. 5 hits.
[Graphical view ]
PROSITEi PS51147. PFTA. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and expression of a cDNA encoding the alpha subunit of rat p21ras protein farnesyltransferase."
    Chen W.-J., Andres D.A., Goldstein J.L., Brown M.S.
    Proc. Natl. Acad. Sci. U.S.A. 88:11368-11372(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Brain.
  2. "Crystal structure of protein farnesyltransferase at 2.25-A resolution."
    Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
    Science 275:1800-1804(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS), SUBUNIT.
  3. Erratum
    Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
    Science 276:21-21(1997)
  4. "Protein farnesyltransferase: structure and implications for substrate binding."
    Dunten P., Kammlott U., Crowther R., Weber D., Palermo R., Birktoft J.
    Biochemistry 37:7907-7912(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-377 IN COMPLEX WITH FNTB, SUBUNIT.
  5. "Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate."
    Long S.B., Casey P.J., Beese L.S.
    Biochemistry 37:9612-9618(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS)IN COMPLEX WITH FNTB, SUBUNIT.
  6. "Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue."
    Strickland C.L., Windsor W.T., Syto R., Wang L., Bond R., Wu Z., Schwartz J., Le H.V., Beese L.S., Weber P.C.
    Biochemistry 37:16601-16611(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 45-377 IN COMPLEX WITH FNTB, SUBUNIT.
  7. Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-377 IN COMPLEX WITH FNTB, SUBUNIT.
  8. "The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures."
    Long S.B., Casey P.J., Beese L.S.
    Structure 8:209-222(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-377 IN COMPLEX WITH FNTB, SUBUNIT.
  9. "The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics."
    Long S.B., Hancock P.J., Kral A.M., Hellinga H.W., Beese L.S.
    Proc. Natl. Acad. Sci. U.S.A. 98:12948-12953(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT.
  10. "Reaction path of protein farnesyltransferase at atomic resolution."
    Long S.B., Casey P.J., Beese L.S.
    Nature 419:645-650(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-377 IN COMPLEX WITH FNTB, SUBUNIT.
  11. "Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase."
    Turek-Etienne T.C., Strickland C.L., Distefano M.D.
    Biochemistry 42:3716-3724(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-377 IN COMPLEX WITH FNTB, SUBUNIT.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 55-369 IN COMPLEX WITH FNTB, SUBUNIT, CATALYTIC ACTIVITY.
  13. "Structure of mammalian protein geranylgeranyltransferase type-I."
    Taylor J.S., Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    EMBO J. 22:5963-5974(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH PGGT1B, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION.
  14. "Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity."
    Reid T.S., Beese L.S.
    Biochemistry 43:6877-6884(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT.
  15. "Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity."
    Reid T.S., Terry K.L., Casey P.J., Beese L.S.
    J. Mol. Biol. 343:417-433(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT.
  16. "Caged protein prenyltransferase substrates: tools for understanding protein prenylation."
    DeGraw A.J., Hast M.A., Xu J., Mullen D., Beese L.S., Barany G., Distefano M.D.
    Chem. Biol. Drug Des. 72:171-181(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS), SUBUNIT, CATALYTIC ACTIVITY, FUNCTION.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH FNTB, SUBUNIT, CATALYTIC ACTIVITY, FUNCTION.

Entry informationi

Entry nameiFNTA_RAT
AccessioniPrimary (citable) accession number: Q04631
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 29, 2014
This is version 122 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3