Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q02293

- FNTB_RAT

UniProt

Q02293 - FNTB_RAT

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Protein farnesyltransferase subunit beta

Gene

Fntb

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

Functioni

Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.4 Publications

Catalytic activityi

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.5 Publications

Cofactori

Binds 1 zinc ion per subunit.12 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei102 – 1021Important for selectivity against geranylgeranyl diphosphateBy similarity
Metal bindingi297 – 2971Zinc; catalytic3 Publications
Metal bindingi299 – 2991Zinc; catalytic3 Publications
Metal bindingi362 – 3621Zinc; via tele nitrogen; catalytic3 Publications

GO - Molecular functioni

  1. farnesyltranstransferase activity Source: Ensembl
  2. protein farnesyltransferase activity Source: RGD
  3. zinc ion binding Source: UniProtKB

GO - Biological processi

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

Keywords - Molecular functioni

Prenyltransferase, Transferase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_227662. Inactivation, recovery and regulation of the phototransduction cascade.
SABIO-RKQ02293.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein farnesyltransferase subunit beta (EC:2.5.1.58)
Short name:
FTase-beta
Alternative name(s):
CAAX farnesyltransferase subunit beta
Ras proteins prenyltransferase subunit beta
Gene namesi
Name:Fntb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 6

Organism-specific databases

RGDi620119. Fntb.

Subcellular locationi

GO - Cellular componenti

  1. microtubule associated complex Source: Ensembl
  2. protein complex Source: RGD
  3. protein farnesyltransferase complex Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437Protein farnesyltransferase subunit betaPRO_0000119763Add
BLAST

Proteomic databases

PaxDbiQ02293.
PRIDEiQ02293.

PTM databases

PhosphoSiteiQ02293.

Expressioni

Gene expression databases

GenevestigatoriQ02293.

Interactioni

Subunit structurei

Heterodimer of FNTA and FNTB.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FntaQ0463114EBI-602454,EBI-602447

Protein-protein interaction databases

DIPiDIP-6132N.
IntActiQ02293. 1 interaction.
MINTiMINT-121917.
STRINGi10116.ENSRNOP00000010588.

Structurei

Secondary structure

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 263
Helixi28 – 336
Helixi43 – 6523
Helixi75 – 8511
Helixi91 – 966
Helixi100 – 11314
Helixi120 – 13314
Beta strandi138 – 1436
Helixi150 – 16314
Helixi166 – 1716
Helixi174 – 18411
Beta strandi191 – 1944
Helixi201 – 21313
Turni219 – 2246
Helixi225 – 2328
Beta strandi237 – 2393
Helixi249 – 26113
Helixi265 – 2673
Helixi270 – 2789
Turni283 – 2853
Beta strandi287 – 2915
Helixi300 – 3034
Turni304 – 3063
Helixi307 – 31711
Beta strandi321 – 3233
Beta strandi325 – 3273
Helixi332 – 34211
Beta strandi348 – 3503
Beta strandi352 – 3554
Helixi360 – 37415
Beta strandi375 – 3784
Beta strandi381 – 3844
Helixi390 – 3923
Turni399 – 4013
Helixi405 – 41511
Helixi424 – 4263
Helixi434 – 4363

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8DX-ray2.00B1-437[»]
1D8EX-ray3.00B1-437[»]
1FPPX-ray2.75B1-437[»]
1FT1X-ray2.25B1-437[»]
1FT2X-ray3.40B22-422[»]
1FTImodel-B22-422[»]
1HZ7model-B41-406[»]
1JCRX-ray2.00B1-437[»]
1JCSX-ray2.20B1-437[»]
1KZOX-ray2.20B1-437[»]
1KZPX-ray2.10B1-437[»]
1KZRmodel-B17-423[»]
1N94X-ray3.50B22-418[»]
1N95X-ray2.30B22-423[»]
1N9AX-ray3.20B22-423[»]
1NI1X-ray2.30B22-423[»]
1NL4X-ray2.70B23-423[»]
1O1RX-ray2.30B1-427[»]
1O1SX-ray2.30B1-427[»]
1O1TX-ray2.10B1-427[»]
1O5MX-ray2.30B1-437[»]
1QBQX-ray2.40B1-437[»]
1QE2model-B41-406[»]
1SA5X-ray2.60B1-437[»]
1TN7X-ray2.30B1-437[»]
1TN8X-ray2.25B1-437[»]
1X81X-ray3.50B22-418[»]
2BEDX-ray2.70B23-423[»]
2FTImodel-B22-422[»]
2R2LX-ray2.23B23-423[»]
2ZIRX-ray2.40B1-437[»]
2ZISX-ray2.60B1-437[»]
3DPYX-ray2.70B1-437[»]
3E30X-ray2.45B1-437[»]
3E32X-ray2.45B1-437[»]
3E33X-ray1.90B1-437[»]
3E34X-ray2.05B1-437[»]
3EU5X-ray2.80B1-427[»]
3EUVX-ray2.75B1-427[»]
3FTImodel-B22-422[»]
3KSLX-ray2.05B1-437[»]
3KSQX-ray2.10B1-437[»]
4GTMX-ray2.20B1-427[»]
4GTOX-ray2.15B1-427[»]
4GTPX-ray2.75B1-427[»]
4GTQX-ray2.60B1-427[»]
4GTRX-ray2.20B1-427[»]
ProteinModelPortaliQ02293.
SMRiQ02293. Positions 22-437.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ02293.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati123 – 16442PFTB 1Add
BLAST
Repeati174 – 21542PFTB 2Add
BLAST
Repeati222 – 26342PFTB 3Add
BLAST
Repeati270 – 31243PFTB 4Add
BLAST
Repeati332 – 37443PFTB 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni248 – 2514Farnesyl diphosphate binding
Regioni291 – 2944Farnesyl diphosphate binding
Regioni300 – 3034Farnesyl diphosphate binding

Sequence similaritiesi

Contains 5 PFTB repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5029.
GeneTreeiENSGT00550000075042.
HOGENOMiHOG000190594.
HOVERGENiHBG008173.
InParanoidiQ02293.
KOiK05954.
OMAiKLLDFLW.
OrthoDBiEOG7P02HV.
PhylomeDBiQ02293.
TreeFamiTF353162.

Family and domain databases

Gene3Di1.50.10.20. 1 hit.
InterProiIPR026872. FTB.
IPR001330. Prenyltrans.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PANTHERiPTHR11774:SF6. PTHR11774:SF6. 1 hit.
PfamiPF00432. Prenyltrans. 2 hits.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.

Sequencei

Sequence statusi: Complete.

Q02293-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASSSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK
60 70 80 90 100
VEEKIQEVFS SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR
110 120 130 140 150
PWLCYWILHS LELLDEPIPQ IVATDVCQFL ELCQSPDGGF GGGPGQYPHL
160 170 180 190 200
APTYAAVNAL CIIGTEEAYN VINREKLLQY LYSLKQPDGS FLMHVGGEVD
210 220 230 240 250
VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG GVPGMEAHGG
260 270 280 290 300
YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY
310 320 330 340 350
SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL
360 370 380 390 400
LDKPGKSRDF YHTCYCLSGL SIAQHFGSGA MLHDVVMGVP ENVLQPTHPV
410 420 430
YNIGPDKVIQ ATTHFLQKPV PGFEECEDAV TSDPATD
Length:437
Mass (Da):48,673
Last modified:April 1, 1993 - v1
Checksum:i41A9D6D79CD319A8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M69056 mRNA. Translation: AAA41176.1.
BC087675 mRNA. Translation: AAH87675.1.
PIRiA40037.
RefSeqiNP_742031.1. NM_172034.2.
UniGeneiRn.8873.

Genome annotation databases

EnsembliENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660.
GeneIDi64511.
KEGGirno:64511.
UCSCiRGD:620119. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M69056 mRNA. Translation: AAA41176.1 .
BC087675 mRNA. Translation: AAH87675.1 .
PIRi A40037.
RefSeqi NP_742031.1. NM_172034.2.
UniGenei Rn.8873.

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 B 1-437 [» ]
1D8E X-ray 3.00 B 1-437 [» ]
1FPP X-ray 2.75 B 1-437 [» ]
1FT1 X-ray 2.25 B 1-437 [» ]
1FT2 X-ray 3.40 B 22-422 [» ]
1FTI model - B 22-422 [» ]
1HZ7 model - B 41-406 [» ]
1JCR X-ray 2.00 B 1-437 [» ]
1JCS X-ray 2.20 B 1-437 [» ]
1KZO X-ray 2.20 B 1-437 [» ]
1KZP X-ray 2.10 B 1-437 [» ]
1KZR model - B 17-423 [» ]
1N94 X-ray 3.50 B 22-418 [» ]
1N95 X-ray 2.30 B 22-423 [» ]
1N9A X-ray 3.20 B 22-423 [» ]
1NI1 X-ray 2.30 B 22-423 [» ]
1NL4 X-ray 2.70 B 23-423 [» ]
1O1R X-ray 2.30 B 1-427 [» ]
1O1S X-ray 2.30 B 1-427 [» ]
1O1T X-ray 2.10 B 1-427 [» ]
1O5M X-ray 2.30 B 1-437 [» ]
1QBQ X-ray 2.40 B 1-437 [» ]
1QE2 model - B 41-406 [» ]
1SA5 X-ray 2.60 B 1-437 [» ]
1TN7 X-ray 2.30 B 1-437 [» ]
1TN8 X-ray 2.25 B 1-437 [» ]
1X81 X-ray 3.50 B 22-418 [» ]
2BED X-ray 2.70 B 23-423 [» ]
2FTI model - B 22-422 [» ]
2R2L X-ray 2.23 B 23-423 [» ]
2ZIR X-ray 2.40 B 1-437 [» ]
2ZIS X-ray 2.60 B 1-437 [» ]
3DPY X-ray 2.70 B 1-437 [» ]
3E30 X-ray 2.45 B 1-437 [» ]
3E32 X-ray 2.45 B 1-437 [» ]
3E33 X-ray 1.90 B 1-437 [» ]
3E34 X-ray 2.05 B 1-437 [» ]
3EU5 X-ray 2.80 B 1-427 [» ]
3EUV X-ray 2.75 B 1-427 [» ]
3FTI model - B 22-422 [» ]
3KSL X-ray 2.05 B 1-437 [» ]
3KSQ X-ray 2.10 B 1-437 [» ]
4GTM X-ray 2.20 B 1-427 [» ]
4GTO X-ray 2.15 B 1-427 [» ]
4GTP X-ray 2.75 B 1-427 [» ]
4GTQ X-ray 2.60 B 1-427 [» ]
4GTR X-ray 2.20 B 1-427 [» ]
ProteinModelPortali Q02293.
SMRi Q02293. Positions 22-437.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6132N.
IntActi Q02293. 1 interaction.
MINTi MINT-121917.
STRINGi 10116.ENSRNOP00000010588.

Chemistry

BindingDBi Q02293.
ChEMBLi CHEMBL2095197.

PTM databases

PhosphoSitei Q02293.

Proteomic databases

PaxDbi Q02293.
PRIDEi Q02293.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000010588 ; ENSRNOP00000010588 ; ENSRNOG00000007660 .
GeneIDi 64511.
KEGGi rno:64511.
UCSCi RGD:620119. rat.

Organism-specific databases

CTDi 2342.
RGDi 620119. Fntb.

Phylogenomic databases

eggNOGi COG5029.
GeneTreei ENSGT00550000075042.
HOGENOMi HOG000190594.
HOVERGENi HBG008173.
InParanoidi Q02293.
KOi K05954.
OMAi KLLDFLW.
OrthoDBi EOG7P02HV.
PhylomeDBi Q02293.
TreeFami TF353162.

Enzyme and pathway databases

Reactomei REACT_227662. Inactivation, recovery and regulation of the phototransduction cascade.
SABIO-RK Q02293.

Miscellaneous databases

EvolutionaryTracei Q02293.
NextBioi 613294.
PROi Q02293.

Gene expression databases

Genevestigatori Q02293.

Family and domain databases

Gene3Di 1.50.10.20. 1 hit.
InterProi IPR026872. FTB.
IPR001330. Prenyltrans.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view ]
PANTHERi PTHR11774:SF6. PTHR11774:SF6. 1 hit.
Pfami PF00432. Prenyltrans. 2 hits.
[Graphical view ]
SUPFAMi SSF48239. SSF48239. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1."
    Chen W.-J., Andres D.A., Goldstein J.L., Russell D.W., Brown M.S.
    Cell 66:327-334(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "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) IN COMPLEX WITH ZINC.
  4. Erratum
    Park H.-W., Boduluri S.R., Mooomaw J.F., Casey P.J., Beese L.S.
    Science 276:21-21(1997)
  5. "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) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR.
  6. "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 FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT.
  7. "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) IN COMPLEX WITH FNTA; ZINC IONS AND FARNESYL DIPHOSPHATE ANALOG, COFACTOR, 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) IN COMPLEX WITH ZINC IONS; FNTA AND KRAS, INTERACTION WITH KRAS, CATALYTIC ACTIVITY, COFACTOR, FUNCTION, 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 FNTA AND GERANYLGERANYL DIPHOSPHATE, 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) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR.
  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 1-427 IN COMPLEX WITH FNTA; GERANYLGERANYL DIPHOSPHATE AND ZINC IONS, COFACTOR, SUBUNIT.
  12. "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 FNTA AND ZINC IONS, COFACTOR, SUBUNIT.
  13. "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 FNTA; FARNESYL DIPHOSPHATE AND ZINC, COFACTOR, CATALYTIC ACTIVITY, SUBUNIT.
  14. "Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase."
    Hast M.A., Fletcher S., Cummings C.G., Pusateri E.E., Blaskovich M.A., Rivas K., Gelb M.H., Van Voorhis W.C., Sebti S.M., Hamilton A.D., Beese L.S.
    Chem. Biol. 16:181-192(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, SUBUNIT.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA AND ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC, SUBUNIT, COFACTOR.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-427 IN COMPLEX WITH FNTA; FARNESYL DIPHOSPHATE AND ZINC IONS, SUBUNIT, COFACTOR, CATALYTIC ACTIVITY, FUNCTION.

Entry informationi

Entry nameiFNTB_RAT
AccessioniPrimary (citable) accession number: Q02293
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 29, 2014
This is version 134 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