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P04601

- NEF_HV1H2

UniProt

P04601 - NEF_HV1H2

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Protein

Protein Nef

Gene

nef

Organism
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocytes function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells. One of the earliest and most abundantly expressed viral proteins.
In infected CD4+ T-lymphocytes, down-regulates the surface MHC-I, mature MHC-II, CD4, CD28, CCR5 and CXCR4 molecules. Mediates internalization and degradation of host CD4 through the interaction of with the cytoplasmic tail of CD4, the recruitment of AP-2 (clathrin adapter protein complex 2), internalization through clathrin coated pits, and subsequent transport to endosomes and lysosomes for degradation. Diverts host MHC-I molecules to the trans-Golgi network-associated endosomal compartments by an endocytic pathway to finally target them for degradation. MHC-I down-regulation may involve AP-1 (clathrin adapter protein complex 1) or possibly Src family kinase-ZAP70/Syk-PI3K cascade recruited by PACS2. In consequence infected cells are masked for immune recognition by cytotoxic T-lymphocytes. Decreasing the number of immune receptors also prevents reinfection by more HIV particles (superinfection).
Bypasses host T-cell signaling by inducing a transcriptional program nearly identical to that of anti-CD3 cell activation. Interaction with TCR-zeta chain up-regulates the Fas ligand (FasL). Increasing surface FasL molecules and decreasing surface MHC-I molecules on infected CD4+ cells send attacking cytotoxic CD8+ T-lymphocytes into apoptosis (By similarity).By similarity
Plays a role in optimizing the host cell environment for viral replication without causing cell death by apoptosis. Protects the infected cells from apoptosis in order to keep them alive until the next virus generation is ready to strike. Inhibits the Fas and TNFR-mediated death signals by blocking MAP3K5. Interacts and decreases the half-life of p53, protecting the infected cell against p53-mediated apoptosis. Inhibits the apoptotic signals regulated by the Bcl-2 family proteins through the formation of a Nef/PI3-kinase/PAK2 complex that leads to activation of PAK2 and induces phosphorylation of Bad (By similarity).By similarity
Extracellular Nef protein targets CD4+ T-lymphocytes for apoptosis by interacting with CXCR4 surface receptors.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei20 – 201Might play a role in AP-1 recruitment to the Nef-MHC-I complex
Sitei57 – 582Cleavage; by viral proteaseBy similarity

GO - Molecular functioni

  1. GTP binding Source: InterPro

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. entry into host cell Source: Reactome
  3. pathogenesis Source: UniProtKB-KW
  4. regulation of defense response to virus by virus Source: Reactome
  5. suppression by virus of host adaptive immune response Source: UniProtKB-KW
  6. suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I Source: UniProtKB-KW
  7. suppression by virus of host antigen processing and presentation of peptide antigen via MHC class II Source: UniProtKB-KW
  8. suppression by virus of host autophagy Source: UniProtKB-KW
  9. uncoating of virus Source: Reactome
  10. viral life cycle Source: Reactome
  11. viral process Source: Reactome
  12. virion assembly Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Host-virus interaction, Inhibition of host adaptive immune response by virus, Inhibition of host autophagy by virus, Inhibition of host MHC class I molecule presentation by virus, Inhibition of host MHC class II molecule presentation by virus, Viral immunoevasion, Virulence

Enzyme and pathway databases

ReactomeiREACT_11068. Nef and signal transduction.
REACT_11103. Nef mediated downregulation of MHC class I complex cell surface expression.
REACT_11139. Nef mediated downregulation of CD28 cell surface expression.
REACT_11166. Nef Mediated CD4 Down-regulation.
REACT_11200. Nef Mediated CD8 Down-regulation.
REACT_6359. Budding and maturation of HIV virion.
REACT_6361. Late Phase of HIV Life Cycle.
REACT_6818. Assembly Of The HIV Virion.
REACT_6903. Binding and entry of HIV virion.
REACT_6965. Uncoating of the HIV Virion.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Nef
Alternative name(s):
3'ORF
Negative factor
Short name:
F-protein
Cleaved into the following chain:
Gene namesi
Name:nef
OrganismiHuman immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Taxonomic identifieri11706 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeLentivirusPrimate lentivirus group
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000002241: Genome

Subcellular locationi

Host cell membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Host cytoplasmhost perinuclear region By similarity. Virion By similarity. Secreted 2 Publications
Note: Predominantly found in the paranuclear area, probably in the TGN. Correct localization requires PACS1. Also associates with the inner plasma membrane through its N-terminal domain. Nef stimulates its own export via the release of exosomes. Also incorporated in virions at a rate of about 10 molecules per virion, where it is cleaved (By similarity).By similarity

GO - Cellular componenti

  1. host cell cytoplasm Source: UniProtKB-KW
  2. host cell plasma membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB-KW
  4. virion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Host cell membrane, Host cytoplasm, Host membrane, Membrane, Secreted, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201M → A: Complete loss of Nef-induced MHC-I down-regulation, MHC-I is internalized but not sequestred in TGN. 1 Publication
Mutagenesisi62 – 654EEEE → AAAA: Complete loss of Nef-induced MHC-I down-regulation, MHC-I is not internalized. Reduced interaction with host PACS1 and PACS2. 2 Publications
Mutagenesisi62 – 654EEEE → AAEA: About 50% loss of Nef-induced MHC-I down-regulation. 2 Publications
Mutagenesisi62 – 654EEEE → AEAA: About 50% loss of Nef-induced MHC-I down-regulation. 2 Publications
Mutagenesisi62 – 654EEEE → DDDD: No effect on Nef-induced MHC-I down-regulation. 2 Publications
Mutagenesisi62 – 643EEE → AAA: About 50% loss of Nef-induced MHC-I down-regulation.
Mutagenesisi62 – 632EE → AA: Almost no effect on Nef-induced MHC-I down-regulation.
Mutagenesisi63 – 653EEE → AAA: About 50% loss of Nef-induced MHC-I down-regulation. 1 Publication
Mutagenesisi63 – 642EE → AA: Almost no effect on Nef-induced MHC-I down-regulation.
Mutagenesisi64 – 652EE → AA: Almost no effect on Nef-induced MHC-I down-regulation.
Mutagenesisi72 – 721P → A: Complete loss of Nef-induced MHC-I down-regulation, MHC-I is not internalized; when associated with A-75. 1 Publication
Mutagenesisi75 – 751P → A: Complete loss of Nef-induced MHC-I down-regulation, MHC-I is not internalized; when associated with A-72. 1 Publication
Mutagenesisi123 – 1231D → E: Complete loss of Nef-induced MHC-I down-regulation, CD4 down-regulation, and enhancement of infectivity. Activates PAK2 twofold over wild-type levels.

Keywords - Diseasei

AIDS

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 206205Protein NefPRO_0000038365Add
BLAST
Chaini58 – 206149C-terminal core proteinBy similarityPRO_0000038366Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity

Post-translational modificationi

The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles (By similarity).By similarity
Phosphorylated on serine residues, probably by host PKC.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Expressioni

Keywords - Developmental stagei

Early protein

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with Nef associated p21-activated kinase (PAK2); this interaction activates PAK2. Associates with the Nef-MHC-I-AP1 complex; this complex is required for MHC-I internalization. Interacts (via C-terminus) with host PI3-kinase (via C-terminus). Interacts with host PACS1; this interaction seems to be weak. Interacts with host PACS2. Interacts with host LCK and MAPK3; these interactions inhibit the kinase activity of the latters. Interacts with host ATP6V1H; this interaction may play a role in CD4 endocytosis. Associates with the CD4-Nef-AP2 complex; this complex is required for CD4 internalization. Interacts with TCR-zeta chain; this interaction up-regulates the Fas ligand (FasL) surface expression. Interacts with various cellular proteins including MAP3K5, beta-COP, HCK, and PTE1. Interacts with human GNB2L1/RACK1; this increases Nef phosphorylation by PKC (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ACOT8O147345EBI-6164028,EBI-1237371From a different organism.

Protein-protein interaction databases

BioGridi1205545. 68 interactions.
IntActiP04601. 8 interactions.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi81 – 9414
Helixi104 – 11815
Beta strandi130 – 1323
Beta strandi136 – 1383
Beta strandi143 – 1475
Helixi150 – 1578
Helixi167 – 1704
Beta strandi172 – 1754
Beta strandi181 – 1855
Helixi188 – 1914
Helixi194 – 1985
Helixi200 – 2023

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RL2X-ray2.39C73-82[»]
4NEEX-ray2.88C/E/H/K63-203[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 5756N-terminal; associates with the host plasma membraneBy similarityAdd
BLAST
Regioni7 – 2620Necessary for MHC-I internalizationCuratedAdd
BLAST
Regioni62 – 654Acidic; stabilizes the interaction of NEF/MHC-I with host AP1M1; necessary for MHC-I internalization and interaction with host PACS1 and PACS2Curated
Regioni69 – 7810SH3-binding; interaction with Src family tyrosine kinasesBy similarity
Regioni108 – 12417Mediates dimerization, Nef-PTE1 interactionBy similarityAdd
BLAST
Regioni148 – 18033Binding to ATP6V1HBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi72 – 754PxxP; stabilizes the interaction of NEF/MHC-I with host AP1M1; necessary for MHC-I internalizationCurated
Motifi164 – 1652Di-leucine internalization motif; necessary for CD4 internalizationCurated
Motifi174 – 1752Diacidic; necessary for CD4 internalizationCurated

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi62 – 654Poly-Glu

Domaini

The N-terminal domain is composed of the N-myristoyl glycine and of a cluster of positively charged amino acids. It is required for inner plasma membrane targeting of Nef and virion incorporation, and thereby for infectivity. This domain is also involved in binding to p53 (By similarity).By similarity
The SH3-binding domain constituted of PxxP motifs mediates binding to several Src family proteins thereby regulating their tyrosine kinase activity. The same motifs also mediates the association with MAPK3, PI3-kinase and TCR-zeta (By similarity).By similarity
The di-leucine internalization motif and a diacidic motif seem to be required for binding to AP-2.
The acidic region may play a stabilizing role in the formation of a ternary complex between Nef, the MHC-I cytoplasmic domain, and AP1M1.

Sequence similaritiesi

Keywords - Domaini

SH3-binding

Family and domain databases

Gene3Di3.30.62.10. 1 hit.
4.10.890.10. 1 hit.
InterProiIPR027480. HIV-1_Nef_anchor.
IPR027481. HIV-1_Nef_core.
IPR001558. HIV_Nef.
[Graphical view]
PfamiPF00469. F-protein. 1 hit.
[Graphical view]
SUPFAMiSSF55671. SSF55671. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P04601-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGGKWSKSSV IGWPTVRERM RRAEPAADRV GAASRDLEKH GAITSSNTAA
60 70 80 90 100
TNAACAWLEA QEEEEVGFPV TPQVPLRPMT YKAAVDLSHF LKEKGGLEGL
110 120 130 140 150
IHSQRRQDIL DLWIYHTQGY FPDWQNYTPG PGVRYPLTFG WCYKLVPVEP
160 170 180 190 200
DKIEEANKGE NTSLLHPVSL HGMDDPEREV LEWRFDSRLA FHHVARELHP

EYFKNC
Length:206
Mass (Da):23,469
Last modified:February 9, 2010 - v5
Checksum:i5A26976E95483E9C
GO

Sequence cautioni

The sequence AAB50263.1 differs from that shown. Reason: Readthrough of a premature stop codon in position 123 that truncates the Nef protein. The sequence displayed is that of wild-type full-length HXB2-R7 clone.
The sequence AAC82597.1 differs from that shown. Reason: Readthrough of a premature stop codon in position 123 that truncates the Nef protein. The sequence displayed is that of wild-type full-length HXB2-R7 clone.
The sequence CAA26946.1 differs from that shown. Reason: Readthrough of a premature stop codon in position 123 that truncates the Nef protein. The sequence displayed is that of wild-type full-length HXB2-R7 clone.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291R → G in CAA26946. (PubMed:2999715)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03187 Genomic RNA. Translation: CAA26946.1. Sequence problems.
K03455 Genomic RNA. Translation: AAB50263.1. Sequence problems.
AF033819 Genomic RNA. Translation: AAC82597.1. Sequence problems.
RefSeqiNP_057857.2. NC_001802.1.

Genome annotation databases

GeneIDi156110.

Cross-referencesi

Web resourcesi

BioAfrica HIV proteomics resource

Nef entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03187 Genomic RNA. Translation: CAA26946.1 . Sequence problems.
K03455 Genomic RNA. Translation: AAB50263.1 . Sequence problems.
AF033819 Genomic RNA. Translation: AAC82597.1 . Sequence problems.
RefSeqi NP_057857.2. NC_001802.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3RL2 X-ray 2.39 C 73-82 [» ]
4NEE X-ray 2.88 C/E/H/K 63-203 [» ]
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1205545. 68 interactions.
IntActi P04601. 8 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 156110.

Enzyme and pathway databases

Reactomei REACT_11068. Nef and signal transduction.
REACT_11103. Nef mediated downregulation of MHC class I complex cell surface expression.
REACT_11139. Nef mediated downregulation of CD28 cell surface expression.
REACT_11166. Nef Mediated CD4 Down-regulation.
REACT_11200. Nef Mediated CD8 Down-regulation.
REACT_6359. Budding and maturation of HIV virion.
REACT_6361. Late Phase of HIV Life Cycle.
REACT_6818. Assembly Of The HIV Virion.
REACT_6903. Binding and entry of HIV virion.
REACT_6965. Uncoating of the HIV Virion.

Family and domain databases

Gene3Di 3.30.62.10. 1 hit.
4.10.890.10. 1 hit.
InterProi IPR027480. HIV-1_Nef_anchor.
IPR027481. HIV-1_Nef_core.
IPR001558. HIV_Nef.
[Graphical view ]
Pfami PF00469. F-protein. 1 hit.
[Graphical view ]
SUPFAMi SSF55671. SSF55671. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Polymorphism of the 3' open reading frame of the virus associated with the acquired immune deficiency syndrome, human T-lymphotropic virus type III."
    Ratner L., Starcich B.R., Josephs S.F., Hahn B.H., Reddy E.P., Livak K.J., Petteway S.R. Jr., Pearson M.L., Haseltine W.A., Arya S.K., Wong-staal F.
    Nucleic Acids Res. 13:8219-8229(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. Ratner L., Fisher A., Jagodzinski L.L., Mitsuya H., Liou R.-S., Gallo R.C., Wong-Staal F.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. "Nef induces CD4 endocytosis: requirement for a critical dileucine motif in the membrane-proximal CD4 cytoplasmic domain."
    Aiken C., Konner J., Landau N.R., Lenburg M.E., Trono D.
    Cell 76:853-864(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: Isolate HXB2-R7.
  5. "Nef-induced CD4 and major histocompatibility complex class I (MHC-I) down-regulation are governed by distinct determinants: N-terminal alpha helix and proline repeat of Nef selectively regulate MHC-I trafficking."
    Mangasarian A., Piguet V., Wang J.-K., Chen Y.-L., Trono D.
    J. Virol. 73:1964-1973(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: Isolate HXB2-R7.
  6. "HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate class I major histocompatibility complexes."
    Piguet V., Wan L., Borel C., Mangasarian A., Demaurex N., Thomas G., Trono D.
    Nat. Cell Biol. 2:163-167(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST PACS1, SUBCELLULAR LOCATION.
    Strain: Isolate HXB2-R7.
  7. Cited for: FUNCTION.
  8. "HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway."
    Blagoveshchenskaya A.D., Thomas L., Feliciangeli S.F., Hung C.-H., Thomas G.
    Cell 111:853-866(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF MET-20; 63-GLU--GLU-65; PRO-72 AND PRO-75.
    Strain: Isolate HXB2D.
  9. "HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail."
    Roeth J.F., Williams M., Kasper M.R., Filzen T.M., Collins K.L.
    J. Cell Biol. 167:903-913(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A AP1-NEF-MHC-I COMPLEX.
  10. "Functional characterization of the human immunodeficiency virus type 1 Nef acidic domain."
    Baugh L.L., Garcia J.V., Foster J.L.
    J. Virol. 82:9657-9667(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACIDIC REGION, INTERACTION WITH HOST PACS1, MUTAGENESIS OF 62-GLU--GLU-65.
  11. "HIV-1 Nef binds PACS-2 to assemble a multikinase cascade that triggers major histocompatibility complex class I (MHC-I) down-regulation: analysis using short interfering RNA and knock-out mice."
    Atkins K.M., Thomas L., Youker R.T., Harriff M.J., Pissani F., You H., Thomas G.
    J. Biol. Chem. 283:11772-11784(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOST PACS2, INTERACTION WITH HOST PACS1, MUTAGENESIS OF 62-GLU--GLU-65.
  12. "The tyrosine binding pocket in the adaptor protein 1 (AP-1) mu1 subunit is necessary for Nef to recruit AP-1 to the major histocompatibility complex class I cytoplasmic tail."
    Wonderlich E.R., Williams M., Collins K.L.
    J. Biol. Chem. 283:3011-3022(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A AP1(MU)-NEF-MHC-I COMPLEX.
  13. "Human immunodeficiency virus type 1 Nef incorporation into virions does not increase infectivity."
    Laguette N., Benichou S., Basmaciogullari S.
    J. Virol. 83:1093-1104(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY VIRAL PROTEASE.
  14. "HIV Nef is secreted in exosomes and triggers apoptosis in bystander CD4(+) T cells."
    Lenassi M., Cagney G., Liao M., Vaupotic T., Bartholomeeusen K., Cheng Y., Krogan N.J., Plemenitas A., Peterlin B.M.
    Traffic 11:110-122(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "An MHC-I cytoplasmic domain/HIV-1 Nef fusion protein binds directly to the mu subunit of the AP-1 endosomal coat complex."
    Singh R.K., Lau D., Noviello C.M., Ghosh P., Guatelli J.C.
    PLoS ONE 4:E8364-E8364(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A AP1(MU)-NEF-MHC-I COMPLEX.

Entry informationi

Entry nameiNEF_HV1H2
AccessioniPrimary (citable) accession number: P04601
Secondary accession number(s): O09780, Q85587
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: February 9, 2010
Last modified: October 29, 2014
This is version 119 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

HIV-1 lineages are divided in three main groups, M (for Major), O (for Outlier), and N (for New, or Non-M, Non-O). The vast majority of strains found worldwide belong to the group M. Group O seems to be endemic to and largely confined to Cameroon and neighboring countries in West Central Africa, where these viruses represent a small minority of HIV-1 strains. The group N is represented by a limited number of isolates from Cameroonian persons. The group M is further subdivided in 9 clades or subtypes (A to D, F to H, J and K).

Keywords - Technical termi

3D-structure, Complete proteome, 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