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O08773

- RGS14_RAT

UniProt

O08773 - RGS14_RAT

Protein

Regulator of G-protein signaling 14

Gene

Rgs14

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Acts as a regulator of G protein signaling (RGS). Modulates G protein alpha subunits nucleotide exchange and hydrolysis activities by functioning either as a GTPase-activating protein (GAP), thereby driving G protein alpha subunits into their inactive GDP-bound form, or as a GDP-dissociation inhibitor (GDI). Confers GDI activity on G(i) alpha subunits GNAI1 and GNAI3, but not G(o) alpha subunit GNAO1 and G(i) alpha subunit GNAI2. Confers GAP activity on G(o) alpha subunit GNAI0 and G(i) alpha subunits GNAI2 and GNAI3. May act as a scaffold integrating G protein and Ras/Raf MAPkinase signaling pathways. Inhibits platelet-derived growth factor (PDGF)-stimulated ERK1/ERK2 phosphorylation; a process depending on its interaction with HRAS and that is reversed by G(i) alpha subunit GNAI1. Acts as a positive modulator of microtubule polymerisation and spindle organization through a G(i)-alpha-dependent mechanism. Plays a role in cell division; required for completion of the first mitotic division of the embryo. Involved in visual memory processing capacity; when overexpressed in the V2 secondary visual cortex area. Involved in hippocampal-based learning and memory; acts as a suppressor of synaptic plasticity in CA2 neurons. Required for the nerve growth factor (NGF)-mediated neurite outgrowth. Involved in stress resistance.7 Publications

    GO - Molecular functioni

    1. GDP-dissociation inhibitor activity Source: UniProtKB
    2. G-protein alpha-subunit binding Source: RGD
    3. GTPase activator activity Source: UniProtKB
    4. microtubule binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein kinase binding Source: UniProtKB
    7. receptor signaling complex scaffold activity Source: UniProtKB
    8. receptor signaling protein activity Source: UniProtKB

    GO - Biological processi

    1. cell division Source: UniProtKB
    2. chromosome segregation Source: UniProtKB
    3. intracellular signal transduction Source: GOC
    4. learning Source: UniProtKB
    5. long-term memory Source: UniProtKB
    6. long-term synaptic potentiation Source: UniProtKB
    7. mitotic nuclear division Source: Ensembl
    8. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
    9. negative regulation of MAP kinase activity Source: UniProtKB
    10. negative regulation of synaptic plasticity Source: UniProtKB
    11. nucleocytoplasmic transport Source: UniProtKB
    12. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
    13. positive regulation of GTPase activity Source: GOC
    14. positive regulation of neurogenesis Source: UniProtKB
    15. regulation of DNA-templated transcription in response to stress Source: UniProtKB
    16. regulation of G-protein coupled receptor protein signaling pathway Source: RGD
    17. response to oxidative stress Source: UniProtKB
    18. spindle organization Source: UniProtKB
    19. termination of G-protein coupled receptor signaling pathway Source: InterPro
    20. visual learning Source: UniProtKB
    21. zygote asymmetric cell division Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, GTPase activation, Signal transduction inhibitor

    Keywords - Biological processi

    Cell cycle, Cell division

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulator of G-protein signaling 14
    Short name:
    RGS14
    Gene namesi
    Name:Rgs14
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 17

    Organism-specific databases

    RGDi620003. Rgs14.

    Subcellular locationi

    Nucleus. NucleusPML body By similarity. Cytoplasm. Membrane. Cell membrane. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Cytoplasmcytoskeletonspindle By similarity. Cytoplasmcytoskeletonspindle pole. Cell projectiondendrite By similarity. Cell projectiondendritic spine By similarity. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity
    Note: Associates with the perinuclear sheaths of microtubules (MTs) surrounding the pronuclei, prior to segregating to the anastral mitotic apparatus and subsequently the barrel-shaped cytoplasmic bridge between the nascent nuclei of the emerging 2-cell embryo. Localizes to a perinuclear compartment near the microtubule-organizing center (MTOC). Expressed in the nucleus during interphase and segregates to the centrosomes and astral MTs during mitosis. Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. Relocalizes to the nucleus in PML nuclear bodies in respons to heat stress. Colocalizes with RIC8A in CA2 hippocampal neurons By similarity. Localizes with spindle poles during metaphase. Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner. Recruited from the cytosol to the plasma membrane by the inactive GDP-bound forms of G(i) alpha subunits GNAI1 and GNAI3. Recruited from the cytosol to membranes by the active GTP-bound form of HRAS. Colocalizes with G(i) alpha subunit GNAI1 and RIC8A at the plasma membrane. Colocalizes with BRAF and RAF1 in both the cytoplasm and membranes.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. centrosome Source: UniProtKB
    3. cytoplasm Source: UniProtKB
    4. dendrite Source: UniProtKB
    5. dendritic spine Source: UniProtKB
    6. intermediate filament cytoskeleton Source: Ensembl
    7. microtubule Source: UniProtKB-KW
    8. nuclear body Source: UniProtKB
    9. nucleus Source: UniProtKB
    10. plasma membrane Source: UniProtKB
    11. PML body Source: UniProtKB-SubCell
    12. postsynaptic density Source: UniProtKB
    13. postsynaptic membrane Source: UniProtKB-KW
    14. spindle Source: UniProtKB
    15. spindle pole Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Microtubule, Nucleus, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi258 – 2581S → A: Inhibits phosphorylation; when associated with A-494. 1 Publication
    Mutagenesisi333 – 3331R → L: Abolishes the inhibition of PDGF-mediated ERK1/ERK2 phosphorylation. Inhibits interaction with HRAS and does not colocalize with active GTP-bound form of HRAS at membranes. Does not inhibit interaction with BRAF or RAF1. 1 Publication
    Mutagenesisi406 – 4061H → A: Does not inhibit interaction and colocalization with active GTP-bound form of HRAS at membranes. Does not inhibit interaction with BRAF or RAF1. 1 Publication
    Mutagenesisi494 – 4941T → A: Does not increase the GDI activity against GNAI1. Does not alter GTPase activity against GNAO1 or GNAI1. Inhibits phosphorylation; when associated with A-258. 1 Publication
    Mutagenesisi494 – 4941T → D: Increases the GDI activity against GNAI1. Does not alter GTPase activity against GNAO1 or GNAI1. 1 Publication
    Mutagenesisi494 – 4941T → E: Increases the GDI activity against GNAI1. Does not alter GTPase activity against GNAO1 or GNAI1. 1 Publication
    Mutagenesisi508 – 5081Q → L: Inhibits the interaction with GNAI1. 1 Publication
    Mutagenesisi518 – 5181L → Y: Increases the interaction with GNAI1. 1 Publication
    Mutagenesisi525 – 5251V → W: Increases the interaction with GNAI1. 1 Publication
    Mutagenesisi529 – 5291F → W: Increases the interaction with GNAI1. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 544544Regulator of G-protein signaling 14PRO_0000204219Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei20 – 201PhosphoserineBy similarity
    Modified residuei42 – 421PhosphoserineBy similarity
    Modified residuei45 – 451PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by PKC. Phosphorylation is increased in presence of forskolin and may enhance the GDI activity on G(i) alpha subunit GNAI1.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiO08773.

    PTM databases

    PhosphoSiteiO08773.

    Expressioni

    Tissue specificityi

    Expressed in neurons of the V2 secondary visual cortex area (at protein level). Expressed at high levels in the brain cortex, hippocampus, striatum, thalamus and substantia nigra, in the lung, and spleen. Low expression has been found in heart, liver, skeletal muscle and testis.2 Publications

    Gene expression databases

    GenevestigatoriO08773.

    Interactioni

    Subunit structurei

    Interacts with GNAO1 and GNAI2. Interacts (via RGS and GoLoco domains) GNAI1; the interaction occurs in the centrosomes. Interacts with RABGEF1; the interactions is GTP-dependent. Interacts with RAP2A; the interactions is GTP-dependent and does not alter its function on G(i) alpha subunits either as GAP or as GDI. Associates with microtubules By similarity. Found in a complex with at least BRAF, HRAS, MAP2K1, MAPK3 and RGS14. Interacts with RIC8A (via C-terminus). Interacts (via RBD 1 domain) with HRAS (active GTP-bound form preferentially). Interacts (via RBD domains) with BRAF (via N-terminus); the interaction mediates the formation of a ternary complex with RAF1. Interacts (via RBD domains) with RAF1 (via N-terminus); the interaction mediates the formation of a ternary complex with BRAF. Interacts with KRAS (active GTP-bound form preferentially), MRAS (active GTP-bound form preferentially), NRAS (active GTP-bound form preferentially) and RRAS (active GTP-bound form preferentially). Interacts with GNAI1 (via active GTP- or inactive GDP-bound forms); the interaction prevents association of RGS14 with centrosomes or nuclear localization. Interacts with GNAI2. Interacts with GNAI3 (via active GTP- or inactive GDP-bound forms); the interaction prevents association of RGS14 with centrosomes or nuclear localization.By similarity5 Publications

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000021596.

    Structurei

    Secondary structure

    1
    544
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi497 – 5059
    Turni506 – 5094
    Helixi510 – 5134
    Helixi521 – 5244

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KJYX-ray2.70B/D496-531[»]
    ProteinModelPortaliO08773.
    SMRiO08773. Positions 56-189, 362-456, 496-531.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO08773.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini67 – 184118RGSPROSITE-ProRule annotationAdd
    BLAST
    Domaini300 – 37172RBD 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini373 – 44371RBD 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini497 – 51923GoLocoPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni297 – 424128Necessary for interaction with RABGEF1By similarityAdd
    BLAST

    Domaini

    The RGS domain is necessary for GTPase-activating protein (GAP) activity for G subunits and localization to the nucleus and centrosomes.1 Publication
    The GoLoco domain is necessary for GDP-dissociation inhibitor (GDI) activity, translocation out of the nucleus and interaction with G(i) alpha subunits GNAI1, GNAI2 and GNAI3.1 Publication
    The RBD domains are necessary for localization to the nucleus and centrosomes.1 Publication

    Sequence similaritiesi

    Contains 1 GoLoco domain.PROSITE-ProRule annotation
    Contains 2 RBD (Ras-binding) domains.PROSITE-ProRule annotation
    Contains 1 RGS domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG282424.
    GeneTreeiENSGT00700000104412.
    HOGENOMiHOG000049111.
    HOVERGENiHBG061568.
    InParanoidiO08773.
    KOiK17706.
    OMAiPPRTQDK.
    OrthoDBiEOG7XDBF0.
    PhylomeDBiO08773.
    TreeFamiTF328814.

    Family and domain databases

    Gene3Di1.10.196.10. 1 hit.
    InterProiIPR003109. GoLoco_motif.
    IPR003116. Raf-like_ras-bd.
    IPR024066. Regulat_G_prot_signal_dom1.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF02188. GoLoco. 1 hit.
    PF02196. RBD. 2 hits.
    PF00615. RGS. 1 hit.
    [Graphical view]
    PRINTSiPR01301. RGSPROTEIN.
    SMARTiSM00390. GoLoco. 1 hit.
    SM00455. RBD. 2 hits.
    SM00315. RGS. 1 hit.
    [Graphical view]
    SUPFAMiSSF48097. SSF48097. 1 hit.
    SSF54236. SSF54236. 2 hits.
    PROSITEiPS50877. GOLOCO. 1 hit.
    PS50898. RBD. 2 hits.
    PS50132. RGS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O08773-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGKPKHLGV PNGRMVLAVS DGELTSTSGS QAQGEGRGSS LSIHSLPSGP    50
    SSPFSTDEQP VASWAQSFER LLQDPRGLAY FTEFLKKEFS AENVTFWQAC 100
    ERFQQIPASD TKQLAQEAHN IYHEFLSSQA LSPVNIDRQA WLSEEVLAQP 150
    RPDMFRAQQL QIFNLMKFDS YARFVKSPLY QECLLAEAEG RPLREPGSSH 200
    LGSPDTARKK PKLKPGKSLP LGVEELGQLP LAEGRPLRKS FRREMPGGAV 250
    NSALRRESQG SLNSSASLDL GFLAFVSSKS ESHRKSLGSG EGESESRPGK 300
    YCCVYLPDGT ASLALARPGL TIRDMLAGIC EKRGLSLPDI KVYLVGKEQK 350
    ALVLDQDCTV LADQEVRLEN RITFQLELVG LERVVRISAK PTKRLQEALQ 400
    PILAKHGLSL DQVVLHRPGE KQLVDLENLV SSVASQTLVL DTLPDAKTRE 450
    ASSIPPCRSQ GCLPRTQTKD SHLPPLSSSL SVEDASGSTG KRQTCDIEGL 500
    VELLNRVQSS GAHDQRGLLR KEDLVLPEFL QLPSQRPGSQ EAPP 544
    Length:544
    Mass (Da):59,492
    Last modified:July 1, 1997 - v1
    Checksum:iFF6B24BD2F593B4E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U92279 mRNA. Translation: AAC53175.1.
    PIRiJC5503.
    RefSeqiNP_446216.1. NM_053764.1.
    UniGeneiRn.9795.

    Genome annotation databases

    EnsembliENSRNOT00000021596; ENSRNOP00000021596; ENSRNOG00000015616.
    GeneIDi114705.
    KEGGirno:114705.
    UCSCiRGD:620003. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U92279 mRNA. Translation: AAC53175.1 .
    PIRi JC5503.
    RefSeqi NP_446216.1. NM_053764.1.
    UniGenei Rn.9795.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KJY X-ray 2.70 B/D 496-531 [» ]
    ProteinModelPortali O08773.
    SMRi O08773. Positions 56-189, 362-456, 496-531.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000021596.

    PTM databases

    PhosphoSitei O08773.

    Proteomic databases

    PRIDEi O08773.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000021596 ; ENSRNOP00000021596 ; ENSRNOG00000015616 .
    GeneIDi 114705.
    KEGGi rno:114705.
    UCSCi RGD:620003. rat.

    Organism-specific databases

    CTDi 10636.
    RGDi 620003. Rgs14.

    Phylogenomic databases

    eggNOGi NOG282424.
    GeneTreei ENSGT00700000104412.
    HOGENOMi HOG000049111.
    HOVERGENi HBG061568.
    InParanoidi O08773.
    KOi K17706.
    OMAi PPRTQDK.
    OrthoDBi EOG7XDBF0.
    PhylomeDBi O08773.
    TreeFami TF328814.

    Miscellaneous databases

    EvolutionaryTracei O08773.
    NextBioi 618837.
    PROi O08773.

    Gene expression databases

    Genevestigatori O08773.

    Family and domain databases

    Gene3Di 1.10.196.10. 1 hit.
    InterProi IPR003109. GoLoco_motif.
    IPR003116. Raf-like_ras-bd.
    IPR024066. Regulat_G_prot_signal_dom1.
    IPR016137. Regulat_G_prot_signal_superfam.
    IPR000342. RGS_dom.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF02188. GoLoco. 1 hit.
    PF02196. RBD. 2 hits.
    PF00615. RGS. 1 hit.
    [Graphical view ]
    PRINTSi PR01301. RGSPROTEIN.
    SMARTi SM00390. GoLoco. 1 hit.
    SM00455. RBD. 2 hits.
    SM00315. RGS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48097. SSF48097. 1 hit.
    SSF54236. SSF54236. 2 hits.
    PROSITEi PS50877. GOLOCO. 1 hit.
    PS50898. RBD. 2 hits.
    PS50132. RGS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor Activity."
      Kimple R.J., De Vries L., Tronchere H., Behe C.I., Morris R.A., Gist Farquhar M., Siderovski D.P.
      J. Biol. Chem. 276:29275-29281(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GNAI1; GNAI2 AND GNAI3.
    3. "Phosphorylation of RGS14 by protein kinase A potentiates its activity toward G alpha i."
      Hollinger S., Ramineni S., Hepler J.R.
      Biochemistry 42:811-819(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, MUTAGENESIS OF SER-258 AND THR-494.
    4. "The RGS14 GoLoco domain discriminates among Galphai isoforms."
      Mittal V., Linder M.E.
      J. Biol. Chem. 279:46772-46778(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN.
    5. "Localization of the GoLoco motif carrier regulator of G-protein signalling 12 and 14 proteins in monkey and rat brain."
      Lopez-Aranda M.F., Acevedo M.J., Carballo F.J., Gutierrez A., Khan Z.U.
      Eur. J. Neurosci. 23:2971-2982(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Brain.
    6. "Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR domain of RGS14 influence its dynamic subcellular localization."
      Shu F.J., Ramineni S., Amyot W., Hepler J.R.
      Cell. Signal. 19:163-176(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GNAI1 AND GNAI3, SUBCELLULAR LOCATION.
    7. "Structure-based protocol for identifying mutations that enhance protein-protein binding affinities."
      Sammond D.W., Eletr Z.M., Purbeck C., Kimple R.J., Siderovski D.P., Kuhlman B.
      J. Mol. Biol. 371:1392-1404(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF GLN-508; LEU-518; VAL-525 AND PHE-529.
    8. Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH BRAF; HRAS; MAP2K1 AND MAPK3, INTERACTION WITH BRAF; HRAS; KRAS; MRAS; NRAS; RAF1 AND RRAS.
    9. Cited for: FUNCTION, TISSUE SPECIFICITY.
    10. "RGS14 is a multifunctional scaffold that integrates G protein and Ras/Raf MAPkinase signalling pathways."
      Shu F.J., Ramineni S., Hepler J.R.
      Cell. Signal. 22:366-376(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BRAF; HRAS AND RAF1, MUTAGENESIS OF ARG-333 AND HIS-406, SUBCELLULAR LOCATION.
    11. "Regulation of longevity by regulator of G-protein signaling (RGS) protein, Loco."
      Lin Y.R., Kim K., Yang Y., Ivessa A., Sadoshima J., Park Y.
      Aging Cell 10:438-447(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Activation of the regulator of G protein signaling 14-Galphai1-GDP signaling complex is regulated by resistance to inhibitors of cholinesterase-8A."
      Vellano C.P., Shu F.J., Ramineni S., Yates C.K., Tall G.G., Hepler J.R.
      Biochemistry 50:752-762(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH GNAI1 AND RIC8A, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiRGS14_RAT
    AccessioniPrimary (citable) accession number: O08773
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 107 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, 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