Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

Q63787

- P85A_RAT

UniProt

Q63787 - P85A_RAT

Protein

Phosphatidylinositol 3-kinase regulatory subunit alpha

Gene

Pik3r1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling By similarity.By similarity

    GO - Molecular functioni

    1. 1-phosphatidylinositol-3-kinase activity Source: RGD
    2. 1-phosphatidylinositol-3-kinase regulator activity Source: RGD
    3. ATPase binding Source: RGD
    4. calmodulin binding Source: RGD
    5. ErbB-3 class receptor binding Source: UniProtKB
    6. estrogen receptor binding Source: RGD
    7. insulin-like growth factor receptor binding Source: UniProtKB
    8. insulin receptor binding Source: UniProtKB
    9. insulin receptor substrate binding Source: UniProtKB
    10. phosphatidylinositol 3-kinase binding Source: RGD
    11. phosphatidylinositol 3-kinase regulator activity Source: UniProtKB
    12. phosphoprotein binding Source: RGD
    13. platelet-derived growth factor receptor binding Source: RGD
    14. protein binding Source: IntAct
    15. protein C-terminus binding Source: RGD
    16. protein domain specific binding Source: RGD
    17. protein kinase binding Source: RGD
    18. receptor binding Source: RGD
    19. receptor tyrosine kinase binding Source: RGD
    20. ubiquitin protein ligase binding Source: RGD

    GO - Biological processi

    1. aging Source: RGD
    2. cellular response to fatty acid Source: RGD
    3. cellular response to insulin stimulus Source: RGD
    4. glucose metabolic process Source: RGD
    5. insulin-like growth factor receptor signaling pathway Source: UniProtKB
    6. insulin receptor signaling pathway Source: UniProtKB
    7. negative regulation of blood pressure Source: RGD
    8. negative regulation of cell-cell adhesion Source: RGD
    9. negative regulation of heart rate Source: RGD
    10. negative regulation of muscle cell apoptotic process Source: RGD
    11. negative regulation of proteolysis Source: RGD
    12. negative regulation of smooth muscle cell proliferation Source: RGD
    13. phosphatidylinositol-3-phosphate biosynthetic process Source: GOC
    14. phosphatidylinositol phosphorylation Source: UniProtKB
    15. positive regulation of cell migration Source: RGD
    16. positive regulation of gene expression Source: RGD
    17. positive regulation of myoblast differentiation Source: RGD
    18. positive regulation of protein phosphorylation Source: RGD
    19. regulation of phosphatidylinositol 3-kinase activity Source: RGD
    20. response to amino acid Source: RGD
    21. response to cAMP Source: RGD
    22. response to dexamethasone Source: RGD
    23. response to drug Source: RGD
    24. response to estradiol Source: RGD
    25. response to ethanol Source: RGD
    26. response to fatty acid Source: RGD
    27. response to fructose Source: RGD
    28. response to glucocorticoid Source: RGD
    29. response to growth factor Source: RGD
    30. response to insulin Source: RGD
    31. response to iron(II) ion Source: RGD
    32. response to nutrient Source: RGD
    33. response to progesterone Source: RGD
    34. response to testosterone Source: RGD
    35. response to yeast Source: RGD

    Enzyme and pathway databases

    ReactomeiREACT_196225. Regulation of signaling by CBL.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol 3-kinase regulatory subunit alpha
    Short name:
    PI3-kinase regulatory subunit alpha
    Short name:
    PI3K regulatory subunit alpha
    Short name:
    PtdIns-3-kinase regulatory subunit alpha
    Alternative name(s):
    Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha
    Short name:
    PI3-kinase subunit p85-alpha
    Short name:
    PtdIns-3-kinase regulatory subunit p85-alpha
    Gene namesi
    Name:Pik3r1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3329. Pik3r1.

    Subcellular locationi

    GO - Cellular componenti

    1. 1-phosphatidylinositol-4-phosphate 3-kinase, class IA complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. membrane Source: RGD
    4. neuron projection Source: RGD
    5. nucleus Source: RGD
    6. phosphatidylinositol 3-kinase complex Source: RGD
    7. plasma membrane Source: RGD
    8. protein complex Source: RGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 724723Phosphatidylinositol 3-kinase regulatory subunit alphaPRO_0000080760Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei467 – 4671PhosphotyrosineBy similarity
    Modified residuei580 – 5801PhosphotyrosineBy similarity
    Modified residuei608 – 6081PhosphoserineBy similarity

    Post-translational modificationi

    Polyubiquitinated in T-cells by CBLB; which does not promote proteasomal degradation but impairs association with CD28 and CD3Z upon T-cell activation.By similarity
    Phosphorylated. Tyrosine phosphorylated in response to signaling by FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylated by CSF1R. Phosphorylated on tyrosine residues by TEK/TIE2. Dephosphorylated by PTPRJ. Phosphorylated by PIK3CA at Ser-608; phosphorylation is stimulated by insulin and PDGF. The relevance of phosphorylation by PIK3CA is however unclear. Phosphorylated in response to KIT and KITLG/SCF. Phosphorylated by FGR and ERBB4 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ63787.
    PRIDEiQ63787.

    PTM databases

    PhosphoSiteiQ63787.

    Expressioni

    Tissue specificityi

    The P85-alpha isoform is widely expressed. Expression of the P55-alpha isoform is highest in brain and skeletal muscle. The P50-alpha isoform is abundant in liver with lower levels in brain and muscle.

    Gene expression databases

    GenevestigatoriQ63787.

    Interactioni

    Subunit structurei

    Heterodimer of a regulatory subunit PIK3R1 and a p110 catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts with phosphorylated LAT, LAX1, TRAT1 and LIME1 upon TCR and/or activation. Interacts with phosphorylated TOM1L1. Interacts with CBLB. The SH2 domains interact with the YTHM motif of phosphorylated INSR in vitro. Also interacts with tyrosine-phosphorylated IGF1R in vitro. Interacts with CD28 and CD3Z upon T-cell activation. Interacts with NISCH, SOCS7 and HCST By similarity. Interacts with IRS1 and phosphorylated IRS4. Interacts with RUFY3. Interacts with FGFR1, FGFR2, FGFR3 and FGFR4 (phosphorylated) Probable. Interacts with AXL, FASLG, FER, FGR, HCK, KIT and BCR By similarity. Interacts with PDGFRA (tyrosine phosphorylated) and PDGFRB (tyrosine phosphorylated). Interacts (via SH2 domain) with CSF1R (tyrosine phosphorylated). Interacts with ERBB4 (phosphorylated). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated). Interacts with LYN (via SH3 domain); this enhances enzyme activity By similarity. Interacts with NTRK1 (phosphorylated upon ligand-binding) By similarity. Interacts with PTK2/FAK1.By similarity2 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    A0MZ672EBI-518443,EBI-1392040
    Dnm1P215752EBI-518443,EBI-80070
    Gabra1P628134EBI-518443,EBI-6258192
    Irs1P355703EBI-518443,EBI-520230
    Khdrbs1Q91V332EBI-518443,EBI-518436
    PDE6GP185452EBI-518443,EBI-2622029From a different organism.

    Protein-protein interaction databases

    BioGridi247545. 7 interactions.
    DIPiDIP-33696N.
    IntActiQ63787. 18 interactions.
    MINTiMINT-2880471.

    Structurei

    Secondary structure

    1
    724
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi324 – 3274
    Helixi340 – 3467
    Beta strandi347 – 3493
    Beta strandi358 – 3603
    Beta strandi363 – 3653
    Beta strandi371 – 3744
    Beta strandi377 – 3804
    Beta strandi385 – 3939
    Helixi403 – 4075
    Beta strandi408 – 4114
    Beta strandi415 – 4173

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FU5NMR-A322-431[»]
    1FU6NMR-A322-431[»]
    ProteinModelPortaliQ63787.
    SMRiQ63787. Positions 1-84, 115-309, 328-600, 614-724.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ63787.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 7977SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini113 – 301189Rho-GAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini333 – 42896SH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini624 – 71895SH2 2PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The SH3 domain mediates the binding to CBLB.By similarity

    Sequence similaritiesi

    Belongs to the PI3K p85 subunit family.Curated
    Contains 1 Rho-GAP domain.PROSITE-ProRule annotation
    Contains 2 SH2 domains.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain, SH3 domain

    Phylogenomic databases

    eggNOGiNOG263689.
    HOGENOMiHOG000008438.
    HOVERGENiHBG082100.
    KOiK02649.
    PhylomeDBiQ63787.

    Family and domain databases

    Gene3Di1.10.555.10. 1 hit.
    3.30.505.10. 2 hits.
    InterProiIPR001720. PI3kinase_P85.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR000980. SH2.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR10155. PTHR10155. 1 hit.
    PfamiPF00620. RhoGAP. 1 hit.
    PF00017. SH2. 2 hits.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    PRINTSiPR00678. PI3KINASEP85.
    PR00401. SH2DOMAIN.
    SMARTiSM00324. RhoGAP. 1 hit.
    SM00252. SH2. 2 hits.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 2 hits.
    PROSITEiPS50238. RHOGAP. 1 hit.
    PS50001. SH2. 2 hits.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform p85-alpha (identifier: Q63787-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLVAL GFSDGQEARP    50
    EDIGWLNGYN ETTGERGDFP GTYVEYIGRK RISPPTPKPR PPRPLPVAPG 100
    SSKTEADTEQ PVLTLPDLAE QFAPPDVAPP LLIKLLEAIE KKGLECSTLY 150
    RTQSSSNPAE LRQLLDCDPP SVDLDVFDEH VLADAFKRYL ADLPNPVIPV 200
    AVYNEMMSLA QEVPSSEDYI QLLKKLIRSP NIPHQYWLTL QYLLKHFFKL 250
    SQASSKNLLN ARALSEIFSH VLFRFPAASS DNTEHLIKAV ELLISAEWSE 300
    RQPAPALPPK PPKPTSIANN SMNNNMSLQD AEWYWGDISR EEVNEKLRDT 350
    ADGTFLVRDA STKMHGDYTL TLRKGGNNKL IKIFHRDGKY GFSDPLTFNS 400
    VVELINHYRN ESLAQYNPKL DVKLLYPVSK YQQDQVVKED NIEAVGKKLH 450
    EYNTQFQEKS REYDRLYEEY TRTSQEIQMK RTAIEAFNDT IKIFEEQCHP 500
    QERYSKDYIE KFKREGNEKE IQRIMHNHDK LKSRISEIID SRRRLEEDLK 550
    KQAAEYREID KRMNSIKPDL IQLRKTRDQY LMWLTQKGVR QKKLNEWLGN 600
    ENTEDQYSLV DDDEDLPHHD EKTWNVGSSN RNKAENLLRG KRDGTFLVRE 650
    SSKQGCYACS VVVDGEVKHC VINKTATGYG FAEPYNLYSS LKELVLHYQH 700
    TSLVQHNDSL NVTLAYPVYA QQRR 724
    Length:724
    Mass (Da):83,531
    Last modified:November 1, 1996 - v1
    Checksum:i95C65CF612873B84
    GO
    Isoform p55-alpha (identifier: Q63787-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-270: Missing.
         271-304: VLFRFPAASSDNTEHLIKAVELLISAEWSERQPA → MYTTVWTMEDLDLECAKTDINCGTDLMFYIEMDP

    Show »
    Length:455
    Mass (Da):53,525
    Checksum:iF28B7DCFCB94F170
    GO
    Isoform p50-alpha (identifier: Q63787-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-300: Missing.
         301-306: RQPAPA → MHNLQT

    Show »
    Length:425
    Mass (Da):50,090
    Checksum:i5C77A94F4E24A11D
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 300299Missing in isoform p50-alpha. 2 PublicationsVSP_004711Add
    BLAST
    Alternative sequencei2 – 270269Missing in isoform p55-alpha. 1 PublicationVSP_004709Add
    BLAST
    Alternative sequencei271 – 30434VLFRF…ERQPA → MYTTVWTMEDLDLECAKTDI NCGTDLMFYIEMDP in isoform p55-alpha. 1 PublicationVSP_004710Add
    BLAST
    Alternative sequencei301 – 3066RQPAPA → MHNLQT in isoform p50-alpha. 2 PublicationsVSP_004712

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D64045 mRNA. Translation: BAA18932.1.
    D64048 mRNA. Translation: BAA18933.1.
    U50412 mRNA. Translation: AAC52846.1.
    D78486 mRNA. Translation: BAA24426.1.
    RefSeqiNP_037137.1. NM_013005.1. [Q63787-1]
    UniGeneiRn.10599.

    Genome annotation databases

    GeneIDi25513.
    KEGGirno:25513.
    UCSCiRGD:3329. rat. [Q63787-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D64045 mRNA. Translation: BAA18932.1 .
    D64048 mRNA. Translation: BAA18933.1 .
    U50412 mRNA. Translation: AAC52846.1 .
    D78486 mRNA. Translation: BAA24426.1 .
    RefSeqi NP_037137.1. NM_013005.1. [Q63787-1 ]
    UniGenei Rn.10599.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FU5 NMR - A 322-431 [» ]
    1FU6 NMR - A 322-431 [» ]
    ProteinModelPortali Q63787.
    SMRi Q63787. Positions 1-84, 115-309, 328-600, 614-724.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247545. 7 interactions.
    DIPi DIP-33696N.
    IntActi Q63787. 18 interactions.
    MINTi MINT-2880471.

    PTM databases

    PhosphoSitei Q63787.

    Proteomic databases

    PaxDbi Q63787.
    PRIDEi Q63787.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25513.
    KEGGi rno:25513.
    UCSCi RGD:3329. rat. [Q63787-1 ]

    Organism-specific databases

    CTDi 5295.
    RGDi 3329. Pik3r1.

    Phylogenomic databases

    eggNOGi NOG263689.
    HOGENOMi HOG000008438.
    HOVERGENi HBG082100.
    KOi K02649.
    PhylomeDBi Q63787.

    Enzyme and pathway databases

    Reactomei REACT_196225. Regulation of signaling by CBL.

    Miscellaneous databases

    EvolutionaryTracei Q63787.
    NextBioi 606957.
    PROi Q63787.

    Gene expression databases

    Genevestigatori Q63787.

    Family and domain databases

    Gene3Di 1.10.555.10. 1 hit.
    3.30.505.10. 2 hits.
    InterProi IPR001720. PI3kinase_P85.
    IPR008936. Rho_GTPase_activation_prot.
    IPR000198. RhoGAP_dom.
    IPR000980. SH2.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR10155. PTHR10155. 1 hit.
    Pfami PF00620. RhoGAP. 1 hit.
    PF00017. SH2. 2 hits.
    PF07653. SH3_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00678. PI3KINASEP85.
    PR00401. SH2DOMAIN.
    SMARTi SM00324. RhoGAP. 1 hit.
    SM00252. SH2. 2 hits.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 2 hits.
    PROSITEi PS50238. RHOGAP. 1 hit.
    PS50001. SH2. 2 hits.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel 55-kDa regulatory subunit for phosphatidylinositol 3-kinase structurally similar to p55PIK is generated by alternative splicing of the p85alpha gene."
      Inukai K., Anai M., van Breda E., Hosaka T., Katagiri H., Funaki M., Fukushima Y., Ogihara T., Yazaki Y., Kikuchi M., Oka Y., Asano T.
      J. Biol. Chem. 271:5317-5320(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS P85-ALPHA AND P55-ALPHA).
      Strain: Wistar.
      Tissue: Brain.
    2. "p85alpha gene generates three isoforms of regulatory subunit for phosphatidylinositol 3-kinase (PI 3-Kinase), p50alpha, p55alpha, and p85alpha, with different PI 3-kinase activity elevating responses to insulin."
      Inukai K., Funaki M., Ogihara T., Katagiri H., Kanda A., Anai M., Fukushima Y., Hosaka T., Suzuki M., Shin B., Takata K., Yazaki Y., Kikuchi M., Oka Y., Asano T.
      J. Biol. Chem. 272:7873-7882(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P50-ALPHA).
      Tissue: Liver.
    3. "Structural organization and alternative splicing of the murine phosphoinositide 3-kinase p85 alpha gene."
      Fruman D.A., Cantley L.C., Carpenter C.L.
      Genomics 37:113-121(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM P50-ALPHA).
      Tissue: Liver.
    4. "Signal transduction by fibroblast growth factor receptor-4 (FGFR-4). Comparison with FGFR-1."
      Vainikka S., Joukov V., Wennstrom S., Bergman M., Pelicci P.G., Alitalo K.
      J. Biol. Chem. 269:18320-18326(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVATION BY FGFR4.
    5. "Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase."
      Chen H.C., Appeddu P.A., Isoda H., Guan J.L.
      J. Biol. Chem. 271:26329-26334(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2/FAK1.
    6. "Insulin receptor substrate 1 binds two novel splice variants of the regulatory subunit of phosphatidylinositol 3-kinase in muscle and brain."
      Antonetti D.A., Algenstaedt P., Kahn C.R.
      Mol. Cell. Biol. 16:2195-2203(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IRS1.
    7. "Stimulation of phosphatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins."
      Ong S.H., Hadari Y.R., Gotoh N., Guy G.R., Schlessinger J., Lax I.
      Proc. Natl. Acad. Sci. U.S.A. 98:6074-6079(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVATION BY FGFR1.

    Entry informationi

    Entry nameiP85A_RAT
    AccessioniPrimary (citable) accession number: Q63787
    Secondary accession number(s): O55085, P70544, Q63790
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 138 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