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P04692

- TPM1_RAT

UniProt

P04692 - TPM1_RAT

Protein

Tropomyosin alpha-1 chain

Gene

Tpm1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (04 Apr 2006)
      Previous versions | rss
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    Functioni

    Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.

    GO - Molecular functioni

    1. actin binding Source: RGD
    2. actin filament binding Source: RGD
    3. protein homodimerization activity Source: RGD
    4. protein N-terminus binding Source: RGD

    GO - Biological processi

    1. actin filament capping Source: RGD
    2. cardiac muscle contraction Source: RGD
    3. muscle contraction Source: RGD
    4. muscle filament sliding Source: BHF-UCL
    5. negative regulation of cell migration Source: BHF-UCL
    6. positive regulation of ATPase activity Source: BHF-UCL
    7. positive regulation of cell adhesion Source: BHF-UCL
    8. positive regulation of stress fiber assembly Source: BHF-UCL
    9. regulation of ATPase activity Source: RGD
    10. ruffle organization Source: BHF-UCL
    11. wound healing Source: BHF-UCL

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_224772. Smooth Muscle Contraction.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tropomyosin alpha-1 chain
    Alternative name(s):
    Alpha-tropomyosin
    Tropomyosin-1
    Gene namesi
    Name:Tpm1
    Synonyms:Alpha-tm, Tpma
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 8

    Organism-specific databases

    RGDi3898. Tpm1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. cytoskeleton Source: UniProtKB-SubCell
    3. protein complex Source: RGD

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 284284Tropomyosin alpha-1 chainPRO_0000205624Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Cross-linki77 – 77Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei283 – 2831Phosphoserine; by DAPK1By similarity

    Post-translational modificationi

    Phosphorylated at Ser-283 by DAPK1 in response to oxidative stress and this phosphorylation enhances stress fiber formation in endothelial cells.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP04692.
    PRIDEiP04692.

    PTM databases

    PhosphoSiteiP04692.

    Expressioni

    Gene expression databases

    ArrayExpressiP04692.
    GenevestigatoriP04692.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta chain. Interacts with HRG (via the HRR domain); the interaction contributes to the antiangiogenic properties of the histidine/proline-rich region (HRR) of HRG By similarity.By similarity

    Protein-protein interaction databases

    BioGridi246968. 4 interactions.
    DIPiDIP-29020N.
    IntActiP04692. 2 interactions.

    Structurei

    Secondary structure

    1
    284
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 1413
    Helixi100 – 1034
    Turni104 – 1074
    Helixi108 – 12316
    Helixi125 – 20884
    Helixi254 – 28128

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IHQNMR-A/B206-209[»]
    1MV4NMR-A/B251-284[»]
    1TMZNMR-A/B1-14[»]
    2B9CX-ray2.30A/B89-208[»]
    2G9JNMR-A/B1-14[»]
    C/D251-284[»]
    3AZDX-ray0.98A/B206-209[»]
    ProteinModelPortaliP04692.
    SMRiP04692. Positions 8-284.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04692.

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1 – 284284Add
    BLAST

    Domaini

    The molecule is in a coiled coil structure that is formed by 2 polypeptide chains. The sequence exhibits a prominent seven-residues periodicity.

    Sequence similaritiesi

    Belongs to the tropomyosin family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG304012.
    GeneTreeiENSGT00550000074494.
    HOVERGENiHBG107404.
    KOiK10373.
    PhylomeDBiP04692.
    TreeFamiTF351519.

    Family and domain databases

    InterProiIPR000533. Tropomyosin.
    [Graphical view]
    PfamiPF00261. Tropomyosin. 1 hit.
    [Graphical view]
    PRINTSiPR00194. TROPOMYOSIN.
    PROSITEiPS00326. TROPOMYOSIN. 1 hit.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P04692-1) [UniParc]FASTAAdd to Basket

    Also known as: Skeletal muscle

    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

    MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL    50
    KGTEDELDKY SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD 100
    RAQERLATAL QKLEEAEKAA DESERGMKVI ESRAQKDEEK MEIQEIQLKE 150
    AKHIAEDADR KYEEVARKLV IIESDLERAE ERAELSEGKC AELEEELKTV 200
    TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE FAERSVTKLE 250
    KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI 284
    Length:284
    Mass (Da):32,681
    Last modified:April 4, 2006 - v3
    Checksum:iE25609F597A72F4D
    GO
    Isoform 2 (identifier: P04692-2) [UniParc]FASTAAdd to Basket

    Also known as: Smooth muscle

    The sequence of this isoform differs from the canonical sequence as follows:
         41-80: DELVSLQKKL...LELAEKKATD → EDISAKEKLL...LLAADETAAK
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLHQTLLELNNM

    Show »
    Length:284
    Mass (Da):32,676
    Checksum:i35056246C3FFA678
    GO
    Isoform 3 (identifier: P04692-3) [UniParc]FASTAAdd to Basket

    Also known as: Brain TMBr-1

    The sequence of this isoform differs from the canonical sequence as follows:
         259-284: ELYAQKLKYKAISEELDHALNDMTSI → QLYHQLEQNRRLTNELKLALNED

    Show »
    Length:281
    Mass (Da):32,495
    Checksum:iE8CA06AF0B96E230
    GO
    Isoform 4 (identifier: P04692-4) [UniParc]FASTAAdd to Basket

    Also known as: Brain TMBr-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: MDAIKKKMQM...LELAEKKATD → MAGSSSLEAV...LDQERKLRET
         259-284: ELYAQKLKYKAISEELDHALNDMTSI → KFLCFSPPKTPSSSRMSHLSELCICLLSS

    Show »
    Length:251
    Mass (Da):28,704
    Checksum:iC361AFDF972CC474
    GO
    Isoform 5 (identifier: P04692-5) [UniParc]FASTAAdd to Basket

    Also known as: Brain TMBr-3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: MDAIKKKMQM...LELAEKKATD → MAGSSSLEAV...LDQERKLRET
         259-284: ELYAQKLKYKAISEELDHALNDMTSI → QLYHQLEQNRRLTNELKLALNED

    Show »
    Length:245
    Mass (Da):28,343
    Checksum:iFD9E17F1B920550F
    GO
    Isoform 6 (identifier: P04692-6) [UniParc]FASTAAdd to Basket

    Also known as: Fibroblast TM-2

    The sequence of this isoform differs from the canonical sequence as follows:
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLHQTLLELNNM

    Show »
    Length:284
    Mass (Da):32,731
    Checksum:iCD7A66BFAEA04540
    GO
    Isoform 7 (identifier: P04692-7) [UniParc]FASTAAdd to Basket

    Also known as: Fibroblast 5a

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: MDAIKKKMQM...LELAEKKATD → MAGSSSLEAV...LDQERKLRET
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLHQTLLELNNM

    Show »
    Length:248
    Mass (Da):28,579
    Checksum:i3D2B523AFAB11BF2
    GO
    Isoform 8 (identifier: P04692-8) [UniParc]FASTAAdd to Basket

    Also known as: Fibroblast 5b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: MDAIKKKMQM...LELAEKKATD → MAGSSSLEAV...LDQERKLRET
         189-212: KCAELEEELKTVTNNLKSLEAQAE → QVRQLEEQLRIMDQTLKALMAAED
         258-284: DELYAQKLKYKAISEELDHALNDMTSI → EKVAHAKEENLSMHQMLHQTLLELNNM

    Show »
    Length:248
    Mass (Da):28,718
    Checksum:i1AC7D77131E5F251
    GO

    Sequence cautioni

    Isoform 2 : The sequence CAA26258.1 differs from that shown. Reason: miscellaneous discrepancy

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521G → A in AAA42252. (PubMed:2320008)Curated
    Sequence conflicti279 – 2791N → K in AAA21801. (PubMed:3558368)Curated
    Sequence conflicti279 – 2791N → K in AAA21805. (PubMed:3352602)Curated
    Isoform 7 (identifier: P04692-7)
    Sequence conflicti239 – 2391H → D in AAA18098. (PubMed:2022655)Curated
    Isoform 8 (identifier: P04692-8)
    Sequence conflicti239 – 2391H → D in AAA18099. (PubMed:2022655)Curated
    Isoform 2 (identifier: P04692-2)
    Sequence conflicti260 – 2601V → G in CAA26258. (PubMed:3838802)Curated
    Sequence conflicti275 – 2751H → D in CAA26258. (PubMed:3838802)Curated
    Isoform 6 (identifier: P04692-6)
    Sequence conflicti275 – 2751H → D in AAA42290. (PubMed:2022655)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8080MDAIK…KKATD → MAGSSSLEAVRRKIRSLQEQ ADAAEERAGSLQRELDQERK LRET in isoform 4, isoform 5, isoform 7 and isoform 8. 2 PublicationsVSP_006581Add
    BLAST
    Alternative sequencei41 – 8040DELVS…KKATD → EDISAKEKLLRASEDERDRV LEELHKAEDSLLAADETAAK in isoform 2. 1 PublicationVSP_006582Add
    BLAST
    Alternative sequencei189 – 21224KCAEL…EAQAE → QVRQLEEQLRIMDQTLKALM AAED in isoform 8. 1 PublicationVSP_006583Add
    BLAST
    Alternative sequencei258 – 28427DELYA…DMTSI → EKVAHAKEENLSMHQMLHQT LLELNNM in isoform 2, isoform 6, isoform 7 and isoform 8. 2 PublicationsVSP_006584Add
    BLAST
    Alternative sequencei259 – 28426ELYAQ…DMTSI → QLYHQLEQNRRLTNELKLAL NED in isoform 3 and isoform 5. 1 PublicationVSP_006585Add
    BLAST
    Alternative sequencei259 – 28426ELYAQ…DMTSI → KFLCFSPPKTPSSSRMSHLS ELCICLLSS in isoform 4. 1 PublicationVSP_006586Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15474
    , M15472, M15473, M16432, M16433 Genomic DNA. Translation: AAA21801.1.
    M18135
    , M16432, M15472, M16433, M15473 Genomic DNA. Translation: AAA21803.1. Different termination.
    M18135, M16432, M16433 Genomic DNA. Translation: AAA21804.1.
    M18135
    , M16432, M15472, M16433 Genomic DNA. Translation: AAA21805.1.
    X02411 mRNA. Translation: CAA26258.1. Sequence problems.
    M34135 mRNA. Translation: AAA42252.1.
    M34134 mRNA. Translation: AAA42253.1.
    M34136 mRNA. Translation: AAA42254.1.
    M34137 Genomic DNA. Translation: AAA40773.1.
    M34138 Genomic DNA. Translation: AAA40774.1.
    M60666 mRNA. Translation: AAA42290.1.
    M60668 mRNA. Translation: AAA18098.1.
    M60669 mRNA. Translation: AAA18099.1.
    X02412 mRNA. Translation: CAA26259.1.
    PIRiA34787.
    A39816.
    B27407.
    B34787.
    C34787.
    C39816.
    D39816.
    RefSeqiNP_001029241.1. NM_001034069.1.
    NP_001029244.1. NM_001034072.1. [P04692-3]
    NP_001029245.1. NM_001034073.1.
    NP_001029246.1. NM_001034074.1.
    NP_001029247.1. NM_001034075.1.
    NP_062004.1. NM_019131.2. [P04692-4]
    XP_006243449.1. XM_006243387.1. [P04692-1]
    XP_006243456.1. XM_006243394.1. [P04692-5]
    UniGeneiRn.87540.

    Genome annotation databases

    EnsembliENSRNOT00000024575; ENSRNOP00000024575; ENSRNOG00000018184. [P04692-3]
    ENSRNOT00000024617; ENSRNOP00000024617; ENSRNOG00000018184.
    ENSRNOT00000048044; ENSRNOP00000048499; ENSRNOG00000018184. [P04692-1]
    GeneIDi24851.
    KEGGirno:24851.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15474
    , M15472 , M15473 , M16432 , M16433 Genomic DNA. Translation: AAA21801.1 .
    M18135
    , M16432 , M15472 , M16433 , M15473 Genomic DNA. Translation: AAA21803.1 . Different termination.
    M18135 , M16432 , M16433 Genomic DNA. Translation: AAA21804.1 .
    M18135
    , M16432 , M15472 , M16433 Genomic DNA. Translation: AAA21805.1 .
    X02411 mRNA. Translation: CAA26258.1 . Sequence problems.
    M34135 mRNA. Translation: AAA42252.1 .
    M34134 mRNA. Translation: AAA42253.1 .
    M34136 mRNA. Translation: AAA42254.1 .
    M34137 Genomic DNA. Translation: AAA40773.1 .
    M34138 Genomic DNA. Translation: AAA40774.1 .
    M60666 mRNA. Translation: AAA42290.1 .
    M60668 mRNA. Translation: AAA18098.1 .
    M60669 mRNA. Translation: AAA18099.1 .
    X02412 mRNA. Translation: CAA26259.1 .
    PIRi A34787.
    A39816.
    B27407.
    B34787.
    C34787.
    C39816.
    D39816.
    RefSeqi NP_001029241.1. NM_001034069.1.
    NP_001029244.1. NM_001034072.1. [P04692-3 ]
    NP_001029245.1. NM_001034073.1.
    NP_001029246.1. NM_001034074.1.
    NP_001029247.1. NM_001034075.1.
    NP_062004.1. NM_019131.2. [P04692-4 ]
    XP_006243449.1. XM_006243387.1. [P04692-1 ]
    XP_006243456.1. XM_006243394.1. [P04692-5 ]
    UniGenei Rn.87540.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1IHQ NMR - A/B 206-209 [» ]
    1MV4 NMR - A/B 251-284 [» ]
    1TMZ NMR - A/B 1-14 [» ]
    2B9C X-ray 2.30 A/B 89-208 [» ]
    2G9J NMR - A/B 1-14 [» ]
    C/D 251-284 [» ]
    3AZD X-ray 0.98 A/B 206-209 [» ]
    ProteinModelPortali P04692.
    SMRi P04692. Positions 8-284.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 246968. 4 interactions.
    DIPi DIP-29020N.
    IntActi P04692. 2 interactions.

    PTM databases

    PhosphoSitei P04692.

    Proteomic databases

    PaxDbi P04692.
    PRIDEi P04692.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000024575 ; ENSRNOP00000024575 ; ENSRNOG00000018184 . [P04692-3 ]
    ENSRNOT00000024617 ; ENSRNOP00000024617 ; ENSRNOG00000018184 .
    ENSRNOT00000048044 ; ENSRNOP00000048499 ; ENSRNOG00000018184 . [P04692-1 ]
    GeneIDi 24851.
    KEGGi rno:24851.

    Organism-specific databases

    CTDi 7168.
    RGDi 3898. Tpm1.

    Phylogenomic databases

    eggNOGi NOG304012.
    GeneTreei ENSGT00550000074494.
    HOVERGENi HBG107404.
    KOi K10373.
    PhylomeDBi P04692.
    TreeFami TF351519.

    Enzyme and pathway databases

    Reactomei REACT_224772. Smooth Muscle Contraction.

    Miscellaneous databases

    EvolutionaryTracei P04692.
    NextBioi 604620.

    Gene expression databases

    ArrayExpressi P04692.
    Genevestigatori P04692.

    Family and domain databases

    InterProi IPR000533. Tropomyosin.
    [Graphical view ]
    Pfami PF00261. Tropomyosin. 1 hit.
    [Graphical view ]
    PRINTSi PR00194. TROPOMYOSIN.
    PROSITEi PS00326. TROPOMYOSIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Comparison of alpha-tropomyosin sequences from smooth and striated muscle."
      Ruiz-Opazo N., Weinberger J., Nadal-Ginard B.
      Nature 315:67-70(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. "Alpha-tropomyosin gene organization. Alternative splicing of duplicated isotype-specific exons accounts for the production of smooth and striated muscle isoforms."
      Ruiz-Opazo N., Nadal-Ginard B.
      J. Biol. Chem. 262:4755-4765(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    3. "The rat alpha-tropomyosin gene generates a minimum of six different mRNAs coding for striated, smooth, and nonmuscle isoforms by alternative splicing."
      Wieczorek D.F., Smith C.W., Nadal-Ginard B.
      Mol. Cell. Biol. 8:679-694(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    4. "Three novel brain tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene through the use of alternative promoters and alternative RNA processing."
      Lees-Miller J.P., Goodwin L.O., Helfman D.M.
      Mol. Cell. Biol. 10:1729-1742(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 3; 4 AND 5).
      Tissue: Brain.
    5. "Four fibroblast tropomyosin isoforms are expressed from the rat alpha-tropomyosin gene via alternative RNA splicing and the use of two promoters."
      Goodwin L.O., Lees-Miller J.P., Leonard M.A., Cheley S.B., Helfman D.M.
      J. Biol. Chem. 266:8408-8415(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 7 AND 8).
    6. "Cloning and characterization of cDNA sequences corresponding to myosin light chains 1, 2, and 3, troponin-C, troponin-T, alpha-tropomyosin, and alpha-actin."
      Garfinkel L.I., Periasamy M., Nadal-Ginard B.
      J. Biol. Chem. 257:11078-11086(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    7. Lubec G., Afjehi-Sadat L., Diao W., Kang S.U., Lubec S.
      Submitted (SEP-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 92-101; 141-149; 218-226 AND 251-270, PARTIAL PROTEIN SEQUENCE (ISOFORMS 4/5/7/8), IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain, Hippocampus and Spinal cord.
    8. "Specificity of dimer formation in tropomyosins: influence of alternatively spliced exons on homodimer and heterodimer assembly."
      Gimona M., Watakabe A., Helfman D.M.
      Proc. Natl. Acad. Sci. U.S.A. 92:9776-9780(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.

    Entry informationi

    Entry nameiTPM1_RAT
    AccessioniPrimary (citable) accession number: P04692
    Secondary accession number(s): P06469
    , P18342, P18343, P18344, P19354, Q53X09, Q63582, Q63608, Q63609
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: April 4, 2006
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 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