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P49418

- AMPH_HUMAN

UniProt

P49418 - AMPH_HUMAN

Protein

Amphiphysin

Gene

AMPH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton.

    GO - Molecular functioni

    1. phospholipid binding Source: FlyBase
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. endocytosis Source: ProtInc
    2. learning Source: Ensembl
    3. synaptic transmission Source: ProtInc
    4. synaptic vesicle endocytosis Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Amphiphysin
    Gene namesi
    Name:AMPH
    Synonyms:AMPH1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:471. AMPH.

    Subcellular locationi

    GO - Cellular componenti

    1. actin cytoskeleton Source: ProtInc
    2. cell junction Source: UniProtKB-KW
    3. leading edge membrane Source: FlyBase
    4. synaptic vesicle Source: ProtInc
    5. synaptic vesicle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24779.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 695695AmphiphysinPRO_0000192947Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei506 – 5061PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP49418.
    PaxDbiP49418.
    PRIDEiP49418.

    PTM databases

    PhosphoSiteiP49418.

    Miscellaneous databases

    PMAP-CutDBP49418.

    Expressioni

    Tissue specificityi

    Neurons, certain endocrine cell types and spermatocytes.

    Gene expression databases

    ArrayExpressiP49418.
    BgeeiP49418.
    CleanExiHS_AMPH.
    GenevestigatoriP49418.

    Organism-specific databases

    HPAiCAB008559.
    HPA019828.
    HPA019829.

    Interactioni

    Subunit structurei

    Heterodimer with BIN1. Binds SH3GLB1 and AP2A2 By similarity. Interacts with AP2B1. Interacts with REPS1 and SGIP1; may be involved in clathrin-mediated endocytosis.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CltaP080813EBI-7121510,EBI-916140From a different organism.
    Necap1P696823EBI-7121510,EBI-7592718From a different organism.
    Necap1Q9CR956EBI-7121510,EBI-7592476From a different organism.
    Tfap2aP581972EBI-7121510,EBI-7069641From a different organism.

    Protein-protein interaction databases

    BioGridi106770. 40 interactions.
    DIPiDIP-40729N.
    IntActiP49418. 8 interactions.
    MINTiMINT-109264.
    STRINGi9606.ENSP00000348602.

    Structurei

    Secondary structure

    1
    695
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi20 – 223
    Helixi24 – 8461
    Helixi92 – 11524
    Helixi117 – 12610
    Helixi128 – 15629
    Helixi163 – 19634
    Helixi198 – 23740
    Helixi382 – 3843

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KY7X-ray2.15P322-330[»]
    1UTCX-ray2.30P/Q379-387[»]
    3SOGX-ray2.30A34-236[»]
    4ATMX-ray1.78A1-242[»]
    ProteinModelPortaliP49418.
    SMRiP49418. Positions 19-239, 618-694.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49418.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 240217BARPROSITE-ProRule annotationAdd
    BLAST
    Domaini622 – 69574SH3PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili10 – 8374Sequence AnalysisAdd
    BLAST
    Coiled coili144 – 19148Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BAR domain.PROSITE-ProRule annotation
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH3 domain

    Phylogenomic databases

    eggNOGiNOG264615.
    HOVERGENiHBG004224.
    KOiK12562.
    OMAiMICNLAE.
    OrthoDBiEOG7XWPND.
    PhylomeDBiP49418.
    TreeFamiTF313542.

    Family and domain databases

    Gene3Di1.20.1270.60. 1 hit.
    InterProiIPR027267. AH/BAR-dom.
    IPR003005. Amphiphysin.
    IPR003017. Amphiphysin_1.
    IPR004148. BAR_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF03114. BAR. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view]
    PRINTSiPR01251. AMPHIPHYSIN.
    PR01252. AMPHIPHYSIN1.
    PR00452. SH3DOMAIN.
    SMARTiSM00721. BAR. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS51021. BAR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49418-1) [UniParc]FASTAAdd to Basket

    Also known as: 128 kDa

    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

    MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE    50
    AEGTRLQREL RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE 100
    KCDVLWEDFH QKLVDGSLLT LDTYLGQFPD IKNRIAKRSR KLVDYDSARH 150
    HLEALQSSKR KDESRISKAE EEFQKAQKVF EEFNVDLQEE LPSLWSRRVG 200
    FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD KAFTIQGAPS 250
    DSGPLRIAKT PSPPEEPSPL PSPTASPNHT LAPASPAPAR PRSPSQTRKG 300
    PPVPPLPKVT PTKELQQENI ISFFEDNFVP EISVTTPSQN EVPEVKKEET 350
    LLDLDFDPFK PEVTPAGSAG VTHSPMSQTL PWDLWTTSTD LVQPASGGSF 400
    NGFTQPQDTS LFTMQTDQSM ICNLAESEQA PPTEPKAEEP LAAVTPAVGL 450
    DLGMDTRAEE PVEEAVIIPG ADADAAVGTL VSAAEGAPGE EAEAEKATVP 500
    AGEGVSLEEA KIGTETTEGA ESAQPEAEEL EATVPQEKVI PSVVIEPASN 550
    HEEEGENEIT IGAEPKETTE DAAPPGPTSE TPELATEQKP IQDPQPTPSA 600
    PAMGAADQLA SAREASQELP PGFLYKVETL HDFEAANSDE LTLQRGDVVL 650
    VVPSDSEADQ DAGWLVGVKE SDWLQYRDLA TYKGLFPENF TRRLD 695
    Length:695
    Mass (Da):76,257
    Last modified:February 1, 1996 - v1
    Checksum:i78B4F75AB75BA357
    GO
    Isoform 2 (identifier: P49418-2) [UniParc]FASTAAdd to Basket

    Also known as: 108 kDa

    The sequence of this isoform differs from the canonical sequence as follows:
         425-466: Missing.

    Show »
    Length:653
    Mass (Da):71,929
    Checksum:i44C1115E3E70B6A9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti218 – 2181K → E.
    Corresponds to variant rs35166354 [ dbSNP | Ensembl ].
    VAR_053004
    Natural varianti376 – 3761M → I.
    Corresponds to variant rs17171345 [ dbSNP | Ensembl ].
    VAR_053005
    Natural varianti496 – 4961K → T.1 Publication
    Corresponds to variant rs35024632 [ dbSNP | Ensembl ].
    VAR_053006

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei425 – 46642Missing in isoform 2. 1 PublicationVSP_000245Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07616 mRNA. Translation: AAA21865.1.
    X81438 mRNA. Translation: CAA57197.1.
    AF034996 mRNA. Translation: AAC02977.1.
    AC011309 Genomic DNA. Translation: AAS07391.1.
    AC012490 Genomic DNA. Translation: AAS07563.1.
    AC007245 Genomic DNA. Translation: AAS07541.1.
    CH236951 Genomic DNA. Translation: EAL23989.1.
    CH236951 Genomic DNA. Translation: EAL23990.1.
    CH471073 Genomic DNA. Translation: EAW94110.1.
    CH471073 Genomic DNA. Translation: EAW94111.1.
    BC034376 mRNA. Translation: AAH34376.1.
    CCDSiCCDS47574.1. [P49418-2]
    CCDS5456.1. [P49418-1]
    PIRiS62400.
    RefSeqiNP_001626.1. NM_001635.3. [P49418-1]
    NP_647477.1. NM_139316.2. [P49418-2]
    UniGeneiHs.592182.

    Genome annotation databases

    EnsembliENST00000325590; ENSP00000317441; ENSG00000078053. [P49418-2]
    ENST00000356264; ENSP00000348602; ENSG00000078053. [P49418-1]
    GeneIDi273.
    KEGGihsa:273.
    UCSCiuc003tgu.3. human. [P49418-1]
    uc003tgv.3. human. [P49418-2]

    Polymorphism databases

    DMDMi1351924.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U07616 mRNA. Translation: AAA21865.1 .
    X81438 mRNA. Translation: CAA57197.1 .
    AF034996 mRNA. Translation: AAC02977.1 .
    AC011309 Genomic DNA. Translation: AAS07391.1 .
    AC012490 Genomic DNA. Translation: AAS07563.1 .
    AC007245 Genomic DNA. Translation: AAS07541.1 .
    CH236951 Genomic DNA. Translation: EAL23989.1 .
    CH236951 Genomic DNA. Translation: EAL23990.1 .
    CH471073 Genomic DNA. Translation: EAW94110.1 .
    CH471073 Genomic DNA. Translation: EAW94111.1 .
    BC034376 mRNA. Translation: AAH34376.1 .
    CCDSi CCDS47574.1. [P49418-2 ]
    CCDS5456.1. [P49418-1 ]
    PIRi S62400.
    RefSeqi NP_001626.1. NM_001635.3. [P49418-1 ]
    NP_647477.1. NM_139316.2. [P49418-2 ]
    UniGenei Hs.592182.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KY7 X-ray 2.15 P 322-330 [» ]
    1UTC X-ray 2.30 P/Q 379-387 [» ]
    3SOG X-ray 2.30 A 34-236 [» ]
    4ATM X-ray 1.78 A 1-242 [» ]
    ProteinModelPortali P49418.
    SMRi P49418. Positions 19-239, 618-694.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106770. 40 interactions.
    DIPi DIP-40729N.
    IntActi P49418. 8 interactions.
    MINTi MINT-109264.
    STRINGi 9606.ENSP00000348602.

    PTM databases

    PhosphoSitei P49418.

    Polymorphism databases

    DMDMi 1351924.

    Proteomic databases

    MaxQBi P49418.
    PaxDbi P49418.
    PRIDEi P49418.

    Protocols and materials databases

    DNASUi 273.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000325590 ; ENSP00000317441 ; ENSG00000078053 . [P49418-2 ]
    ENST00000356264 ; ENSP00000348602 ; ENSG00000078053 . [P49418-1 ]
    GeneIDi 273.
    KEGGi hsa:273.
    UCSCi uc003tgu.3. human. [P49418-1 ]
    uc003tgv.3. human. [P49418-2 ]

    Organism-specific databases

    CTDi 273.
    GeneCardsi GC07M038423.
    HGNCi HGNC:471. AMPH.
    HPAi CAB008559.
    HPA019828.
    HPA019829.
    MIMi 600418. gene.
    neXtProti NX_P49418.
    PharmGKBi PA24779.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264615.
    HOVERGENi HBG004224.
    KOi K12562.
    OMAi MICNLAE.
    OrthoDBi EOG7XWPND.
    PhylomeDBi P49418.
    TreeFami TF313542.

    Miscellaneous databases

    EvolutionaryTracei P49418.
    GeneWikii Amphiphysin.
    GenomeRNAii 273.
    NextBioi 1081.
    PMAP-CutDB P49418.
    PROi P49418.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49418.
    Bgeei P49418.
    CleanExi HS_AMPH.
    Genevestigatori P49418.

    Family and domain databases

    Gene3Di 1.20.1270.60. 1 hit.
    InterProi IPR027267. AH/BAR-dom.
    IPR003005. Amphiphysin.
    IPR003017. Amphiphysin_1.
    IPR004148. BAR_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF03114. BAR. 1 hit.
    PF14604. SH3_9. 1 hit.
    [Graphical view ]
    PRINTSi PR01251. AMPHIPHYSIN.
    PR01252. AMPHIPHYSIN1.
    PR00452. SH3DOMAIN.
    SMARTi SM00721. BAR. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS51021. BAR. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Autoimmunity in stiff-man syndrome with breast cancer is targeted to the C-terminal region of human amphiphysin, a protein similar to the yeast proteins, Rvs167 and Rvs161."
      David C., Solimena M., de Camilli P.
      FEBS Lett. 351:73-79(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Cerebellum.
    2. "Primary structure of human amphiphysin, the dominant autoantigen of paraneoplastic stiff-man syndrome, and mapping of its gene (AMPH) to chromosome 7p13-p14."
      Yamamoto R., Li X., Winter S., Francke U., Kilimann M.W.
      Hum. Mol. Genet. 4:265-268(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. "Expression of amphiphysin I, an autoantigen of paraneoplastic neurological syndromes, in breast cancer."
      Floyd S.R., Butler M.H., Cremona O., David C., Freyberg Z., Zhang X., Solimena M., Tokunaga A., Ishizu H., Tsutsui K., De Camilli P.V.
      Mol. Med. 4:29-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Mammary gland.
    4. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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], VARIANT THR-496.
      Tissue: Brain.
    8. "Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly."
      Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y., Mills I.G., Benmerah A., McMahon H.T.
      PLoS Biol. 4:E262-E262(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AP2B1.
    9. "Intersectin 1 forms complexes with SGIP1 and Reps1 in clathrin-coated pits."
      Dergai O., Novokhatska O., Dergai M., Skrypkina I., Tsyba L., Moreau J., Rynditch A.
      Biochem. Biophys. Res. Commun. 402:408-413(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH REPS1 AND SGIP1.
    10. "Accessory protein recruitment motifs in clathrin-mediated endocytosis."
      Brett T.J., Traub L.M., Fremont D.H.
      Structure 10:797-809(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 322-330 IN COMPLEX WITH AP2A2.

    Entry informationi

    Entry nameiAMPH_HUMAN
    AccessioniPrimary (citable) accession number: P49418
    Secondary accession number(s): A4D1X8
    , A4D1X9, O43538, Q75MJ8, Q75MK5, Q75MM3, Q8N4G0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 141 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Antibodies against AMPH are detected in patients with stiff-man syndrome, a rare disease of the central nervous system characterized by progressive rigidity of the body musculature with superimposed painful spasms.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3