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Q8BH64

- EHD2_MOUSE

UniProt

Q8BH64 - EHD2_MOUSE

Protein

EH domain-containing protein 2

Gene

Ehd2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Plays a role in membrane reorganization in response to nucleotide hydrolysis. Binds to liposomes and deforms them into tubules. Plays a role in membrane trafficking between the plasma membrane and endosomes. Important for the internalization of GLUT4. Required for fusion of myoblasts to skeletal muscle myotubes. Required for normal translocation of FER1L5 to the plasma membrane. Binds ATP; does not bind GTP.3 Publications

    Enzyme regulationi

    The very low intrinsic ATPase activity is increased upon interaction with liposomes.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei220 – 2201ATP
    Binding sitei258 – 2581ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi65 – 728ATP
    Calcium bindingi494 – 50512Add
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium ion binding Source: InterPro
    3. GTPase activity Source: InterPro
    4. GTP binding Source: InterPro
    5. protein binding Source: MGI
    6. protein domain specific binding Source: MGI

    GO - Biological processi

    1. cortical actin cytoskeleton organization Source: MGI
    2. endocytic recycling Source: UniProtKB
    3. endocytosis Source: MGI
    4. positive regulation of endocytic recycling Source: UniProtKB
    5. positive regulation of myoblast fusion Source: UniProtKB
    6. protein localization to plasma membrane Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    ATP-binding, Calcium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198649. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    EH domain-containing protein 2
    Gene namesi
    Name:Ehd2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:2154274. Ehd2.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein; Cytoplasmic side. Endosome membrane By similarity; Peripheral membrane protein By similarity
    Note: Colocalizes with GLUT4 in intracellular tubulovesicular structures that are associated with cortical F-actin. Colocalizes with FER1L5 at plasma membrane in myoblasts and myotubes.

    GO - Cellular componenti

    1. caveola Source: MGI
    2. membrane Source: MGI
    3. perinuclear region of cytoplasm Source: MGI
    4. plasma membrane Source: UniProtKB
    5. recycling endosome membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi65 – 651G → R: Inhibits myoblast fusion. 1 Publication
    Mutagenesisi72 – 721T → A: Abolishes ATP binding. 1 Publication
    Mutagenesisi94 – 941T → A: Abolishes increase of intrinsic ATPase activity upon interaction with membranes. 1 Publication
    Mutagenesisi157 – 1571I → Q: Increases intrinsic ATPase activity. 1 Publication
    Mutagenesisi167 – 1671R → E: Increases intrinsic ATPase activity. 1 Publication
    Mutagenesisi322 – 3221F → A: Abolishes localization at the plasma membrane; reduces increase of intrinsic ATPase activity upon interaction with membranes. 1 Publication
    Mutagenesisi324 – 3241K → D: Abolishes localization at the plasma membrane. 1 Publication
    Mutagenesisi327 – 3271K → D: Abolishes localization at the plasma membrane; abolishes increase of intrinsic ATPase activity upon interaction with membranes. 1 Publication
    Mutagenesisi328 – 3281K → D: Abolishes localization at the plasma membrane; reduces increase of intrinsic ATPase activity upon interaction with membranes. 1 Publication
    Mutagenesisi329 – 3291K → D: Abolishes localization at the plasma membrane. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 543543EH domain-containing protein 2PRO_0000322643Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei438 – 4381Phosphoserine2 Publications
    Modified residuei468 – 4681PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8BH64.
    PaxDbiQ8BH64.
    PRIDEiQ8BH64.

    PTM databases

    PhosphoSiteiQ8BH64.

    Expressioni

    Tissue specificityi

    Detected in lung and adipocytes. Detected at lower levels in heart and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiQ8BH64.
    BgeeiQ8BH64.
    CleanExiMM_EHD2.
    GenevestigatoriQ8BH64.

    Interactioni

    Subunit structurei

    Interacts with EHD1. May also interact with EHD3 and EHD4 By similarity. Interacts with Asn-Pro-Phe (NPF) motifs in target proteins. Homodimer and homooligomer. Interacts with MYOF and EHBP1. Interacts with FER1L5 (via second C2 domain).By similarity4 Publications

    Protein-protein interaction databases

    DIPiDIP-46806N.
    IntActiQ8BH64. 2 interactions.

    Structurei

    Secondary structure

    1
    543
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 3212
    Helixi34 – 396
    Helixi42 – 443
    Helixi52 – 565
    Beta strandi60 – 667
    Helixi71 – 799
    Beta strandi96 – 1027
    Beta strandi104 – 1096
    Beta strandi134 – 1418
    Helixi145 – 1473
    Beta strandi150 – 1534
    Helixi171 – 18111
    Beta strandi183 – 1908
    Helixi191 – 1933
    Helixi198 – 20710
    Helixi211 – 2133
    Beta strandi214 – 2196
    Turni220 – 2234
    Helixi226 – 24419
    Beta strandi252 – 2554
    Beta strandi258 – 2603
    Helixi268 – 28316
    Turni284 – 2885
    Helixi289 – 31729
    Beta strandi320 – 3234
    Helixi324 – 34623
    Helixi350 – 3523
    Helixi356 – 3649
    Helixi368 – 3703
    Helixi376 – 38712
    Helixi389 – 40315
    Helixi405 – 4073
    Beta strandi411 – 4144
    Helixi416 – 4194
    Helixi447 – 45913
    Beta strandi466 – 4683
    Helixi469 – 4768
    Helixi477 – 4793
    Helixi483 – 49311
    Beta strandi498 – 5025
    Helixi503 – 51816
    Helixi528 – 5303
    Helixi533 – 5353

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QPTX-ray3.10A1-543[»]
    4CIDX-ray3.00A5-543[»]
    ProteinModelPortaliQ8BH64.
    SMRiQ8BH64. Positions 1-539.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8BH64.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 286232Dynamin-type GAdd
    BLAST
    Domaini449 – 53789EHPROSITE-ProRule annotationAdd
    BLAST
    Domaini481 – 51636EF-handPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The EH domain interacts with Asn-Pro-Phe (NPF) motifs of target proteins.

    Sequence similaritiesi

    Contains 1 EF-hand domain.PROSITE-ProRule annotation
    Contains 1 EH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG136252.
    GeneTreeiENSGT00700000104190.
    HOGENOMiHOG000242040.
    HOVERGENiHBG018183.
    InParanoidiQ8BH64.
    KOiK12469.
    OMAiAPNEGKL.
    OrthoDBiEOG757CX9.
    PhylomeDBiQ8BH64.
    TreeFamiTF314429.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR001401. Dynamin_GTPase.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000261. EPS15_homology.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00350. Dynamin_N. 1 hit.
    [Graphical view]
    SMARTiSM00027. EH. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS50031. EH. 1 hit.
    PS51718. G_DYNAMIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8BH64-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFSWLKKGGA RGQRPEAIRT VTSSLKELYR TKLLPLEEHY RFGSFHSPAL    50
    EDADFDGKPM VLVAGQYSTG KTSFIQYLLE QEVPGSRVGP EPTTDCFVAV 100
    MHGETEGTVP GNALVVDPEK PFRKLNPFGN TFLNRFMCAQ LPNQVLESIS 150
    IIDTPGILSG AKQRVSRGYD FPAVLRWFAE RVDLIILLFD AHKLEISDEF 200
    SEAIGALRGH EDKIRVVLNK ADMVETQQLM RVYGALMWAL GKVVGTPEVL 250
    RVYIGSFWSQ PLLVPDNRRL FELEEQDLFR DIQGLPRHAA LRKLNDLVKR 300
    ARLVRVHAYI ISYLKKEMPT VFGKENKKKQ LILKLPVIFA KIQLEHHISP 350
    GDFPDCQKMQ ELLMAHDFTK FHSLKPKLLE ALDDMLAQDI AKLMPLLRQE 400
    ELESVEAGVQ GGAFEGTRMG PFVERGPDEA IEDGEEGSED DAEWVVTKDK 450
    SKYDEIFYNL APADGKLSGS KAKTWMVGTK LPNSVLGRIW KLSDVDRDGM 500
    LDDEEFALAS HLIEAKLEGH GLPTNLPRRL VPPSKRRQKG SAE 543
    Length:543
    Mass (Da):61,174
    Last modified:March 1, 2003 - v1
    Checksum:i47637795B0B1096E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti181 – 1811R → S in BAC32789. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY531389 mRNA. Translation: AAS48536.1.
    AK031203 mRNA. Translation: BAC27298.1.
    AK046566 mRNA. Translation: BAC32789.1.
    AK048356 mRNA. Translation: BAC33310.1.
    AK050243 mRNA. Translation: BAC34142.1.
    AK084455 mRNA. Translation: BAC39188.1.
    AK085016 mRNA. Translation: BAC39339.1.
    BC113161 mRNA. Translation: AAI13162.1.
    CCDSiCCDS20842.1.
    RefSeqiNP_694708.2. NM_153068.3.
    UniGeneiMm.138215.
    Mm.438817.

    Genome annotation databases

    EnsembliENSMUST00000098799; ENSMUSP00000096397; ENSMUSG00000074364.
    GeneIDi259300.
    KEGGimmu:259300.
    UCSCiuc009fgt.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY531389 mRNA. Translation: AAS48536.1 .
    AK031203 mRNA. Translation: BAC27298.1 .
    AK046566 mRNA. Translation: BAC32789.1 .
    AK048356 mRNA. Translation: BAC33310.1 .
    AK050243 mRNA. Translation: BAC34142.1 .
    AK084455 mRNA. Translation: BAC39188.1 .
    AK085016 mRNA. Translation: BAC39339.1 .
    BC113161 mRNA. Translation: AAI13162.1 .
    CCDSi CCDS20842.1.
    RefSeqi NP_694708.2. NM_153068.3.
    UniGenei Mm.138215.
    Mm.438817.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QPT X-ray 3.10 A 1-543 [» ]
    4CID X-ray 3.00 A 5-543 [» ]
    ProteinModelPortali Q8BH64.
    SMRi Q8BH64. Positions 1-539.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-46806N.
    IntActi Q8BH64. 2 interactions.

    PTM databases

    PhosphoSitei Q8BH64.

    Proteomic databases

    MaxQBi Q8BH64.
    PaxDbi Q8BH64.
    PRIDEi Q8BH64.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000098799 ; ENSMUSP00000096397 ; ENSMUSG00000074364 .
    GeneIDi 259300.
    KEGGi mmu:259300.
    UCSCi uc009fgt.1. mouse.

    Organism-specific databases

    CTDi 30846.
    MGIi MGI:2154274. Ehd2.

    Phylogenomic databases

    eggNOGi NOG136252.
    GeneTreei ENSGT00700000104190.
    HOGENOMi HOG000242040.
    HOVERGENi HBG018183.
    InParanoidi Q8BH64.
    KOi K12469.
    OMAi APNEGKL.
    OrthoDBi EOG757CX9.
    PhylomeDBi Q8BH64.
    TreeFami TF314429.

    Enzyme and pathway databases

    Reactomei REACT_198649. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    EvolutionaryTracei Q8BH64.
    NextBioi 392043.
    PROi Q8BH64.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BH64.
    Bgeei Q8BH64.
    CleanExi MM_EHD2.
    Genevestigatori Q8BH64.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR001401. Dynamin_GTPase.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    IPR000261. EPS15_homology.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00350. Dynamin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00027. EH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00018. EF_HAND_1. 1 hit.
    PS50222. EF_HAND_2. 1 hit.
    PS50031. EH. 1 hit.
    PS51718. G_DYNAMIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "EHD2 and the novel EH domain binding protein EHBP1 couple endocytosis to the actin cytoskeleton."
      Guilherme A., Soriano N.A., Bose S., Holik J., Bose A., Pomerleau D.P., Furcinitti P., Leszyk J., Corvera S., Czech M.P.
      J. Biol. Chem. 279:10593-10605(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EHBP1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
      Strain: C57BL/6.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Adipose tissue, Embryonic eye, Embryonic head, Embryonic lung, Forelimb and Liver.
    3. "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].
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    5. "The endocytic recycling protein EHD2 interacts with myoferlin to regulate myoblast fusion."
      Doherty K.R., Demonbreun A.R., Wallace G.Q., Cave A., Posey A.D., Heretis K., Pytel P., McNally E.M.
      J. Biol. Chem. 283:20252-20260(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYOF, MUTAGENESIS OF GLY-65, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    7. "Endocytic recycling proteins EHD1 and EHD2 interact with fer-1-like-5 (Fer1L5) and mediate myoblast fusion."
      Posey A.D. Jr., Pytel P., Gardikiotes K., Demonbreun A.R., Rainey M., George M., Band H., McNally E.M.
      J. Biol. Chem. 286:7379-7388(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH FER1L5 AND MYOF.
    8. "Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling."
      Daumke O., Lundmark R., Vallis Y., Martens S., Butler P.J.G., McMahon H.T.
      Nature 449:923-927(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND CALCIUM IONS, SUBUNIT, SUBCELLULAR LOCATION, ENZYME REGULATION, MUTAGENESIS OF THR-72; THR-94; ILE-157; ARG-167; PHE-322; LYS-324; LYS-327; LYS-328 AND LYS-329.

    Entry informationi

    Entry nameiEHD2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BH64
    Secondary accession number(s): Q8BL28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 18, 2008
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 116 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3