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P58252

- EF2_MOUSE

UniProt

P58252 - EF2_MOUSE

Protein

Elongation factor 2

Gene

Eef2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi26 – 338GTPBy similarity
    Nucleotide bindingi104 – 1085GTPBy similarity
    Nucleotide bindingi158 – 1614GTPBy similarity

    GO - Molecular functioni

    1. GTPase activity Source: MGI
    2. GTP binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. translation elongation factor activity Source: UniProtKB-KW

    GO - Biological processi

    1. GTP catabolic process Source: GOC
    2. hematopoietic progenitor cell differentiation Source: MGI
    3. translational elongation Source: MGI

    Keywords - Molecular functioni

    Elongation factor

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elongation factor 2
    Short name:
    EF-2
    Gene namesi
    Name:Eef2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:95288. Eef2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. polysome Source: MGI
    3. ribonucleoprotein complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 858857Elongation factor 2PRO_0000091002Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei54 – 541PhosphothreonineBy similarity
    Modified residuei57 – 571PhosphothreonineBy similarity
    Modified residuei59 – 591PhosphothreonineBy similarity
    Modified residuei152 – 1521N6-succinyllysine1 Publication
    Modified residuei235 – 2351N6-acetyllysineBy similarity
    Modified residuei239 – 2391N6-acetyllysine1 Publication
    Modified residuei272 – 2721N6-acetyllysine; alternate1 Publication
    Modified residuei272 – 2721N6-succinyllysine; alternate1 Publication
    Modified residuei275 – 2751N6-acetyllysine1 Publication
    Modified residuei435 – 4351PhosphothreonineBy similarity
    Modified residuei439 – 4391N6-acetyllysine1 Publication
    Modified residuei445 – 4451N6-acetyllysine1 Publication
    Modified residuei502 – 5021PhosphoserineBy similarity
    Modified residuei572 – 5721N6-succinyllysine1 Publication
    Modified residuei619 – 6191N6-acetyllysine1 Publication
    Modified residuei715 – 7151DiphthamideBy similarity

    Post-translational modificationi

    Phosphorylation by EF-2 kinase completely inactivates EF-2.By similarity
    Diphthamide is 2-[3-carboxyamido-3-(trimethyl-ammonio)propyl]histidine. Diphthamide can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin A, thus arresting protein synthesis By similarity.By similarity
    ISGylated.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP58252.
    PaxDbiP58252.
    PRIDEiP58252.

    2D gel databases

    COMPLUYEAST-2DPAGEP58252.
    REPRODUCTION-2DPAGEP58252.

    PTM databases

    PhosphoSiteiP58252.

    Expressioni

    Gene expression databases

    ArrayExpressiP58252.
    BgeeiP58252.
    CleanExiMM_EEF2.
    GenevestigatoriP58252.

    Interactioni

    Subunit structurei

    Component of the mRNA surveillance SURF complex, at least composed of ERF1, ERF3 (ERF3A or ERF3B), EEF2, UPF1/RENT1, SMG1, SMG8 and SMG9.By similarity

    Protein-protein interaction databases

    BioGridi199387. 8 interactions.
    IntActiP58252. 11 interactions.
    MINTiMINT-1862939.

    Structurei

    3D structure databases

    ProteinModelPortaliP58252.
    SMRiP58252. Positions 3-858.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 362346tr-type GPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily.PROSITE-ProRule annotation
    Contains 1 tr-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0480.
    GeneTreeiENSGT00750000117652.
    HOGENOMiHOG000231589.
    HOVERGENiHBG001838.
    InParanoidiP58252.
    KOiK03234.
    OMAiRWAPVPE.
    OrthoDBiEOG7WDN1S.
    PhylomeDBiP58252.
    TreeFamiTF300575.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR000795. EF_GTP-bd_dom.
    IPR009022. EFG_III-V.
    IPR000640. EFG_V.
    IPR027417. P-loop_NTPase.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR005225. Small_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR005517. Transl_elong_EFG/EF2_IV.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view]
    PfamiPF00679. EFG_C. 1 hit.
    PF14492. EFG_II. 1 hit.
    PF03764. EFG_IV. 1 hit.
    PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view]
    PRINTSiPR00315. ELONGATNFCT.
    SMARTiSM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view]
    SUPFAMiSSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsiTIGR00231. small_GTP. 1 hit.
    PROSITEiPS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P58252-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVNFTVDQIR AIMDKKANIR NMSVIAHVDH GKSTLTDSLV CKAGIIASAR    50
    AGETRFTDTR KDEQERCITI KSTAISLFYE LSENDLNFIK QSKDGSGFLI 100
    NLIDSPGHVD FSSEVTAALR VTDGALVVVD CVSGVCVQTE TVLRQAIAER 150
    IKPVLMMNKM DRALLELQLE PEELYQTFQR IVENVNVIIS TYGEGESGPM 200
    GNIMIDPVLG TVGFGSGLHG WAFTLKQFAE MYVAKFAAKG EGQLSAAERA 250
    KKVEDMMKKL WGDRYFDPAN GKFSKSANSP DGKKLPRTFC QLILDPIFKV 300
    FDAIMNFRKE ETAKLIEKLD IKLDSEDKDK EGKPLLKAVM RRWLPAGDAL 350
    LQMITIHLPS PVTAQKYRCE LLYEGPPDDE AAMGIKSCDP KGPLMMYISK 400
    MVPTSDKGRF YAFGRVFSGV VSTGLKVRIM GPNYTPGKKE DLYLKPIQRT 450
    ILMMGRYVEP IEDVPCGNIV GLVGVDQFLV KTGTITTFEH AHNMRVMKFS 500
    VSPVVRVAVE AKNPADLPKL VEGLKRLAKS DPMVQCIIEE SGEHIIAGAG 550
    ELHLEICLKD LEEDHACIPI KKSDPVVSYR ETVSEESNVL CLSKSPNKHN 600
    RLYMKARPFP DGLAEDIDKG EVSARQELKA RARYLAEKYE WDVAEARKIW 650
    CFGPDGTGPN ILTDITKGVQ YLNEIKDSVV AGFQWATKEG ALCEENMRGV 700
    RFDVHDVTLH ADAIHRGGGQ IIPTARRCLY ASVLTAQPRL MEPIYLVEIQ 750
    CPEQVVGGIY GVLNRKRGHV FEESQVAGTP MFVVKAYLPV NESFGFTADL 800
    RSNTGGQAFP QCVFDHWQIL PGDPFDNSSR PSQVVAETRK RKGLKEGIPA 850
    LDNFLDKL 858
    Length:858
    Mass (Da):95,314
    Last modified:January 23, 2007 - v2
    Checksum:i0569DFFB9B1DB5F6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK040474 mRNA. Translation: BAC30601.1.
    AK077866 mRNA. Translation: BAC37041.1.
    AK087985 mRNA. Translation: BAC40076.1.
    AK145545 mRNA. Translation: BAE26498.1.
    AK146947 mRNA. Translation: BAE27556.1.
    AK151487 mRNA. Translation: BAE30440.1.
    AK151812 mRNA. Translation: BAE30710.1.
    AK151945 mRNA. Translation: BAE30820.1.
    AK152146 mRNA. Translation: BAE30983.1.
    AK152447 mRNA. Translation: BAE31226.1.
    AK152587 mRNA. Translation: BAE31336.1.
    AK152826 mRNA. Translation: BAE31527.1.
    AK153275 mRNA. Translation: BAE31861.1.
    AK155325 mRNA. Translation: BAE33192.1.
    AK159806 mRNA. Translation: BAE35386.1.
    AK163063 mRNA. Translation: BAE37177.1.
    AK166212 mRNA. Translation: BAE38631.1.
    AK166596 mRNA. Translation: BAE38882.1.
    AK166747 mRNA. Translation: BAE38989.1.
    AK166751 mRNA. Translation: BAE38992.1.
    AK166851 mRNA. Translation: BAE39070.1.
    AK166968 mRNA. Translation: BAE39151.1.
    AK167093 mRNA. Translation: BAE39249.1.
    AK167109 mRNA. Translation: BAE39257.1.
    AK167115 mRNA. Translation: BAE39263.1.
    AK167221 mRNA. Translation: BAE39346.1.
    AK168794 mRNA. Translation: BAE40627.1.
    AK168827 mRNA. Translation: BAE40654.1.
    AK168874 mRNA. Translation: BAE40692.1.
    AK169013 mRNA. Translation: BAE40810.1.
    BC007152 mRNA. Translation: AAH07152.1.
    CCDSiCCDS35993.1.
    RefSeqiNP_031933.1. NM_007907.2.
    UniGeneiMm.326799.
    Mm.482883.
    Mm.486637.

    Genome annotation databases

    EnsembliENSMUST00000047864; ENSMUSP00000046101; ENSMUSG00000034994.
    GeneIDi13629.
    KEGGimmu:13629.
    UCSCiuc007gge.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK040474 mRNA. Translation: BAC30601.1 .
    AK077866 mRNA. Translation: BAC37041.1 .
    AK087985 mRNA. Translation: BAC40076.1 .
    AK145545 mRNA. Translation: BAE26498.1 .
    AK146947 mRNA. Translation: BAE27556.1 .
    AK151487 mRNA. Translation: BAE30440.1 .
    AK151812 mRNA. Translation: BAE30710.1 .
    AK151945 mRNA. Translation: BAE30820.1 .
    AK152146 mRNA. Translation: BAE30983.1 .
    AK152447 mRNA. Translation: BAE31226.1 .
    AK152587 mRNA. Translation: BAE31336.1 .
    AK152826 mRNA. Translation: BAE31527.1 .
    AK153275 mRNA. Translation: BAE31861.1 .
    AK155325 mRNA. Translation: BAE33192.1 .
    AK159806 mRNA. Translation: BAE35386.1 .
    AK163063 mRNA. Translation: BAE37177.1 .
    AK166212 mRNA. Translation: BAE38631.1 .
    AK166596 mRNA. Translation: BAE38882.1 .
    AK166747 mRNA. Translation: BAE38989.1 .
    AK166751 mRNA. Translation: BAE38992.1 .
    AK166851 mRNA. Translation: BAE39070.1 .
    AK166968 mRNA. Translation: BAE39151.1 .
    AK167093 mRNA. Translation: BAE39249.1 .
    AK167109 mRNA. Translation: BAE39257.1 .
    AK167115 mRNA. Translation: BAE39263.1 .
    AK167221 mRNA. Translation: BAE39346.1 .
    AK168794 mRNA. Translation: BAE40627.1 .
    AK168827 mRNA. Translation: BAE40654.1 .
    AK168874 mRNA. Translation: BAE40692.1 .
    AK169013 mRNA. Translation: BAE40810.1 .
    BC007152 mRNA. Translation: AAH07152.1 .
    CCDSi CCDS35993.1.
    RefSeqi NP_031933.1. NM_007907.2.
    UniGenei Mm.326799.
    Mm.482883.
    Mm.486637.

    3D structure databases

    ProteinModelPortali P58252.
    SMRi P58252. Positions 3-858.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199387. 8 interactions.
    IntActi P58252. 11 interactions.
    MINTi MINT-1862939.

    PTM databases

    PhosphoSitei P58252.

    2D gel databases

    COMPLUYEAST-2DPAGE P58252.
    REPRODUCTION-2DPAGE P58252.

    Proteomic databases

    MaxQBi P58252.
    PaxDbi P58252.
    PRIDEi P58252.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000047864 ; ENSMUSP00000046101 ; ENSMUSG00000034994 .
    GeneIDi 13629.
    KEGGi mmu:13629.
    UCSCi uc007gge.2. mouse.

    Organism-specific databases

    CTDi 1938.
    MGIi MGI:95288. Eef2.

    Phylogenomic databases

    eggNOGi COG0480.
    GeneTreei ENSGT00750000117652.
    HOGENOMi HOG000231589.
    HOVERGENi HBG001838.
    InParanoidi P58252.
    KOi K03234.
    OMAi RWAPVPE.
    OrthoDBi EOG7WDN1S.
    PhylomeDBi P58252.
    TreeFami TF300575.

    Miscellaneous databases

    ChiTaRSi EEF2. mouse.
    NextBioi 284312.
    PROi P58252.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P58252.
    Bgeei P58252.
    CleanExi MM_EEF2.
    Genevestigatori P58252.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    3.30.70.240. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR000795. EF_GTP-bd_dom.
    IPR009022. EFG_III-V.
    IPR000640. EFG_V.
    IPR027417. P-loop_NTPase.
    IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR005225. Small_GTP-bd_dom.
    IPR009000. Transl_B-barrel.
    IPR005517. Transl_elong_EFG/EF2_IV.
    IPR004161. Transl_elong_EFTu/EF1A_2.
    [Graphical view ]
    Pfami PF00679. EFG_C. 1 hit.
    PF14492. EFG_II. 1 hit.
    PF03764. EFG_IV. 1 hit.
    PF00009. GTP_EFTU. 1 hit.
    PF03144. GTP_EFTU_D2. 1 hit.
    [Graphical view ]
    PRINTSi PR00315. ELONGATNFCT.
    SMARTi SM00838. EFG_C. 1 hit.
    SM00889. EFG_IV. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50447. SSF50447. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF54211. SSF54211. 1 hit.
    SSF54980. SSF54980. 2 hits.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS00301. G_TR_1. 1 hit.
    PS51722. G_TR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 and NOD.
      Tissue: Bone marrow, Forelimb, Kidney, Liver, Mammary gland and Thymus.
    2. "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].
    3. Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10 AND 499-506, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic fibroblast.
    4. Lubec G., Klug S., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-10; 33-50; 163-180; 240-249; 288-308; 416-426; 581-594; 606-625; 668-688; 717-726; 728-739; 768-801 AND 846-858, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    5. Cited for: ISGYLATION.
    6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239; LYS-272; LYS-275; LYS-439; LYS-445 AND LYS-619, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-152; LYS-272 AND LYS-572, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiEF2_MOUSE
    AccessioniPrimary (citable) accession number: P58252
    Secondary accession number(s): Q544E4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 29, 2001
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3