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P21981

- TGM2_MOUSE

UniProt

P21981 - TGM2_MOUSE

Protein

Protein-glutamine gamma-glutamyltransferase 2

Gene

Tgm2

Organism
Mus musculus (Mouse)
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 4 (18 Mar 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins.

    Catalytic activityi

    Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.PROSITE-ProRule annotation

    Cofactori

    Binds 1 calcium ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei277 – 2771PROSITE-ProRule annotation
    Active sitei335 – 3351PROSITE-ProRule annotation
    Active sitei358 – 3581PROSITE-ProRule annotation
    Metal bindingi398 – 3981CalciumBy similarity
    Metal bindingi400 – 4001CalciumBy similarity
    Metal bindingi447 – 4471CalciumBy similarity
    Metal bindingi452 – 4521CalciumBy similarity

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. GTP binding Source: UniProtKB
    3. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB
    4. transaminase activity Source: MGI

    GO - Biological processi

    1. apoptotic cell clearance Source: Ensembl
    2. blood vessel remodeling Source: Ensembl
    3. branching involved in salivary gland morphogenesis Source: MGI
    4. G-protein coupled receptor signaling pathway Source: UniProtKB
    5. isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine Source: Ensembl
    6. negative regulation of endoplasmic reticulum calcium ion concentration Source: UniProt
    7. peptide cross-linking Source: UniProtKB
    8. phospholipase C-activating G-protein coupled receptor signaling pathway Source: MGI
    9. positive regulation of apoptotic process Source: Ensembl
    10. positive regulation of cell adhesion Source: UniProtKB
    11. positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Source: Ensembl
    12. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    13. positive regulation of inflammatory response Source: Ensembl
    14. positive regulation of mitochondrial calcium ion concentration Source: UniProt
    15. positive regulation of smooth muscle cell proliferation Source: Ensembl
    16. protein homooligomerization Source: Ensembl
    17. salivary gland cavitation Source: MGI

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-glutamine gamma-glutamyltransferase 2 (EC:2.3.2.13)
    Alternative name(s):
    Tissue transglutaminase
    Transglutaminase C
    Short name:
    TG(C)
    Short name:
    TGC
    Short name:
    TGase C
    Transglutaminase-2
    Short name:
    TGase-2
    Gene namesi
    Name:Tgm2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:98731. Tgm2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: UniProtKB
    3. membrane Source: UniProtKB
    4. mitochondrion Source: Ensembl
    5. plasma membrane Source: Ensembl
    6. proteinaceous extracellular matrix Source: UniProtKB

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 686685Protein-glutamine gamma-glutamyltransferase 2PRO_0000213708Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei468 – 4681N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP21981.
    PaxDbiP21981.
    PRIDEiP21981.

    PTM databases

    PhosphoSiteiP21981.

    Expressioni

    Gene expression databases

    ArrayExpressiP21981.
    BgeeiP21981.
    CleanExiMM_TGM2.
    GenevestigatoriP21981.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi204168. 2 interactions.
    IntActiP21981. 3 interactions.
    MINTiMINT-1869474.

    Structurei

    3D structure databases

    ProteinModelPortaliP21981.
    SMRiP21981. Positions 4-686.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG80379.
    GeneTreeiENSGT00740000115156.
    HOGENOMiHOG000231695.
    HOVERGENiHBG004342.
    InParanoidiP21981.
    KOiK05625.
    OMAiANGRDHH.
    OrthoDBiEOG7WT40M.
    PhylomeDBiP21981.
    TreeFamiTF324278.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    3.90.260.10. 1 hit.
    InterProiIPR023608. Gln_gamma-glutamylTfrase_euk.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002931. Transglutaminase-like.
    IPR008958. Transglutaminase_C.
    IPR013808. Transglutaminase_CS.
    IPR001102. Transglutaminase_N.
    [Graphical view]
    PANTHERiPTHR11590. PTHR11590. 1 hit.
    PfamiPF00927. Transglut_C. 2 hits.
    PF01841. Transglut_core. 1 hit.
    PF00868. Transglut_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000459. TGM_EBP42. 1 hit.
    SMARTiSM00460. TGc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49309. SSF49309. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEiPS00547. TRANSGLUTAMINASES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P21981-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEELLLERC DLEIQANGRD HHTADLCQEK LVLRRGQRFR LTLYFEGRGY    50
    EASVDSLTFG AVTGPDPSEE AGTKARFSLS DNVEEGSWSA SVLDQQDNVL 100
    SLQLCTPANA PIGLYRLSLE ASTGYQGSSF VLGHFILLYN AWCPADDVYL 150
    DSEEERREYV LTQQGFIYQG SVKFIKSVPW NFGQFEDGIL DTCLMLLDMN 200
    PKFLKNRSRD CSRRSSPIYV GRVVSAMVNC NDDQGVLLGR WDNNYGDGIS 250
    PMAWIGSVDI LRRWKEHGCQ QVKYGQCWVF AAVACTVLRC LGIPTRVVTN 300
    YNSAHDQNSN LLIEYFRNEF GELESNKSEM IWNFHCWVES WMTRPDLQPG 350
    YEGWQAIDPT PQEKSEGTYC CGPVSVRAIK EGDLSTKYDA PFVFAEVNAD 400
    VVDWIRQEDG SVLKSINRSL VVGQKISTKS VGRDDREDIT HTYKYPEGSP 450
    EEREVFTKAN HLNKLAEKEE TGVAMRIRVG DSMSMGNDFD VFAHIGNDTS 500
    ETRECRLLLC ARTVSYNGVL GPECGTEDIN LTLDPYSENS IPLRILYEKY 550
    SGCLTESNLI KVRGLLIEPA ANSYLLAERD LYLENPEIKI RVLGEPKQNR 600
    KLVAEVSLKN PLSDPLYDCI FTVEGAGLTK EQKSVEVSDP VPAGDLVKAR 650
    VDLFPTDIGL HKLVVNFQCD KLKSVKGYRN VIIGPA 686
    Length:686
    Mass (Da):77,061
    Last modified:March 18, 2008 - v4
    Checksum:i9B64B074D3F837DE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti32 – 332VL → LV in AAA40420. (PubMed:1670766)Curated
    Sequence conflicti51 – 511E → Q in AAA40420. (PubMed:1670766)Curated
    Sequence conflicti51 – 511E → Q in AAD37501. (PubMed:10334875)Curated
    Sequence conflicti186 – 1861E → Q in AAA40420. (PubMed:1670766)Curated
    Sequence conflicti226 – 2261A → D in AAA40420. (PubMed:1670766)Curated
    Sequence conflicti325 – 3251S → T in AAA40420. (PubMed:1670766)Curated
    Sequence conflicti357 – 3571I → L in AAA40420. (PubMed:1670766)Curated
    Sequence conflicti357 – 3571I → L in AAD37501. (PubMed:10334875)Curated
    Sequence conflicti396 – 3961E → K in BAC40899. (PubMed:16141072)Curated
    Sequence conflicti408 – 4092ED → DE in AAA40420. (PubMed:1670766)Curated
    Sequence conflicti415 – 4162SI → WM in AAA40420. (PubMed:1670766)Curated
    Sequence conflicti421 – 4211V → I in AAA40420. (PubMed:1670766)Curated
    Sequence conflicti481 – 4855DSMSM → QYEH in AAA40420. (PubMed:1670766)Curated
    Sequence conflicti539 – 5391N → K in BAE38690. (PubMed:16141072)Curated
    Sequence conflicti552 – 5521G → D in AAA40420. (PubMed:1670766)Curated
    Sequence conflicti583 – 5831L → V in AAA40420. (PubMed:1670766)Curated
    Sequence conflicti583 – 5831L → V in AAD37501. (PubMed:10334875)Curated
    Sequence conflicti654 – 6541F → S in AAA40420. (PubMed:1670766)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55154 mRNA. Translation: AAA40420.1.
    AF114266 mRNA. Translation: AAD37501.1.
    AF076928 mRNA. Translation: AAC62014.1.
    AK052912 mRNA. Translation: BAC35200.1.
    AK080224 mRNA. Translation: BAC37852.1.
    AK080593 mRNA. Translation: BAC37952.1.
    AK089481 mRNA. Translation: BAC40899.1.
    AK143712 mRNA. Translation: BAE25511.1.
    AK151776 mRNA. Translation: BAE30682.1.
    AK152152 mRNA. Translation: BAE30987.1.
    AK152627 mRNA. Translation: BAE31370.1.
    AK159255 mRNA. Translation: BAE34936.1.
    AK166302 mRNA. Translation: BAE38690.1.
    AK168990 mRNA. Translation: BAE40790.1.
    AK169356 mRNA. Translation: BAE41105.1.
    AL669824 Genomic DNA. Translation: CAM23188.1.
    BC016492 mRNA. Translation: AAH16492.1.
    U24148 Genomic DNA. No translation available.
    CCDSiCCDS16985.1.
    PIRiB39045.
    RefSeqiNP_033399.1. NM_009373.3.
    UniGeneiMm.330731.

    Genome annotation databases

    EnsembliENSMUST00000103122; ENSMUSP00000099411; ENSMUSG00000037820.
    GeneIDi21817.
    KEGGimmu:21817.
    UCSCiuc008npr.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55154 mRNA. Translation: AAA40420.1 .
    AF114266 mRNA. Translation: AAD37501.1 .
    AF076928 mRNA. Translation: AAC62014.1 .
    AK052912 mRNA. Translation: BAC35200.1 .
    AK080224 mRNA. Translation: BAC37852.1 .
    AK080593 mRNA. Translation: BAC37952.1 .
    AK089481 mRNA. Translation: BAC40899.1 .
    AK143712 mRNA. Translation: BAE25511.1 .
    AK151776 mRNA. Translation: BAE30682.1 .
    AK152152 mRNA. Translation: BAE30987.1 .
    AK152627 mRNA. Translation: BAE31370.1 .
    AK159255 mRNA. Translation: BAE34936.1 .
    AK166302 mRNA. Translation: BAE38690.1 .
    AK168990 mRNA. Translation: BAE40790.1 .
    AK169356 mRNA. Translation: BAE41105.1 .
    AL669824 Genomic DNA. Translation: CAM23188.1 .
    BC016492 mRNA. Translation: AAH16492.1 .
    U24148 Genomic DNA. No translation available.
    CCDSi CCDS16985.1.
    PIRi B39045.
    RefSeqi NP_033399.1. NM_009373.3.
    UniGenei Mm.330731.

    3D structure databases

    ProteinModelPortali P21981.
    SMRi P21981. Positions 4-686.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204168. 2 interactions.
    IntActi P21981. 3 interactions.
    MINTi MINT-1869474.

    Chemistry

    ChEMBLi CHEMBL2079853.

    PTM databases

    PhosphoSitei P21981.

    Proteomic databases

    MaxQBi P21981.
    PaxDbi P21981.
    PRIDEi P21981.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000103122 ; ENSMUSP00000099411 ; ENSMUSG00000037820 .
    GeneIDi 21817.
    KEGGi mmu:21817.
    UCSCi uc008npr.1. mouse.

    Organism-specific databases

    CTDi 7052.
    MGIi MGI:98731. Tgm2.

    Phylogenomic databases

    eggNOGi NOG80379.
    GeneTreei ENSGT00740000115156.
    HOGENOMi HOG000231695.
    HOVERGENi HBG004342.
    InParanoidi P21981.
    KOi K05625.
    OMAi ANGRDHH.
    OrthoDBi EOG7WT40M.
    PhylomeDBi P21981.
    TreeFami TF324278.

    Miscellaneous databases

    NextBioi 301224.
    PROi P21981.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21981.
    Bgeei P21981.
    CleanExi MM_TGM2.
    Genevestigatori P21981.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    3.90.260.10. 1 hit.
    InterProi IPR023608. Gln_gamma-glutamylTfrase_euk.
    IPR013783. Ig-like_fold.
    IPR014756. Ig_E-set.
    IPR002931. Transglutaminase-like.
    IPR008958. Transglutaminase_C.
    IPR013808. Transglutaminase_CS.
    IPR001102. Transglutaminase_N.
    [Graphical view ]
    PANTHERi PTHR11590. PTHR11590. 1 hit.
    Pfami PF00927. Transglut_C. 2 hits.
    PF01841. Transglut_core. 1 hit.
    PF00868. Transglut_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000459. TGM_EBP42. 1 hit.
    SMARTi SM00460. TGc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49309. SSF49309. 2 hits.
    SSF81296. SSF81296. 1 hit.
    PROSITEi PS00547. TRANSGLUTAMINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of cDNA clones to mouse macrophage and human endothelial cell tissue transglutaminases."
      Gentile V., Saydak M., Chiocca E.A., Akande O., Birckbichler P.J., Lee K.N., Stein J.P., Davies P.J.A.
      J. Biol. Chem. 266:478-483(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Macrophage.
    2. "Organization and chromosomal mapping of mouse Gh/tissue transglutaminase gene (Tgm2)."
      Nanda N., Iismaa S.E., Copeland N.G., Gilbert D.J., Jenkins N., Graham R.M., Sutrave P.
      Arch. Biochem. Biophys. 366:151-156(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129/SvJ.
    3. "Mapping and sequencing of the murine 'tissue' transglutaminase (Tgm2) gene: absence of mutations in MRLlpr/lpr mice."
      D'Amato M., Iannicola C., Monteriu G., Piacentini M.
      Cell Death Differ. 6:216-217(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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: Brain cortex, Dendritic cell, Embryonic heart, Heart, Macrophage, Mammary gland and Spleen.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "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].
      Strain: NMRI.
      Tissue: Mammary tumor.
    7. "Identification and characterization of a versatile retinoid response element (retinoic acid receptor response element-retinoid X receptor response element) in the mouse tissue transglutaminase gene promoter."
      Nagy L., Saydak M., Shipley N., Lu S., Basilion J.P., Yan Z.H., Syka P., Chandraratna R.A.S., Stein J.P., Heyman R.A., Davies P.J.A.
      J. Biol. Chem. 271:4355-4365(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
      Strain: Swiss.
    8. Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-19; 41-74; 158-173; 215-222; 290-327; 550-561; 564-589; 601-609; 634-648 AND 651-671, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic fibroblast.
    9. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 378-387, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.
    10. "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-468, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiTGM2_MOUSE
    AccessioniPrimary (citable) accession number: P21981
    Secondary accession number(s): O88901
    , Q3TLV2, Q8C217, Q91VG9, Q9R1F7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: March 18, 2008
    Last modified: October 1, 2014
    This is version 141 of the entry and version 4 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