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Q08188

- TGM3_HUMAN

UniProt

Q08188 - TGM3_HUMAN

Protein

Protein-glutamine gamma-glutamyltransferase E

Gene

TGM3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 4 (01 Sep 2009)
      Previous versions | rss
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    Functioni

    Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold By similarity. In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath.By similarity

    Catalytic activityi

    Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.2 PublicationsPROSITE-ProRule annotation

    Cofactori

    Binds 3 calcium ions per subunit. Binds 1 calcium ion as a zymogen, and binds 2 more calcium ions, or other divalent metal cations, after proteolytic processing.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi222 – 2221Calcium 1; via carbonyl oxygen2 Publications
    Metal bindingi225 – 2251Calcium 12 Publications
    Metal bindingi227 – 2271Calcium 1; via carbonyl oxygen2 Publications
    Metal bindingi228 – 2281Calcium 12 Publications
    Metal bindingi230 – 2301Calcium 1; via carbonyl oxygen2 Publications
    Active sitei273 – 2731PROSITE-ProRule annotation
    Metal bindingi302 – 3021Calcium 22 Publications
    Metal bindingi304 – 3041Calcium 22 Publications
    Metal bindingi306 – 3061Calcium 22 Publications
    Metal bindingi308 – 3081Calcium 2; via carbonyl oxygen2 Publications
    Metal bindingi325 – 3251Calcium 22 Publications
    Active sitei331 – 3311PROSITE-ProRule annotation
    Active sitei354 – 3541PROSITE-ProRule annotation
    Metal bindingi394 – 3941Calcium 32 Publications
    Metal bindingi416 – 4161Calcium 3; via carbonyl oxygen2 Publications
    Metal bindingi444 – 4441Calcium 32 Publications
    Metal bindingi449 – 4491Calcium 32 Publications
    Sitei467 – 4682Cleavage; by CTSL

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. catalytic activity Source: UniProtKB
    3. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB
    4. transferase activity, transferring acyl groups Source: UniProtKB

    GO - Biological processi

    1. cell envelope organization Source: UniProtKB
    2. cellular protein modification process Source: UniProtKB
    3. hair follicle morphogenesis Source: UniProtKB
    4. keratinization Source: UniProtKB-KW
    5. keratinocyte differentiation Source: UniProtKB
    6. peptide cross-linking Source: UniProtKB
    7. protein tetramerization Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Keratinization

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein-glutamine gamma-glutamyltransferase E (EC:2.3.2.13)
    Alternative name(s):
    Transglutaminase E
    Short name:
    TG(E)
    Short name:
    TGE
    Short name:
    TGase E
    Transglutaminase-3
    Short name:
    TGase-3
    Cleaved into the following 2 chains:
    Gene namesi
    Name:TGM3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11779. TGM3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36492.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 467466Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chainPRO_0000033652Add
    BLAST
    Chaini468 – 693226Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chainPRO_0000033653Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei111 – 1111Phosphotyrosine1 Publication
    Modified residuei112 – 1121Phosphothreonine1 Publication

    Post-translational modificationi

    Activated by proteolytic processing. In vitro activation is commonly achieved by cleavage with dispase, a neutral bacterial protease. Dispase cleavage site was proposed to lie between Ser-470 and Ser-471 (PubMed:8099584) or between Pro-465 and Phe-466 (PubMed:16565075). Physiological activation may be catalyzed by CTSL and, to a lesser extent, by CTSS, but not by CTSB, CTSD nor CTSV (PubMed:16565075).2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein, Zymogen

    Proteomic databases

    MaxQBiQ08188.
    PaxDbiQ08188.
    PeptideAtlasiQ08188.
    PRIDEiQ08188.

    PTM databases

    PhosphoSiteiQ08188.

    Expressioni

    Gene expression databases

    BgeeiQ08188.
    CleanExiHS_TGM3.
    GenevestigatoriQ08188.

    Organism-specific databases

    HPAiHPA004728.

    Interactioni

    Subunit structurei

    Consists of two polypeptide chains, which are synthesized as a precursor form of a single polypeptide.2 Publications

    Protein-protein interaction databases

    BioGridi112911. 10 interactions.
    IntActiQ08188. 6 interactions.
    MINTiMINT-7950929.
    STRINGi9606.ENSP00000370867.

    Structurei

    Secondary structure

    1
    693
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 105
    Helixi13 – 197
    Beta strandi31 – 333
    Beta strandi38 – 469
    Beta strandi53 – 597
    Beta strandi61 – 633
    Turni66 – 694
    Beta strandi70 – 7910
    Beta strandi82 – 9211
    Beta strandi95 – 1017
    Beta strandi109 – 11911
    Beta strandi122 – 13413
    Helixi149 – 1557
    Beta strandi160 – 1678
    Beta strandi170 – 1778
    Helixi185 – 1939
    Helixi197 – 2015
    Helixi203 – 2086
    Helixi209 – 2113
    Helixi213 – 22311
    Turni227 – 2293
    Beta strandi231 – 2355
    Helixi247 – 2493
    Helixi253 – 26210
    Beta strandi268 – 2714
    Helixi273 – 28715
    Beta strandi291 – 30010
    Beta strandi305 – 3139
    Turni322 – 3254
    Beta strandi326 – 33712
    Turni341 – 3433
    Helixi345 – 3473
    Beta strandi349 – 3535
    Beta strandi356 – 3594
    Helixi372 – 3776
    Turni383 – 3853
    Helixi386 – 3949
    Beta strandi396 – 4038
    Turni404 – 4074
    Beta strandi408 – 42619
    Beta strandi433 – 4353
    Helixi437 – 4404
    Beta strandi444 – 4463
    Helixi447 – 46014
    Beta strandi482 – 4898
    Beta strandi499 – 5079
    Beta strandi509 – 5113
    Beta strandi513 – 52412
    Beta strandi530 – 54314
    Beta strandi548 – 5558
    Helixi557 – 5604
    Turni561 – 5633
    Beta strandi569 – 5779
    Beta strandi584 – 5918
    Beta strandi597 – 6037
    Beta strandi611 – 6188
    Beta strandi621 – 6233
    Beta strandi627 – 6337
    Turni635 – 6373
    Beta strandi638 – 6403
    Beta strandi642 – 6465
    Beta strandi654 – 6618
    Beta strandi667 – 67711
    Beta strandi680 – 69213

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1L9MX-ray2.10A/B2-693[»]
    1L9NX-ray2.10A/B2-693[»]
    1NUDX-ray2.70A/B2-693[»]
    1NUFX-ray2.70A2-693[»]
    1NUGX-ray2.40A/B2-693[»]
    ProteinModelPortaliQ08188.
    SMRiQ08188. Positions 2-693.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ08188.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG80379.
    HOVERGENiHBG004342.
    InParanoidiQ08188.
    KOiK05620.
    OMAiEILPTRS.
    OrthoDBiEOG7WT40M.
    PhylomeDBiQ08188.
    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.

    Q08188-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAALGVQSIN WQTAFNRQAH HTDKFSSQEL ILRRGQNFQV LMIMNKGLGS    50
    NERLEFIVST GPYPSESAMT KAVFPLSNGS SGGWSAVLQA SNGNTLTISI 100
    SSPASAPIGR YTMALQIFSQ GGISSVKLGT FILLFNPWLN VDSVFMGNHA 150
    EREEYVQEDA GIIFVGSTNR IGMIGWNFGQ FEEDILSICL SILDRSLNFR 200
    RDAATDVASR NDPKYVGRVL SAMINSNDDN GVLAGNWSGT YTGGRDPRSW 250
    NGSVEILKNW KKSGFSPVRY GQCWVFAGTL NTALRSLGIP SRVITNFNSA 300
    HDTDRNLSVD VYYDPMGNPL DKGSDSVWNF HVWNEGWFVR SDLGPSYGGW 350
    QVLDATPQER SQGVFQCGPA SVIGVREGDV QLNFDMPFIF AEVNADRITW 400
    LYDNTTGKQW KNSVNSHTIG RYISTKAVGS NARMDVTDKY KYPEGSDQER 450
    QVFQKALGKL KPNTPFAATS SMGLETEEQE PSIIGKLKVA GMLAVGKEVN 500
    LVLLLKNLSR DTKTVTVNMT AWTIIYNGTL VHEVWKDSAT MSLDPEEEAE 550
    HPIKISYAQY EKYLKSDNMI RITAVCKVPD ESEVVVERDI ILDNPTLTLE 600
    VLNEARVRKP VNVQMLFSNP LDEPVRDCVL MVEGSGLLLG NLKIDVPTLG 650
    PKEGSRVRFD ILPSRSGTKQ LLADFSCNKF PAIKAMLSID VAE 693
    Length:693
    Mass (Da):76,632
    Last modified:September 1, 2009 - v4
    Checksum:iEAFAC0C9A8AA5FD6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti58 – 592VS → DT in AAA61155. (PubMed:8099584)Curated
    Sequence conflicti251 – 2511N → G in AAA61155. (PubMed:8099584)Curated
    Sequence conflicti324 – 3241S → G in BAF84040. (PubMed:14702039)Curated
    Sequence conflicti346 – 3461S → P in AAA61155. (PubMed:8099584)Curated
    Sequence conflicti674 – 6741D → G in BAF84040. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131T → K.6 Publications
    Corresponds to variant rs214803 [ dbSNP | Ensembl ].
    VAR_040067
    Natural varianti163 – 1631I → L.1 Publication
    Corresponds to variant rs6048066 [ dbSNP | Ensembl ].
    VAR_040068
    Natural varianti249 – 2491S → N.1 Publication
    Corresponds to variant rs214814 [ dbSNP | Ensembl ].
    VAR_040069
    Natural varianti562 – 5621K → R.1 Publication
    Corresponds to variant rs1042617 [ dbSNP | Ensembl ].
    VAR_040070
    Natural varianti654 – 6541G → R.5 Publications
    Corresponds to variant rs214830 [ dbSNP | Ensembl ].
    VAR_040071
    Natural varianti687 – 6871L → M.1 Publication
    Corresponds to variant rs45581032 [ dbSNP | Ensembl ].
    VAR_055360

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10386 mRNA. Translation: AAA61155.1.
    AK290324 mRNA. Translation: BAF83013.1.
    AK291351 mRNA. Translation: BAF84040.1.
    AK315236 mRNA. Translation: BAG37663.1.
    EF102483 Genomic DNA. Translation: ABK41960.1.
    AL031678 Genomic DNA. Translation: CAB37633.1.
    CH471133 Genomic DNA. Translation: EAX10601.1.
    CH471133 Genomic DNA. Translation: EAX10602.1.
    BC109075 mRNA. Translation: AAI09076.1.
    BC109076 mRNA. Translation: AAI09077.1.
    CCDSiCCDS33435.1.
    PIRiA45991.
    RefSeqiNP_003236.3. NM_003245.3.
    UniGeneiHs.2022.

    Genome annotation databases

    EnsembliENST00000381458; ENSP00000370867; ENSG00000125780.
    GeneIDi7053.
    KEGGihsa:7053.
    UCSCiuc002wfx.4. human.

    Polymorphism databases

    DMDMi257051080.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10386 mRNA. Translation: AAA61155.1 .
    AK290324 mRNA. Translation: BAF83013.1 .
    AK291351 mRNA. Translation: BAF84040.1 .
    AK315236 mRNA. Translation: BAG37663.1 .
    EF102483 Genomic DNA. Translation: ABK41960.1 .
    AL031678 Genomic DNA. Translation: CAB37633.1 .
    CH471133 Genomic DNA. Translation: EAX10601.1 .
    CH471133 Genomic DNA. Translation: EAX10602.1 .
    BC109075 mRNA. Translation: AAI09076.1 .
    BC109076 mRNA. Translation: AAI09077.1 .
    CCDSi CCDS33435.1.
    PIRi A45991.
    RefSeqi NP_003236.3. NM_003245.3.
    UniGenei Hs.2022.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1L9M X-ray 2.10 A/B 2-693 [» ]
    1L9N X-ray 2.10 A/B 2-693 [» ]
    1NUD X-ray 2.70 A/B 2-693 [» ]
    1NUF X-ray 2.70 A 2-693 [» ]
    1NUG X-ray 2.40 A/B 2-693 [» ]
    ProteinModelPortali Q08188.
    SMRi Q08188. Positions 2-693.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112911. 10 interactions.
    IntActi Q08188. 6 interactions.
    MINTi MINT-7950929.
    STRINGi 9606.ENSP00000370867.

    Chemistry

    ChEMBLi CHEMBL3363.
    DrugBanki DB00130. L-Glutamine.

    PTM databases

    PhosphoSitei Q08188.

    Polymorphism databases

    DMDMi 257051080.

    Proteomic databases

    MaxQBi Q08188.
    PaxDbi Q08188.
    PeptideAtlasi Q08188.
    PRIDEi Q08188.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381458 ; ENSP00000370867 ; ENSG00000125780 .
    GeneIDi 7053.
    KEGGi hsa:7053.
    UCSCi uc002wfx.4. human.

    Organism-specific databases

    CTDi 7053.
    GeneCardsi GC20P002224.
    HGNCi HGNC:11779. TGM3.
    HPAi HPA004728.
    MIMi 600238. gene.
    neXtProti NX_Q08188.
    PharmGKBi PA36492.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG80379.
    HOVERGENi HBG004342.
    InParanoidi Q08188.
    KOi K05620.
    OMAi EILPTRS.
    OrthoDBi EOG7WT40M.
    PhylomeDBi Q08188.
    TreeFami TF324278.

    Miscellaneous databases

    EvolutionaryTracei Q08188.
    GeneWikii TGM3.
    GenomeRNAii 7053.
    NextBioi 27579.
    PROi Q08188.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q08188.
    CleanExi HS_TGM3.
    Genevestigatori Q08188.

    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. "The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse."
      Kim I.-G., Gorman J.J., Park S.-C., Chung S.-I., Steinert P.M.
      J. Biol. Chem. 268:12682-12690(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LYS-13; ARG-562 AND ARG-654.
      Tissue: Foreskin.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LYS-13 AND ARG-654.
      Tissue: Tongue.
    3. NIEHS SNPs program
      Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-13; LEU-163; ASN-249; ARG-654 AND MET-687.
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LYS-13 AND ARG-654.
    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], VARIANTS LYS-13 AND ARG-654.
    7. Bienvenut W.V., Bensaad K., Vousden K.H.
      Submitted (FEB-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13 AND 670-684, VARIANT LYS-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Osteosarcoma.
    8. "Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification."
      Cheng T., Hitomi K., van Vlijmen-Willems I.M., de Jongh G.J., Yamamoto K., Nishi K., Watts C., Reinheckel T., Schalkwijk J., Zeeuwen P.L.
      J. Biol. Chem. 281:15893-15899(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 468-479, PROTEOLYTIC CLEAVAGE BY CTSL.
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-111 AND THR-112, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Three-dimensional structure of the human transglutaminase 3 enzyme: binding of calcium ions changes structure for activation."
      Ahvazi B., Kim H.C., Kee S.H., Nemes Z., Steinert P.M.
      EMBO J. 21:2055-2067(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-693 IN COMPLEX WITH CALCIUM, COFACTOR, CATALYTIC ACTIVITY.
    12. "Roles of calcium ions in the activation and activity of the transglutaminase 3 enzyme."
      Ahvazi B., Boeshans K.M., Idler W., Baxa U., Steinert P.M.
      J. Biol. Chem. 278:23834-23841(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 2-693 IN COMPLEX WITH CALCIUM AND MAGNESIUM, COFACTOR, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiTGM3_HUMAN
    AccessioniPrimary (citable) accession number: Q08188
    Secondary accession number(s): A8K5N6
    , B2RCR6, D3DVX1, O95933, Q32ML9, Q32MM0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: September 1, 2009
    Last modified: October 1, 2014
    This is version 143 of the entry and version 4 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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