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P21980

- TGM2_HUMAN

UniProt

P21980 - TGM2_HUMAN

Protein

Protein-glutamine gamma-glutamyltransferase 2

Gene

TGM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 166 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      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. GTP binding Source: Ensembl
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein-glutamine gamma-glutamyltransferase activity Source: UniProtKB

    GO - Biological processi

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

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    SignaLinkiP21980.

    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 H
    Short name:
    TGase H
    Transglutaminase-2
    Short name:
    TGase-2
    Gene namesi
    Name:TGM2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11778. TGM2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProt
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrion Source: UniProt
    4. plasma membrane Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA36491.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 687686Protein-glutamine gamma-glutamyltransferase 2PRO_0000213707Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei468 – 4681N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP21980.
    PaxDbiP21980.
    PeptideAtlasiP21980.
    PRIDEiP21980.

    PTM databases

    PhosphoSiteiP21980.

    Miscellaneous databases

    PMAP-CutDBP21980.

    Expressioni

    Inductioni

    By retinoic acid.

    Gene expression databases

    ArrayExpressiP21980.
    BgeeiP21980.
    CleanExiHS_TGM2.
    GenevestigatoriP21980.

    Organism-specific databases

    HPAiCAB002598.
    HPA021019.
    HPA029518.

    Interactioni

    Subunit structurei

    Monomer.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AKAP13Q128024EBI-727668,EBI-1373806
    COL18A1P390602EBI-727668,EBI-2566375
    FN1P027513EBI-727668,EBI-1220319
    RELAQ042063EBI-727668,EBI-73886
    VHLP4033710EBI-727668,EBI-301246

    Protein-protein interaction databases

    BioGridi112910. 65 interactions.
    DIPiDIP-33557N.
    IntActiP21980. 40 interactions.
    MINTiMINT-88880.
    STRINGi9606.ENSP00000355330.

    Structurei

    Secondary structure

    1
    687
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115
    Helixi14 – 207
    Helixi24 – 263
    Beta strandi28 – 303
    Beta strandi32 – 343
    Beta strandi39 – 4810
    Turni52 – 543
    Beta strandi55 – 6612
    Turni69 – 724
    Beta strandi73 – 797
    Beta strandi89 – 957
    Beta strandi97 – 1059
    Beta strandi113 – 12311
    Beta strandi126 – 13813
    Helixi153 – 1597
    Beta strandi164 – 1707
    Beta strandi172 – 18110
    Helixi189 – 19810
    Helixi201 – 2055
    Helixi207 – 2137
    Helixi217 – 22610
    Turni227 – 2293
    Turni231 – 2344
    Beta strandi235 – 2395
    Turni251 – 2533
    Helixi258 – 2669
    Turni267 – 2693
    Beta strandi272 – 2754
    Helixi277 – 29115
    Beta strandi295 – 30410
    Beta strandi306 – 3094
    Helixi311 – 3177
    Beta strandi332 – 34211
    Beta strandi347 – 3504
    Beta strandi353 – 3575
    Beta strandi365 – 3695
    Helixi376 – 3805
    Turni387 – 3893
    Helixi390 – 3978
    Beta strandi400 – 4045
    Beta strandi412 – 4143
    Beta strandi419 – 42911
    Beta strandi433 – 4386
    Helixi440 – 4434
    Beta strandi447 – 4493
    Helixi450 – 46011
    Turni468 – 4714
    Beta strandi473 – 4786
    Beta strandi489 – 4979
    Beta strandi499 – 5013
    Beta strandi503 – 51412
    Beta strandi520 – 53415
    Beta strandi538 – 5469
    Helixi548 – 5514
    Turni552 – 5543
    Beta strandi560 – 56910
    Turni570 – 5734
    Beta strandi574 – 58310
    Beta strandi590 – 5956
    Beta strandi598 – 6014
    Beta strandi603 – 6108
    Beta strandi613 – 6153
    Beta strandi619 – 6257
    Turni627 – 6293
    Beta strandi634 – 6385
    Beta strandi647 – 6548
    Beta strandi658 – 6603
    Beta strandi662 – 6698
    Beta strandi671 – 6733
    Beta strandi676 – 6827

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FAUmodel-A1-687[»]
    1KV3X-ray2.80A/B/C/D/E/F1-687[»]
    2Q3ZX-ray2.00A1-687[»]
    3LY6X-ray3.14A/B/C1-687[»]
    3S3JX-ray2.25A2-687[»]
    3S3PX-ray2.50A2-687[»]
    3S3SX-ray2.30A2-687[»]
    ProteinModelPortaliP21980.
    SMRiP21980. Positions 4-687.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP21980.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG80379.
    HOGENOMiHOG000231695.
    HOVERGENiHBG004342.
    InParanoidiP21980.
    KOiK05625.
    OMAiANGRDHH.
    OrthoDBiEOG7WT40M.
    PhylomeDBiP21980.
    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]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P21980-1) [UniParc]FASTAAdd to Basket

    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

    MAEELVLERC DLELETNGRD HHTADLCREK LVVRRGQPFW LTLHFEGRNY    50
    EASVDSLTFS VVTGPAPSQE AGTKARFPLR DAVEEGDWTA TVVDQQDCTL 100
    SLQLTTPANA PIGLYRLSLE ASTGYQGSSF VLGHFILLFN AWCPADAVYL 150
    DSEEERQEYV LTQQGFIYQG SAKFIKNIPW NFGQFEDGIL DICLILLDVN 200
    PKFLKNAGRD CSRRSSPVYV GRVVSGMVNC NDDQGVLLGR WDNNYGDGVS 250
    PMSWIGSVDI LRRWKNHGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN 300
    YNSAHDQNSN LLIEYFRNEF GEIQGDKSEM IWNFHCWVES WMTRPDLQPG 350
    YEGWQALDPT PQEKSEGTYC CGPVPVRAIK EGDLSTKYDA PFVFAEVNAD 400
    VVDWIQQDDG SVHKSINRSL IVGLKISTKS VGRDEREDIT HTYKYPEGSS 450
    EEREAFTRAN HLNKLAEKEE TGMAMRIRVG QSMNMGSDFD VFAHITNNTA 500
    EEYVCRLLLC ARTVSYNGIL GPECGTKYLL NLNLEPFSEK SVPLCILYEK 550
    YRDCLTESNL IKVRALLVEP VINSYLLAER DLYLENPEIK IRILGEPKQK 600
    RKLVAEVSLQ NPLPVALEGC TFTVEGAGLT EEQKTVEIPD PVEAGEEVKV 650
    RMDLLPLHMG LHKLVVNFES DKLKAVKGFR NVIIGPA 687
    Length:687
    Mass (Da):77,329
    Last modified:January 23, 2002 - v2
    Checksum:i7DA33FF335DE7B37
    GO
    Isoform 2 (identifier: P21980-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         539-548: EKSVPLCILY → GKALCSWSIC
         549-687: Missing.

    Show »
    Length:548
    Mass (Da):61,678
    Checksum:i8C2F43A4D1029AC2
    GO
    Isoform 3 (identifier: P21980-3) [UniParc]FASTAAdd to Basket

    Also known as: TGH2

    The sequence of this isoform differs from the canonical sequence as follows:
         287-349: VLRCLGIPTR...SWMTRPDLQP → GELHAGMWVM...LSNSHPSSGC
         350-687: Missing.

    Show »
    Length:349
    Mass (Da):38,671
    Checksum:i37E1EE27C243CCC5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti51 – 511E → Q in AAA63261. (PubMed:1670766)Curated
    Sequence conflicti186 – 1861E → Q in AAA63261. (PubMed:1670766)Curated
    Sequence conflicti224 – 2241V → G in AAA63261. (PubMed:1670766)Curated
    Sequence conflicti533 – 5331N → T in AAA63261. (PubMed:1670766)Curated
    Sequence conflicti655 – 6551L → V in AAA63261. (PubMed:1670766)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti76 – 761R → H.1 Publication
    Corresponds to variant rs41274720 [ dbSNP | Ensembl ].
    VAR_052553
    Natural varianti214 – 2141R → H.1 Publication
    Corresponds to variant rs45530133 [ dbSNP | Ensembl ].
    VAR_055357
    Natural varianti324 – 3241Q → R.1 Publication
    Corresponds to variant rs45567334 [ dbSNP | Ensembl ].
    VAR_055358
    Natural varianti330 – 3301M → R in patients with early-onset diabetes type 2; pathological significance unknown. 1 Publication
    VAR_037998
    Natural varianti331 – 3311I → N in patients with early-onset diabetes type 2; pathological significance unknown. 1 Publication
    VAR_037999
    Natural varianti436 – 4361R → W.1 Publication
    Corresponds to variant rs45629036 [ dbSNP | Ensembl ].
    VAR_055359
    Natural varianti536 – 5361P → S.1 Publication
    Corresponds to variant rs45556333 [ dbSNP | Ensembl ].
    VAR_052554
    Natural varianti660 – 6601G → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036554

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei287 – 34963VLRCL…PDLQP → GELHAGMWVMSPGRGHEEHW SRNQDIPALVLPPATNTLNA LCGLEPVTTLSGPLSNSHPS SGC in isoform 3. 1 PublicationVSP_006413Add
    BLAST
    Alternative sequencei350 – 687338Missing in isoform 3. 1 PublicationVSP_006414Add
    BLAST
    Alternative sequencei539 – 54810EKSVPLCILY → GKALCSWSIC in isoform 2. 2 PublicationsVSP_006411
    Alternative sequencei549 – 687139Missing in isoform 2. 2 PublicationsVSP_006412Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55153 mRNA. Translation: AAA63261.1.
    M98478 mRNA. Translation: AAA36739.1.
    S81734 mRNA. Translation: AAB36379.1.
    AY675221 mRNA. Translation: AAT79353.1.
    AK291714 mRNA. Translation: BAF84403.1.
    AK314618 mRNA. Translation: BAG37184.1.
    DQ523828 Genomic DNA. Translation: ABF47109.1.
    AL031651 Genomic DNA. Translation: CAB66115.1.
    CH471077 Genomic DNA. Translation: EAW76040.1.
    CH471077 Genomic DNA. Translation: EAW76042.1.
    CH471077 Genomic DNA. Translation: EAW76044.1.
    BC003551 mRNA. Translation: AAH03551.1.
    CCDSiCCDS13302.1. [P21980-1]
    PIRiA39045.
    A44302.
    S68092.
    RefSeqiNP_004604.2. NM_004613.2. [P21980-1]
    NP_945189.1. NM_198951.1. [P21980-2]
    UniGeneiHs.517033.

    Genome annotation databases

    EnsembliENST00000361475; ENSP00000355330; ENSG00000198959. [P21980-1]
    GeneIDi7052.
    KEGGihsa:7052.
    UCSCiuc002xhr.3. human. [P21980-1]
    uc002xht.3. human. [P21980-2]
    uc002xhu.3. human. [P21980-3]

    Polymorphism databases

    DMDMi20141877.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Tissue transglutaminase entry

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M55153 mRNA. Translation: AAA63261.1 .
    M98478 mRNA. Translation: AAA36739.1 .
    S81734 mRNA. Translation: AAB36379.1 .
    AY675221 mRNA. Translation: AAT79353.1 .
    AK291714 mRNA. Translation: BAF84403.1 .
    AK314618 mRNA. Translation: BAG37184.1 .
    DQ523828 Genomic DNA. Translation: ABF47109.1 .
    AL031651 Genomic DNA. Translation: CAB66115.1 .
    CH471077 Genomic DNA. Translation: EAW76040.1 .
    CH471077 Genomic DNA. Translation: EAW76042.1 .
    CH471077 Genomic DNA. Translation: EAW76044.1 .
    BC003551 mRNA. Translation: AAH03551.1 .
    CCDSi CCDS13302.1. [P21980-1 ]
    PIRi A39045.
    A44302.
    S68092.
    RefSeqi NP_004604.2. NM_004613.2. [P21980-1 ]
    NP_945189.1. NM_198951.1. [P21980-2 ]
    UniGenei Hs.517033.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FAU model - A 1-687 [» ]
    1KV3 X-ray 2.80 A/B/C/D/E/F 1-687 [» ]
    2Q3Z X-ray 2.00 A 1-687 [» ]
    3LY6 X-ray 3.14 A/B/C 1-687 [» ]
    3S3J X-ray 2.25 A 2-687 [» ]
    3S3P X-ray 2.50 A 2-687 [» ]
    3S3S X-ray 2.30 A 2-687 [» ]
    ProteinModelPortali P21980.
    SMRi P21980. Positions 4-687.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112910. 65 interactions.
    DIPi DIP-33557N.
    IntActi P21980. 40 interactions.
    MINTi MINT-88880.
    STRINGi 9606.ENSP00000355330.

    Chemistry

    BindingDBi P21980.
    ChEMBLi CHEMBL2730.
    DrugBanki DB00130. L-Glutamine.

    PTM databases

    PhosphoSitei P21980.

    Polymorphism databases

    DMDMi 20141877.

    Proteomic databases

    MaxQBi P21980.
    PaxDbi P21980.
    PeptideAtlasi P21980.
    PRIDEi P21980.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361475 ; ENSP00000355330 ; ENSG00000198959 . [P21980-1 ]
    GeneIDi 7052.
    KEGGi hsa:7052.
    UCSCi uc002xhr.3. human. [P21980-1 ]
    uc002xht.3. human. [P21980-2 ]
    uc002xhu.3. human. [P21980-3 ]

    Organism-specific databases

    CTDi 7052.
    GeneCardsi GC20M036756.
    HGNCi HGNC:11778. TGM2.
    HPAi CAB002598.
    HPA021019.
    HPA029518.
    MIMi 190196. gene.
    neXtProti NX_P21980.
    PharmGKBi PA36491.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG80379.
    HOGENOMi HOG000231695.
    HOVERGENi HBG004342.
    InParanoidi P21980.
    KOi K05625.
    OMAi ANGRDHH.
    OrthoDBi EOG7WT40M.
    PhylomeDBi P21980.
    TreeFami TF324278.

    Enzyme and pathway databases

    SignaLinki P21980.

    Miscellaneous databases

    ChiTaRSi TGM2. human.
    EvolutionaryTracei P21980.
    GeneWikii Tissue_transglutaminase.
    GenomeRNAii 7052.
    NextBioi 27573.
    PMAP-CutDB P21980.
    PROi P21980.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P21980.
    Bgeei P21980.
    CleanExi HS_TGM2.
    Genevestigatori P21980.

    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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Endothelial cell.
    2. "A retinoic acid-inducible mRNA from human erythroleukemia cells encodes a novel tissue transglutaminase homologue."
      Fraij B.M., Birckbichler P.J., Patterson M.K. Jr., Lee K.N., Gonzales R.A.
      J. Biol. Chem. 267:22616-22623(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "A third human tissue transglutaminase homologue as a result of alternative gene transcripts."
      Fraij B.M., Gonzales R.A.
      Biochim. Biophys. Acta 1306:63-74(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    4. Bayardo M.P., de Urraza P., Chirdo F.G.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Colon adenocarcinoma.
    5. "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] (ISOFORM 1).
      Tissue: Placenta.
    6. NIEHS SNPs program
      Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-76; HIS-214; ARG-324; TRP-436 AND SER-536.
    7. "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].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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] (ISOFORM 2).
      Tissue: Kidney.
    10. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-9; 365-377; 565-590; 635-649 AND 664-674, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Transglutaminase 2 undergoes a large conformational change upon activation."
      Pinkas D.M., Strop P., Brunger A.T., Khosla C.
      PLoS Biol. 5:E327-E327(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    14. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-660.
    15. Cited for: VARIANTS ARG-330 AND ASN-331.

    Entry informationi

    Entry nameiTGM2_HUMAN
    AccessioniPrimary (citable) accession number: P21980
    Secondary accession number(s): E1P5V9
    , Q16436, Q6B838, Q9BTN7, Q9UH35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 166 of the entry and version 2 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