| Tag | Content |
|---|
| CPLM ID | CPLM-021850 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Protein-glutamine gamma-glutamyltransferase K |
Protein Synonyms/Alias | Epidermal TGase; Transglutaminase K; TG(K); TGK; TGase K; Transglutaminase-1; TGase-1 |
Gene Name | Tgm1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 186 | HVIIPVGKGGSGGWK | ubiquitination | [1] | | 198 | GWKAQVTKNNGHNLN | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Responsible for cross- linking epidermal proteins during formation of the stratum corneum (By similarity). |
Sequence Annotation | ACT_SITE 376 376 By similarity.
ACT_SITE 435 435 By similarity.
ACT_SITE 458 458 By similarity.
METAL 498 498 Calcium (By similarity).
METAL 500 500 Calcium (By similarity).
METAL 547 547 Calcium (By similarity).
METAL 552 552 Calcium (By similarity).
MOD_RES 23 23 Phosphoserine (By similarity).
MOD_RES 71 71 Phosphoserine.
MOD_RES 83 83 Phosphoserine (By similarity).
MOD_RES 91 91 Phosphoserine.
MOD_RES 94 94 Phosphoserine. |
Keyword | Acyltransferase; Calcium; Complete proteome; Keratinization; Membrane; Metal-binding; Phosphoprotein; Reference proteome; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 815 AA |
Protein Sequence | MEGPRSDVGR WGRSPWQPPT TPSPEPEPEP EPDRRSRSRR GGGRSFWARC CGCCSCGNRG 60
DDDWGPEPSG SRSRGTSSRG RDSRGGRRPE SRGSGVNAAG DGTIREGMLV VTGVDLLCSR 120
SDQNRREHHT DEFEYDELIV RRGQPFHMIL FLNREYESSD RIALELLIGS NPEVGKGTHV 180
IIPVGKGGSG GWKAQVTKNN GHNLNLRVHT SPNAIIGKFQ FTVRTRSEAG EFQLPFDPRN 240
EIYILFNPWC PEDIVYVDHE DWRQEYVLNE SGRIYYGTEA QIGERTWNYG QFDHGVLDAC 300
LYILDRRGMP YGGRGDPVSV SRVVSAMVNS LDDNGVLIGN WTGDYSRGTN PSAWVGSVEI 360
LLSYLRTGYS VPYGQCWVFA GVTTTVLRCL GFATRTVTNF NSAHDTDTSL TMDIYFDENM 420
KPLEHLNHDS VWNFHVWNDC WMKRPDLPSG FDGWQVVDAT PQETSSGIFC CGPCSVESVK 480
NGLVYMKYDT PFIFAEVNSD KVYWQRQDDG SFKIVYVEEK AIGTLIVTKA IHSNNREDIT 540
HIYKHPEGSE AERRAVEKAA AHGSKPNVYA TRDSAEDVAM QVEAQDAVMG QDLAVSVVLT 600
NRGSSRRTVK LHLYLCVTYY TGVSGPTFKE AKKEVTLAPG ASDSVTMPVA YKEYKPHLVD 660
QGAMLLNVSG HVKESGQVLA KQHTFRLRTP DLSLTLLGAA VVGQECGVQI VFKNPLPVTL 720
TNVVFRLEGS GLQRPKVLNV GDIGGNETVT LRQTFVPVRP GPRQLIASLD SPQLSQVHGV 780
IQVDVAPASG GSGFSDAGGD SRSGENIPMA YRGGA 815 |
Gene Ontology | GO:0005913; C:cell-cell adherens junction; IDA:MGI. GO:0031224; C:intrinsic to membrane; IEA:Compara. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:EC. GO:0031424; P:keratinization; IEA:UniProtKB-KW. GO:0009887; P:organ morphogenesis; IMP:MGI. GO:0018149; P:peptide cross-linking; IEA:InterPro. GO:0019538; P:protein metabolic process; TAS:MGI. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |