GenomeNet

Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: TGM5_HUMAN B4DPS8_HUMAN
LinkDB: TGM5_HUMAN B4DPS8_HUMAN
Original site: TGM5_HUMAN B4DPS8_HUMAN 
ID   TGM5_HUMAN              Reviewed;         720 AA.
AC   O43548; O43549; Q0VF40; Q9UEZ4;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   30-AUG-2017, entry version 155.
DE   RecName: Full=Protein-glutamine gamma-glutamyltransferase 5;
DE            EC=2.3.2.13;
DE   AltName: Full=Transglutaminase X;
DE            Short=TG(X);
DE            Short=TGX;
DE            Short=TGase X;
DE   AltName: Full=Transglutaminase-5;
DE            Short=TGase-5;
GN   Name=TGM5; Synonyms=TGMX;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC   TISSUE=Foreskin;
RX   PubMed=9452468; DOI=10.1074/jbc.273.6.3452;
RA   Aeschlimann D., Koeller M.K., Allen-Hoffmann B.L., Mosher D.F.;
RT   "Isolation of a cDNA encoding a novel member of the transglutaminase
RT   gene family from human keratinocytes. Detection and identification of
RT   transglutaminase gene products based on reverse transcription-
RT   polymerase chain reaction with degenerate primers.";
RL   J. Biol. Chem. 273:3452-3460(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-67 AND GLY-352.
RX   PubMed=11390390; DOI=10.1074/jbc.M102553200;
RA   Grenard P., Bates M.K., Aeschlimann D.;
RT   "Evolution of transglutaminase genes: identification of a
RT   transglutaminase gene cluster on human chromosome 15q15. Structure of
RT   the gene encoding transglutaminase X and a novel gene family member,
RT   transglutaminase Z.";
RL   J. Biol. Chem. 276:33066-33078(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-16, SUBCELLULAR LOCATION, ACETYLATION AT ALA-2,
RP   INDUCTION BY TPA AND CALCIUM, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=15290349; DOI=10.1007/s00726-004-0093-5;
RA   Rufini A., Vilbois F., Paradisi A., Oddi S., Tartaglione R., Leta A.,
RA   Bagetta G., Guerrieri P., Finazzi-Agro' A., Melino G., Candi E.;
RT   "Transglutaminase 5 is acetylated at the N-terminal end.";
RL   Amino Acids 26:425-430(2004).
RN   [5]
RP   VARIANT PSS2 CYS-113, VARIANT MET-109, CHARACTERIZATION OF VARIANT
RP   PSS2 CYS-113, AND CHARACTERIZATION OF VARIANT MET-109.
RX   PubMed=16380904; DOI=10.1086/497707;
RA   Cassidy A.J., van Steensel M.A.M., Steijlen P.M., van Geel M.,
RA   van der Velden J., Morley S.M., Terrinoni A., Melino G., Candi E.,
RA   McLean W.H.I.;
RT   "A homozygous missense mutation in TGM5 abolishes epidermal
RT   transglutaminase 5 activity and causes acral peeling skin syndrome.";
RL   Am. J. Hum. Genet. 77:909-917(2005).
CC   -!- FUNCTION: Catalyzes the cross-linking of proteins and the
CC       conjugation of polyamines to proteins. Contributes to the
CC       formation of the cornified cell envelope of keratinocytes.
CC   -!- CATALYTIC ACTIVITY: Protein glutamine + alkylamine = protein N(5)-
CC       alkylglutamine + NH(3). {ECO:0000255|PROSITE-ProRule:PRU10024}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15290349}.
CC       Note=Associated with intermediate filaments.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=O43548-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=O43548-2; Sequence=VSP_006415;
CC   -!- TISSUE SPECIFICITY: Expressed in foreskin keratinocytes.
CC   -!- INDUCTION: By 12-O-tetradecanoylphorbol-13-acetate (TPA) and
CC       calcium in NHEK cells. {ECO:0000269|PubMed:15290349}.
CC   -!- DISEASE: Peeling skin syndrome 2 (PSS2) [MIM:609796]: A non-
CC       inflammatory and localized form of peeling skin syndrome, a
CC       genodermatosis characterized by the continuous shedding of the
CC       outer layers of the epidermis. In PSS2 patients, skin peeling is
CC       painless and strictly limited to the dorsa of the hands and feet.
CC       It is accompanied by painless erythema and spontaneous non-
CC       scarring healing. Ultrastructural and histological analysis shows
CC       a level of blistering high in the epidermis at the stratum
CC       granulosum-stratum corneum junction.
CC       {ECO:0000269|PubMed:16380904}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the transglutaminase superfamily.
CC       Transglutaminase family. {ECO:0000305}.
DR   EMBL; AF035960; AAC02978.1; -; mRNA.
DR   EMBL; AF035961; AAC02979.1; -; mRNA.
DR   EMBL; AF206510; AAF23981.1; -; Genomic_DNA.
DR   EMBL; AF206502; AAF23981.1; JOINED; Genomic_DNA.
DR   EMBL; AF206503; AAF23981.1; JOINED; Genomic_DNA.
DR   EMBL; AF206504; AAF23981.1; JOINED; Genomic_DNA.
DR   EMBL; AF206505; AAF23981.1; JOINED; Genomic_DNA.
DR   EMBL; AF206506; AAF23981.1; JOINED; Genomic_DNA.
DR   EMBL; AF206507; AAF23981.1; JOINED; Genomic_DNA.
DR   EMBL; AF206508; AAF23981.1; JOINED; Genomic_DNA.
DR   EMBL; AF206509; AAF23981.1; JOINED; Genomic_DNA.
DR   EMBL; BC119009; AAI19010.1; -; mRNA.
DR   CCDS; CCDS32211.1; -. [O43548-2]
DR   CCDS; CCDS32212.1; -. [O43548-1]
DR   RefSeq; NP_004236.1; NM_004245.3. [O43548-2]
DR   RefSeq; NP_963925.2; NM_201631.3. [O43548-1]
DR   UniGene; Hs.129719; -.
DR   ProteinModelPortal; O43548; -.
DR   SMR; O43548; -.
DR   BioGrid; 114742; 13.
DR   IntAct; O43548; 3.
DR   STRING; 9606.ENSP00000220420; -.
DR   DrugBank; DB00130; L-Glutamine.
DR   iPTMnet; O43548; -.
DR   PhosphoSitePlus; O43548; -.
DR   BioMuta; TGM5; -.
DR   MaxQB; O43548; -.
DR   PaxDb; O43548; -.
DR   PeptideAtlas; O43548; -.
DR   PRIDE; O43548; -.
DR   Ensembl; ENST00000220420; ENSP00000220420; ENSG00000104055. [O43548-1]
DR   Ensembl; ENST00000349114; ENSP00000220419; ENSG00000104055. [O43548-2]
DR   GeneID; 9333; -.
DR   KEGG; hsa:9333; -.
DR   UCSC; uc001zrd.2; human. [O43548-1]
DR   CTD; 9333; -.
DR   DisGeNET; 9333; -.
DR   GeneCards; TGM5; -.
DR   HGNC; HGNC:11781; TGM5.
DR   MalaCards; TGM5; -.
DR   MIM; 603805; gene.
DR   MIM; 609796; phenotype.
DR   neXtProt; NX_O43548; -.
DR   OpenTargets; ENSG00000104055; -.
DR   Orphanet; 263534; Acral peeling skin syndrome.
DR   PharmGKB; PA36494; -.
DR   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   GeneTree; ENSGT00760000119108; -.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   InParanoid; O43548; -.
DR   KO; K05622; -.
DR   PhylomeDB; O43548; -.
DR   TreeFam; TF324278; -.
DR   Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR   GenomeRNAi; 9333; -.
DR   PRO; PR:O43548; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   Bgee; ENSG00000104055; -.
DR   CleanEx; HS_TGM5; -.
DR   ExpressionAtlas; O43548; baseline and differential.
DR   Genevisible; O43548; HS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; TAS:Reactome.
DR   GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
DR   GO; GO:0070268; P:cornification; TAS:Reactome.
DR   GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR   GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 3.
DR   Gene3D; 3.90.260.10; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   InterPro; IPR023608; Transglutaminase_animal.
DR   InterPro; IPR013808; Transglutaminase_AS.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   InterPro; IPR001102; Transglutaminase_N.
DR   Pfam; PF00927; Transglut_C; 2.
DR   Pfam; PF01841; Transglut_core; 1.
DR   Pfam; PF00868; Transglut_N; 1.
DR   PIRSF; PIRSF000459; TGM_EBP42; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF49309; SSF49309; 2.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Alternative splicing; Calcium;
KW   Complete proteome; Cytoplasm; Direct protein sequencing;
KW   Disease mutation; Metal-binding; Polymorphism; Reference proteome;
KW   Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:15290349}.
FT   CHAIN         2    720       Protein-glutamine gamma-
FT                                glutamyltransferase 5.
FT                                /FTId=PRO_0000213713.
FT   ACT_SITE    278    278       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    337    337       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   ACT_SITE    360    360       {ECO:0000255|PROSITE-ProRule:PRU10024}.
FT   METAL       400    400       Calcium. {ECO:0000250}.
FT   METAL       402    402       Calcium. {ECO:0000250}.
FT   METAL       448    448       Calcium. {ECO:0000250}.
FT   METAL       453    453       Calcium. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000269|PubMed:15290349}.
FT   VAR_SEQ      64    145       Missing (in isoform Short).
FT                                {ECO:0000303|PubMed:9452468}.
FT                                /FTId=VSP_006415.
FT   VARIANT      67     67       P -> S (in dbSNP:rs757598618).
FT                                {ECO:0000269|PubMed:11390390}.
FT                                /FTId=VAR_013248.
FT   VARIANT     109    109       T -> M (in dbSNP:rs113463533).
FT                                {ECO:0000269|PubMed:16380904}.
FT                                /FTId=VAR_025848.
FT   VARIANT     113    113       G -> C (in PSS2; completely abolishes the
FT                                enzyme activity; dbSNP:rs112292549).
FT                                {ECO:0000269|PubMed:16380904}.
FT                                /FTId=VAR_025849.
FT   VARIANT     352    352       A -> G (in dbSNP:rs28756768).
FT                                {ECO:0000269|PubMed:11390390}.
FT                                /FTId=VAR_013249.
FT   VARIANT     504    504       V -> M (in dbSNP:rs7171797).
FT                                /FTId=VAR_052564.
FT   VARIANT     521    521       Q -> R (in dbSNP:rs35985214).
FT                                /FTId=VAR_052565.
SQ   SEQUENCE   720 AA;  80778 MW;  9CF68884B48BAE1C CRC64;
     MAQGLEVALT DLQSSRNNVR HHTEEITVDH LLVRRGQAFN LTLYFRNRSF QPGLDNIIFV
     VETGPLPDLA LGTRAVFSLA RHHSPSPWIA WLETNGATST EVSLCAPPTA AVGRYLLKIH
     IDSFQGSVTA YQLGEFILLF NPWCPEDAVY LDSEPQRQEY VMNDYGFIYQ GSKNWIRPCP
     WNYGQFEDKI IDICLKLLDK SLHFQTDPAT DCALRGSPVY VSRVVCAMIN SNDDNGVLNG
     NWSENYTDGA NPAEWTGSVA ILKQWNATGC QPVRYGQCWV FAAVMCTVMR CLGIPTRVIT
     NFDSGHDTDG NLIIDEYYDN TGRILGNKKK DTIWNFHVWN ECWMARKDLP PAYGGWQVLD
     ATPQEMSNGV YCCGPASVRA IKEGEVDLNY DTPFVFSMVN ADCMSWLVQG GKEQKLHQDT
     SSVGNFISTK SIQSDERDDI TENYKYEEGS LQERQVFLKA LQKLKARSFH GSQRGAELQP
     SRPTSLSQDS PRSLHTPSLR PSDVVQVSLK FKLLDPPNMG QDICFVLLAL NMSSQFKDLK
     VNLSAQSLLH DGSPLSPFWQ DTAFITLSPK EAKTYPCKIS YSQYSQYLST DKLIRISALG
     EEKSSPEKIL VNKIITLSYP SITINVLGAA VVNQPLSIQV IFSNPLSEQV EDCVLTVEGS
     GLFKKQQKVF LGVLKPQHQA SIILETVPFK SGQRQIQANM RSNKFKDIKG YRNVYVDFAL
//
  All links  
Ontology (8)   
   GO (8)   
Disease (2)   
   OMIM (2)   
Drug (1)   
   DrugBank (1)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (10)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   HGNC (1)   
   ENSEMBL-UP (5)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (12)   
   EMBL (12)   
Protein domain (12)   
   InterPro (7)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (5)   
   PubMed (5)   
All databases (53)   

Download RDF
ID   B4DPS8_HUMAN            Unreviewed;       493 AA.
AC   B4DPS8;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   05-JUL-2017, entry version 46.
DE   SubName: Full=cDNA FLJ60773, highly similar to Protein-glutamine gamma-glutamyltransferase 5(EC 2.3.2.13) {ECO:0000313|EMBL:BAG60690.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG60690.1};
RN   [1] {ECO:0000313|EMBL:BAG60690.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K.,
RA   Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y.,
RA   Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M.,
RA   Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project focused on splicing variants.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK298479; BAG60690.1; -; mRNA.
DR   RefSeq; NP_004236.1; NM_004245.3.
DR   RefSeq; NP_963925.2; NM_201631.3.
DR   UniGene; Hs.129719; -.
DR   PaxDb; B4DPS8; -.
DR   PeptideAtlas; B4DPS8; -.
DR   PRIDE; B4DPS8; -.
DR   GeneID; 9333; -.
DR   KEGG; hsa:9333; -.
DR   CTD; 9333; -.
DR   PharmGKB; PA36494; -.
DR   eggNOG; ENOG410IFMV; Eukaryota.
DR   eggNOG; ENOG410XQEZ; LUCA.
DR   HOGENOM; HOG000231695; -.
DR   HOVERGEN; HBG004342; -.
DR   KO; K05622; -.
DR   GenomeRNAi; 9333; -.
DR   Genevisible; B4DPS8; HS.
DR   GO; GO:0003810; F:protein-glutamine gamma-glutamyltransferase activity; IEA:InterPro.
DR   GO; GO:0018149; P:peptide cross-linking; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
DR   Gene3D; 3.90.260.10; -; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002931; Transglutaminase-like.
DR   InterPro; IPR013808; Transglutaminase_AS.
DR   InterPro; IPR008958; Transglutaminase_C.
DR   Pfam; PF00927; Transglut_C; 2.
DR   Pfam; PF01841; Transglut_core; 1.
DR   SMART; SM00460; TGc; 1.
DR   SUPFAM; SSF49309; SSF49309; 2.
DR   PROSITE; PS00547; TRANSGLUTAMINASES; 1.
PE   2: Evidence at transcript level;
KW   Transferase {ECO:0000313|EMBL:BAG60690.1}.
FT   DOMAIN       43    136       TGc. {ECO:0000259|SMART:SM00460}.
SQ   SEQUENCE   493 AA;  55118 MW;  26CD70A0731B0A29 CRC64;
     MINSNDDNGV LNGNWSENYT DGANPAEWTG SVAILKQWNA TGCQPVRYGQ CWVFAAVMCT
     VMRCLGIPTR VITNFDSGHD TDGNLIIDEY YDNTGRILGN KKKDTIWNFH VWNECWMARK
     DPPPGYGGWQ VLDATPQEMS NGVYCCGPAS VRAIKEGEVD LNYDTPFVFS MVNADCMSWL
     VQGGKEQKLH QDTSSVGNFI STKSIQSDER DDITENYKYE EGSLQERQVF LKALQKLKAR
     SFHGSQRGAE LQPSRPTSLS QDSPRSLHTP SLRPSDVVQV SLKFKLLDPP NMGQDICFVL
     LALNMSSQFK DLKVNLSAQS LLHDGSPLSP FWQDTAFITL SPKEAKTYPC KISYSQYSQY
     LSTDKLIRIS ALGEEKSSPE KILVNKIITL SYPSITINVL GAAVVNQPLS IQVIFSNPLS
     EQVEDCVLTV EGSGLFKKQQ KVFLGVLKPQ HQASIILETV PFKSGQRQIQ ANMRSNKFKD
     IKGYRNVYVD FAL
//
  All links  
Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (8)   
   InterPro (4)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (18)   

Download RDF
DBGET integrated database retrieval system