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Q08188

- TGM3_HUMAN

UniProt

Q08188 - TGM3_HUMAN

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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

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

Ca2+2 PublicationsNote: Binds 3 Ca(2+) cations per subunit. Binds 1 Ca(2+) as a zymogen, and binds 2 more Ca(2+) cations, 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
Complete GO annotation...

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
Complete GO annotation...

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. 14 interactions.
IntActiQ08188. 5 interactions.
MINTiMINT-7950929.
STRINGi9606.ENSP00000370867.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119108.
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

        10         20         30         40         50
MAALGVQSIN WQTAFNRQAH HTDKFSSQEL ILRRGQNFQV LMIMNKGLGS
60 70 80 90 100
NERLEFIVST GPYPSESAMT KAVFPLSNGS SGGWSAVLQA SNGNTLTISI
110 120 130 140 150
SSPASAPIGR YTMALQIFSQ GGISSVKLGT FILLFNPWLN VDSVFMGNHA
160 170 180 190 200
EREEYVQEDA GIIFVGSTNR IGMIGWNFGQ FEEDILSICL SILDRSLNFR
210 220 230 240 250
RDAATDVASR NDPKYVGRVL SAMINSNDDN GVLAGNWSGT YTGGRDPRSW
260 270 280 290 300
NGSVEILKNW KKSGFSPVRY GQCWVFAGTL NTALRSLGIP SRVITNFNSA
310 320 330 340 350
HDTDRNLSVD VYYDPMGNPL DKGSDSVWNF HVWNEGWFVR SDLGPSYGGW
360 370 380 390 400
QVLDATPQER SQGVFQCGPA SVIGVREGDV QLNFDMPFIF AEVNADRITW
410 420 430 440 450
LYDNTTGKQW KNSVNSHTIG RYISTKAVGS NARMDVTDKY KYPEGSDQER
460 470 480 490 500
QVFQKALGKL KPNTPFAATS SMGLETEEQE PSIIGKLKVA GMLAVGKEVN
510 520 530 540 550
LVLLLKNLSR DTKTVTVNMT AWTIIYNGTL VHEVWKDSAT MSLDPEEEAE
560 570 580 590 600
HPIKISYAQY EKYLKSDNMI RITAVCKVPD ESEVVVERDI ILDNPTLTLE
610 620 630 640 650
VLNEARVRKP VNVQMLFSNP LDEPVRDCVL MVEGSGLLLG NLKIDVPTLG
660 670 680 690
PKEGSRVRFD ILPSRSGTKQ LLADFSCNKF PAIKAMLSID VAE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 14 interactions.
IntActi Q08188. 5 interactions.
MINTi MINT-7950929.
STRINGi 9606.ENSP00000370867.

Chemistry

BindingDBi Q08188.
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 GC20P002276.
HGNCi HGNC:11779. TGM3.
HPAi HPA004728.
MIMi 600238. gene.
neXtProti NX_Q08188.
PharmGKBi PA36492.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG80379.
GeneTreei ENSGT00760000119108.
HOVERGENi HBG004342.
InParanoidi Q08188.
KOi K05620.
OMAi EILPTRS.
OrthoDBi EOG7WT40M.
PhylomeDBi Q08188.
TreeFami TF324278.

Miscellaneous databases

ChiTaRSi TGM3. human.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 145 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