TGM5_HUMAN - dbPTM
TGM5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TGM5_HUMAN
UniProt AC O43548
Protein Name Protein-glutamine gamma-glutamyltransferase 5
Gene Name TGM5
Organism Homo sapiens (Human).
Sequence Length 720
Subcellular Localization Cytoplasm . Associated with intermediate filaments.
Protein Description Catalyzes the cross-linking of proteins and the conjugation of polyamines to proteins. Contributes to the formation of the cornified cell envelope of keratinocytes..
Protein Sequence MAQGLEVALTDLQSSRNNVRHHTEEITVDHLLVRRGQAFNLTLYFRNRSFQPGLDNIIFVVETGPLPDLALGTRAVFSLARHHSPSPWIAWLETNGATSTEVSLCAPPTAAVGRYLLKIHIDSFQGSVTAYQLGEFILLFNPWCPEDAVYLDSEPQRQEYVMNDYGFIYQGSKNWIRPCPWNYGQFEDKIIDICLKLLDKSLHFQTDPATDCALRGSPVYVSRVVCAMINSNDDNGVLNGNWSENYTDGANPAEWTGSVAILKQWNATGCQPVRYGQCWVFAAVMCTVMRCLGIPTRVITNFDSGHDTDGNLIIDEYYDNTGRILGNKKKDTIWNFHVWNECWMARKDLPPAYGGWQVLDATPQEMSNGVYCCGPASVRAIKEGEVDLNYDTPFVFSMVNADCMSWLVQGGKEQKLHQDTSSVGNFISTKSIQSDERDDITENYKYEEGSLQERQVFLKALQKLKARSFHGSQRGAELQPSRPTSLSQDSPRSLHTPSLRPSDVVQVSLKFKLLDPPNMGQDICFVLLALNMSSQFKDLKVNLSAQSLLHDGSPLSPFWQDTAFITLSPKEAKTYPCKISYSQYSQYLSTDKLIRISALGEEKSSPEKILVNKIITLSYPSITINVLGAAVVNQPLSIQVIFSNPLSEQVEDCVLTVEGSGLFKKQQKVFLGVLKPQHQASIILETVPFKSGQRQIQANMRSNKFKDIKGYRNVYVDFAL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAQGLEVAL
------CCCCCEEEH
16.4915290349
10PhosphorylationQGLEVALTDLQSSRN
CCCEEEHHHHHHHCC
25.5628122231
14PhosphorylationVALTDLQSSRNNVRH
EEHHHHHHHCCCCCC
38.2628122231
15PhosphorylationALTDLQSSRNNVRHH
EHHHHHHHCCCCCCC
26.5228122231
78PhosphorylationLGTRAVFSLARHHSP
HHHHHHHHHHHCCCC
17.9622964224
217PhosphorylationTDCALRGSPVYVSRV
CCHHHCCCCEEEEEE
12.5428796482
220PhosphorylationALRGSPVYVSRVVCA
HHCCCCEEEEEEEEE
8.9728796482
468PhosphorylationLQKLKARSFHGSQRG
HHHHHHHHCCCCCCC
26.8430631047
481PhosphorylationRGAELQPSRPTSLSQ
CCCCCCCCCCCCCCC
37.6230631047
484PhosphorylationELQPSRPTSLSQDSP
CCCCCCCCCCCCCCC
40.98-
485PhosphorylationLQPSRPTSLSQDSPR
CCCCCCCCCCCCCCC
28.80-
490PhosphorylationPTSLSQDSPRSLHTP
CCCCCCCCCCCCCCC
17.99-
498PhosphorylationPRSLHTPSLRPSDVV
CCCCCCCCCCHHHCE
37.8624719451
568PhosphorylationDTAFITLSPKEAKTY
CEEEEEECHHHHCCC
25.8524719451
575PhosphorylationSPKEAKTYPCKISYS
CHHHHCCCCCEEEHH
13.1122817900
581PhosphorylationTYPCKISYSQYSQYL
CCCCEEEHHHHHHHC
11.8522817900
587PhosphorylationSYSQYSQYLSTDKLI
EHHHHHHHCCCCCEE
9.1822817900
681PhosphorylationLKPQHQASIILETVP
CCCHHHEEEEEEECC
12.0022210691
686PhosphorylationQASIILETVPFKSGQ
HEEEEEEECCCCCCH
29.9922210691
691PhosphorylationLETVPFKSGQRQIQA
EEECCCCCCHHHHHH
40.3022210691

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TGM5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TGM5_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TGM5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPICE_HUMANSPICE1physical
28514442
RFTN1_HUMANRFTN1physical
28514442
UBB_HUMANUBBphysical
28514442
BCD1_HUMANZNHIT6physical
28514442
DOCK7_HUMANDOCK7physical
28514442
PDZ11_HUMANPDZD11physical
28514442
IF4E2_HUMANEIF4E2physical
28514442
RPA43_HUMANTWISTNBphysical
28514442
INT14_HUMANVWA9physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609796Peeling skin syndrome 2 (PSS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00130L-Glutamine
Regulatory Network of TGM5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Transglutaminase 5 is acetylated at the N-terminal end.";
Rufini A., Vilbois F., Paradisi A., Oddi S., Tartaglione R., Leta A.,Bagetta G., Guerrieri P., Finazzi-Agro' A., Melino G., Candi E.;
Amino Acids 26:425-430(2004).
Cited for: PROTEIN SEQUENCE OF 2-16, SUBCELLULAR LOCATION, ACETYLATION AT ALA-2,INDUCTION BY TPA AND CALCIUM, AND MASS SPECTROMETRY.

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