TCAM1_HUMAN - dbPTM
TCAM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCAM1_HUMAN
UniProt AC Q8IUC6
Protein Name TIR domain-containing adapter molecule 1
Gene Name TICAM1
Organism Homo sapiens (Human).
Sequence Length 712
Subcellular Localization Cytoplasmic vesicle, autophagosome . Colocalizes with UBQLN1 in the autophagosome.
Protein Description Involved in innate immunity against invading pathogens. Adapter used by TLR3 and TLR4 (through TICAM2) to mediate NF-kappa-B and interferon-regulatory factor (IRF) activation, and to induce apoptosis. Ligand binding to these receptors results in TRIF recruitment through its TIR domain. Distinct protein-interaction motifs allow recruitment of the effector proteins TBK1, TRAF6 and RIPK1, which in turn, lead to the activation of transcription factors IRF3 and IRF7, NF-kappa-B and FADD respectively..
Protein Sequence MACTGPSLPSAFDILGAAGQDKLLYLKHKLKTPRPGCQGQDLLHAMVLLKLGQETEARISLEALKADAVARLVARQWAGVDSTEDPEEPPDVSWAVARLYHLLAEEKLCPASLRDVAYQEAVRTLSSRDDHRLGELQDEARNRCGWDIAGDPGSIRTLQSNLGCLPPSSALPSGTRSLPRPIDGVSDWSQGCSLRSTGSPASLASNLEISQSPTMPFLSLHRSPHGPSKLCDDPQASLVPEPVPGGCQEPEEMSWPPSGEIASPPELPSSPPPGLPEVAPDATSTGLPDTPAAPETSTNYPVECTEGSAGPQSLPLPILEPVKNPCSVKDQTPLQLSVEDTTSPNTKPCPPTPTTPETSPPPPPPPPSSTPCSAHLTPSSLFPSSLESSSEQKFYNFVILHARADEHIALRVREKLEALGVPDGATFCEDFQVPGRGELSCLQDAIDHSAFIILLLTSNFDCRLSLHQVNQAMMSNLTRQGSPDCVIPFLPLESSPAQLSSDTASLLSGLVRLDEHSQIFARKVANTFKPHRLQARKAMWRKEQDTRALREQSQHLDGERMQAAALNAAYSAYLQSYLSYQAQMEQLQVAFGSHMSFGTGAPYGARMPFGGQVPLGAPPPFPTWPGCPQPPPLHAWQAGTPPPPSPQPAAFPQSLPFPQSPAFPTASPAPPQSPGLQPLIIHHAQMVQLGLNNHMWNQRGSQAPEDKTQEAE
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
60PhosphorylationQETEARISLEALKAD
CCCHHHHCHHHHHHH
18.0118669648
65UbiquitinationRISLEALKADAVARL
HHCHHHHHHHHHHHH
51.79-
82O-linked_GlycosylationRQWAGVDSTEDPEEP
HHHCCCCCCCCCCCC
31.15OGP
175PhosphorylationSSALPSGTRSLPRPI
HHCCCCCCCCCCCCC
22.7923403867
177PhosphorylationALPSGTRSLPRPIDG
CCCCCCCCCCCCCCC
42.4323403867
196PhosphorylationSQGCSLRSTGSPASL
CCCCCCCCCCCCHHH
42.2720068231
197PhosphorylationQGCSLRSTGSPASLA
CCCCCCCCCCCHHHH
34.9324114839
199PhosphorylationCSLRSTGSPASLASN
CCCCCCCCCHHHHHC
19.8518669648
205PhosphorylationGSPASLASNLEISQS
CCCHHHHHCCEECCC
47.4421712546
210PhosphorylationLASNLEISQSPTMPF
HHHCCEECCCCCCCE
18.4125850435
212PhosphorylationSNLEISQSPTMPFLS
HCCEECCCCCCCEEE
18.6225850435
214PhosphorylationLEISQSPTMPFLSLH
CEECCCCCCCEEEEC
42.6025850435
219PhosphorylationSPTMPFLSLHRSPHG
CCCCCEEEECCCCCC
23.6225850435
223PhosphorylationPFLSLHRSPHGPSKL
CEEEECCCCCCCCCC
15.5324114839
263PhosphorylationPPSGEIASPPELPSS
CCCCCCCCCCCCCCC
46.8022468782
341PhosphorylationLQLSVEDTTSPNTKP
CEEEEECCCCCCCCC
18.7025627689
342PhosphorylationQLSVEDTTSPNTKPC
EEEEECCCCCCCCCC
55.2825627689
343PhosphorylationLSVEDTTSPNTKPCP
EEEECCCCCCCCCCC
20.4625627689
346PhosphorylationEDTTSPNTKPCPPTP
ECCCCCCCCCCCCCC
39.4825627689
388PhosphorylationLFPSSLESSSEQKFY
HCCCCCCCCCHHHCE
44.45-
389PhosphorylationFPSSLESSSEQKFYN
CCCCCCCCCHHHCEE
28.63-
390PhosphorylationPSSLESSSEQKFYNF
CCCCCCCCHHHCEEE
54.01-
500PhosphorylationESSPAQLSSDTASLL
CCCHHHCCHHHHHHH
17.68-
570PhosphorylationAAALNAAYSAYLQSY
HHHHHHHHHHHHHHH
7.45-
573PhosphorylationLNAAYSAYLQSYLSY
HHHHHHHHHHHHHHH
10.19-
577PhosphorylationYSAYLQSYLSYQAQM
HHHHHHHHHHHHHHH
6.16-
707UbiquitinationGSQAPEDKTQEAE--
CCCCCCHHHCCCC--
50.902190698

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
210SPhosphorylationKinaseTBK1Q9UHD2
Uniprot
-KUbiquitinationE3 ubiquitin ligaseTANKQ92844
PMID:20047764
-KUbiquitinationE3 ubiquitin ligaseTRAF2Q12933
PMID:20047764
-KUbiquitinationE3 ubiquitin ligaseTRAF6Q9Y4K3
PMID:20047764
-KUbiquitinationE3 ubiquitin ligaseKCTD10Q9H3F6
PMID:32484264
-KUbiquitinationE3 ubiquitin ligaseWWP2O00308
PMID:23479606

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
6Kubiquitylation

28747347
210SPhosphorylation

25636800

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 TCAM1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RIPK1_HUMANRIPK1physical
15064760
RN216_HUMANRNF216physical
16968706
TRAF2_HUMANTRAF2physical
20047764
TRAF6_HUMANTRAF6physical
20047764
TANK_HUMANTANKphysical
21903422
TBK1_HUMANTBK1physical
21903422
UBQL1_HUMANUBQLN1physical
21695056
TLR4_HUMANTLR4physical
19656901
TBK1_HUMANTBK1physical
19656901
TRAF1_HUMANTRAF1physical
14982987
TRAF2_HUMANTRAF2physical
14982987
TRAF3_HUMANTRAF3physical
14982987
TRAF5_HUMANTRAF5physical
14982987
TRAF6_HUMANTRAF6physical
14982987
TLR3_HUMANTLR3physical
14982987
TNAP3_HUMANTNFAIP3physical
15474016
TRAF6_HUMANTRAF6physical
15474016
TRI56_HUMANTRIM56physical
22948160
TRAF4_HUMANTRAF4physical
16052631
TRAF1_HUMANTRAF1physical
16323247
TRAF6_HUMANTRAF6physical
14530355
TBK1_HUMANTBK1physical
14530355
TCAM2_HUMANTICAM2physical
12721283
MAVS_HUMANMAVSphysical
16153868
TRAF1_HUMANTRAF1physical
19795416
TRAF2_HUMANTRAF2physical
19795416
TRAF6_HUMANTRAF6physical
19795416
TRI38_HUMANTRIM38physical
23056470
KSYK_HUMANSYKphysical
23962979
TCAM1_HUMANTICAM1physical
24577058
CARM1_HUMANCARM1physical
26186194
TRAF6_HUMANTRAF6physical
24812060
RIPK1_HUMANRIPK1physical
25736436
TRAF6_HUMANTRAF6physical
25736436
TBK1_HUMANTBK1physical
25736436
TCAM2_HUMANTICAM2physical
25736436
TBK1_HUMANTBK1physical
28049150
CARM1_HUMANCARM1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614850Herpes simplex encephalitis 4 (HSE4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TCAM1_HUMAN

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Related Literatures of Post-Translational Modification

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