dbPTM

TRAF1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRAF1_MOUSE
UniProt AC	P39428
Protein Name	TNF receptor-associated factor 1
Gene Name	Traf1
Organism	Mus musculus (Mouse).
Sequence Length	409
Subcellular Localization	Cytoplasm.
Protein Description	Adapter molecule that regulates the activation of NF-kappa-B and JNK. Plays a role in the regulation of cell survival and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part of a E3 ubiquitin-protein ligase complex that promotes ubiquitination of target proteins, such as MAP3K14. The TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2 (By similarity)..
Protein Sequence	MASSSAPDENEFQFGCPPAPCQDPSEPRVLCCTACLSENLRDDEDRICPKCRADNLHPVSPGSPLTQEKVHSDVAEAEIMCPFAGVGCSFKGSPQSMQEHEATSQSSHLYLLLAVLKEWKSSPGSNLGSAPMALERNLSELQLQAAVEATGDLEVDCYRAPCCESQEELALQHLVKEKLLAQLEEKLRVFANIVAVLNKEVEASHLALAASIHQSQLDREHILSLEQRVVELQQTLAQKDQVLGKLEHSLRLMEEASFDGTFLWKITNVTKRCHESVCGRTVSLFSPAFYTAKYGYKLCLRLYLNGDGSGKKTHLSLFIVIMRGEYDALLPWPFRNKVTFMLLDQNNREHAIDAFRPDLSSASFQRPQSETNVASGCPLFFPLSKLQSPKHAYVKDDTMFLKCIVDTSA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
60	Phosphorylation	ADNLHPVSPGSPLTQ CCCCCCCCCCCCCCC	28.17	28725479
63	Phosphorylation	LHPVSPGSPLTQEKV CCCCCCCCCCCCHHH	21.81	28725479
66	Phosphorylation	VSPGSPLTQEKVHSD CCCCCCCCCHHHCCC	37.76	28833060
93	Phosphorylation	VGCSFKGSPQSMQEH CCCCCCCCCHHHHHH	21.98	25293948
96	Phosphorylation	SFKGSPQSMQEHEAT CCCCCCHHHHHHCCC	26.31	25293948
103	Phosphorylation	SMQEHEATSQSSHLY HHHHHCCCCHHHHHH	25.06	25293948
104	Phosphorylation	MQEHEATSQSSHLYL HHHHCCCCHHHHHHH	34.80	25293948
106	Phosphorylation	EHEATSQSSHLYLLL HHCCCCHHHHHHHHH	21.35	25293948
107	Phosphorylation	HEATSQSSHLYLLLA HCCCCHHHHHHHHHH	15.18	25293948
110	Phosphorylation	TSQSSHLYLLLAVLK CCHHHHHHHHHHHHH	7.00	25293948
139	Phosphorylation	MALERNLSELQLQAA CHHHHCCCHHHHHHH	39.55	18429822
165	Phosphorylation	YRAPCCESQEELALQ EECCCCCCHHHHHHH	29.04	22942356
291	Phosphorylation	LFSPAFYTAKYGYKL HCCHHHHHHHHCCCE	15.37	24759943

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
139	S	Phosphorylation	Kinase	PKN1	Q16512	PSP
139	S	Phosphorylation	Kinase	PKN1	P70268	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRAF1_MOUSE !!

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 TRAF1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TRAF1_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TRAF1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Negative regulation of constitutive NF-kappaB and JNK signaling byPKN1-mediated phosphorylation of TRAF1."; Kato T. Jr., Gotoh Y., Hoffmann A., Ono Y.; Genes Cells 13:509-520(2008). Cited for: FUNCTION, PHOSPHORYLATION AT SER-139, INTERACTION WITH TNFRSF1B, ANDMUTAGENESIS OF SER-139.	18429822 [Abstract]