TRAF1_HUMAN - dbPTM
TRAF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRAF1_HUMAN
UniProt AC Q13077
Protein Name TNF receptor-associated factor 1
Gene Name TRAF1
Organism Homo sapiens (Human).
Sequence Length 416
Subcellular Localization
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..
Protein Sequence MASSSGSSPRPAPDENEFPFGCPPTVCQDPKEPRALCCAGCLSENPRNGEDQICPKCRGEDLQSISPGSRLRTQEKAHPEVAEAGIGCPFAGVGCSFKGSPQSVQEHEVTSQTSHLNLLLGFMKQWKARLGCGLESGPMALEQNLSDLQLQAAVEVAGDLEVDCYRAPCSESQEELALQHFMKEKLLAELEGKLRVFENIVAVLNKEVEASHLALATSIHQSQLDRERILSLEQRVVELQQTLAQKDQALGKLEQSLRLMEEASFDGTFLWKITNVTRRCHESACGRTVSLFSPAFYTAKYGYKLCLRLYLNGDGTGKRTHLSLFIVIMRGEYDALLPWPFRNKVTFMLLDQNNREHAIDAFRPDLSSASFQRPQSETNVASGCPLFFPLSKLQSPKHAYVKDDTMFLKCIVETST
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
3Phosphorylation-----MASSSGSSPR
-----CCCCCCCCCC
24.6030108239
4Phosphorylation----MASSSGSSPRP
----CCCCCCCCCCC
29.2230108239
5Phosphorylation---MASSSGSSPRPA
---CCCCCCCCCCCC
39.9528450419
7Phosphorylation-MASSSGSSPRPAPD
-CCCCCCCCCCCCCC
38.8330108239
8PhosphorylationMASSSGSSPRPAPDE
CCCCCCCCCCCCCCC
28.5829507054
43PhosphorylationLCCAGCLSENPRNGE
EEECCCCCCCCCCCC
39.1330108239
61UbiquitinationCPKCRGEDLQSISPG
CCCCCCCCCCCCCCC
53.4822817900
63UbiquitinationKCRGEDLQSISPGSR
CCCCCCCCCCCCCCC
51.5522817900
64PhosphorylationCRGEDLQSISPGSRL
CCCCCCCCCCCCCCC
32.1228450419
66PhosphorylationGEDLQSISPGSRLRT
CCCCCCCCCCCCCCC
28.5830266825
69PhosphorylationLQSISPGSRLRTQEK
CCCCCCCCCCCCCHH
31.3730266825
71UbiquitinationSISPGSRLRTQEKAH
CCCCCCCCCCCHHHC
8.1222817900
96PhosphorylationPFAGVGCSFKGSPQS
CCCCCCCCCCCCCCC
24.8630108239
100PhosphorylationVGCSFKGSPQSVQEH
CCCCCCCCCCCHHEE
21.9830108239
103PhosphorylationSFKGSPQSVQEHEVT
CCCCCCCCHHEEECC
29.2030108239
110PhosphorylationSVQEHEVTSQTSHLN
CHHEEECCCHHHHHH
16.4830108239
111PhosphorylationVQEHEVTSQTSHLNL
HHEEECCCHHHHHHH
36.3130108239
113PhosphorylationEHEVTSQTSHLNLLL
EEECCCHHHHHHHHH
20.2030108239
114PhosphorylationHEVTSQTSHLNLLLG
EECCCHHHHHHHHHH
20.5230108239
124UbiquitinationNLLLGFMKQWKARLG
HHHHHHHHHHHHHHC
51.2322817900
127UbiquitinationLGFMKQWKARLGCGL
HHHHHHHHHHHCCCC
22.5722817900
146PhosphorylationMALEQNLSDLQLQAA
CCHHHCHHHHHHHHH
43.77-
170PhosphorylationDCYRAPCSESQEELA
EEEECCCCCCHHHHH
38.9430108239
172PhosphorylationYRAPCSESQEELALQ
EECCCCCCHHHHHHH
26.9730108239
183UbiquitinationLALQHFMKEKLLAEL
HHHHHHHHHHHHHHH
51.2422817900
185UbiquitinationLQHFMKEKLLAELEG
HHHHHHHHHHHHHHH
43.1922817900
193UbiquitinationLLAELEGKLRVFENI
HHHHHHHHHHHHHHH
24.6022817900
275UbiquitinationTFLWKITNVTRRCHE
EEEEEEECHHHHHHH
36.3125015289
310PhosphorylationYKLCLRLYLNGDGTG
CEEEEEEEECCCCCC
7.53-
316PhosphorylationLYLNGDGTGKRTHLS
EEECCCCCCCCCEEE
44.24-
320PhosphorylationGDGTGKRTHLSLFIV
CCCCCCCCEEEEEEE
30.5622210691
323PhosphorylationTGKRTHLSLFIVIMR
CCCCCEEEEEEEEEC
17.4022210691
395PhosphorylationFPLSKLQSPKHAYVK
EEHHHCCCCCCEEEC
46.4826091039
397UbiquitinationLSKLQSPKHAYVKDD
HHHCCCCCCEEECCC
46.2225015289

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
-KUbiquitinationE3 ubiquitin ligaseRNF31Q96EP0
PMID:25996949
-KUbiquitinationE3 ubiquitin ligaseBIRC2Q13490
PMID:15468071
-KUbiquitinationE3 ubiquitin ligaseBIRC3Q13489
PMID:15468071

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRAF1_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 TRAF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF2_HUMANTRAF2physical
14743216
SRC_HUMANSRCphysical
10635328
CFLAR_HUMANCFLARphysical
9208847
M3K5_HUMANMAP3K5physical
9774977
RIPK2_HUMANRIPK2physical
9705938
TANK_HUMANTANKphysical
8710854
CFLAR_HUMANCFLARphysical
10837247
TNR17_HUMANTNFRSF17physical
10903733
TNAP3_HUMANTNFAIP3physical
9928991
RIPK1_HUMANRIPK1physical
8612133
TRADD_HUMANTRADDphysical
8565075
BIRC2_HUMANBIRC2physical
8943045
BIRC2_HUMANBIRC2physical
21903422
DBLOH_HUMANDIABLOphysical
21903422
HOIL1_HUMANRBCK1physical
21903422
RNF31_HUMANRNF31physical
21903422
TRAF2_HUMANTRAF2physical
21903422
SRC_HUMANSRCphysical
15707590
SH3K1_HUMANSH3KBP1physical
15707590
TRAF2_HUMANTRAF2physical
10544141
TNR1B_HUMANTNFRSF1Bphysical
7859281
TRAF2_HUMANTRAF2physical
15383523
TCAM1_HUMANTICAM1physical
16323247
TRAF2_HUMANTRAF2physical
9500555
M3K14_HUMANMAP3K14physical
9275204
TRAF2_HUMANTRAF2physical
14557256
TR19L_HUMANRELTphysical
11313261
TR13C_HUMANTNFRSF13Cphysical
19698991
TRAF3_HUMANTRAF3physical
9718306
TRAF2_HUMANTRAF2physical
9718306
TRAF1_HUMANTRAF1physical
9718306
TRADD_HUMANTRADDphysical
19287455
TNR1A_HUMANTNFRSF1Aphysical
19287455
TRAF2_HUMANTRAF2physical
19287455
RIPK1_HUMANRIPK1physical
19287455
IKKA_HUMANCHUKphysical
19287455
TNR9_HUMANTNFRSF9physical
15941918
TNR4_HUMANTNFRSF4physical
15941918
TRAF1_HUMANTRAF1physical
8069916
TRAF2_HUMANTRAF2physical
8069916
NF2IP_HUMANNFATC2IPphysical
11435475
ZMY11_HUMANZMYND11physical
20138174
UBE2O_HUMANUBE2Ophysical
23381138
TNR1B_HUMANTNFRSF1Bphysical
18429822
M3K14_HUMANMAP3K14physical
23543740
TRAF6_HUMANTRAF6physical
21988832
TRAF1_HUMANTRAF1physical
25416956
TRAF6_HUMANTRAF6physical
25416956
ZNF20_HUMANZNF20physical
25416956
ZN124_HUMANZNF124physical
25416956
TCL1A_HUMANTCL1Aphysical
25416956
AK17A_HUMANAKAP17Aphysical
25416956
RIPK1_HUMANRIPK1physical
25416956
CFLAR_HUMANCFLARphysical
25416956
LATS1_HUMANLATS1physical
25416956
NGAP_HUMANRASAL2physical
25416956
NUP58_HUMANNUPL1physical
25416956
JOS1_HUMANJOSD1physical
25416956
TSSC4_HUMANTSSC4physical
25416956
NEBL_HUMANNEBLphysical
25416956
GLRX3_HUMANGLRX3physical
25416956
MARE2_HUMANMAPRE2physical
25416956
PRDM7_HUMANPRDM7physical
25416956
SNW1_HUMANSNW1physical
25416956
ASPP1_HUMANPPP1R13Bphysical
25416956
SIK3_HUMANSIK3physical
25416956
HEY2_HUMANHEY2physical
25416956
ZFY26_HUMANZFYVE26physical
25416956
CHSP1_HUMANCARHSP1physical
25416956
GORS2_HUMANGORASP2physical
25416956
A1CF_HUMANA1CFphysical
25416956
MYEF2_HUMANMYEF2physical
25416956
PF21A_HUMANPHF21Aphysical
25416956
WAC_HUMANWACphysical
25416956
SPG21_HUMANSPG21physical
25416956
POP5_HUMANPOP5physical
25416956
ZN581_HUMANZNF581physical
25416956
NB5R2_HUMANCYB5R2physical
25416956
CCHCR_HUMANCCHCR1physical
25416956
QRIC1_HUMANQRICH1physical
25416956
MIC19_HUMANCHCHD3physical
25416956
CA109_HUMANC1orf109physical
25416956
CN105_HUMANC14orf105physical
25416956
FA86C_HUMANFAM86C1physical
25416956
RBM41_HUMANRBM41physical
25416956
RYDEN_HUMANC19orf66physical
25416956
TRPV6_HUMANTRPV6physical
25416956
SKT_HUMANKIAA1217physical
25416956
P66B_HUMANGATAD2Bphysical
25416956
Z512B_HUMANZNF512Bphysical
25416956
NUFP2_HUMANNUFIP2physical
25416956
CC146_HUMANCCDC146physical
25416956
DMRT3_HUMANDMRT3physical
25416956
MET17_HUMANMETTL17physical
25416956
DPTOR_HUMANDEPTORphysical
25416956
SCNM1_HUMANSCNM1physical
25416956
ZFY21_HUMANZFYVE21physical
25416956
ARSJ_HUMANARSJphysical
25416956
ZC21C_HUMANZC2HC1Cphysical
25416956
DOK3_HUMANDOK3physical
25416956
FXL18_HUMANFBXL18physical
25416956
THAP7_HUMANTHAP7physical
25416956
CDCA3_HUMANCDCA3physical
25416956
RASF5_HUMANRASSF5physical
25416956
PKHN1_HUMANPLEKHN1physical
25416956
F161A_HUMANFAM161Aphysical
25416956
BEX2_HUMANBEX2physical
25416956
ZN587_HUMANZNF587physical
25416956
FBF1_HUMANFBF1physical
25416956
CC120_HUMANCCDC120physical
25416956
CE030_HUMANC5orf30physical
25416956
ZN502_HUMANZNF502physical
25416956
SYCE1_HUMANSYCE1physical
25416956
HAUS1_HUMANHAUS1physical
25416956
TBC16_HUMANTBC1D16physical
25416956
ZN440_HUMANZNF440physical
25416956
CA216_HUMANC1orf216physical
25416956
RBM45_HUMANRBM45physical
25416956
ZN572_HUMANZNF572physical
25416956
ZN417_HUMANZNF417physical
25416956
C2CD6_HUMANALS2CR11physical
25416956
S2548_HUMANSLC25A48physical
25416956
ZN564_HUMANZNF564physical
25416956
CC116_HUMANCCDC116physical
25416956
OLIG3_HUMANOLIG3physical
25416956
MORN3_HUMANMORN3physical
25416956
SRCRL_HUMANSSC5Dphysical
25416956
RTP5_HUMANRTP5physical
25416956
TRI42_HUMANTRIM42physical
25416956
KLH38_HUMANKLHL38physical
25416956
ZN662_HUMANZNF662physical
25416956
TRAF6_HUMANTRAF6physical
21516116
AB17A_HUMANABHD17Aphysical
21516116
FBF1_HUMANFBF1physical
21516116
ZN697_HUMANZNF697physical
21516116
RNF31_HUMANRNF31physical
25996949
TNAP3_HUMANTNFAIP3physical
25996949
UBC_HUMANUBCphysical
25996949
TRAF3_HUMANTRAF3physical
25996949
TRAF2_HUMANTRAF2physical
25996949
TBK1_HUMANTBK1physical
25996949
FBX28_HUMANFBXO28physical
25996949
HTRA2_HUMANHTRA2physical
25996949
TANK_HUMANTANKphysical
25996949
BIRC2_HUMANBIRC2physical
25996949
GOGA3_HUMANGOLGA3physical
25996949
ECI2_HUMANECI2physical
25996949
ECH1_HUMANECH1physical
25996949
BIRC3_HUMANBIRC3physical
25996949
TBB4B_HUMANTUBB4Bphysical
25996949
PBX1_HUMANPBX1physical
25996949
SKP1_HUMANSKP1physical
25996949
PBX2_HUMANPBX2physical
25996949
APC_HUMANAPCphysical
25996949
DCAF7_HUMANDCAF7physical
25996949
DBLOH_HUMANDIABLOphysical
25996949
OTUD4_HUMANOTUD4physical
25996949
E2AK3_HUMANEIF2AK3physical
25996949
SQSTM_HUMANSQSTM1physical
25996949
HOIL1_HUMANRBCK1physical
25996949
SHRPN_HUMANSHARPINphysical
25996949
TNIP1_HUMANTNIP1physical
25996949
NEMO_HUMANIKBKGphysical
25996949
VAV3_HUMANVAV3physical
27507811
NEMO_HUMANIKBKGphysical
27893701
TANK_HUMANTANKphysical
28514442
TRAF6_HUMANTRAF6physical
28514442
FBX28_HUMANFBXO28physical
28514442
OTUD4_HUMANOTUD4physical
28514442
SNX29_HUMANSNX29physical
28514442
TBK1_HUMANTBK1physical
28514442
OSBL6_HUMANOSBPL6physical
28514442
PKNX1_HUMANPKNOX1physical
28514442
RBCC1_HUMANRB1CC1physical
28514442
UBB_HUMANUBBphysical
28514442
HYEP_HUMANEPHX1physical
28514442
PEX13_HUMANPEX13physical
28514442
ECI2_HUMANECI2physical
28514442
CUL1_HUMANCUL1physical
28514442
ZMYM6_HUMANZMYM6physical
28514442
OSBL3_HUMANOSBPL3physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRAF1_HUMAN

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"Mass spectrometric analysis of tumor necrosis factor receptor-associated factor 1 ubiquitination mediated by cellular inhibitor ofapoptosis 2.";
Lee J.S., Hong U.S., Lee T.H., Yoon S.K., Yoon J.B.;
Proteomics 4:3376-3382(2004).
Cited for: UBIQUITINATION AT LYS-185 AND LYS-193, MASS SPECTROMETRY, ANDMUTAGENESIS OF LYS-185 AND LYS-193.

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