UniProt ID | TRAF2_HUMAN | |
---|---|---|
UniProt AC | Q12933 | |
Protein Name | TNF receptor-associated factor 2 | |
Gene Name | TRAF2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 501 | |
Subcellular Localization | Cytoplasm . | |
Protein Description | Regulates activation of NF-kappa-B and JNK and plays a central role in the regulation of cell survival and apoptosis. Required for normal antibody isotype switching from IgM to IgG. Has E3 ubiquitin-protein ligase activity and promotes 'Lys-63'-linked ubiquitination of target proteins, such as BIRC3, RIPK1 and TICAM1. Is an essential constituent of several E3 ubiquitin-protein ligase complexes, where it promotes the ubiquitination of target proteins by bringing them into contact with other E3 ubiquitin ligases. Regulates BIRC2 and BIRC3 protein levels by inhibiting their autoubiquitination and subsequent degradation; this does not depend on the TRAF2 RING-type zinc finger domain. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR. In complex with BIRC2 or BIRC3, promotes ubiquitination of IKBKE.. | |
Protein Sequence | MAAASVTPPGSLELLQPGFSKTLLGTKLEAKYLCSACRNVLRRPFQAQCGHRYCSFCLASILSSGPQNCAACVHEGIYEEGISILESSSAFPDNAARREVESLPAVCPSDGCTWKGTLKEYESCHEGRCPLMLTECPACKGLVRLGEKERHLEHECPERSLSCRHCRAPCCGADVKAHHEVCPKFPLTCDGCGKKKIPREKFQDHVKTCGKCRVPCRFHAIGCLETVEGEKQQEHEVQWLREHLAMLLSSVLEAKPLLGDQSHAGSELLQRCESLEKKTATFENIVCVLNREVERVAMTAEACSRQHRLDQDKIEALSSKVQQLERSIGLKDLAMADLEQKVLEMEASTYDGVFIWKISDFARKRQEAVAGRIPAIFSPAFYTSRYGYKMCLRIYLNGDGTGRGTHLSLFFVVMKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPDVTSSSFQRPVNDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAAASVTPP ------CCCCCCCCC | 16.25 | 21406692 | |
5 | Phosphorylation | ---MAAASVTPPGSL ---CCCCCCCCCCCC | 23.07 | 29255136 | |
5 (in isoform 2) | Phosphorylation | - | 23.07 | 21406692 | |
7 (in isoform 2) | Phosphorylation | - | 22.67 | 21406692 | |
7 | Phosphorylation | -MAAASVTPPGSLEL -CCCCCCCCCCCCHH | 22.67 | 29255136 | |
11 | Phosphorylation | ASVTPPGSLELLQPG CCCCCCCCCHHCCCC | 25.17 | 29255136 | |
11 (in isoform 2) | Phosphorylation | - | 25.17 | 21406692 | |
20 | Phosphorylation | ELLQPGFSKTLLGTK HHCCCCCCCHHCCCH | 30.55 | 20068231 | |
21 | Ubiquitination | LLQPGFSKTLLGTKL HCCCCCCCHHCCCHH | 40.71 | 21890473 | |
21 | Ubiquitination | LLQPGFSKTLLGTKL HCCCCCCCHHCCCHH | 40.71 | 21890473 | |
21 | Ubiquitination | LLQPGFSKTLLGTKL HCCCCCCCHHCCCHH | 40.71 | 21890473 | |
21 (in isoform 1) | Ubiquitination | - | 40.71 | 21890473 | |
21 (in isoform 2) | Ubiquitination | - | 40.71 | 21890473 | |
21 | Ubiquitination | LLQPGFSKTLLGTKL HCCCCCCCHHCCCHH | 40.71 | 11907583 | |
22 (in isoform 2) | Phosphorylation | - | 26.47 | 21406692 | |
22 | Phosphorylation | LQPGFSKTLLGTKLE CCCCCCCHHCCCHHH | 26.47 | 20068231 | |
26 | Phosphorylation | FSKTLLGTKLEAKYL CCCHHCCCHHHHHHH | 32.21 | 20068231 | |
26 (in isoform 2) | Phosphorylation | - | 32.21 | 21406692 | |
27 (in isoform 1) | Ubiquitination | - | 42.40 | 21890473 | |
27 | Ubiquitination | SKTLLGTKLEAKYLC CCHHCCCHHHHHHHH | 42.40 | 19150425 | |
27 (in isoform 2) | Ubiquitination | - | 42.40 | 21890473 | |
31 | Acetylation | LGTKLEAKYLCSACR CCCHHHHHHHHHHHH | 29.40 | 27452117 | |
31 | Ubiquitination | LGTKLEAKYLCSACR CCCHHHHHHHHHHHH | 29.40 | 19150425 | |
32 | Phosphorylation | GTKLEAKYLCSACRN CCHHHHHHHHHHHHH | 21.71 | 28152594 | |
55 | Phosphorylation | QCGHRYCSFCLASIL HCCCCCHHHHHHHHH | 15.29 | 22817900 | |
102 | Phosphorylation | AARREVESLPAVCPS HHHHHHHCCCEECCC | 44.84 | 30108239 | |
117 | Phosphorylation | DGCTWKGTLKEYESC CCCCEECCHHHHHHC | 30.81 | 18981220 | |
119 | Ubiquitination | CTWKGTLKEYESCHE CCEECCHHHHHHCCC | 59.07 | - | |
121 | Phosphorylation | WKGTLKEYESCHEGR EECCHHHHHHCCCCC | 16.14 | - | |
123 | Phosphorylation | GTLKEYESCHEGRCP CCHHHHHHCCCCCCC | 21.63 | 27251275 | |
140 | Ubiquitination | LTECPACKGLVRLGE EEECCCCCHHHHCCH | 58.34 | 21890473 | |
140 | Ubiquitination | LTECPACKGLVRLGE EEECCCCCHHHHCCH | 58.34 | 21890473 | |
140 | Ubiquitination | LTECPACKGLVRLGE EEECCCCCHHHHCCH | 58.34 | 21890473 | |
140 (in isoform 1) | Ubiquitination | - | 58.34 | 21890473 | |
140 | Ubiquitination | LTECPACKGLVRLGE EEECCCCCHHHHCCH | 58.34 | 21890473 | |
160 | Phosphorylation | EHECPERSLSCRHCR CCCCCCCCCCCCCCC | 23.99 | 29214152 | |
162 | Phosphorylation | ECPERSLSCRHCRAP CCCCCCCCCCCCCCC | 15.45 | 28555341 | |
176 | Ubiquitination | PCCGADVKAHHEVCP CCCCCCHHHHHCCCC | 42.42 | - | |
184 | Ubiquitination | AHHEVCPKFPLTCDG HHHCCCCCCCCCCCC | 55.26 | - | |
192 (in isoform 2) | Ubiquitination | - | 4.63 | 21890473 | |
201 | Ubiquitination | KKKIPREKFQDHVKT CCCCCHHHHHHHHHH | 49.99 | - | |
207 | Ubiquitination | EKFQDHVKTCGKCRV HHHHHHHHHCCCCCC | 34.38 | - | |
231 | Ubiquitination | LETVEGEKQQEHEVQ EEEECCHHHHHHHHH | 69.04 | - | |
255 | Ubiquitination | LSSVLEAKPLLGDQS HHHHHHHHHCCCCCC | 27.16 | 21890473 | |
255 | Ubiquitination | LSSVLEAKPLLGDQS HHHHHHHHHCCCCCC | 27.16 | 21890473 | |
255 (in isoform 1) | Ubiquitination | - | 27.16 | 21890473 | |
255 | Ubiquitination | LSSVLEAKPLLGDQS HHHHHHHHHCCCCCC | 27.16 | 19150425 | |
259 (in isoform 2) | Ubiquitination | - | 38.30 | - | |
262 | Phosphorylation | KPLLGDQSHAGSELL HHCCCCCCHHHHHHH | 21.75 | 23312004 | |
274 | Phosphorylation | ELLQRCESLEKKTAT HHHHHHHHHHHHHCC | 45.51 | - | |
277 | Ubiquitination | QRCESLEKKTATFEN HHHHHHHHHHCCHHH | 61.80 | - | |
278 | Ubiquitination | RCESLEKKTATFENI HHHHHHHHHCCHHHE | 33.73 | - | |
287 | Glutathionylation | ATFENIVCVLNREVE CCHHHEEEHHCHHHH | 2.26 | 22555962 | |
307 (in isoform 2) | Ubiquitination | - | 31.03 | 21890473 | |
313 | Ubiquitination | QHRLDQDKIEALSSK HHCCCHHHHHHHHHH | 36.49 | 21890473 | |
313 | Ubiquitination | QHRLDQDKIEALSSK HHCCCHHHHHHHHHH | 36.49 | 21890473 | |
313 (in isoform 1) | Ubiquitination | - | 36.49 | 21890473 | |
313 | 2-Hydroxyisobutyrylation | QHRLDQDKIEALSSK HHCCCHHHHHHHHHH | 36.49 | - | |
313 | Ubiquitination | QHRLDQDKIEALSSK HHCCCHHHHHHHHHH | 36.49 | 21890473 | |
320 | Ubiquitination | KIEALSSKVQQLERS HHHHHHHHHHHHHHH | 40.46 | 21890473 | |
320 | Ubiquitination | KIEALSSKVQQLERS HHHHHHHHHHHHHHH | 40.46 | 21890473 | |
320 (in isoform 1) | Ubiquitination | - | 40.46 | 21890473 | |
320 | Ubiquitination | KIEALSSKVQQLERS HHHHHHHHHHHHHHH | 40.46 | 21890473 | |
331 | Ubiquitination | LERSIGLKDLAMADL HHHHHCHHHHHHHHH | 45.54 | 21890473 | |
331 | Ubiquitination | LERSIGLKDLAMADL HHHHHCHHHHHHHHH | 45.54 | 21890473 | |
331 (in isoform 1) | Ubiquitination | - | 45.54 | 21890473 | |
331 | Ubiquitination | LERSIGLKDLAMADL HHHHHCHHHHHHHHH | 45.54 | 21890473 | |
335 | Sulfoxidation | IGLKDLAMADLEQKV HCHHHHHHHHHHHHH | 3.76 | 21406390 | |
365 (in isoform 2) | Ubiquitination | - | 33.74 | 21890473 | |
372 (in isoform 2) | Ubiquitination | - | 23.21 | 21890473 | |
383 (in isoform 2) | Ubiquitination | - | 10.56 | 21890473 | |
401 | Phosphorylation | IYLNGDGTGRGTHLS EEECCCCCCCCCCEE | 28.57 | - | |
431 | Phosphorylation | WPFNQKVTLMLLDQN CCCCCCEEEEEECCC | 17.31 | - | |
477 | Ubiquitination | PLFCPVSKMEAKNSY CCEEECHHHCCCCCC | 40.78 | - | |
481 | Ubiquitination | PVSKMEAKNSYVRDD ECHHHCCCCCCCCCC | 32.87 | 21890473 | |
481 | Ubiquitination | PVSKMEAKNSYVRDD ECHHHCCCCCCCCCC | 32.87 | 21890473 | |
481 (in isoform 1) | Ubiquitination | - | 32.87 | 21890473 | |
481 | Ubiquitination | PVSKMEAKNSYVRDD ECHHHCCCCCCCCCC | 32.87 | 19150425 | |
533 (in isoform 2) | Ubiquitination | - | 21890473 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
11 | S | Phosphorylation | Kinase | IKKE | Q14164 | PSP |
55 | S | Phosphorylation | Kinase | PRKCZ | Q05513 | GPS |
117 | T | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
117 | T | Phosphorylation | Kinase | PKC | - | Uniprot |
- | K | Ubiquitination | E3 ubiquitin ligase | BIRC2 | Q13490 | PMID:11907583 |
- | K | Ubiquitination | E3 ubiquitin ligase | TRAF2 | Q12933 | PMID:20876871 |
- | K | Ubiquitination | E3 ubiquitin ligase | STUB1 | Q9UNE7 | PMID:21793045 |
* 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 TRAF2_HUMAN !! |
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. |
loading...
Acetylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7 AND SER-11, AND MASSSPECTROMETRY. | |
"TRAF2 phosphorylation modulates tumor necrosis factor alpha-inducedgene expression and cell resistance to apoptosis."; Blackwell K., Zhang L., Thomas G.S., Sun S., Nakano H., Habelhah H.; Mol. Cell. Biol. 29:303-314(2009). Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH TNFRSF1A; RIPK1 AND IKKB,MUTAGENESIS OF SER-11, AND PHOSPHORYLATION AT SER-11. | |
"PKC phosphorylation of TRAF2 mediates IKKalpha/beta recruitment andK63-linked polyubiquitination."; Li S., Wang L., Dorf M.E.; Mol. Cell 33:30-42(2009). Cited for: FUNCTION, INTERACTION WITH IKKA; IKKB; TAB2 AND TAB3, UBIQUITINATIONAT LYS-31, PHOSPHORYLATION AT THR-117, MUTAGENESIS OF THR-117,UBIQUITINATION, AND SUBCELLULAR LOCATION. | |
Ubiquitylation | |
Reference | PubMed |
"PKC phosphorylation of TRAF2 mediates IKKalpha/beta recruitment andK63-linked polyubiquitination."; Li S., Wang L., Dorf M.E.; Mol. Cell 33:30-42(2009). Cited for: FUNCTION, INTERACTION WITH IKKA; IKKB; TAB2 AND TAB3, UBIQUITINATIONAT LYS-31, PHOSPHORYLATION AT THR-117, MUTAGENESIS OF THR-117,UBIQUITINATION, AND SUBCELLULAR LOCATION. |