UniProt ID | FAF2_HUMAN | |
---|---|---|
UniProt AC | Q96CS3 | |
Protein Name | FAS-associated factor 2 | |
Gene Name | FAF2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 445 | |
Subcellular Localization | Cytoplasm . Lipid droplet . Endoplasmic reticulum . | |
Protein Description | Plays an important role in endoplasmic reticulum-associated degradation (ERAD) that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. [PubMed: 18711132] | |
Protein Sequence | MAAPEERDLTQEQTEKLLQFQDLTGIESMDQCRHTLEQHNWNIEAAVQDRLNEQEGVPSVFNPPPSRPLQVNTADHRIYSYVVSRPQPRGLLGWGYYLIMLPFRFTYYTILDIFRFALRFIRPDPRSRVTDPVGDIVSFMHSFEEKYGRAHPVFYQGTYSQALNDAKRELRFLLVYLHGDDHQDSDEFCRNTLCAPEVISLINTRMLFWACSTNKPEGYRVSQALRENTYPFLAMIMLKDRRMTVVGRLEGLIQPDDLINQLTFIMDANQTYLVSERLEREERNQTQVLRQQQDEAYLASLRADQEKERKKREERERKRRKEEEVQQQKLAEERRRQNLQEEKERKLECLPPEPSPDDPESVKIIFKLPNDSRVERRFHFSQSLTVIHDFLFSLKESPEKFQIEANFPRRVLPCIPSEEWPNPPTLQEAGLSHTEVLFVQDLTDE | |
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 | ------MAAPEERDL ------CCCHHHCCC | 31.55 | 19413330 | |
10 | Phosphorylation | APEERDLTQEQTEKL CHHHCCCCHHHHHHH | 34.06 | 25159151 | |
14 | Phosphorylation | RDLTQEQTEKLLQFQ CCCCHHHHHHHHHHH | 34.04 | - | |
16 | Ubiquitination | LTQEQTEKLLQFQDL CCHHHHHHHHHHHCH | 58.86 | 23503661 | |
24 | Phosphorylation | LLQFQDLTGIESMDQ HHHHHCHHCCCCHHH | 44.39 | 28348404 | |
28 | Phosphorylation | QDLTGIESMDQCRHT HCHHCCCCHHHHHHH | 26.24 | 29214152 | |
29 | Sulfoxidation | DLTGIESMDQCRHTL CHHCCCCHHHHHHHH | 2.40 | 21406390 | |
32 | Glutathionylation | GIESMDQCRHTLEQH CCCCHHHHHHHHHHC | 2.76 | 22555962 | |
59 | Phosphorylation | NEQEGVPSVFNPPPS HHCCCCCCCCCCCCC | 36.61 | 28555341 | |
66 | Phosphorylation | SVFNPPPSRPLQVNT CCCCCCCCCCCCCCC | 52.91 | 28555341 | |
79 | Phosphorylation | NTADHRIYSYVVSRP CCCCCEEEEEECCCC | 8.23 | 27273156 | |
80 | Phosphorylation | TADHRIYSYVVSRPQ CCCCEEEEEECCCCC | 14.74 | 25884760 | |
81 | Phosphorylation | ADHRIYSYVVSRPQP CCCEEEEEECCCCCC | 6.47 | 28796482 | |
84 | Phosphorylation | RIYSYVVSRPQPRGL EEEEEECCCCCCCCC | 28.35 | 27251275 | |
101 | Ubiquitination | WGYYLIMLPFRFTYY CCEEEEECCHHCHHH | 2.62 | 23503661 | |
107 | Phosphorylation | MLPFRFTYYTILDIF ECCHHCHHHHHHHHH | 8.90 | 22468782 | |
108 | Phosphorylation | LPFRFTYYTILDIFR CCHHCHHHHHHHHHH | 5.57 | 22468782 | |
122 | Ubiquitination | RFALRFIRPDPRSRV HHHHHHHCCCCCCCC | 27.19 | 23000965 | |
142 | Phosphorylation | DIVSFMHSFEEKYGR HHHHHHHHHHHHHCC | 23.67 | 24719451 | |
146 | Ubiquitination | FMHSFEEKYGRAHPV HHHHHHHHHCCCCCE | 45.89 | 21906983 | |
155 | Phosphorylation | GRAHPVFYQGTYSQA CCCCCEEECCCHHHH | 13.28 | 28152594 | |
158 | Phosphorylation | HPVFYQGTYSQALND CCEEECCCHHHHHHH | 12.41 | 28152594 | |
159 | Phosphorylation | PVFYQGTYSQALNDA CEEECCCHHHHHHHH | 12.95 | 28152594 | |
160 | Phosphorylation | VFYQGTYSQALNDAK EEECCCHHHHHHHHH | 14.60 | 28152594 | |
167 | Acetylation | SQALNDAKRELRFLL HHHHHHHHHHHHHEE | 49.63 | 19608861 | |
167 | Ubiquitination | SQALNDAKRELRFLL HHHHHHHHHHHHHEE | 49.63 | 23000965 | |
167 | 2-Hydroxyisobutyrylation | SQALNDAKRELRFLL HHHHHHHHHHHHHEE | 49.63 | - | |
167 | Malonylation | SQALNDAKRELRFLL HHHHHHHHHHHHHEE | 49.63 | 26320211 | |
194 | Ubiquitination | EFCRNTLCAPEVISL HHHHHCCCHHHHHHH | 5.82 | 23503661 | |
194 | Glutathionylation | EFCRNTLCAPEVISL HHHHHCCCHHHHHHH | 5.82 | 22555962 | |
215 | Acetylation | FWACSTNKPEGYRVS HHHHCCCCCCCCCHH | 44.53 | 26051181 | |
215 | Ubiquitination | FWACSTNKPEGYRVS HHHHCCCCCCCCCHH | 44.53 | - | |
229 | Phosphorylation | SQALRENTYPFLAMI HHHHHHCCCCEEEEE | 28.02 | 28674151 | |
239 | Ubiquitination | FLAMIMLKDRRMTVV EEEEEECCCCCEEEH | 31.63 | 23503661 | |
244 | Phosphorylation | MLKDRRMTVVGRLEG ECCCCCEEEHHEHHC | 15.38 | 24719451 | |
262 | Ubiquitination | PDDLINQLTFIMDAN HHHHHHHHEEEEECC | 3.50 | 23503661 | |
265 | Ubiquitination | LINQLTFIMDANQTY HHHHHEEEEECCCCE | 1.74 | 23503661 | |
266 | Ubiquitination | INQLTFIMDANQTYL HHHHEEEEECCCCEE | 3.30 | 23503661 | |
273 | Ubiquitination | MDANQTYLVSERLER EECCCCEEHHHHHHH | 3.77 | 22817900 | |
276 | Ubiquitination | NQTYLVSERLEREER CCCEEHHHHHHHHHH | 54.53 | 22817900 | |
284 | Ubiquitination | RLEREERNQTQVLRQ HHHHHHHHHHHHHHH | 53.16 | 27667366 | |
286 | Phosphorylation | EREERNQTQVLRQQQ HHHHHHHHHHHHHHH | 24.97 | 22210691 | |
297 | Phosphorylation | RQQQDEAYLASLRAD HHHHCHHHHHHHHHH | 10.76 | 29978859 | |
298 | Ubiquitination | QQQDEAYLASLRADQ HHHCHHHHHHHHHHH | 3.17 | 22817900 | |
300 | Phosphorylation | QDEAYLASLRADQEK HCHHHHHHHHHHHHH | 18.78 | 29978859 | |
301 | Ubiquitination | DEAYLASLRADQEKE CHHHHHHHHHHHHHH | 4.32 | 22817900 | |
307 | Ubiquitination | SLRADQEKERKKREE HHHHHHHHHHHHHHH | 58.13 | 23503661 | |
310 | Ubiquitination | ADQEKERKKREERER HHHHHHHHHHHHHHH | 58.22 | 23503661 | |
311 | Ubiquitination | DQEKERKKREERERK HHHHHHHHHHHHHHH | 71.86 | 23503661 | |
318 | Ubiquitination | KREERERKRRKEEEV HHHHHHHHHHHHHHH | 52.37 | 23000965 | |
321 | Ubiquitination | ERERKRRKEEEVQQQ HHHHHHHHHHHHHHH | 73.78 | 21906983 | |
322 | Ubiquitination | RERKRRKEEEVQQQK HHHHHHHHHHHHHHH | 58.54 | 23000965 | |
329 | Ubiquitination | EEEVQQQKLAEERRR HHHHHHHHHHHHHHH | 45.38 | 21906983 | |
343 | Ubiquitination | RQNLQEEKERKLECL HHHHHHHHHHHHCCC | 63.17 | 21906983 | |
346 | Ubiquitination | LQEEKERKLECLPPE HHHHHHHHHCCCCCC | 50.13 | 29901268 | |
346 | Acetylation | LQEEKERKLECLPPE HHHHHHHHHCCCCCC | 50.13 | 26051181 | |
350 | Ubiquitination | KERKLECLPPEPSPD HHHHHCCCCCCCCCC | 6.06 | 23000965 | |
355 | Ubiquitination | ECLPPEPSPDDPESV CCCCCCCCCCCHHHC | 39.02 | 23000965 | |
355 | Phosphorylation | ECLPPEPSPDDPESV CCCCCCCCCCCHHHC | 39.02 | 30266825 | |
361 | Phosphorylation | PSPDDPESVKIIFKL CCCCCHHHCEEEEEC | 33.81 | 30266825 | |
363 | Ubiquitination | PDDPESVKIIFKLPN CCCHHHCEEEEECCC | 39.09 | 23000965 | |
367 | Ubiquitination | ESVKIIFKLPNDSRV HHCEEEEECCCCCCH | 53.26 | 23000965 | |
367 | Acetylation | ESVKIIFKLPNDSRV HHCEEEEECCCCCCH | 53.26 | 25953088 | |
367 | Malonylation | ESVKIIFKLPNDSRV HHCEEEEECCCCCCH | 53.26 | 26320211 | |
383 | Phosphorylation | RRFHFSQSLTVIHDF HEEECCCHHHHHHHH | 25.47 | 27251275 | |
385 | Phosphorylation | FHFSQSLTVIHDFLF EECCCHHHHHHHHHH | 23.74 | 27251275 | |
393 | Phosphorylation | VIHDFLFSLKESPEK HHHHHHHHCCCCCCC | 40.45 | 24719451 | |
395 | Ubiquitination | HDFLFSLKESPEKFQ HHHHHHCCCCCCCCC | 55.75 | 23000965 | |
400 | Ubiquitination | SLKESPEKFQIEANF HCCCCCCCCCEEECC | 46.05 | 23000965 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FAF2_HUMAN !! |
* 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 FAF2_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. |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-167, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-79, AND MASSSPECTROMETRY. |