UniProt ID | 1433T_HUMAN | |
---|---|---|
UniProt AC | P27348 | |
Protein Name | 14-3-3 protein theta | |
Gene Name | YWHAQ | |
Organism | Homo sapiens (Human). | |
Sequence Length | 245 | |
Subcellular Localization | Cytoplasm. In neurons, axonally transported to the nerve terminals. | |
Protein Description | Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Negatively regulates the kinase activity of PDPK1.. | |
Protein Sequence | MEKTELIQKAKLAEQAERYDDMATCMKAVTEQGAELSNEERNLLSVAYKNVVGGRRSAWRVISSIEQKTDTSDKKLQLIKDYREKVESELRSICTTVLELLDKYLIANATNPESKVFYLKMKGDYFRYLAEVACGDDRKQTIDNSQGAYQEAFDISKKEMQPTHPIRLGLALNFSVFYYEILNNPELACTLAKTAFDEAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDSAGEECDAAEGAEN | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MEKTELIQ -------CCHHHHHH | 12.29 | 25944712 | |
3 | Acetylation | -----MEKTELIQKA -----CCHHHHHHHH | 46.10 | 19608861 | |
3 | Ubiquitination | -----MEKTELIQKA -----CCHHHHHHHH | 46.10 | 23000965 | |
4 | Phosphorylation | ----MEKTELIQKAK ----CCHHHHHHHHH | 23.79 | 26270265 | |
9 | Acetylation | EKTELIQKAKLAEQA CHHHHHHHHHHHHHH | 40.26 | 23236377 | |
9 | Ubiquitination | EKTELIQKAKLAEQA CHHHHHHHHHHHHHH | 40.26 | 23000965 | |
9 | Malonylation | EKTELIQKAKLAEQA CHHHHHHHHHHHHHH | 40.26 | 26320211 | |
9 | Neddylation | EKTELIQKAKLAEQA CHHHHHHHHHHHHHH | 40.26 | 32015554 | |
11 | Acetylation | TELIQKAKLAEQAER HHHHHHHHHHHHHHH | 56.09 | 25953088 | |
11 | Ubiquitination | TELIQKAKLAEQAER HHHHHHHHHHHHHHH | 56.09 | 23000965 | |
19 | Phosphorylation | LAEQAERYDDMATCM HHHHHHHHHHHHHHH | 14.06 | 29396449 | |
24 | Phosphorylation | ERYDDMATCMKAVTE HHHHHHHHHHHHHHH | 13.39 | 29396449 | |
25 | S-nitrosylation | RYDDMATCMKAVTEQ HHHHHHHHHHHHHHH | 1.59 | 2212679 | |
25 | Glutathionylation | RYDDMATCMKAVTEQ HHHHHHHHHHHHHHH | 1.59 | 22555962 | |
25 | S-nitrosocysteine | RYDDMATCMKAVTEQ HHHHHHHHHHHHHHH | 1.59 | - | |
27 | Ubiquitination | DDMATCMKAVTEQGA HHHHHHHHHHHHHHH | 41.68 | 21906983 | |
27 | Acetylation | DDMATCMKAVTEQGA HHHHHHHHHHHHHHH | 41.68 | 25953088 | |
30 | Phosphorylation | ATCMKAVTEQGAELS HHHHHHHHHHHHHCC | 27.70 | 21601212 | |
37 | Phosphorylation | TEQGAELSNEERNLL HHHHHHCCHHHHHHH | 33.43 | 20873877 | |
45 | Phosphorylation | NEERNLLSVAYKNVV HHHHHHHHHHHHCHH | 14.10 | 19664994 | |
48 | Phosphorylation | RNLLSVAYKNVVGGR HHHHHHHHHCHHCCC | 10.84 | 22617229 | |
49 | Sumoylation | NLLSVAYKNVVGGRR HHHHHHHHCHHCCCH | 33.26 | 28112733 | |
49 | Succinylation | NLLSVAYKNVVGGRR HHHHHHHHCHHCCCH | 33.26 | 23954790 | |
49 | Acetylation | NLLSVAYKNVVGGRR HHHHHHHHCHHCCCH | 33.26 | 19608861 | |
49 | Ubiquitination | NLLSVAYKNVVGGRR HHHHHHHHCHHCCCH | 33.26 | 23000965 | |
57 | Phosphorylation | NVVGGRRSAWRVISS CHHCCCHHHHHHHHH | 30.72 | 20068231 | |
63 | Phosphorylation | RSAWRVISSIEQKTD HHHHHHHHHHHHCCC | 23.54 | 27273156 | |
64 | Phosphorylation | SAWRVISSIEQKTDT HHHHHHHHHHHCCCC | 21.01 | 23911959 | |
68 | Acetylation | VISSIEQKTDTSDKK HHHHHHHCCCCCHHH | 35.26 | 19608861 | |
68 | Ubiquitination | VISSIEQKTDTSDKK HHHHHHHCCCCCHHH | 35.26 | 23000965 | |
68 | Malonylation | VISSIEQKTDTSDKK HHHHHHHCCCCCHHH | 35.26 | 26320211 | |
74 | Ubiquitination | QKTDTSDKKLQLIKD HCCCCCHHHHHHHHH | 55.97 | 23000965 | |
75 | Ubiquitination | KTDTSDKKLQLIKDY CCCCCHHHHHHHHHH | 46.59 | 23000965 | |
80 | Succinylation | DKKLQLIKDYREKVE HHHHHHHHHHHHHHH | 58.25 | 23954790 | |
80 | Acetylation | DKKLQLIKDYREKVE HHHHHHHHHHHHHHH | 58.25 | 25953088 | |
80 | Ubiquitination | DKKLQLIKDYREKVE HHHHHHHHHHHHHHH | 58.25 | 23000965 | |
82 | Nitration | KLQLIKDYREKVESE HHHHHHHHHHHHHHH | 18.70 | - | |
82 | Phosphorylation | KLQLIKDYREKVESE HHHHHHHHHHHHHHH | 18.70 | 21406692 | |
85 | Succinylation | LIKDYREKVESELRS HHHHHHHHHHHHHHH | 42.16 | 23954790 | |
85 | Ubiquitination | LIKDYREKVESELRS HHHHHHHHHHHHHHH | 42.16 | 23000965 | |
85 | Acetylation | LIKDYREKVESELRS HHHHHHHHHHHHHHH | 42.16 | 23749302 | |
88 | Phosphorylation | DYREKVESELRSICT HHHHHHHHHHHHHHH | 44.94 | 24719451 | |
92 | Phosphorylation | KVESELRSICTTVLE HHHHHHHHHHHHHHH | 34.34 | 20068231 | |
94 | S-nitrosocysteine | ESELRSICTTVLELL HHHHHHHHHHHHHHH | 2.48 | - | |
94 | S-nitrosylation | ESELRSICTTVLELL HHHHHHHHHHHHHHH | 2.48 | 19483679 | |
95 | Phosphorylation | SELRSICTTVLELLD HHHHHHHHHHHHHHH | 20.47 | 20068231 | |
96 | Phosphorylation | ELRSICTTVLELLDK HHHHHHHHHHHHHHH | 20.77 | 28348404 | |
103 | Ubiquitination | TVLELLDKYLIANAT HHHHHHHHHHHHCCC | 41.76 | 21906983 | |
104 | Phosphorylation | VLELLDKYLIANATN HHHHHHHHHHHCCCC | 11.74 | 20068231 | |
104 | Nitration | VLELLDKYLIANATN HHHHHHHHHHHCCCC | 11.74 | - | |
110 | Phosphorylation | KYLIANATNPESKVF HHHHHCCCCCCCCEE | 51.63 | 20068231 | |
114 | Phosphorylation | ANATNPESKVFYLKM HCCCCCCCCEEEEEE | 35.06 | 20068231 | |
115 | Succinylation | NATNPESKVFYLKMK CCCCCCCCEEEEEEC | 34.40 | 23954790 | |
115 | Acetylation | NATNPESKVFYLKMK CCCCCCCCEEEEEEC | 34.40 | 19608861 | |
115 | Ubiquitination | NATNPESKVFYLKMK CCCCCCCCEEEEEEC | 34.40 | 23000965 | |
120 | Acetylation | ESKVFYLKMKGDYFR CCCEEEEEECCCHHH | 27.47 | 25825284 | |
120 | Ubiquitination | ESKVFYLKMKGDYFR CCCEEEEEECCCHHH | 27.47 | 23000965 | |
122 | Ubiquitination | KVFYLKMKGDYFRYL CEEEEEECCCHHHHH | 47.22 | 23000965 | |
122 | Acetylation | KVFYLKMKGDYFRYL CEEEEEECCCHHHHH | 47.22 | 26822725 | |
125 | Phosphorylation | YLKMKGDYFRYLAEV EEEECCCHHHHHHHH | 9.91 | 21253578 | |
128 | Phosphorylation | MKGDYFRYLAEVACG ECCCHHHHHHHHHCC | 10.60 | 24927040 | |
134 | Glutathionylation | RYLAEVACGDDRKQT HHHHHHHCCCCCCCC | 8.09 | 22555962 | |
134 | S-nitrosylation | RYLAEVACGDDRKQT HHHHHHHCCCCCCCC | 8.09 | 20140087 | |
134 | S-nitrosocysteine | RYLAEVACGDDRKQT HHHHHHHCCCCCCCC | 8.09 | - | |
139 | Acetylation | VACGDDRKQTIDNSQ HHCCCCCCCCCCCCC | 59.80 | 11921019 | |
139 | Ubiquitination | VACGDDRKQTIDNSQ HHCCCCCCCCCCCCC | 59.80 | 22053931 | |
139 | Malonylation | VACGDDRKQTIDNSQ HHCCCCCCCCCCCCC | 59.80 | 26320211 | |
141 | Phosphorylation | CGDDRKQTIDNSQGA CCCCCCCCCCCCCCH | 33.08 | 22186773 | |
145 | Phosphorylation | RKQTIDNSQGAYQEA CCCCCCCCCCHHHHH | 26.66 | 28152594 | |
149 | Phosphorylation | IDNSQGAYQEAFDIS CCCCCCHHHHHHHCC | 17.45 | 28152594 | |
156 | O-linked_Glycosylation | YQEAFDISKKEMQPT HHHHHHCCHHHCCCC | 39.25 | 30379171 | |
156 | Phosphorylation | YQEAFDISKKEMQPT HHHHHHCCHHHCCCC | 39.25 | 22186783 | |
157 | Acetylation | QEAFDISKKEMQPTH HHHHHCCHHHCCCCC | 53.76 | 23236377 | |
157 | Ubiquitination | QEAFDISKKEMQPTH HHHHHCCHHHCCCCC | 53.76 | 23000965 | |
158 | Acetylation | EAFDISKKEMQPTHP HHHHCCHHHCCCCCC | 52.18 | 18525141 | |
158 | Ubiquitination | EAFDISKKEMQPTHP HHHHCCHHHCCCCCC | 52.18 | 23000965 | |
160 | Sulfoxidation | FDISKKEMQPTHPIR HHCCHHHCCCCCCCC | 8.75 | 28183972 | |
193 | Ubiquitination | ELACTLAKTAFDEAI HHHHHHHHHHHHHHH | 43.42 | - | |
205 | Phosphorylation | EAIAELDTLNEDSYK HHHHHHHCCCCCCCC | 44.07 | 27732954 | |
210 | Phosphorylation | LDTLNEDSYKDSTLI HHCCCCCCCCCHHHH | 28.09 | 28102081 | |
211 | Phosphorylation | DTLNEDSYKDSTLIM HCCCCCCCCCHHHHH | 31.01 | 119397 | |
212 | Methylation | TLNEDSYKDSTLIMQ CCCCCCCCCHHHHHH | 49.51 | - | |
212 | Ubiquitination | TLNEDSYKDSTLIMQ CCCCCCCCCHHHHHH | 49.51 | 16196087 | |
214 | Phosphorylation | NEDSYKDSTLIMQLL CCCCCCCHHHHHHHH | 22.44 | 22617229 | |
215 | Phosphorylation | EDSYKDSTLIMQLLR CCCCCCHHHHHHHHH | 30.36 | 19664994 | |
218 | Sulfoxidation | YKDSTLIMQLLRDNL CCCHHHHHHHHHCCC | 2.30 | 21406390 | |
226 | Phosphorylation | QLLRDNLTLWTSDSA HHHHCCCEEEECCCC | 26.89 | 23927012 | |
229 | Phosphorylation | RDNLTLWTSDSAGEE HCCCEEEECCCCCCC | 26.26 | 30266825 | |
230 | Phosphorylation | DNLTLWTSDSAGEEC CCCEEEECCCCCCCC | 20.27 | 25463755 | |
232 | Phosphorylation | LTLWTSDSAGEECDA CEEEECCCCCCCCCH | 37.63 | 20201521 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
232 | S | Phosphorylation | Kinase | BCR | P11274 | PSP |
232 | S | Phosphorylation | Kinase | CK2A1 | P68400 | PSP |
232 | S | Phosphorylation | Kinase | CSNK1A1 | P48729 | GPS |
232 | S | Phosphorylation | Kinase | CK1-FAMILY | - | GPS |
232 | S | Phosphorylation | Kinase | CK1_GROUP | - | PhosphoELM |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
232 | S | Phosphorylation |
| 9360956 |
* 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 1433T_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 MET-1; LYS-3; LYS-49; LYS-68 ANDLYS-115, 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 SER-232, AND MASSSPECTROMETRY. | |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASSSPECTROMETRY. | |
"14-3-3 is phosphorylated by casein kinase I on residue 233.Phosphorylation at this site in vivo regulates Raf/14-3-3interaction."; Dubois T., Rommel C., Howell S., Steinhussen U., Soneji Y.,Morrice N., Moelling K., Aitken A.; J. Biol. Chem. 272:28882-28888(1997). Cited for: PHOSPHORYLATION AT SER-232, AND MASS SPECTROMETRY. |