UniProt ID | SEBP2_HUMAN | |
---|---|---|
UniProt AC | Q96T21 | |
Protein Name | Selenocysteine insertion sequence-binding protein 2 | |
Gene Name | SECISBP2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 854 | |
Subcellular Localization |
Isoform 1: Nucleus . Isoform 2: Mitochondrion . |
|
Protein Description | Binds to the SECIS element in the 3'-UTR of some mRNAs encoding selenoproteins. Binding is stimulated by SELB.. | |
Protein Sequence | MASEGPREPESEGIKLSADVKPFVPRFAGLNVAWLESSEACVFPSSAATYYPFVQEPPVTEQKIYTEDMAFGASTFPPQYLSSEITLHPYAYSPYTLDSTQNVYSVPGSQYLYNQPSCYRGFQTVKHRNENTCPLPQEMKALFKKKTYDEKKTYDQQKFDSERADGTISSEIKSARGSHHLSIYAENSLKSDGYHKRTDRKSRIIAKNVSTSKPEFEFTTLDFPELQGAENNMSEIQKQPKWGPVHSVSTDISLLREVVKPAAVLSKGEIVVKNNPNESVTANAATNSPSCTRELSWTPMGYVVRQTLSTELSAAPKNVTSMINLKTIASSADPKNVSIPSSEALSSDPSYNKEKHIIHPTQKSKASQGSDLEQNEASRKNKKKKEKSTSKYEVLTVQEPPRIEDAEEFPNLAVASERRDRIETPKFQSKQQPQDNFKNNVKKSQLPVQLDLGGMLTALEKKQHSQHAKQSSKPVVVSVGAVPVLSKECASGERGRRMSQMKTPHNPLDSSAPLMKKGKQREIPKAKKPTSLKKIILKERQERKQRLQENAVSPAFTSDDTQDGESGGDDQFPEQAELSGPEGMDELISTPSVEDKSEEPPGTELQRDTEASHLAPNHTTFPKIHSRRFRDYCSQMLSKEVDACVTDLLKELVRFQDRMYQKDPVKAKTKRRLVLGLREVLKHLKLKKLKCVIISPNCEKIQSKGGLDDTLHTIIDYACEQNIPFVFALNRKALGRSLNKAVPVSVVGIFSYDGAQDQFHKMVELTVAARQAYKTMLENVQQELVGEPRPQAPPSLPTQGPSCPAEDGPPALKEKEEPHYIEIWKKHLEAYSGCTLELEESLEASTSQMMNLNL | |
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 | ------MASEGPREP ------CCCCCCCCC | 19.11 | - | |
15 | Acetylation | EPESEGIKLSADVKP CCCCCCCCCCCCCCC | 47.44 | 12433889 | |
21 | Ubiquitination | IKLSADVKPFVPRFA CCCCCCCCCCCCCCC | 33.03 | - | |
26 | Methylation | DVKPFVPRFAGLNVA CCCCCCCCCCCCEEE | 28.84 | 115493599 | |
58 | Ubiquitination | YPFVQEPPVTEQKIY CCCCCCCCCCCCEEE | 44.93 | - | |
60 | Phosphorylation | FVQEPPVTEQKIYTE CCCCCCCCCCEEECC | 38.17 | 29759185 | |
65 | Phosphorylation | PVTEQKIYTEDMAFG CCCCCEEECCCCCCC | 15.88 | 29759185 | |
66 | Phosphorylation | VTEQKIYTEDMAFGA CCCCEEECCCCCCCC | 29.05 | 29759185 | |
90 | Ubiquitination | SEITLHPYAYSPYTL CCEEECCCCCCCCCC | 13.87 | - | |
105 | Ubiquitination | DSTQNVYSVPGSQYL CCCCCEEECCHHHHH | 19.97 | - | |
126 | Ubiquitination | YRGFQTVKHRNENTC HCCCCCCCCCCCCCC | 39.99 | - | |
140 | Ubiquitination | CPLPQEMKALFKKKT CCCCHHHHHHHCCCC | 40.98 | - | |
158 | Ubiquitination | KKTYDQQKFDSERAD CCCCCHHHHCHHHCC | 45.57 | - | |
173 | Ubiquitination | GTISSEIKSARGSHH CCCHHHHHHCCCCCC | 33.73 | - | |
174 | Phosphorylation | TISSEIKSARGSHHL CCHHHHHHCCCCCCE | 28.94 | 20044836 | |
176 | Methylation | SSEIKSARGSHHLSI HHHHHHCCCCCCEEE | 54.99 | 115493607 | |
184 | Phosphorylation | GSHHLSIYAENSLKS CCCCEEEEEECCCCC | 12.41 | 25159151 | |
199 | Ubiquitination | DGYHKRTDRKSRIIA CCCCCCCCCCCCEEE | 61.10 | - | |
238 | Ubiquitination | NNMSEIQKQPKWGPV CCHHHHHHCCCCCCC | 74.38 | - | |
247 | Phosphorylation | PKWGPVHSVSTDISL CCCCCCCCCCCCHHH | 20.28 | 23186163 | |
249 | Phosphorylation | WGPVHSVSTDISLLR CCCCCCCCCCHHHHH | 24.31 | 25954137 | |
250 | Phosphorylation | GPVHSVSTDISLLRE CCCCCCCCCHHHHHH | 34.89 | 25954137 | |
253 | Phosphorylation | HSVSTDISLLREVVK CCCCCCHHHHHHHHC | 24.94 | 23186163 | |
260 | Ubiquitination | SLLREVVKPAAVLSK HHHHHHHCHHHEECC | 33.83 | - | |
267 | Ubiquitination | KPAAVLSKGEIVVKN CHHHEECCCEEEECC | 57.30 | - | |
273 | Ubiquitination | SKGEIVVKNNPNESV CCCEEEECCCCCCCC | 39.86 | - | |
285 | Ubiquitination | ESVTANAATNSPSCT CCCEEECCCCCCCCC | 13.71 | - | |
286 | Phosphorylation | SVTANAATNSPSCTR CCEEECCCCCCCCCC | 33.54 | 25159151 | |
288 | Phosphorylation | TANAATNSPSCTREL EEECCCCCCCCCCEE | 17.52 | 25159151 | |
290 | Phosphorylation | NAATNSPSCTRELSW ECCCCCCCCCCEECC | 28.13 | 21712546 | |
292 | Phosphorylation | ATNSPSCTRELSWTP CCCCCCCCCEECCCC | 31.36 | 29978859 | |
296 | Phosphorylation | PSCTRELSWTPMGYV CCCCCEECCCCCCCC | 24.93 | 28857561 | |
307 | Phosphorylation | MGYVVRQTLSTELSA CCCCHHHHHCHHHCC | 16.47 | - | |
326 | Ubiquitination | VTSMINLKTIASSAD CCCCEEHHHHHCCCC | 33.14 | - | |
335 | Ubiquitination | IASSADPKNVSIPSS HHCCCCCCCCCCCCH | 71.21 | - | |
338 | Phosphorylation | SADPKNVSIPSSEAL CCCCCCCCCCCHHHH | 37.87 | 29978859 | |
341 | Phosphorylation | PKNVSIPSSEALSSD CCCCCCCCHHHHCCC | 38.86 | 29978859 | |
341 | O-linked_Glycosylation | PKNVSIPSSEALSSD CCCCCCCCHHHHCCC | 38.86 | 30379171 | |
342 | Phosphorylation | KNVSIPSSEALSSDP CCCCCCCHHHHCCCC | 22.87 | 28985074 | |
346 | Phosphorylation | IPSSEALSSDPSYNK CCCHHHHCCCCCCCC | 39.48 | 29978859 | |
347 | Phosphorylation | PSSEALSSDPSYNKE CCHHHHCCCCCCCCC | 55.16 | 29978859 | |
350 | Phosphorylation | EALSSDPSYNKEKHI HHHCCCCCCCCCCCC | 46.45 | 29978859 | |
351 | Phosphorylation | ALSSDPSYNKEKHII HHCCCCCCCCCCCCC | 35.32 | 29978859 | |
353 | Ubiquitination | SSDPSYNKEKHIIHP CCCCCCCCCCCCCCH | 60.96 | - | |
355 | Ubiquitination | DPSYNKEKHIIHPTQ CCCCCCCCCCCCHHH | 41.53 | - | |
361 | Phosphorylation | EKHIIHPTQKSKASQ CCCCCCHHHHCCCCC | 34.17 | 25690035 | |
364 | Phosphorylation | IIHPTQKSKASQGSD CCCHHHHCCCCCCCH | 24.52 | 25247763 | |
367 | Phosphorylation | PTQKSKASQGSDLEQ HHHHCCCCCCCHHHH | 38.52 | 30108239 | |
370 | Phosphorylation | KSKASQGSDLEQNEA HCCCCCCCHHHHHHH | 31.24 | 25159151 | |
378 | Phosphorylation | DLEQNEASRKNKKKK HHHHHHHHHHHHHHH | 37.29 | 21406692 | |
384 | Ubiquitination | ASRKNKKKKEKSTSK HHHHHHHHHCCCCCC | 68.71 | - | |
388 | Phosphorylation | NKKKKEKSTSKYEVL HHHHHCCCCCCCEEE | 38.72 | 26657352 | |
392 | Phosphorylation | KEKSTSKYEVLTVQE HCCCCCCCEEEECCC | 15.84 | 28796482 | |
396 | Phosphorylation | TSKYEVLTVQEPPRI CCCCEEEECCCCCCC | 25.89 | 28796482 | |
424 | Phosphorylation | ERRDRIETPKFQSKQ HHHHCCCCCCCCCCC | 29.43 | 29978859 | |
429 | Phosphorylation | IETPKFQSKQQPQDN CCCCCCCCCCCCCCC | 35.25 | 29978859 | |
499 | Phosphorylation | GERGRRMSQMKTPHN CCCHHCHHHCCCCCC | 25.88 | 24719451 | |
533 | Acetylation | AKKPTSLKKIILKER CCCCCCHHHHHHHHH | 41.51 | 24431589 | |
609 | Phosphorylation | GTELQRDTEASHLAP CCCCCCCCHHHHCCC | 35.32 | 24732914 | |
612 | Phosphorylation | LQRDTEASHLAPNHT CCCCCHHHHCCCCCC | 16.89 | 24732914 | |
619 | Phosphorylation | SHLAPNHTTFPKIHS HHCCCCCCCCCCHHH | 36.45 | 24732914 | |
620 | Phosphorylation | HLAPNHTTFPKIHSR HCCCCCCCCCCHHHH | 30.32 | 24732914 | |
632 | Ubiquitination | HSRRFRDYCSQMLSK HHHHHHHHHHHHHHH | 6.97 | - | |
646 | Phosphorylation | KEVDACVTDLLKELV HHHHHHHHHHHHHHH | 22.33 | 28258704 | |
650 | Ubiquitination | ACVTDLLKELVRFQD HHHHHHHHHHHHHHH | 57.19 | - | |
660 | Phosphorylation | VRFQDRMYQKDPVKA HHHHHHHHCCCCCCH | 17.19 | 18083107 | |
662 | Ubiquitination | FQDRMYQKDPVKAKT HHHHHHCCCCCCHHH | 46.65 | - | |
803 | Glutathionylation | LPTQGPSCPAEDGPP CCCCCCCCCCCCCCC | 4.10 | 22833525 | |
815 | Ubiquitination | GPPALKEKEEPHYIE CCCCCCCCCCCCHHH | 66.83 | - | |
820 | Phosphorylation | KEKEEPHYIEIWKKH CCCCCCCHHHHHHHH | 15.80 | 28796482 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of SEBP2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SEBP2_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 SEBP2_HUMAN !! |
Kegg Disease | ||||||
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There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
609698 | Abnormal thyroid hormone metabolism (ATHYHM) | |||||
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 |
"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. |