UniProt ID | SPAG7_HUMAN | |
---|---|---|
UniProt AC | O75391 | |
Protein Name | Sperm-associated antigen 7 | |
Gene Name | SPAG7 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 227 | |
Subcellular Localization | Nucleus . | |
Protein Description | ||
Protein Sequence | MADLLGSILSSMEKPPSLGDQETRRKAREQAARLKKLQEQEKQQKVEFRKRMEKEVSDFIQDSGQIKKKFQPMNKIERSILHDVVEVAGLTSFSFGEDDDCRYVMIFKKEFAPSDEELDSYRRGEEWDPQKAEEKRKLKELAQRQEEEAAQQGPVVVSPASDYKDKYSHLIGKGAAKDAAHMLQANKTYGCVPVANKRDTRSIEEAMNEIRAKKRLRQSGEELPPTS | |
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 | ------MADLLGSIL ------CHHHHHHHH | 19.03 | 22223895 | |
7 | Phosphorylation | -MADLLGSILSSMEK -CHHHHHHHHHHCCC | 21.96 | 22199227 | |
10 | Phosphorylation | DLLGSILSSMEKPPS HHHHHHHHHCCCCCC | 26.43 | 22199227 | |
11 | Phosphorylation | LLGSILSSMEKPPSL HHHHHHHHCCCCCCC | 27.76 | 22199227 | |
17 | Phosphorylation | SSMEKPPSLGDQETR HHCCCCCCCCCHHHH | 54.21 | 25159151 | |
23 | Phosphorylation | PSLGDQETRRKAREQ CCCCCHHHHHHHHHH | 30.09 | 27732954 | |
45 | Ubiquitination | QEQEKQQKVEFRKRM HHHHHHHHHHHHHHH | 41.04 | - | |
57 | Phosphorylation | KRMEKEVSDFIQDSG HHHHHHHHHHHHCCC | 28.09 | 20068231 | |
63 | Phosphorylation | VSDFIQDSGQIKKKF HHHHHHCCCHHHHHC | 19.07 | 20068231 | |
67 | Ubiquitination | IQDSGQIKKKFQPMN HHCCCHHHHHCCCCC | 41.86 | 21890473 | |
103 | Phosphorylation | GEDDDCRYVMIFKKE CCCCCCCEEEEEECC | 10.74 | 19413330 | |
109 | Ubiquitination | RYVMIFKKEFAPSDE CEEEEEECCCCCCHH | 47.52 | - | |
114 | Phosphorylation | FKKEFAPSDEELDSY EECCCCCCHHHHHHH | 54.98 | 30266825 | |
120 | Phosphorylation | PSDEELDSYRRGEEW CCHHHHHHHHCCCCC | 32.91 | 28152594 | |
121 | Phosphorylation | SDEELDSYRRGEEWD CHHHHHHHHCCCCCC | 12.19 | 28152594 | |
139 | Ubiquitination | AEEKRKLKELAQRQE HHHHHHHHHHHHHHH | 54.43 | - | |
158 | Phosphorylation | QQGPVVVSPASDYKD HHCCEEECCCHHCHH | 11.79 | 19664994 | |
161 | Phosphorylation | PVVVSPASDYKDKYS CEEECCCHHCHHHHH | 44.87 | 30266825 | |
163 | Phosphorylation | VVSPASDYKDKYSHL EECCCHHCHHHHHHH | 20.70 | 30266825 | |
164 | Acetylation | VSPASDYKDKYSHLI ECCCHHCHHHHHHHH | 53.38 | 26051181 | |
166 | Acetylation | PASDYKDKYSHLIGK CCHHCHHHHHHHHCC | 44.49 | 19608861 | |
166 | Ubiquitination | PASDYKDKYSHLIGK CCHHCHHHHHHHHCC | 44.49 | 19608861 | |
167 | Phosphorylation | ASDYKDKYSHLIGKG CHHCHHHHHHHHCCC | 16.08 | 23927012 | |
168 | Phosphorylation | SDYKDKYSHLIGKGA HHCHHHHHHHHCCCH | 19.98 | 23927012 | |
173 | Ubiquitination | KYSHLIGKGAAKDAA HHHHHHCCCHHHHHH | 38.08 | 21890473 | |
177 | Methylation | LIGKGAAKDAAHMLQ HHCCCHHHHHHHHHH | 47.57 | 115980669 | |
187 | Acetylation | AHMLQANKTYGCVPV HHHHHCCCCCCEEEC | 46.25 | 26051181 | |
188 | Phosphorylation | HMLQANKTYGCVPVA HHHHCCCCCCEEECC | 25.59 | 28152594 | |
189 | Phosphorylation | MLQANKTYGCVPVAN HHHCCCCCCEEECCC | 15.33 | 28152594 | |
197 | Ubiquitination | GCVPVANKRDTRSIE CEEECCCCCCCCCHH | 41.74 | - | |
197 | Acetylation | GCVPVANKRDTRSIE CEEECCCCCCCCCHH | 41.74 | 25953088 | |
200 | Phosphorylation | PVANKRDTRSIEEAM ECCCCCCCCCHHHHH | 30.28 | 28450419 | |
202 | Phosphorylation | ANKRDTRSIEEAMNE CCCCCCCCHHHHHHH | 36.12 | 23401153 | |
207 | Sulfoxidation | TRSIEEAMNEIRAKK CCCHHHHHHHHHHHH | 5.38 | 21406390 | |
219 | Phosphorylation | AKKRLRQSGEELPPT HHHHHHHCCCCCCCC | 41.56 | 23401153 | |
226 | Phosphorylation | SGEELPPTS------ CCCCCCCCC------ | 45.16 | 25159151 | |
227 | O-linked_Glycosylation | GEELPPTS------- CCCCCCCC------- | 43.95 | 23301498 | |
227 | Phosphorylation | GEELPPTS------- CCCCCCCC------- | 43.95 | 29396449 |
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 SPAG7_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPAG7_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 SPAG7_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of SPAG7_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 |
"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. | |
"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-166, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, 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-114 AND SER-158, ANDMASS SPECTROMETRY. | |
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction."; Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; Mol. Cell. Proteomics 6:1952-1967(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-121, AND MASSSPECTROMETRY. |