UniProt ID | SRPK2_HUMAN | |
---|---|---|
UniProt AC | P78362 | |
Protein Name | SRSF protein kinase 2 | |
Gene Name | SRPK2 {ECO:0000312|EMBL:AAH68547.1} | |
Organism | Homo sapiens (Human). | |
Sequence Length | 688 | |
Subcellular Localization | Cytoplasm. Nucleus. Shuttles between the nucleus and the cytoplasm. KAT5/TIP60 inhibits its nuclear translocation. Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation. | |
Protein Description | Serine/arginine-rich protein-specific kinase which specifically phosphorylates its substrates at serine residues located in regions rich in arginine/serine dipeptides, known as RS domains and is involved in the phosphorylation of SR splicing factors and the regulation of splicing. Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is done by the phosphorylation of SRSF2, leading to the suppression of p53/TP53 phosphorylation thereby relieving the repressive effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation. Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28. Can mediate hepatitis B virus (HBV) core protein phosphorylation. Plays a negative role in the regulation of HBV replication through a mechanism not involving the phosphorylation of the core protein but by reducing the packaging efficiency of the pregenomic RNA (pgRNA) without affecting the formation of the viral core particles.. | |
Protein Sequence | MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPPPLPDPTPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKIIEENITSAAPSNDQDGEYCPEVKLKTTGLEEAAEAETAKDNGEAEDQEEKEDAEKENIEKDEDDVDQELANIDPTWIESPKTNGHIENGPFSLEQQLDDEDDDEEDCPNPEEYNLDEPNAESDYTYSSSYEQFNGELPNGRHKIPESQFPEFSTSLFSGSLEPVACGSVLSEGSPLTEQEESSPSHDRSRTVSASSTGDLPKAKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSVNSEKSS ------CCCCCCCCC | 29.97 | 23663014 | |
5 | Phosphorylation | ---MSVNSEKSSSSE ---CCCCCCCCCCCC | 44.22 | 23663014 | |
8 | Phosphorylation | MSVNSEKSSSSERPE CCCCCCCCCCCCCCC | 31.25 | 23663014 | |
9 | Phosphorylation | SVNSEKSSSSERPEP CCCCCCCCCCCCCCC | 49.29 | 23663014 | |
10 | Phosphorylation | VNSEKSSSSERPEPQ CCCCCCCCCCCCCCC | 43.22 | 23401153 | |
11 | Phosphorylation | NSEKSSSSERPEPQQ CCCCCCCCCCCCCCC | 39.30 | 23663014 | |
41 | Phosphorylation | PPPLPDPTPPEPEEE CCCCCCCCCCCCHHH | 59.88 | 28464451 | |
52 | Phosphorylation | PEEEILGSDDEEQED CHHHCCCCCCCCCCC | 38.14 | 20363803 | |
63 | Phosphorylation | EQEDPADYCKGGYHP CCCCHHHHCCCCCCC | 9.73 | 20873877 | |
110 | Acetylation | GKRFVAMKVVKSAQH CCEEEEEEHHHHCHH | 33.85 | 25953088 | |
110 | Ubiquitination | GKRFVAMKVVKSAQH CCEEEEEEHHHHCHH | 33.85 | - | |
127 | Acetylation | ETALDEIKLLKCVRE HHHHHHHHHHHHHHC | 45.80 | 26051181 | |
127 | Ubiquitination | ETALDEIKLLKCVRE HHHHHHHHHHHHHHC | 45.80 | - | |
129 | Phosphorylation | ALDEIKLLKCVRESD HHHHHHHHHHHHCCC | 3.25 | 27642862 | |
130 | Ubiquitination | LDEIKLLKCVRESDP HHHHHHHHHHHCCCC | 40.91 | - | |
179 | Ubiquitination | HLLKWIIKSNYQGLP HHHHHHHHCCCCCCC | 24.42 | 21890473 | |
180 | Phosphorylation | LLKWIIKSNYQGLPV HHHHHHHCCCCCCCH | 30.29 | 28796482 | |
182 | Phosphorylation | KWIIKSNYQGLPVRC HHHHHCCCCCCCHHH | 15.85 | 28796482 | |
190 | Ubiquitination | QGLPVRCVKSIIRQV CCCCHHHHHHHHHHH | 3.69 | 21890473 | |
203 | Phosphorylation | QVLQGLDYLHSKCKI HHHHHHHHHHHCCEE | 16.03 | 26074081 | |
206 | Phosphorylation | QGLDYLHSKCKIIHT HHHHHHHHCCEEEEC | 36.83 | 26074081 | |
209 | Ubiquitination | DYLHSKCKIIHTDIK HHHHHCCEEEECCCC | 48.72 | - | |
213 | Phosphorylation | SKCKIIHTDIKPENI HCCEEEECCCCHHHE | 29.07 | 26074081 | |
216 | Ubiquitination | KIIHTDIKPENILMC EEEECCCCHHHEEEE | 49.44 | - | |
228 | Phosphorylation | LMCVDDAYVRRMAAE EEEECHHHHHHHHHH | 11.07 | 26074081 | |
237 | Phosphorylation | RRMAAEATEWQKAGA HHHHHHHHHHHHCCC | 29.30 | 22210691 | |
241 | Ubiquitination | AEATEWQKAGAPPPS HHHHHHHHCCCCCCC | 50.27 | - | |
248 | Phosphorylation | KAGAPPPSGSAVSTA HCCCCCCCCCCCCCC | 51.67 | 25159151 | |
250 | Phosphorylation | GAPPPSGSAVSTAPQ CCCCCCCCCCCCCCC | 29.81 | 25159151 | |
253 | Phosphorylation | PPSGSAVSTAPQQKP CCCCCCCCCCCCCCC | 20.68 | 28555341 | |
254 | Phosphorylation | PSGSAVSTAPQQKPI CCCCCCCCCCCCCCC | 35.44 | 28555341 | |
259 | Phosphorylation | VSTAPQQKPIGKISK CCCCCCCCCCCCCCH | 33.10 | 27251275 | |
285 | Ubiquitination | RQAELLEKRLQEIEE HHHHHHHHHHHHHHH | 59.38 | - | |
300 | Ubiquitination | LEREAERKIIEENIT HHHHHHHHHHHHHCC | 39.27 | - | |
307 | Phosphorylation | KIIEENITSAAPSND HHHHHHCCCCCCCCC | 24.72 | 29978859 | |
308 | Phosphorylation | IIEENITSAAPSNDQ HHHHHCCCCCCCCCC | 20.73 | 29978859 | |
312 | Phosphorylation | NITSAAPSNDQDGEY HCCCCCCCCCCCCCC | 48.59 | 29978859 | |
319 | Phosphorylation | SNDQDGEYCPEVKLK CCCCCCCCCCCCEEE | 20.87 | 28796482 | |
324 | Acetylation | GEYCPEVKLKTTGLE CCCCCCCEEEECCHH | 42.47 | 26051181 | |
326 | Ubiquitination | YCPEVKLKTTGLEEA CCCCCEEEECCHHHH | 38.02 | - | |
327 | Phosphorylation | CPEVKLKTTGLEEAA CCCCEEEECCHHHHH | 36.21 | 28555341 | |
328 | Phosphorylation | PEVKLKTTGLEEAAE CCCEEEECCHHHHHH | 37.88 | 21815630 | |
330 | Phosphorylation | VKLKTTGLEEAAEAE CEEEECCHHHHHHHH | 5.16 | 27642862 | |
376 | Phosphorylation | ELANIDPTWIESPKT HHHCCCCCEECCCCC | 35.01 | 22496350 | |
380 | Phosphorylation | IDPTWIESPKTNGHI CCCCEECCCCCCCCC | 23.67 | 25159151 | |
383 | Phosphorylation | TWIESPKTNGHIENG CEECCCCCCCCCCCC | 50.22 | 26074081 | |
391 | Phosphorylation | NGHIENGPFSLEQQL CCCCCCCCCCHHHCC | 27.51 | 27251275 | |
393 | Phosphorylation | HIENGPFSLEQQLDD CCCCCCCCHHHCCCC | 33.84 | 26074081 | |
423 | Phosphorylation | LDEPNAESDYTYSSS CCCCCCCCCCCCCCC | 33.24 | - | |
427 | Phosphorylation | NAESDYTYSSSYEQF CCCCCCCCCCCHHHH | 10.59 | - | |
448 | Phosphorylation | GRHKIPESQFPEFST CCCCCCHHHCCCCCC | 31.59 | 28985074 | |
469 | Phosphorylation | LEPVACGSVLSEGSP CCCEECCCCCCCCCC | 21.55 | 28348404 | |
472 | Phosphorylation | VACGSVLSEGSPLTE EECCCCCCCCCCCCC | 37.44 | 25921289 | |
475 | Phosphorylation | GSVLSEGSPLTEQEE CCCCCCCCCCCCCCC | 16.82 | 25921289 | |
478 | Phosphorylation | LSEGSPLTEQEESSP CCCCCCCCCCCCCCC | 38.72 | 25921289 | |
483 | Phosphorylation | PLTEQEESSPSHDRS CCCCCCCCCCCCCCC | 46.96 | 26657352 | |
484 | Phosphorylation | LTEQEESSPSHDRSR CCCCCCCCCCCCCCC | 33.43 | 28464451 | |
486 | Phosphorylation | EQEESSPSHDRSRTV CCCCCCCCCCCCCCC | 39.71 | 22210691 | |
490 | Phosphorylation | SSPSHDRSRTVSASS CCCCCCCCCCCCHHH | 38.06 | 23663014 | |
492 | Phosphorylation | PSHDRSRTVSASSTG CCCCCCCCCCHHHCC | 21.76 | 25463755 | |
494 | Phosphorylation | HDRSRTVSASSTGDL CCCCCCCCHHHCCCC | 23.09 | 29255136 | |
495 | Phosphorylation | DRSRTVSASSTGDLP CCCCCCCHHHCCCCC | 11.81 | 27251275 | |
496 | Phosphorylation | RSRTVSASSTGDLPK CCCCCCHHHCCCCCH | 22.41 | 29255136 | |
497 | Phosphorylation | SRTVSASSTGDLPKA CCCCCHHHCCCCCHH | 35.81 | 29255136 | |
498 | Phosphorylation | RTVSASSTGDLPKAK CCCCHHHCCCCCHHH | 32.02 | 29255136 | |
503 | Ubiquitination | SSTGDLPKAKTRAAD HHCCCCCHHHHHHHH | 70.57 | - | |
505 | Phosphorylation | TGDLPKAKTRAADLL CCCCCHHHHHHHHHC | 44.67 | 27251275 | |
508 | Phosphorylation | LPKAKTRAADLLVNP CCHHHHHHHHHCCCC | 15.57 | 27251275 | |
509 | Phosphorylation | PKAKTRAADLLVNPL CHHHHHHHHHCCCCC | 12.51 | 27251275 | |
527 | Ubiquitination | NADKIRVKIADLGNA CCCCEEEEEHHHCCC | 23.48 | - | |
539 | Acetylation | GNACWVHKHFTEDIQ CCCEEEEHHHCCCHH | 30.69 | 25825284 | |
539 | Ubiquitination | GNACWVHKHFTEDIQ CCCEEEEHHHCCCHH | 30.69 | - | |
542 | Phosphorylation | CWVHKHFTEDIQTRQ EEEEHHHCCCHHHCC | 32.25 | 23403867 | |
547 | Phosphorylation | HFTEDIQTRQYRSIE HHCCCHHHCCCEEEE | 21.77 | 29255136 | |
548 | Methylation | FTEDIQTRQYRSIEV HCCCHHHCCCEEEEE | 18.37 | - | |
588 | Phosphorylation | DYLFEPHSGEDYSRD CCCCCCCCCCCCCCC | 55.37 | - | |
608 | Phosphorylation | HIIELLGSIPRHFAL HHHHHHCCCCHHHHH | 29.41 | 25849741 | |
616 | Phosphorylation | IPRHFALSGKYSREF CCHHHHHCCCHHHHH | 29.79 | 21712546 | |
618 | Acetylation | RHFALSGKYSREFFN HHHHHCCCHHHHHHH | 36.36 | 26051181 | |
618 | Ubiquitination | RHFALSGKYSREFFN HHHHHCCCHHHHHHH | 36.36 | - | |
637 | Ubiquitination | LRHITKLKPWSLFDV HHHCCCCCCCHHHHH | 46.10 | - | |
640 | O-linked_Glycosylation | ITKLKPWSLFDVLVE CCCCCCCHHHHHHHH | 27.90 | 30059200 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
492 | T | Phosphorylation | Kinase | AKT1 | P31749 | Uniprot |
494 | S | Phosphorylation | Kinase | P70S6K | P23443 | PSP |
494 | S | Phosphorylation | Kinase | SRPK2 | P78362 | PSP |
497 | S | Phosphorylation | Kinase | CK1A | P48729 | PSP |
588 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
492 | T | Phosphorylation |
| 19592491 |
* 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 SRPK2_HUMAN !! |
Kegg Disease | |
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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 | |
DB00173 | Adenine |
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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-494, AND MASSSPECTROMETRY. | |
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-497 ANDTHR-498, AND MASS SPECTROMETRY. | |
"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-494 AND SER-497, ANDMASS SPECTROMETRY. | |
"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-380; SER-494; SER-497AND THR-547, AND MASS SPECTROMETRY. | |
"Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cellcycle and cell death in neurons."; Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.; J. Biol. Chem. 284:24512-24525(2009). Cited for: FUNCTION, PHOSPHORYLATION AT THR-492 BY PKB/AKT1, AND INTERACTION WITHPKB/AKT1; YWHAB; YWHAE AND SFN. | |
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-319, AND MASSSPECTROMETRY. |