SRPK1
entrez
6732
canonical
uniprot
Q96SB4
canonical
ensembl
ENSG00000096063
resolver
ensp
ENSP00000362931
resolver
genesymbol
SRPK1
resolver
hgnc
HGNC:11305
resolver
uniprot
B4DS61
resolver
uniprot
Q12890
resolver
uniprot
Q5R364
resolver
uniprot
Q5R365
resolver
uniprot
Q8IY12
resolver
uniprot_entry
SRPK1_HUMAN
resolver
uniprot_sec
B4DS61
resolver
uniprot_sec
Q12890
resolver
uniprot_sec
Q5R364
resolver
uniprot_sec
Q5R365
resolver
uniprot_sec
Q8IY12
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phosphorylation on Ser-51 and Ser-555. {ECO:0000269|PubMed:12565829}.
uniprot
proteins
amino_acid_sequence
MERKVLALQARKKRTKAKKDKAQRKSETQHRGSAPHSESDLPEQEEEILGSDDDEQEDPNDYCKGGYHLVKIGDLFNGRYHVIRKLGWGHFSTVWLSWDIQGKKFVAMKVVKSAEHYTETALDEIRLLKSVRNSDPNDPNREMVVQLLDDFKISGVNGTHICMVFEVLGHHLLKWIIKSNYQGLPLPCVKKIIQQVLQGLDYLHTKCRIIHTDIKPENILLSVNEQYIRRLAAEATEWQRSGAPPPSGSAVSTAPQPKPADKMSKNKKKKLKKKQKRQAELLEKRMQEIEEMEKESGPGQKRPNKQEESESPVERPLKENPPNKMTQEKLEESSTIGQDQTLMERDTEGGAAEINCNGVIEVINYTQNSNNETLRHKEDLHNANDCDVQNLNQESSFLSSQNGDSSTSQETDSCTPITSEVSDTMVCQSSSTVGQSFSEQHISQLQESIRAEIPCEDEQEQEHNGPLDNKGKSTAGNFLVNPLEPKNAEKLKVKIADLGNACWVHKHFTEDIQTRQYRSLEVLIGSGYNTPADIWSTACMAFELATGDYLFEPHSGEEYTRDEDHIALIIELLGKVPRKLIVAGKYSKEFFTKKGDLKHITKLKPWGLFEVLVEKYEWSQEEAAGFTDFLLPMLELIPEKRATAAECLRHPWLNS
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: 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. Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Can influence additional steps of mRNA maturation, as well as other cellular activities, such as chromatin reorganization in somatic and sperm cells and cell cycle progression. Isoform 2 phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a directional (C-terminal to N-terminal) and a dual-track mechanism incorporating both processive phosphorylation (in which the kinase stays attached to the substrate after each round of phosphorylation) and distributive phosphorylation steps (in which the kinase and substrate dissociate after each phosphorylation event). The RS domain of SRSF1 binds first to a docking groove in the large lobe of the kinase domain of SRPK1. This induces certain structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and initiate phosphorylation. The cycles continue for several phosphorylation steps in a processive manner (steps 1-8) until the last few phosphorylation steps (approximately steps 9-12). During that time, a mechanical stress induces the unfolding of the beta-4 motif in RRM2, which then docks at the docking groove of SRPK1. This also signals RRM2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed. Isoform 2 can mediate hepatitis B virus (HBV) core protein phosphorylation. It 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. Isoform 1 and isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform 2 plays a decisive role in determining cell fate in K-562 leukemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation. Phosphorylates the N-terminus of ERC1 (PubMed:30745339). {ECO:0000269|PubMed:10049757, ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:11509566, ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:14555757, ECO:0000269|PubMed:15034300, ECO:0000269|PubMed:16122776, ECO:0000269|PubMed:16209947, ECO:0000269|PubMed:18155240, ECO:0000269|PubMed:18687337, ECO:0000269|PubMed:19240134, ECO:0000269|PubMed:19477182, ECO:0000269|PubMed:19886675, ECO:0000269|PubMed:20708644, ECO:0000269|PubMed:30745339, ECO:0000269|PubMed:8208298, ECO:0000269|PubMed:9237760}.
uniprot
proteins
mass_dalton
74325
uniprot
proteins
mutagenesis
MUTAGEN 37; /note="S->A: No effect on protein phosphorylation."; /evidence="ECO:0000269|PubMed:12565829"; MUTAGEN 51; /note="S->A: Protein phosphorylation impaired at this position."; /evidence="ECO:0000269|PubMed:12565829"; MUTAGEN 222; /note="S->A: No effect on protein phosphorylation."; /evidence="ECO:0000269|PubMed:12565829"; MUTAGEN 311; /note="S->G: No effect on protein phosphorylation."; /evidence="ECO:0000269|PubMed:12565829"; MUTAGEN 436; /note="S->G: No effect on protein phosphorylation."; /evidence="ECO:0000269|PubMed:12565829"; MUTAGEN 555; /note="S->A: Protein phosphorylation impaired at this position."; /evidence="ECO:0000269|PubMed:12565829"; MUTAGEN 619; /note="S->A: No effect on protein phosphorylation."; /evidence="ECO:0000269|PubMed:12565829
uniprot
proteins
protein_family
CMGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10049757
uniprot
proteins
pubmed
10390541
uniprot
proteins
pubmed
11509566
uniprot
proteins
pubmed
12134018
uniprot
proteins
pubmed
12565829
uniprot
proteins
pubmed
14555757
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15034300
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16122776
uniprot
proteins
pubmed
16209947
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17223538
uniprot
proteins
pubmed
18155240
uniprot
proteins
pubmed
18342604
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18687337
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19240134
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19477182
uniprot
proteins
pubmed
19553338
uniprot
proteins
pubmed
19674106
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19886675
uniprot
proteins
pubmed
20708644
uniprot
proteins
pubmed
21157427
uniprot
proteins
pubmed
21205200
uniprot
proteins
pubmed
21205204
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28076779
uniprot
proteins
pubmed
30745339
uniprot
proteins
pubmed
8208298
uniprot
proteins
pubmed
9237760
uniprot
proteins
sequence_length
655
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus. Nucleus matrix. Microsome. Note=Shuttles between the nucleus and the cytoplasm. Inhibition of the Hsp90 ATPase activity, osmotic stress and interaction with HHV-1 ICP27 protein can induce its translocation to the nucleus. KAT5/TIP60 inhibits its nuclear translocation.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus matrix. Microsome. Note=Mainly localized in the microsomal fraction and the cytoplasm, and to a lesser extent in the nuclear matrix.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28076779}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28076779}. Nucleus speckle {ECO:0000269|PubMed:28076779}. Chromosome {ECO:0000269|PubMed:28076779}. Note=Preferentially localizes to the promoter of gene coding regions. {ECO:0000269|PubMed:28076779}.
uniprot
proteins