SRPK2
entrez
6733
canonical
uniprot
P78362
canonical
ensembl
ENSG00000135250
resolver
ensp
ENSP00000349863
resolver
ensp
ENSP00000377262
resolver
ensp
ENSP00000417357
resolver
ensp
ENSP00000419791
resolver
ensp
ENSP00000420208
resolver
ensp
ENSP00000516319
resolver
ensp
ENSP00000651249
resolver
ensp
ENSP00000678812
resolver
enst
ENST00000460391
resolver
enst
ENST00000482862
resolver
genesymbol
SRPK2
resolver
hgnc
HGNC:11306
resolver
uniprot
A0A994J591
resolver
uniprot
A8MVX2
resolver
uniprot
C9J2M4
resolver
uniprot
O75220
resolver
uniprot
O75221
resolver
uniprot
Q6NUL0
resolver
uniprot
Q6V1X2
resolver
uniprot
Q8IYQ3
resolver
uniprot_entry
A0A994J591_HUMAN
resolver
uniprot_entry
C9J2M4_HUMAN
resolver
uniprot_entry
SRPK2_HUMAN
resolver
uniprot_sec
A8MVX2
resolver
uniprot_sec
O75220
resolver
uniprot_sec
O75221
resolver
uniprot_sec
Q6NUL0
resolver
uniprot_sec
Q6V1X2
resolver
uniprot_sec
Q8IYQ3
resolver
activity_regulation
ACTIVITY REGULATION: Activated by phosphorylation on Ser-52 and Ser-588. {ECO:0000250|UniProtKB:Q96SB4}.
uniprot
proteins
amino_acid_sequence
MSVNSEKSSSSERPEPQQKAPLVPPPPPPPPPPPPPLPDPTPPEPEEEILGSDDEEQEDPADYCKGGYHPVKIGDLFNGRYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVKSAQHYTETALDEIKLLKCVRESDPSDPNKDMVVQLIDDFKISGMNGIHVCMVFEVLGHHLLKWIIKSNYQGLPVRCVKSIIRQVLQGLDYLHSKCKIIHTDIKPENILMCVDDAYVRRMAAEATEWQKAGAPPPSGSAVSTAPQQKPIGKISKNKKKKLKKKQKRQAELLEKRLQEIEELEREAERKIIEENITSAAPSNDQDGEYCPEVKLKTTGLEEAAEAETAKDNGEAEDQEEKEDAEKENIEKDEDDVDQELANIDPTWIESPKTNGHIENGPFSLEQQLDDEDDDEEDCPNPEEYNLDEPNAESDYTYSSSYEQFNGELPNGRHKIPESQFPEFSTSLFSGSLEPVACGSVLSEGSPLTEQEESSPSHDRSRTVSASSTGDLPKAKTRAADLLVNPLDPRNADKIRVKIADLGNACWVHKHFTEDIQTRQYRSIEVLIGAGYSTPADIWSTACMAFELATGDYLFEPHSGEDYSRDEDHIAHIIELLGSIPRHFALSGKYSREFFNRRGELRHITKLKPWSLFDVLVEKYGWPHEDAAQFTDFLIPMLEMVPEKRASAGECLRHPWLNS
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 (PubMed:18559500, PubMed:21056976, PubMed:9472028). Promotes neuronal apoptosis by up-regulating cyclin-D1 (CCND1) expression (PubMed:19592491). 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 (PubMed:21205200). Phosphorylates ACIN1, and redistributes it from the nuclear speckles to the nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-regulation (PubMed:18559500). Plays an essential role in spliceosomal B complex formation via the phosphorylation of DDX23/PRP28 (PubMed:18425142). Probably by phosphorylating DDX23, leads to the suppression of incorrect R-loops formed during transcription; R-loops are composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA (PubMed:28076779). Can mediate hepatitis B virus (HBV) core protein phosphorylation (PubMed:12134018). 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 (PubMed:16122776). Phosphorylates the N-terminus of ERC1 (By similarity). {ECO:0000250|UniProtKB:O54781, ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:16122776, ECO:0000269|PubMed:18425142, ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21056976, ECO:0000269|PubMed:21205200, ECO:0000269|PubMed:28076779, ECO:0000269|PubMed:9472028}.
uniprot
proteins
mass_dalton
77527
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-492 by PKB/AKT1 enhances its stimulatory activity in triggering cyclin-D1 (CCND1) expression and promoting apoptosis in neurons, which can be blocked by YWHAB. It also enhances its protein kinase activity toward ACIN1 and SRSF2, promotes its nuclear translocation and prevents its proteolytic cleavage. {ECO:0000269|PubMed:19592491}.; PTM: Proteolytically cleaved at Asp-139 and Asp-403 by caspase-3 during apoptotic cell death. Cleavage at Asp-139 which is the major site of cleavage, produces a small N-terminal fragment that translocates into nucleus and promotes VP16-induced apoptosis. {ECO:0000269|PubMed:21056976}.
uniprot
proteins
protein_family
CMGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
12134018
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16122776
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
18425142
uniprot
proteins
pubmed
18559500
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19592491
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21056976
uniprot
proteins
pubmed
21157427
uniprot
proteins
pubmed
21205200
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28076779
uniprot
proteins
pubmed
9472028
uniprot
proteins
sequence_length
688
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21056976, ECO:0000269|PubMed:21157427, ECO:0000269|PubMed:28076779, ECO:0000269|PubMed:9472028}. Nucleus, nucleoplasm {ECO:0000269|PubMed:21157427, ECO:0000269|PubMed:28076779, ECO:0000269|PubMed:9472028}. Nucleus speckle {ECO:0000269|PubMed:28076779, ECO:0000269|PubMed:9472028}. Chromosome {ECO:0000269|PubMed:28076779}. Note=Shuttles between the nucleus and the cytoplasm (PubMed:19592491, PubMed:21056976, PubMed:21157427). KAT5/TIP60 inhibits its nuclear translocation (PubMed:21157427). Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation (PubMed:19592491). Preferentially localizes across the entire gene coding region (PubMed:28076779). During transcription, accumulates at chromatin loci where unscheduled R-loops form and colocalizes with paused 'Ser-5'-phosphorylated POLR2A/RNA polymerase II and helicase DDX23 (PubMed:28076779). {ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21056976, ECO:0000269|PubMed:21157427, ECO:0000269|PubMed:28076779}.
uniprot
proteins