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P78362

- SRPK2_HUMAN

UniProt

P78362 - SRPK2_HUMAN

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Protein
SRSF protein kinase 2
Gene
SRPK2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.8 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.2 Publications

Cofactori

Magnesium.2 Publications

Enzyme regulationi

Activated by phosphorylation on Ser-52 and Ser-588 By similarity.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101ATP By similarityBy similarity
Sitei139 – 1402Cleavage; by caspase-3
Active sitei214 – 2141Proton acceptor By similarity
Sitei403 – 4042Cleavage; by caspase-3

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi87 – 959ATP By similarityBy similarity

GO - Molecular functioni

  1. 14-3-3 protein binding Source: BHF-UCL
  2. ATP binding Source: UniProtKB
  3. magnesium ion binding Source: UniProtKB
  4. poly(A) RNA binding Source: UniProtKB
  5. protein binding Source: IntAct
  6. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. RNA splicing Source: UniProtKB
  2. angiogenesis Source: BHF-UCL
  3. cell differentiation Source: UniProtKB-KW
  4. innate immune response Source: BHF-UCL
  5. intracellular signal transduction Source: UniProtKB
  6. negative regulation of viral genome replication Source: BHF-UCL
  7. nuclear speck organization Source: BHF-UCL
  8. positive regulation of cell cycle Source: BHF-UCL
  9. positive regulation of cell proliferation Source: BHF-UCL
  10. positive regulation of gene expression Source: BHF-UCL
  11. positive regulation of neuron apoptotic process Source: BHF-UCL
  12. positive regulation of viral genome replication Source: BHF-UCL
  13. protein phosphorylation Source: UniProtKB
  14. regulation of mRNA splicing, via spliceosome Source: UniProtKB
  15. spliceosomal complex assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Differentiation, mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiP78362.

Names & Taxonomyi

Protein namesi
Recommended name:
SRSF protein kinase 2 (EC:2.7.11.1)
Alternative name(s):
SFRS protein kinase 2
Serine/arginine-rich protein-specific kinase 2
Short name:
SR-protein-specific kinase 2
Cleaved into the following 2 chains:
Gene namesi
Name:SRPK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:11306. SRPK2.

Subcellular locationi

Cytoplasm. Nucleus
Note: Shuttles between the nucleus and the cytoplasm. KAT5/TIP60 inhibits its nuclear translocation. Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleolus Source: HPA
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36130.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 688688SRSF protein kinase 2
PRO_0000086677Add
BLAST
Chaini1 – 139139SRSF protein kinase 2 N-terminal
PRO_0000414751Add
BLAST
Chaini140 – 688549SRSF protein kinase 2 C-terminal
PRO_0000414752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521Phosphoserine; by CK2 By similarityBy similarity
Modified residuei380 – 3801Phosphoserine2 Publications
Modified residuei492 – 4921Phosphothreonine; by PKB/AKT11 Publication
Modified residuei494 – 4941Phosphoserine3 Publications
Modified residuei497 – 4971Phosphoserine4 Publications
Modified residuei588 – 5881Phosphoserine; by CK2 By similarityBy similarity

Post-translational modificationi

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.
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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP78362.
PaxDbiP78362.
PRIDEiP78362.

PTM databases

PhosphoSiteiP78362.

Expressioni

Tissue specificityi

Highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.1 Publication

Gene expression databases

ArrayExpressiP78362.
BgeeiP78362.
CleanExiHS_SRPK2.
GenevestigatoriP78362.

Organism-specific databases

HPAiHPA015522.
HPA020876.

Interactioni

Subunit structurei

Interacts with PKB/AKT1 in a phosphorylation-dependent manner. The phosphorylated form (by PKB/AKT1) interacts with YWHAB and YWHAE. Interaction with YWHAB suppresses its cleavage by caspases and inhibits the release of its N-terminal pro-apoptotic fragment. Interacts with SFN. Associates with U4/U6-U5 tri-small nuclear ribonucleoproteins (U4/U6-U5 tri-snRNPs).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARGLU1Q9NWB62EBI-593303,EBI-2808785
HNRNPCP079102EBI-593303,EBI-357966
LUC7LQ9NQ292EBI-593303,EBI-473747
LUC7L2Q9Y3832EBI-593303,EBI-352851
MMTAG2Q9BU762EBI-593303,EBI-742459
PRPF38AQ8NAV12EBI-593303,EBI-715374
RBM23Q86U062EBI-593303,EBI-780319
RBM39Q144984EBI-593303,EBI-395290
RBM8AQ9Y5S92EBI-593303,EBI-447231
SNRNP27Q8WVK22EBI-593303,EBI-2512550
SNRNP70P086213EBI-593303,EBI-1049228
SRSF7Q166292EBI-593303,EBI-398885
SRSF8Q9BRL62EBI-593303,EBI-6380719
U2AF1Q010814EBI-593303,EBI-632461
U2AF2P263684EBI-593303,EBI-742339
YTHDC1Q96MU73EBI-593303,EBI-2849854
YWHABP319462EBI-593303,EBI-359815

Protein-protein interaction databases

BioGridi112611. 214 interactions.
IntActiP78362. 223 interactions.
MINTiMINT-1468300.
STRINGi9606.ENSP00000377262.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni78 – 803
Beta strandi81 – 899
Beta strandi91 – 10010
Turni101 – 1044
Beta strandi105 – 1128
Helixi116 – 13419
Helixi140 – 1445
Beta strandi150 – 1567
Beta strandi159 – 1668
Helixi173 – 1797
Turni180 – 1823
Helixi187 – 20620
Helixi217 – 2193
Beta strandi220 – 2223
Helixi226 – 2338
Helixi518 – 5203
Turni521 – 5233
Beta strandi526 – 5283
Helixi531 – 5333
Helixi548 – 5503
Helixi553 – 5575
Helixi564 – 57916
Helixi594 – 60613
Helixi611 – 6144
Helixi620 – 6234
Beta strandi630 – 6323
Helixi641 – 6499
Helixi653 – 66614
Helixi671 – 6733
Helixi677 – 6815
Helixi684 – 6863

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X7GX-ray2.50A51-688[»]
ProteinModelPortaliP78362.
SMRiP78362. Positions 64-283, 508-688.

Miscellaneous databases

EvolutionaryTraceiP78362.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 684604Protein kinase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0515.
HOVERGENiHBG108512.
KOiK08831.
OMAiYCPEVKL.
OrthoDBiEOG70S74X.
PhylomeDBiP78362.
TreeFamiTF105334.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 2 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P78362-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSVNSEKSSS SERPEPQQKA PLVPPPPPPP PPPPPPLPDP TPPEPEEEIL    50
GSDDEEQEDP ADYCKGGYHP VKIGDLFNGR YHVIRKLGWG HFSTVWLCWD 100
MQGKRFVAMK VVKSAQHYTE TALDEIKLLK CVRESDPSDP NKDMVVQLID 150
DFKISGMNGI HVCMVFEVLG HHLLKWIIKS NYQGLPVRCV KSIIRQVLQG 200
LDYLHSKCKI IHTDIKPENI LMCVDDAYVR RMAAEATEWQ KAGAPPPSGS 250
AVSTAPQQKP IGKISKNKKK KLKKKQKRQA ELLEKRLQEI EELEREAERK 300
IIEENITSAA PSNDQDGEYC PEVKLKTTGL EEAAEAETAK DNGEAEDQEE 350
KEDAEKENIE KDEDDVDQEL ANIDPTWIES PKTNGHIENG PFSLEQQLDD 400
EDDDEEDCPN PEEYNLDEPN AESDYTYSSS YEQFNGELPN GRHKIPESQF 450
PEFSTSLFSG SLEPVACGSV LSEGSPLTEQ EESSPSHDRS RTVSASSTGD 500
LPKAKTRAAD LLVNPLDPRN ADKIRVKIAD LGNACWVHKH FTEDIQTRQY 550
RSIEVLIGAG YSTPADIWST ACMAFELATG DYLFEPHSGE DYSRDEDHIA 600
HIIELLGSIP RHFALSGKYS REFFNRRGEL RHITKLKPWS LFDVLVEKYG 650
WPHEDAAQFT DFLIPMLEMV PEKRASAGEC LRHPWLNS 688
Length:688
Mass (Da):77,527
Last modified:July 13, 2010 - v3
Checksum:iACCAF2A887444EC2
GO
Isoform 2 (identifier: P78362-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: MSVNSEKSSSSER → MSSRKVLAIQARKRRPKREKHPKK

Show »
Length:699
Mass (Da):79,029
Checksum:i70B084ABA32CC3DB
GO

Sequence cautioni

The sequence AAQ63886.1 differs from that shown. Reason: The cDNA appears to contain a duplicated region.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti43 – 431P → L.1 Publication
Corresponds to variant rs34699980 [ dbSNP | Ensembl ].
VAR_041114
Natural varianti243 – 2431G → D in a glioblastoma multiforme sample; somatic mutation. 1 Publication
VAR_041115
Natural varianti426 – 4261T → P.1 Publication
Corresponds to variant rs55743527 [ dbSNP | Ensembl ].
VAR_041116
Natural varianti486 – 4861S → F.1 Publication
Corresponds to variant rs56112661 [ dbSNP | Ensembl ].
VAR_041117
Natural varianti515 – 5151P → T.1 Publication
Corresponds to variant rs56017595 [ dbSNP | Ensembl ].
VAR_041118
Natural varianti608 – 6081S → N.
Corresponds to variant rs1050413 [ dbSNP | Ensembl ].
VAR_060390
Natural varianti615 – 6151L → I.
Corresponds to variant rs1050418 [ dbSNP | Ensembl ].
VAR_057111

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1313MSVNS…SSSER → MSSRKVLAIQARKRRPKREK HPKK in isoform 2.
VSP_039386Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371P → R in AAH68547. 1 Publication
Sequence conflicti236 – 2372AT → P in AAC05299. 1 Publication
Sequence conflicti521 – 5211A → R in AAC05299. 1 Publication
Sequence conflicti601 – 6011H → L in AAC29141. 1 Publication
Sequence conflicti608 – 6092SI → KV in AAC29141. 1 Publication
Sequence conflicti612 – 6165HFALS → KYAML in AAC29141. 1 Publication
Sequence conflicti621 – 6211R → K in AAC29141. 1 Publication
Sequence conflicti625 – 6273NRR → TRK in AAC29141. 1 Publication
Sequence conflicti640 – 6401S → G in AAH68547. 1 Publication
Sequence conflicti681 – 6811Missing in AAC05299. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U88666 mRNA. Translation: AAC05299.1.
AC005070 Genomic DNA. Translation: AAC29140.1.
AC005070 Genomic DNA. Translation: AAC29141.1.
AC004884 Genomic DNA. No translation available.
AC073138 Genomic DNA. No translation available.
CH471070 Genomic DNA. Translation: EAW83359.1.
BC035214 mRNA. Translation: AAH35214.1.
BC068547 mRNA. Translation: AAH68547.1.
BE781215 mRNA. No translation available.
AY354201 mRNA. Translation: AAQ63886.1. Sequence problems.
CCDSiCCDS34724.1. [P78362-2]
CCDS5735.1. [P78362-1]
RefSeqiNP_001265202.1. NM_001278273.1. [P78362-1]
NP_872633.1. NM_182691.2. [P78362-1]
NP_872634.1. NM_182692.2. [P78362-2]
UniGeneiHs.285197.

Genome annotation databases

EnsembliENST00000357311; ENSP00000349863; ENSG00000135250. [P78362-1]
ENST00000393651; ENSP00000377262; ENSG00000135250. [P78362-2]
ENST00000489828; ENSP00000419791; ENSG00000135250. [P78362-1]
GeneIDi6733.
KEGGihsa:6733.
UCSCiuc003vct.4. human. [P78362-1]
uc003vcv.4. human. [P78362-2]

Polymorphism databases

DMDMi300669676.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U88666 mRNA. Translation: AAC05299.1 .
AC005070 Genomic DNA. Translation: AAC29140.1 .
AC005070 Genomic DNA. Translation: AAC29141.1 .
AC004884 Genomic DNA. No translation available.
AC073138 Genomic DNA. No translation available.
CH471070 Genomic DNA. Translation: EAW83359.1 .
BC035214 mRNA. Translation: AAH35214.1 .
BC068547 mRNA. Translation: AAH68547.1 .
BE781215 mRNA. No translation available.
AY354201 mRNA. Translation: AAQ63886.1 . Sequence problems.
CCDSi CCDS34724.1. [P78362-2 ]
CCDS5735.1. [P78362-1 ]
RefSeqi NP_001265202.1. NM_001278273.1. [P78362-1 ]
NP_872633.1. NM_182691.2. [P78362-1 ]
NP_872634.1. NM_182692.2. [P78362-2 ]
UniGenei Hs.285197.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2X7G X-ray 2.50 A 51-688 [» ]
ProteinModelPortali P78362.
SMRi P78362. Positions 64-283, 508-688.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112611. 214 interactions.
IntActi P78362. 223 interactions.
MINTi MINT-1468300.
STRINGi 9606.ENSP00000377262.

Chemistry

BindingDBi P78362.
ChEMBLi CHEMBL5668.
GuidetoPHARMACOLOGYi 2209.

PTM databases

PhosphoSitei P78362.

Polymorphism databases

DMDMi 300669676.

Proteomic databases

MaxQBi P78362.
PaxDbi P78362.
PRIDEi P78362.

Protocols and materials databases

DNASUi 6733.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357311 ; ENSP00000349863 ; ENSG00000135250 . [P78362-1 ]
ENST00000393651 ; ENSP00000377262 ; ENSG00000135250 . [P78362-2 ]
ENST00000489828 ; ENSP00000419791 ; ENSG00000135250 . [P78362-1 ]
GeneIDi 6733.
KEGGi hsa:6733.
UCSCi uc003vct.4. human. [P78362-1 ]
uc003vcv.4. human. [P78362-2 ]

Organism-specific databases

CTDi 6733.
GeneCardsi GC07M104751.
H-InvDB HIX0006976.
HGNCi HGNC:11306. SRPK2.
HPAi HPA015522.
HPA020876.
MIMi 602980. gene.
neXtProti NX_P78362.
PharmGKBi PA36130.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOVERGENi HBG108512.
KOi K08831.
OMAi YCPEVKL.
OrthoDBi EOG70S74X.
PhylomeDBi P78362.
TreeFami TF105334.

Enzyme and pathway databases

SignaLinki P78362.

Miscellaneous databases

ChiTaRSi SRPK2. human.
EvolutionaryTracei P78362.
GeneWikii SRPK2.
GenomeRNAii 6733.
NextBioi 26266.
PROi P78362.
SOURCEi Search...

Gene expression databases

ArrayExpressi P78362.
Bgeei P78362.
CleanExi HS_SRPK2.
Genevestigatori P78362.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 2 hits.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 2 hits.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "SRPK2: a differentially expressed SR protein-specific kinase involved in mediating the interaction and localization of pre-mRNA splicing factors in mammalian cells."
    Wang H.-Y., Lin W., Dyck J.A., Yeakley J.M., Songyang Z., Cantley L.C., Fu X.-D.
    J. Cell Biol. 140:737-750(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Fetal brain.
  2. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-99 (ISOFORM 2).
    Tissue: Retinoblastoma, Skin and Testis.
  5. Sha J.H., Zhou Z.M., Li J.M.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-537 (ISOFORM 1).
    Tissue: Testis.
  6. "Identification of SRPK1 and SRPK2 as the major cellular protein kinases phosphorylating hepatitis B virus core protein."
    Daub H., Blencke S., Habenberger P., Kurtenbach A., Dennenmoser J., Wissing J., Ullrich A., Cotten M.
    J. Virol. 76:8124-8137(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF HEPATITIS B VIRUS CORE PROTEIN.
  7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
    Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
    Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Suppression of hepatitis B virus replication by SRPK1 and SRPK2 via a pathway independent of the phosphorylation of the viral core protein."
    Zheng Y., Fu X.D., Ou J.H.
    Virology 342:150-158(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEGATIVE REGULATION OF HEPATITIS B VIRUS (HBV) REPLICATION.
  9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Serine/arginine protein-specific kinase 2 promotes leukemia cell proliferation by phosphorylating acinus and regulating cyclin A1."
    Jang S.W., Yang S.J., Ehlen A., Dong S., Khoury H., Chen J., Persson J.L., Ye K.
    Cancer Res. 68:4559-4570(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ACIN1, INTERACTION WITH ACIN1.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Phosphorylation of human PRP28 by SRPK2 is required for integration of the U4/U6-U5 tri-snRNP into the spliceosome."
    Mathew R., Hartmuth K., Moehlmann S., Urlaub H., Ficner R., Luehrmann R.
    Nat. Struct. Mol. Biol. 15:435-443(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DDX23/PRP28, ASSOCIATION WITH U4/U6-U5 TRI-SNRNPS.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT THR-492 BY PKB/AKT1, INTERACTION WITH PKB/AKT1; YWHAB; YWHAE AND SFN.
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-494 AND SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Acetylation and phosphorylation of SRSF2 control cell fate decision in response to cisplatin."
    Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C., Brambilla E., Gazzeri S., Eymin B.
    EMBO J. 30:510-523(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SRSF2, SUBCELLULAR LOCATION.
  20. "Serine-arginine protein kinases: a small protein kinase family with a large cellular presence."
    Giannakouros T., Nikolakaki E., Mylonis I., Georgatsou E.
    FEBS J. 278:570-586(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  21. "The N-terminal fragment from caspase-cleaved serine/arginine protein-specific kinase2 (SRPK2) translocates into the nucleus and promotes apoptosis."
    Hong Y., Jang S.W., Ye K.
    J. Biol. Chem. 286:777-786(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CASPASE-3 CLEAVAGE AT ASP-139 AND ASP-403, SUBCELLULAR LOCATION.
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-497, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-43; ASP-243; PRO-426; PHE-486 AND THR-515.

Entry informationi

Entry nameiSRPK2_HUMAN
AccessioniPrimary (citable) accession number: P78362
Secondary accession number(s): A8MVX2
, O75220, O75221, Q6NUL0, Q6V1X2, Q8IYQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: July 13, 2010
Last modified: July 9, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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