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Q96SB4

- SRPK1_HUMAN

UniProt

Q96SB4 - SRPK1_HUMAN

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Protein

SRSF protein kinase 1

Gene

SRPK1

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. 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 leukaemic cell line: isoform 2 favors proliferation where as isoform 1 favors differentiation.16 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.6 Publications

Cofactori

Magnesium.6 Publications

Enzyme regulationi

Activated by phosphorylation on Ser-51 and Ser-555.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091ATP1 PublicationPROSITE-ProRule annotation
Active sitei213 – 2131Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi86 – 949ATP1 PublicationPROSITE-ProRule annotation
Nucleotide bindingi166 – 1683ATP1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. protein kinase activity Source: ProtInc
  5. protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  1. chromosome segregation Source: UniProtKB
  2. innate immune response Source: BHF-UCL
  3. intracellular signal transduction Source: UniProtKB
  4. mRNA processing Source: UniProtKB-KW
  5. negative regulation of viral genome replication Source: BHF-UCL
  6. positive regulation of viral genome replication Source: BHF-UCL
  7. protein phosphorylation Source: UniProtKB
  8. regulation of mRNA processing Source: UniProtKB
  9. regulation of mRNA splicing, via spliceosome Source: UniProtKB
  10. RNA splicing Source: ProtInc
  11. sperm chromatin condensation Source: UniProtKB
  12. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Chromosome partition, Differentiation, Host-virus interaction, mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ96SB4.

Names & Taxonomyi

Protein namesi
Recommended name:
SRSF protein kinase 1 (EC:2.7.11.1)
Alternative name(s):
SFRS protein kinase 1
Serine/arginine-rich protein-specific kinase 1
Short name:
SR-protein-specific kinase 1
Gene namesi
Name:SRPK1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:11305. SRPK1.

Subcellular locationi

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.
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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB-KW
  3. nucleus Source: UniProtKB
  4. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Microsome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi37 – 371S → A: No effect on protein phosphorylation. 1 Publication
Mutagenesisi51 – 511S → A: Protein phosphorylation impaired at this position. 1 Publication
Mutagenesisi222 – 2221S → A: No effect on protein phosphorylation. 1 Publication
Mutagenesisi311 – 3111S → G: No effect on protein phosphorylation. 1 Publication
Mutagenesisi436 – 4361S → G: No effect on protein phosphorylation. 1 Publication
Mutagenesisi555 – 5551S → A: Protein phosphorylation impaired at this position. 1 Publication
Mutagenesisi619 – 6191S → A: No effect on protein phosphorylation. 1 Publication

Organism-specific databases

PharmGKBiPA36129.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 655655SRSF protein kinase 1PRO_0000086674Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511Phosphoserine; by CK25 Publications
Modified residuei309 – 3091PhosphoserineBy similarity
Modified residuei311 – 3111Phosphoserine1 Publication
Modified residuei555 – 5551Phosphoserine; by CK21 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ96SB4.
PaxDbiQ96SB4.
PRIDEiQ96SB4.

PTM databases

PhosphoSiteiQ96SB4.

Expressioni

Tissue specificityi

Isoform 2 is predominantly expressed in the testis but is also present at lower levels in heart, ovary, small intestine, liver, kidney, pancreas and skeletal muscle. Isoform 1 is only seen in the testis, at lower levels than isoform 2. Highly expressed in different erythroid and lymphoid cell lines, with isoform 2 being far more abundant than isoform 1.3 Publications

Gene expression databases

BgeeiQ96SB4.
CleanExiHS_SRPK1.
ExpressionAtlasiQ96SB4. baseline and differential.
GenevestigatoriQ96SB4.

Organism-specific databases

HPAiHPA016431.
HPA056486.

Interactioni

Subunit structurei

Monomer. Isoform 2 is found in a multisubunit complex containing seven proteins, named toposome, which separates entangled circular chromatin DNA during chromosome segregation. Isoform 2 interacts with HHV-1 ICP27 protein. Isoform 2 interacts with DNAJB1/HSP40 and AHSA1/AHA1 and this mediates formation of a complex with the Hsp70 /Hsp90 machinery. Isoform 1 is found in a complex with: DHX9, MOV10, MATR3, HNRNPU, NCL, DDX21, HSD17B4, PABPC1, HNRNPM, IGF2BP1, SYNCRIP, RPL3, VIM, YBX1, NPM1, HNRNPA2B1, HNRNPC, RPLP0, RPL7A and RALY. Isoform 2 binds to IGF2BP1, SYNCRIP, HNRNPA2B1 and HNRNPC. Isoform 1 and isoform 2 interact with SAFB which inhibits its activity. Isoform 2 interacts with SAFB2 which inhibits its activity.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A7Y3Z34EBI-539478,EBI-7321730From a different organism.
DGCR8Q8WYQ53EBI-539478,EBI-528411
LUC7LQ9NQ292EBI-539478,EBI-473747
LUC7L2Q9Y3832EBI-539478,EBI-352851
PRPF38AQ8NAV12EBI-539478,EBI-715374
RBM39Q144982EBI-539478,EBI-395290
RBM8AQ9Y5S92EBI-539478,EBI-447231
RNPS1Q152872EBI-539478,EBI-395959
SAFBQ154242EBI-5773439,EBI-348298
SafbO884532EBI-539478,EBI-539530From a different organism.
SRPK3Q9UPE12EBI-539478,EBI-6381269
SRSF1Q079553EBI-539478,EBI-398920
SRSF7Q166292EBI-539478,EBI-398885
SRSF8Q9BRL62EBI-539478,EBI-6380719
TP53P046373EBI-539478,EBI-366083
YTHDC1Q96MU73EBI-539478,EBI-2849854

Protein-protein interaction databases

BioGridi112610. 207 interactions.
DIPiDIP-33888N.
IntActiQ96SB4. 218 interactions.
MINTiMINT-262701.
STRINGi9606.ENSP00000391069.

Structurei

Secondary structure

1
655
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni77 – 793
Beta strandi80 – 889
Beta strandi90 – 9910
Turni100 – 1034
Beta strandi104 – 1118
Helixi115 – 13319
Helixi139 – 1435
Beta strandi147 – 1559
Beta strandi158 – 1658
Beta strandi168 – 1714
Helixi172 – 1787
Turni179 – 1813
Helixi186 – 20520
Helixi216 – 2183
Beta strandi219 – 2213
Helixi225 – 23511
Helixi485 – 4906
Beta strandi493 – 4953
Helixi498 – 5003
Beta strandi502 – 5065
Helixi515 – 5173
Helixi520 – 5245
Helixi531 – 54616
Beta strandi557 – 5593
Helixi561 – 57313
Helixi578 – 5836
Helixi587 – 5893
Beta strandi595 – 5995
Helixi608 – 6147
Helixi620 – 63011
Helixi631 – 6344
Helixi638 – 6403
Helixi644 – 6485
Helixi651 – 6544

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WAKX-ray1.73A42-655[»]
1WBPX-ray2.40A42-655[»]
3BEGX-ray2.90A58-255[»]
A474-655[»]
ProteinModelPortaliQ96SB4.
SMRiQ96SB4. Positions 63-263, 477-655.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96SB4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini80 – 653574Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00530000063566.
HOGENOMiHOG000171558.
HOVERGENiHBG108512.
InParanoidiQ96SB4.
KOiK15409.
OrthoDBiEOG70S74X.
PhylomeDBiQ96SB4.
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.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 22 Publications (identifier: Q96SB4-2) [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

        10         20         30         40         50
MERKVLALQA RKKRTKAKKD KAQRKSETQH RGSAPHSESD LPEQEEEILG
60 70 80 90 100
SDDDEQEDPN DYCKGGYHLV KIGDLFNGRY HVIRKLGWGH FSTVWLSWDI
110 120 130 140 150
QGKKFVAMKV VKSAEHYTET ALDEIRLLKS VRNSDPNDPN REMVVQLLDD
160 170 180 190 200
FKISGVNGTH ICMVFEVLGH HLLKWIIKSN YQGLPLPCVK KIIQQVLQGL
210 220 230 240 250
DYLHTKCRII HTDIKPENIL LSVNEQYIRR LAAEATEWQR SGAPPPSGSA
260 270 280 290 300
VSTAPQPKPA DKMSKNKKKK LKKKQKRQAE LLEKRMQEIE EMEKESGPGQ
310 320 330 340 350
KRPNKQEESE SPVERPLKEN PPNKMTQEKL EESSTIGQDQ TLMERDTEGG
360 370 380 390 400
AAEINCNGVI EVINYTQNSN NETLRHKEDL HNANDCDVQN LNQESSFLSS
410 420 430 440 450
QNGDSSTSQE TDSCTPITSE VSDTMVCQSS STVGQSFSEQ HISQLQESIR
460 470 480 490 500
AEIPCEDEQE QEHNGPLDNK GKSTAGNFLV NPLEPKNAEK LKVKIADLGN
510 520 530 540 550
ACWVHKHFTE DIQTRQYRSL EVLIGSGYNT PADIWSTACM AFELATGDYL
560 570 580 590 600
FEPHSGEEYT RDEDHIALII ELLGKVPRKL IVAGKYSKEF FTKKGDLKHI
610 620 630 640 650
TKLKPWGLFE VLVEKYEWSQ EEAAGFTDFL LPMLELIPEK RATAAECLRH

PWLNS
Length:655
Mass (Da):74,325
Last modified:October 14, 2008 - v2
Checksum:i900E980FE1C16B9A
GO
Isoform 1 (identifier: Q96SB4-3) [UniParc]FASTAAdd to Basket

Also known as: 1a

The sequence of this isoform differs from the canonical sequence as follows:
     4-4: K → KGERWSGLRH...FALHPSLSPA

Note: Due to intron retention.

Show »
Length:826
Mass (Da):92,412
Checksum:i9E4D86DE22A10D32
GO

Sequence cautioni

The sequence CAI20544.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI20545.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti210 – 2101I → T in AAH38292. (PubMed:15489334)Curated
Sequence conflicti360 – 3601I → L AA sequence (PubMed:12134018)Curated
Sequence conflicti363 – 3631I → L AA sequence (PubMed:12134018)Curated
Sequence conflicti400 – 4012SQ → LP in AAA20530. (PubMed:8208298)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721I → T.
Corresponds to variant rs35519113 [ dbSNP | Ensembl ].
VAR_051669

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei4 – 41K → KGERWSGLRHEGQWSPGRGP GQRRELRLTAAVRFPDVRRP STEVAPPHTPCLWAAGPRPS FRASSGAGRSRPLFPARPAR ALGPLQGPALGGRRRPPPAR PLTRPETPPAHPARALLCAP WAASPTPAASPSPQPPPRQA PQPGLAPLLGLHPHLGRLLS STFALHPSLSPA in isoform 1. 1 PublicationVSP_042130

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09564 mRNA. Translation: AAA20530.1.
AJ318054 mRNA. Translation: CAC39299.1.
Z99128 Genomic DNA. Translation: CAI20544.1. Sequence problems.
Z99128 Genomic DNA. Translation: CAI20545.1. Sequence problems.
BC038292 mRNA. Translation: AAH38292.1.
CCDSiCCDS47415.1. [Q96SB4-2]
PIRiS45337.
RefSeqiNP_003128.3. NM_003137.4. [Q96SB4-2]
UniGeneiHs.443861.

Genome annotation databases

EnsembliENST00000373825; ENSP00000362931; ENSG00000096063. [Q96SB4-2]
GeneIDi6732.
KEGGihsa:6732.
UCSCiuc003olh.3. human. [Q96SB4-2]

Polymorphism databases

DMDMi209572680.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U09564 mRNA. Translation: AAA20530.1 .
AJ318054 mRNA. Translation: CAC39299.1 .
Z99128 Genomic DNA. Translation: CAI20544.1 . Sequence problems.
Z99128 Genomic DNA. Translation: CAI20545.1 . Sequence problems.
BC038292 mRNA. Translation: AAH38292.1 .
CCDSi CCDS47415.1. [Q96SB4-2 ]
PIRi S45337.
RefSeqi NP_003128.3. NM_003137.4. [Q96SB4-2 ]
UniGenei Hs.443861.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WAK X-ray 1.73 A 42-655 [» ]
1WBP X-ray 2.40 A 42-655 [» ]
3BEG X-ray 2.90 A 58-255 [» ]
A 474-655 [» ]
ProteinModelPortali Q96SB4.
SMRi Q96SB4. Positions 63-263, 477-655.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112610. 207 interactions.
DIPi DIP-33888N.
IntActi Q96SB4. 218 interactions.
MINTi MINT-262701.
STRINGi 9606.ENSP00000391069.

Chemistry

BindingDBi Q96SB4.
ChEMBLi CHEMBL4375.
GuidetoPHARMACOLOGYi 2208.

PTM databases

PhosphoSitei Q96SB4.

Polymorphism databases

DMDMi 209572680.

Proteomic databases

MaxQBi Q96SB4.
PaxDbi Q96SB4.
PRIDEi Q96SB4.

Protocols and materials databases

DNASUi 6732.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373825 ; ENSP00000362931 ; ENSG00000096063 . [Q96SB4-2 ]
GeneIDi 6732.
KEGGi hsa:6732.
UCSCi uc003olh.3. human. [Q96SB4-2 ]

Organism-specific databases

CTDi 6732.
GeneCardsi GC06M035898.
H-InvDB HIX0005813.
HGNCi HGNC:11305. SRPK1.
HPAi HPA016431.
HPA056486.
MIMi 601939. gene.
neXtProti NX_Q96SB4.
PharmGKBi PA36129.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00530000063566.
HOGENOMi HOG000171558.
HOVERGENi HBG108512.
InParanoidi Q96SB4.
KOi K15409.
OrthoDBi EOG70S74X.
PhylomeDBi Q96SB4.
TreeFami TF105334.

Enzyme and pathway databases

SignaLinki Q96SB4.

Miscellaneous databases

EvolutionaryTracei Q96SB4.
GeneWikii SRPK1.
GenomeRNAii 6732.
NextBioi 26262.
PROi Q96SB4.
SOURCEi Search...

Gene expression databases

Bgeei Q96SB4.
CleanExi HS_SRPK1.
ExpressionAtlasi Q96SB4. baseline and differential.
Genevestigatori Q96SB4.

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. "A serine kinase regulates intracellular localization of splicing factors in the cell cycle."
    Gui J.F., Lane W.S., Fu X.-D.
    Nature 369:678-682(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION.
    Tissue: Cervix carcinoma.
  2. "Cloning and characterization of an alternatively spliced form of SR protein kinase 1 that interacts specifically with scaffold attachment factor-B."
    Nikolakaki E., Kohen R., Hartmann A.M., Stamm S., Georgatsou E., Giannakouros T.
    J. Biol. Chem. 276:40175-40182(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH SAFB.
    Tissue: Testis1 Publication.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    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 2).
    Tissue: TestisImported.
  5. "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: PROTEIN SEQUENCE OF 330-345 AND 353-375, FUNCTION IN PHOSPHORYLATION OF HEPATITIS B VIRUS CORE PROTEIN.
  6. "Identification of toposome, a novel multisubunit complex containing topoisomerase IIalpha."
    Lee C.G., Hague L.K., Li H., Donnelly R.
    Cell Cycle 3:638-647(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 376-400 AND 616-636, FUNCTION, IDENTIFICATION IN A TOPOSOME COMPLEX.
  7. "A protein related to splicing factor U2AF35 that interacts with U2AF65 and SR proteins in splicing of pre-mRNA."
    Tronchere H., Wang J., Fu X.D.
    Nature 388:397-400(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ZRSR2.
  8. "SRPK1 and LBR protein kinases show identical substrate specificities."
    Papoutsopoulou S., Nikolakaki E., Giannakouros T.
    Biochem. Biophys. Res. Commun. 255:602-607(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF LBR.
  9. "SR protein-specific kinase 1 is highly expressed in testis and phosphorylates protamine 1."
    Papoutsopoulou S., Nikolakaki E., Chalepakis G., Kruft V., Chevaillier P., Giannakouros T.
    Nucleic Acids Res. 27:2972-2980(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PRM1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  10. "Processive phosphorylation of alternative splicing factor/splicing factor 2."
    Aubol B.E., Chakrabarti S., Ngo J., Shaffer J., Nolen B., Fu X.-D., Ghosh G., Adams J.A.
    Proc. Natl. Acad. Sci. U.S.A. 100:12601-12606(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SFRS1.
  11. "Protein kinase CK2 phosphorylates and activates the SR protein-specific kinase 1."
    Mylonis I., Giannakouros T.
    Biochem. Biophys. Res. Commun. 301:650-656(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION AT SER-51 AND SER-555, MUTAGENESIS OF SER-37; SER-51; SER-222; SER-311; SER-436; SER-555 AND SER-619.
  12. "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.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Ordered multi-site phosphorylation of the splicing factor ASF/SF2 by SRPK1."
    Ma C.T., Velazquez-Dones A., Hagopian J.C., Ghosh G., Fu X.D., Adams J.A.
    J. Mol. Biol. 376:55-68(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SRSF1, THE MECHANISM OF PHOSPHORYATION.
  15. "Adaptable molecular interactions guide phosphorylation of the SR protein ASF/SF2 by SRPK1."
    Hagopian J.C., Ma C.T., Meade B.R., Albuquerque C.P., Ngo J.C., Ghosh G., Jennings P.A., Fu X.D., Adams J.A.
    J. Mol. Biol. 382:894-909(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SRSF1, THE MECHANISM OF PHOSPHORYATION.
  16. "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-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "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].
  19. "Allosteric interactions direct binding and phosphorylation of ASF/SF2 by SRPK1."
    Huynh N., Ma C.T., Giang N., Hagopian J., Ngo J., Adams J., Ghosh G.
    Biochemistry 48:11432-11440(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SRSF1, THE MECHANISM OF PHOSPHORYATION.
  20. "The enzymatic activity of SR protein kinases 1 and 1a is negatively affected by interaction with scaffold attachment factors B1 and 2."
    Tsianou D., Nikolakaki E., Tzitzira A., Bonanou S., Giannakouros T., Georgatsou E.
    FEBS J. 276:5212-5227(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SAFB/SAFB1 AND SAFB2.
  21. "Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones."
    Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.
    Genes Dev. 23:482-495(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DNAJB1/HSP40 AND AHSA1/AHA1.
  22. "Regiospecific phosphorylation control of the SR protein ASF/SF2 by SRPK1."
    Ma C.T., Hagopian J.C., Ghosh G., Fu X.D., Adams J.A.
    J. Mol. Biol. 390:618-634(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SRSF1, THE MECHANISM OF PHOSPHORYATION.
  23. "Arginine methylation of the ICP27 RGG box regulates the functional interactions of ICP27 with SRPK1 and Aly/REF during herpes simplex virus 1 infection."
    Souki S.K., Sandri-Goldin R.M.
    J. Virol. 83:8970-8975(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-1 ICP27 PROTEIN.
  24. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  25. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION OF ISOFORM 1 IN A COMPLEX WITH DHX9; MOV10; MATR3; HNRNPU; NCL; DDX21; HSD17B4; PABPC1; HNRNPM; IGF2BP1; SYNCRIP; RPL3; VIM; YBX1; NPM1; HNRNPA2B1; HNRNPC; RPLP0; RPL7A AND RALY.
  26. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. "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: SUBCELLULAR LOCATION.
  28. "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.
  29. "Phosphorylation mechanism and structure of serine-arginine protein kinases."
    Ghosh G., Adams J.A.
    FEBS J. 278:587-597(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  30. "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-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "Interplay between SRPK and Clk/Sty kinases in phosphorylation of the splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2."
    Ngo J.C.K., Chakrabarti S., Ding J.-H., Velazquez-Dones A., Nolen B., Aubol B.E., Adams J.A., Fu X.-D., Ghosh G.
    Mol. Cell 20:77-89(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 42-438 IN COMPLEX WITH ATP AND SUBSTRATE PEPTIDE, FUNCTION, INTERACTION WITH SFRS1.
  32. Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 42-655, SUBUNIT.
  33. "A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1."
    Ngo J.C., Giang K., Chakrabarti S., Ma C.T., Huynh N., Hagopian J.C., Dorrestein P.C., Fu X.D., Adams J.A., Ghosh G.
    Mol. Cell 29:563-576(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 58-655 IN COMPLEX WITH SRSF1, MECHANISM OF PHOSPHORYLATION OF SRSF1.

Entry informationi

Entry nameiSRPK1_HUMAN
AccessioniPrimary (citable) accession number: Q96SB4
Secondary accession number(s): Q12890
, Q5R364, Q5R365, Q8IY12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: October 14, 2008
Last modified: October 29, 2014
This is version 133 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

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