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Reviewed (UniProtKB/Swiss-Prot)

Note: Proteins listed in ProtBank™ database are NOT off-the-shelf [catalog] proteins. Customized protein production request can be made for any protein in this database by clicking on the corresponding button under "Quick Quote". Please ensure sequence accuracy and/or make any necessary modifications prior to submitting your quote request

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Reviewed (UniProtKB/Swiss-Prot)


Name Gene Symbol Rec Full Name Protein Information Quick Quote  Price,
Turnaround
SRSF1_BOVIN, Bos taurus (cattle) SRSF1 Splicing factor, arginine/serine-rich 1 Functions
wild_type
Starting from $1600,
4 weeks
Protein Domains
mutant
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Protein Names | ProteinIDs  | Organism | Gene Names  | GeneID | Genome Annotation(Ensembl) |  Protein Sequence | 
General annotation |  References | Order
Protein Names
Recommended name:
 Serine/arginine-rich splicing factor 1;
Alternative name(s):
 Splicing factor, arginine/serine-rich 1
Protein IDs
(Accession numbers)
UniProtKB
 Q0VCY7
NCBI RefSeq

NP_001069862.1, NM_001076394.1.
Organism
Latin Name/
(Common Name)
Bos taurus (Bovine).
Taxonomic Identifier (NCBI)
 9913
Gene Names
 SRSF1 [GenPool]
GeneID

615796
Genome
Annotation (Ensembl)

ENSBTAT00000049486, ENSBTAP00000046374; ENSBTAG00000014766
Protein Sequence
 
SEQUENCE   248 AA;  27745 MW;  C28A0B2F112EA713 CRC64;
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE
FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE
NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF
RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR
HSRSRSRT
General annotation
Function
 Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE- dependent splicing (By similarity).
Cofactor
Subunit structure
 Consists of two polypeptides of p32 and p33. In vitro, self-associates and binds SRSF2, SNRNP70 and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with SAFB/SAFB1. Interacts with PSIP1/LEDGF. Interacts with SRPK1. Identified in the spliceosome C complex. Interacts with RSRC1 (via Arg/Ser-rich domain). Interacts with ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-terminus) (By similarity).
Subcellular location

Cytoplasm (By similarity). Nucleus (By similarity). Nucleus speckle (By similarity). Note=Shuttles between the nucleus and the cytoplasm (By similarity).
Tissue specificity
Induction
Domain
 Both the RS domain and an RRM domain are required for nucleocytoplasmic shuttling (By similarity).
Post-translational modification

Extensively phosphorylated on serine residues in the RSdomain. This may regulate nucleocytoplasmic shuttling (Bysimilarity).

Arg-96 is dimethylated, probably to asymmetricdimethylarginine (By similarity).
Involvement in disease

References

  • Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.

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Comparative Toxicogenomics Database | Order
Protein Domain Databases
InterPro

IPR012677, Nucleotide-bd_a/b_plait.

IPR000504, RRM_dom.
Gene3D

G3DSA:3.30.70.330, a_b_plait_nuc_bd; 2.
PANTHER
Pfam

PF00076, RRM_1; 2.
PRINTS
SUPFAM
PROSITE

PS50102, RRM; 2.
3D Structure
Database (PDB)
Entry
Method
Resolution (A)
Chain
Positions
PDBsum
Sequence
Annotation
Feature key
Position(s)
Length
Description
Initiator methionine 1 1 Removed (By similarity).
Polypeptide chain 2 - 248 247 Serine/arginine-rich splicing factor 1. /FTId=PRO_0000287724.
Domain 16 - 91 76 RRM 1.
Domain 121 - 195 75 RRM 2.
Region 198 - 247 50 Interacts with SAFB1 (By similarity).
Compositionally biased region 94 - 113 20 Gly-rich (hinge region).
Compositionally biased region 198 - 247 50 Arg/Ser-rich (RS domain).
Posttranslational modification of a residue 2 1 N-acetylserine (Potential).
Posttranslational modification of a residue 2 1 Phosphoserine (By similarity).
Posttranslational modification of a residue 38 1 N6-acetyllysine (By similarity).
Posttranslational modification of a residue 93 1 Omega-N-methylarginine (By similarity).
Posttranslational modification of a residue 97 1 Omega-N-methylated arginine (By
Posttranslational modification of a residue 109 1 Omega-N-methylarginine (By similarity).
Posttranslational modification of a residue 179 1 N6-acetyllysine (By similarity).
Posttranslational modification of a residue 189 1 Phosphotyrosine (By similarity).
Posttranslational modification of a residue 199 1 Phosphoserine (By similarity).
Posttranslational modification of a residue 201 1 Phosphoserine (By similarity).
Posttranslational modification of a residue 202 1 Phosphotyrosine (By similarity).
Posttranslational modification of a residue 205 1 Phosphoserine (By similarity).
Posttranslational modification of a residue 231 1 Phosphoserine (By similarity).
Posttranslational modification of a residue 234 1 Phosphoserine (By similarity).
Posttranslational modification of a residue 237 1 Phosphotyrosine (By similarity).
Posttranslational modification of a residue 238 1 Phosphoserine (By similarity).
Protein-protein
Interaction
Databases
DIP
IntAct
MINT
STRING

Q0VCY7
Binary Interactions
With
Entry
#Exp.
IntAct
Enzyme and Pathway Databases
Pathway
Interaction DB
Reactome
Phylogenomic Database
HOVERGEN

HBG002295
InParanoid

Q0VCY7
OMA

RSHEVCA
OrthoDB

EOG4WH8N5
Proteomics
Database (PRIDE)

Q0VCY7
Comparative
Toxicogenomics
Database (CTD)

6426
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