Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 232 (16 Oct 2019)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Serine/arginine-rich splicing factor 1

Gene

SRSF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. 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. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRNA-binding
Biological processmRNA processing, mRNA splicing, mRNA transport, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72165 mRNA Splicing - Minor Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-73856 RNA Polymerase II Transcription Termination

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q07955

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Serine/arginine-rich splicing factor 1
Alternative name(s):
Alternative-splicing factor 1
Short name:
ASF-1
Splicing factor, arginine/serine-rich 1
pre-mRNA-splicing factor SF2, P33 subunit
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SRSF1
Synonyms:ASF, SF2, SF2P33, SFRS1
ORF Names:OK/SW-cl.3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:10780 SRSF1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
600812 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q07955

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi58 – 59FV → SR in FV1; loss of ability to activate splicing. Slight reduction in splice site switching activity and no effect on RNA-binding. 1 Publication2
Mutagenesisi93R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-97 and Ala-109. 1 Publication1
Mutagenesisi97R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-109. 1 Publication1
Mutagenesisi109R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-97. 1 Publication1
Mutagenesisi162 – 163FV → SR in FV2; loss of ability to activate splicing. Great reduction in splice site switching activity and RNA-binding. 1 Publication2
Mutagenesisi162F → A in AV; loss of ability to activate splicing. Great reduction in splice site switching activity and no effect on RNA-binding. 1 Publication1
Mutagenesisi162F → D: Reduced nucleocytoplasmic shuttling; when associated with D-190. 1 Publication1
Mutagenesisi180F → D: Reduced nucleocytoplasmic shuttling; when associated with D-162. 1 Publication1
Mutagenesisi182 – 248Missing in MR-B; strongly inhibits splicing. 1 PublicationAdd BLAST67
Mutagenesisi182 – 199Missing in MR-E; loss of ability to activate splicing. 1 PublicationAdd BLAST18
Mutagenesisi192 – 248Missing in MR-A; loss of ability to activate splicing. 1 PublicationAdd BLAST57
Mutagenesisi192 – 199Missing in MR-D; loss of ability to activate splicing. 1 Publication8
Mutagenesisi199 – 224Missing in RS-A; loss of ability to activate splicing but retains splice site switching. 1 PublicationAdd BLAST26
Mutagenesisi215 – 248Missing in RS-C; loss of ability to activate splicing but retains splice site switching. 1 PublicationAdd BLAST34
Mutagenesisi226 – 248Missing in RS-B; retains both splice activation and splice site switching activity. 1 PublicationAdd BLAST23

Organism-specific databases

DisGeNET

More...
DisGeNETi
6426

Open Targets

More...
OpenTargetsi
ENSG00000136450

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA35696

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q07955

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB09130 Copper

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
SRSF1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
730773

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000819112 – 248Serine/arginine-rich splicing factor 1Add BLAST247

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei38N6-acetyllysine; alternateCombined sources1
Cross-linki38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei93Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei93Omega-N-methylarginine; alternateCombined sources1
Modified residuei97Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei97Omega-N-methylarginine; alternateCombined sources1
Modified residuei109Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei109Omega-N-methylarginine; alternateCombined sources1
Modified residuei111Omega-N-methylarginineCombined sources1
Modified residuei133PhosphoserineCombined sources1
Modified residuei179N6-acetyllysineCombined sources1
Modified residuei199PhosphoserineCombined sources1
Modified residuei201PhosphoserineCombined sources1
Modified residuei202PhosphotyrosineCombined sources1
Modified residuei205PhosphoserineCombined sources1
Modified residuei231PhosphoserineCombined sources1
Modified residuei234PhosphoserineCombined sources1
Modified residuei238PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by SRPK1 at multiple serines in its RS domain via 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 to a docking groove in the large lobe of the kinase domain of SRPK1 and this induces certain structural changes in SRPK1 and/or RRM 2 domain of SRSF1, allowing RRM 2 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 RRM 2, which then docks at the docking groove of SRPK1. This also signals RRM 2 to begin to dissociate, which facilitates SRSF1 dissociation after phosphorylation is completed.5 Publications
Asymmetrically dimethylated at arginines, probably by PRMT1, methylation promotes localization to nuclear speckles.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q07955

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q07955

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q07955

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q07955

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q07955

PeptideAtlas

More...
PeptideAtlasi
Q07955

PRoteomics IDEntifications database

More...
PRIDEi
Q07955

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
58560 [Q07955-1]
58561 [Q07955-2]
58562 [Q07955-3]

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
Q07955-1 [Q07955-1]
Q07955-2 [Q07955-2]
Q07955-3 [Q07955-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q07955

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q07955

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q07955

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
Q07955

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000136450 Expressed in 241 organ(s), highest expression level in oviduct epithelium

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q07955 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q07955 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB013073
HPA061301

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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).

Interacts with SRPK1 and a sliding docking interaction is essential for its sequential and processive phosphorylation by SRPK1.

Interacts with NXF1.

Interacts with CCNL1, CCNL2 and CDK11B (PubMed:18216018).

Interacts with RRP1B (PubMed:23604122).

13 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
112324, 206 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q07955

Database of interacting proteins

More...
DIPi
DIP-2155N

Protein interaction database and analysis system

More...
IntActi
Q07955, 91 interactors

Molecular INTeraction database

More...
MINTi
Q07955

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000258962

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1248
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q07955

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q07955

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini16 – 91RRM 1PROSITE-ProRule annotationAdd BLAST76
Domaini121 – 195RRM 2PROSITE-ProRule annotationAdd BLAST75

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni198 – 247Interaction with SAFB1Add BLAST50

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi94 – 113Gly-rich (hinge region)Add BLAST20
Compositional biasi198 – 247Arg/Ser-rich (RS domain)Add BLAST50

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The RRM 2 domain plays an important role in governing both the binding mode and the phosphorylation mechanism of the RS domain by SRPK1. RS domain and RRM 2 are uniquely positioned to initiate a highly directional (C-terminus to N-terminus) phosphorylation reaction in which the RS domain slides through an extended electronegative channel separating the docking groove of SRPK1 and the active site. RRM 2 binds toward the periphery of the active site and guides the directional phosphorylation mechanism. Both the RS domain and an RRM domain are required for nucleocytoplasmic shuttling.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the splicing factor SR family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0105 Eukaryota
COG0724 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155585

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q07955

KEGG Orthology (KO)

More...
KOi
K12890

Database of Orthologous Groups

More...
OrthoDBi
1321443at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q07955

TreeFam database of animal gene trees

More...
TreeFami
TF106261

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12597 RRM1_SRSF1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.70.330, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
IPR029538 SRSF1
IPR034520 SRSF1_RRM1

The PANTHER Classification System

More...
PANTHERi
PTHR23147:SF44 PTHR23147:SF44, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00076 RRM_1, 2 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00360 RRM, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54928 SSF54928, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50102 RRM, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform ASF-1 (identifier: Q07955-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR
60 70 80 90 100
RGGPPFAFVE FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG
110 120 130 140 150
GGGGGGAPRG RYGPPSRRSE NRVVVSGLPP SGSWQDLKDH MREAGDVCYA
160 170 180 190 200
DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF RSHEGETAYI RVKVDGPRSP
210 220 230 240
SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR HSRSRSRT
Length:248
Mass (Da):27,745
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC28A0B2F112EA713
GO
Isoform ASF-2 (identifier: Q07955-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     185-248: GETAYIRVKV...PRHSRSRSRT → FCLSNREKLP...NCFVQNGLKC

Show »
Length:292
Mass (Da):31,999
Checksum:iC9502AC70F373EAC
GO
Isoform ASF-3 (identifier: Q07955-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     185-201: GETAYIRVKVDGPRSPS → VGYTRILFFDQNWIQWS
     202-248: Missing.

Note: May be due to intron retention.
Show »
Length:201
Mass (Da):22,460
Checksum:iB9AC6495A491613D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3KTL2J3KTL2_HUMAN
Serine/arginine-rich-splicing facto...
SRSF1 SFRS1, hCG_1774411
253Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3KSR8J3KSR8_HUMAN
Serine/arginine-rich-splicing facto...
SRSF1
143Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3QQV5J3QQV5_HUMAN
Serine/arginine-rich-splicing facto...
SRSF1 SFRS1, hCG_1774411
65Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
J3KSW7J3KSW7_HUMAN
Serine/arginine-rich-splicing facto...
SRSF1
73Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03548889P → S in a breast cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_005856185 – 248GETAY…SRSRT → FCLSNREKLPTSGLKLMGPE VQVMEDLDLEAVVVAEAVAE ATAGVAVTPQGEAEDHHAIL PVIADLALVHKMIGDTFCRT HVVYSFPLFSTIFSFFNSNC FVQNGLKC in isoform ASF-2. 1 PublicationAdd BLAST64
Alternative sequenceiVSP_005857185 – 201GETAY…PRSPS → VGYTRILFFDQNWIQWS in isoform ASF-3. 1 PublicationAdd BLAST17
Alternative sequenceiVSP_005858202 – 248Missing in isoform ASF-3. 1 PublicationAdd BLAST47

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M72709 mRNA Translation: AAA35565.1
M72709 mRNA Translation: AAA35564.1
M69040 mRNA Translation: AAA03476.1
AB062124 mRNA Translation: BAB93456.1
AK312781 mRNA Translation: BAG35644.1
CH471109 Genomic DNA Translation: EAW94485.1
CH471109 Genomic DNA Translation: EAW94486.1
BC010264 mRNA Translation: AAH10264.1
BC033785 mRNA Translation: AAH33785.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS11600.1 [Q07955-1]
CCDS58580.1 [Q07955-3]

Protein sequence database of the Protein Information Resource

More...
PIRi
A40040
B40040
C40040

NCBI Reference Sequences

More...
RefSeqi
NP_001071634.1, NM_001078166.1 [Q07955-3]
NP_008855.1, NM_006924.4 [Q07955-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000258962; ENSP00000258962; ENSG00000136450 [Q07955-1]
ENST00000581979; ENSP00000463223; ENSG00000136450 [Q07955-3]
ENST00000582730; ENSP00000462215; ENSG00000136450 [Q07955-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
6426

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:6426

UCSC genome browser

More...
UCSCi
uc002ivi.4 human [Q07955-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M72709 mRNA Translation: AAA35565.1
M72709 mRNA Translation: AAA35564.1
M69040 mRNA Translation: AAA03476.1
AB062124 mRNA Translation: BAB93456.1
AK312781 mRNA Translation: BAG35644.1
CH471109 Genomic DNA Translation: EAW94485.1
CH471109 Genomic DNA Translation: EAW94486.1
BC010264 mRNA Translation: AAH10264.1
BC033785 mRNA Translation: AAH33785.1
CCDSiCCDS11600.1 [Q07955-1]
CCDS58580.1 [Q07955-3]
PIRiA40040
B40040
C40040
RefSeqiNP_001071634.1, NM_001078166.1 [Q07955-3]
NP_008855.1, NM_006924.4 [Q07955-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1X4ANMR-A1-96[»]
2M7SNMR-A106-195[»]
2M8DNMR-B107-196[»]
2O3DNMR-A107-215[»]
3BEGX-ray2.90B105-219[»]
4C0OX-ray2.56C/D106-230[»]
SMRiQ07955
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi112324, 206 interactors
CORUMiQ07955
DIPiDIP-2155N
IntActiQ07955, 91 interactors
MINTiQ07955
STRINGi9606.ENSP00000258962

Chemistry databases

DrugBankiDB09130 Copper

PTM databases

iPTMnetiQ07955
PhosphoSitePlusiQ07955
SwissPalmiQ07955

Polymorphism and mutation databases

BioMutaiSRSF1
DMDMi730773

Proteomic databases

EPDiQ07955
jPOSTiQ07955
MassIVEiQ07955
MaxQBiQ07955
PaxDbiQ07955
PeptideAtlasiQ07955
PRIDEiQ07955
ProteomicsDBi58560 [Q07955-1]
58561 [Q07955-2]
58562 [Q07955-3]
TopDownProteomicsiQ07955-1 [Q07955-1]
Q07955-2 [Q07955-2]
Q07955-3 [Q07955-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
6426

Genome annotation databases

EnsembliENST00000258962; ENSP00000258962; ENSG00000136450 [Q07955-1]
ENST00000581979; ENSP00000463223; ENSG00000136450 [Q07955-3]
ENST00000582730; ENSP00000462215; ENSG00000136450 [Q07955-3]
GeneIDi6426
KEGGihsa:6426
UCSCiuc002ivi.4 human [Q07955-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
6426
DisGeNETi6426

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SRSF1
HGNCiHGNC:10780 SRSF1
HPAiCAB013073
HPA061301
MIMi600812 gene
neXtProtiNX_Q07955
OpenTargetsiENSG00000136450
PharmGKBiPA35696

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0105 Eukaryota
COG0724 LUCA
GeneTreeiENSGT00940000155585
InParanoidiQ07955
KOiK12890
OrthoDBi1321443at2759
PhylomeDBiQ07955
TreeFamiTF106261

Enzyme and pathway databases

ReactomeiR-HSA-159236 Transport of Mature mRNA derived from an Intron-Containing Transcript
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72165 mRNA Splicing - Minor Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-73856 RNA Polymerase II Transcription Termination
SIGNORiQ07955

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
SRSF1 human
EvolutionaryTraceiQ07955

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
ASF/SF2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
6426
PharosiQ07955
PMAP-CutDBiQ07955

Protein Ontology

More...
PROi
PR:Q07955

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000136450 Expressed in 241 organ(s), highest expression level in oviduct epithelium
ExpressionAtlasiQ07955 baseline and differential
GenevisibleiQ07955 HS

Family and domain databases

CDDicd12597 RRM1_SRSF1, 1 hit
Gene3Di3.30.70.330, 2 hits
InterProiView protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
IPR029538 SRSF1
IPR034520 SRSF1_RRM1
PANTHERiPTHR23147:SF44 PTHR23147:SF44, 1 hit
PfamiView protein in Pfam
PF00076 RRM_1, 2 hits
SMARTiView protein in SMART
SM00360 RRM, 2 hits
SUPFAMiSSF54928 SSF54928, 1 hit
PROSITEiView protein in PROSITE
PS50102 RRM, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSRSF1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q07955
Secondary accession number(s): B2R6Z7, D3DTZ3, Q13809
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: October 16, 2019
This is version 232 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again