Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/arginine-rich splicing factor 1

Gene

SRSF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Molecular functioni

  • mRNA binding Source: MGI
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

  • alternative mRNA splicing, via spliceosome Source: GO_Central
  • cardiac muscle contraction Source: Ensembl
  • in utero embryonic development Source: Ensembl
  • mRNA 3'-end processing Source: Reactome
  • mRNA 5'-splice site recognition Source: UniProtKB
  • mRNA export from nucleus Source: Reactome
  • mRNA processing Source: ProtInc
  • mRNA splice site selection Source: ProtInc
  • mRNA splicing, via spliceosome Source: UniProtKB
  • RNA export from nucleus Source: Reactome
  • termination of RNA polymerase II transcription Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
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.
SIGNORiQ07955.

Names & Taxonomyi

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
Gene namesi
Name:SRSF1
Synonyms:ASF, SF2, SF2P33, SFRS1
ORF Names:OK/SW-cl.3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:10780. SRSF1.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • nuclear speck Source: MGI
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi58 – 592FV → SR in FV1; loss of ability to activate splicing. Slight reduction in splice site switching activity and no effect on RNA-binding. 1 Publication
Mutagenesisi93 – 931R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-97 and Ala-109. 1 Publication
Mutagenesisi97 – 971R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-109. 1 Publication
Mutagenesisi109 – 1091R → A: Predominantly localizes to cytoplasm and fails to modulate splicing of endogenous pre-mRNAs; when associated with Ala-93 and Ala-97. 1 Publication
Mutagenesisi162 – 1632FV → SR in FV2; loss of ability to activate splicing. Great reduction in splice site switching activity and RNA-binding. 1 Publication
Mutagenesisi162 – 1621F → A in AV; loss of ability to activate splicing. Great reduction in splice site switching activity and no effect on RNA-binding. 1 Publication
Mutagenesisi162 – 1621F → D: Reduced nucleocytoplasmic shuttling; when associated with D-190. 1 Publication
Mutagenesisi180 – 1801F → D: Reduced nucleocytoplasmic shuttling; when associated with D-162. 1 Publication
Mutagenesisi182 – 24867Missing in MR-B; strongly inhibits splicing. 1 PublicationAdd
BLAST
Mutagenesisi182 – 19918Missing in MR-E; loss of ability to activate splicing. 1 PublicationAdd
BLAST
Mutagenesisi192 – 24857Missing in MR-A; loss of ability to activate splicing. 1 PublicationAdd
BLAST
Mutagenesisi192 – 1998Missing in MR-D; loss of ability to activate splicing. 1 Publication
Mutagenesisi199 – 22426Missing in RS-A; loss of ability to activate splicing but retains splice site switching. 1 PublicationAdd
BLAST
Mutagenesisi215 – 24834Missing in RS-C; loss of ability to activate splicing but retains splice site switching. 1 PublicationAdd
BLAST
Mutagenesisi226 – 24823Missing in RS-B; retains both splice activation and splice site switching activity. 1 PublicationAdd
BLAST

Organism-specific databases

PharmGKBiPA35696.

Polymorphism and mutation databases

BioMutaiSRSF1.
DMDMi730773.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 248247Serine/arginine-rich splicing factor 1PRO_0000081911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei38 – 381N6-acetyllysine; alternateCombined sources
Cross-linki38 – 38Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Modified residuei93 – 931Asymmetric dimethylarginine1 Publication
Modified residuei97 – 971Asymmetric dimethylarginine1 Publication
Modified residuei109 – 1091Asymmetric dimethylarginine1 Publication
Modified residuei133 – 1331PhosphoserineCombined sources
Modified residuei179 – 1791N6-acetyllysineCombined sources
Modified residuei199 – 1991PhosphoserineCombined sources
Modified residuei201 – 2011PhosphoserineCombined sources
Modified residuei202 – 2021PhosphotyrosineCombined sources
Modified residuei205 – 2051PhosphoserineCombined sources
Modified residuei231 – 2311PhosphoserineCombined sources
Modified residuei234 – 2341PhosphoserineCombined sources
Modified residuei238 – 2381PhosphoserineCombined sources

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

EPDiQ07955.
MaxQBiQ07955.
PaxDbiQ07955.
PeptideAtlasiQ07955.
PRIDEiQ07955.
TopDownProteomicsiQ07955-1. [Q07955-1]
Q07955-2. [Q07955-2]
Q07955-3. [Q07955-3]

PTM databases

iPTMnetiQ07955.
PhosphoSiteiQ07955.
SwissPalmiQ07955.

Miscellaneous databases

PMAP-CutDBQ07955.

Expressioni

Gene expression databases

BgeeiENSG00000136450.
CleanExiHS_SFRS1.
ExpressionAtlasiQ07955. baseline and differential.
GenevisibleiQ07955. HS.

Organism-specific databases

HPAiCAB013073.
HPA061301.

Interactioni

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).12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CIR1Q86X953EBI-398920,EBI-627102
NFYAP235115EBI-398920,EBI-389739
NXF1Q9UBU95EBI-398920,EBI-398874
SRPK1Q96SB43EBI-398920,EBI-539478
Srpk1O705515EBI-398920,EBI-593343From a different organism.
Srpk2O547813EBI-398920,EBI-593325From a different organism.
TRAF5O004632EBI-398920,EBI-523498

Protein-protein interaction databases

BioGridi112324. 173 interactions.
DIPiDIP-2155N.
IntActiQ07955. 54 interactions.
MINTiMINT-5000565.
STRINGi9606.ENSP00000258962.

Structurei

Secondary structure

1
248
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 228Combined sources
Helixi29 – 368Combined sources
Helixi37 – 393Combined sources
Beta strandi42 – 476Combined sources
Beta strandi50 – 545Combined sources
Beta strandi57 – 626Combined sources
Helixi64 – 7411Combined sources
Beta strandi85 – 873Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi122 – 1276Combined sources
Helixi134 – 1418Combined sources
Helixi142 – 1443Combined sources
Beta strandi147 – 1526Combined sources
Beta strandi158 – 1647Combined sources
Helixi165 – 17410Combined sources
Turni175 – 1773Combined sources
Beta strandi179 – 1813Combined sources
Beta strandi183 – 1853Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi191 – 1977Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi206 – 2083Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4ANMR-A1-96[»]
2M7SNMR-A106-195[»]
2M8DNMR-B107-196[»]
2O3DNMR-A107-215[»]
3BEGX-ray2.90B105-219[»]
4C0OX-ray2.56C/D106-230[»]
ProteinModelPortaliQ07955.
SMRiQ07955. Positions 6-102, 116-197.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07955.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 9176RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini121 – 19575RRM 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni198 – 24750Interacts with SAFB1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi94 – 11320Gly-rich (hinge region)Add
BLAST
Compositional biasi198 – 24750Arg/Ser-rich (RS domain)Add
BLAST

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

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0105. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ07955.
KOiK12890.
PhylomeDBiQ07955.
TreeFamiTF106261.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform ASF-1 (identifier: Q07955-1) [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

        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
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891P → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_035488

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei185 – 24864GETAY…SRSRT → FCLSNREKLPTSGLKLMGPE VQVMEDLDLEAVVVAEAVAE ATAGVAVTPQGEAEDHHAIL PVIADLALVHKMIGDTFCRT HVVYSFPLFSTIFSFFNSNC FVQNGLKC in isoform ASF-2. 1 PublicationVSP_005856Add
BLAST
Alternative sequencei185 – 20117GETAY…PRSPS → VGYTRILFFDQNWIQWS in isoform ASF-3. 1 PublicationVSP_005857Add
BLAST
Alternative sequencei202 – 24847Missing in isoform ASF-3. 1 PublicationVSP_005858Add
BLAST

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]
UniGeneiHs.68714.
Hs.710026.
Hs.744140.

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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

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]
UniGeneiHs.68714.
Hs.710026.
Hs.744140.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4ANMR-A1-96[»]
2M7SNMR-A106-195[»]
2M8DNMR-B107-196[»]
2O3DNMR-A107-215[»]
3BEGX-ray2.90B105-219[»]
4C0OX-ray2.56C/D106-230[»]
ProteinModelPortaliQ07955.
SMRiQ07955. Positions 6-102, 116-197.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112324. 173 interactions.
DIPiDIP-2155N.
IntActiQ07955. 54 interactions.
MINTiMINT-5000565.
STRINGi9606.ENSP00000258962.

PTM databases

iPTMnetiQ07955.
PhosphoSiteiQ07955.
SwissPalmiQ07955.

Polymorphism and mutation databases

BioMutaiSRSF1.
DMDMi730773.

Proteomic databases

EPDiQ07955.
MaxQBiQ07955.
PaxDbiQ07955.
PeptideAtlasiQ07955.
PRIDEiQ07955.
TopDownProteomicsiQ07955-1. [Q07955-1]
Q07955-2. [Q07955-2]
Q07955-3. [Q07955-3]

Protocols and materials databases

DNASUi6426.
Structural Biology KnowledgebaseSearch...

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

CTDi6426.
GeneCardsiSRSF1.
H-InvDBHIX0173551.
HGNCiHGNC:10780. SRSF1.
HPAiCAB013073.
HPA061301.
MIMi600812. gene.
neXtProtiNX_Q07955.
PharmGKBiPA35696.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0105. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00700000104103.
HOVERGENiHBG002295.
InParanoidiQ07955.
KOiK12890.
PhylomeDBiQ07955.
TreeFamiTF106261.

Enzyme and pathway databases

ReactomeiR-HSA-109688. Cleavage of Growing Transcript in the Termination Region.
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.
SIGNORiQ07955.

Miscellaneous databases

ChiTaRSiSRSF1. human.
EvolutionaryTraceiQ07955.
GeneWikiiASF/SF2.
GenomeRNAii6426.
PMAP-CutDBQ07955.
PROiQ07955.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000136450.
CleanExiHS_SFRS1.
ExpressionAtlasiQ07955. baseline and differential.
GenevisibleiQ07955. HS.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSRSF1_HUMAN
AccessioniPrimary (citable) accession number: Q07955
Secondary accession number(s): B2R6Z7, D3DTZ3, Q13809
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 202 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 17
    Human chromosome 17: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.