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Protein

Serine/arginine-rich splicing factor 7

Gene

SRSF7

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

Functioni

Required for pre-mRNA splicing. Can also modulate alternative splicing in vitro. Represses the splicing of MAPT/Tau exon 10. May function as export adapter involved in mRNA nuclear export such as of histone H2A. Binds mRNA which is thought to be transferred to the NXF1-NXT1 heterodimer for export (TAP/NXF1 pathway); enhances NXF1-NXT1 RNA-binding activity. RNA-binding is semi-sequence specific.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri104 – 12017CCHC-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • mRNA 3'-end processing Source: Reactome
  • mRNA export from nucleus Source: Reactome
  • mRNA processing Source: ProtInc
  • mRNA splicing, via spliceosome Source: Reactome
  • negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  • RNA export from nucleus Source: Reactome
  • RNA splicing Source: ProtInc
  • termination of RNA polymerase II transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing, mRNA transport, Transport

Keywords - Ligandi

Metal-binding, RNA-binding, Zinc

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.
SIGNORiQ16629.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/arginine-rich splicing factor 7
Alternative name(s):
Splicing factor 9G8
Splicing factor, arginine/serine-rich 7
Gene namesi
Name:SRSF7
Synonyms:SFRS7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:10789. SRSF7.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi87 – 882RR → EE: Abolishes interaction with NXF1. 1 Publication
Mutagenesisi97 – 982RR → EE: Abolishes interaction with NXF1. 1 Publication

Organism-specific databases

PharmGKBiPA35705.

Polymorphism and mutation databases

BioMutaiSRSF7.
DMDMi3929380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Serine/arginine-rich splicing factor 7PRO_0000081932Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241N6-acetyllysineCombined sources
Modified residuei32 – 321PhosphoserineCombined sources
Modified residuei163 – 1631PhosphoserineCombined sources
Modified residuei165 – 1651PhosphoserineCombined sources
Modified residuei167 – 1671PhosphoserineCombined sources
Modified residuei181 – 1811PhosphoserineBy similarity
Modified residuei183 – 1831PhosphoserineBy similarity
Modified residuei192 – 1921PhosphoserineCombined sources
Modified residuei194 – 1941PhosphoserineCombined sources
Modified residuei196 – 1961PhosphoserineCombined sources
Modified residuei231 – 2311PhosphoserineCombined sources
Modified residuei233 – 2331PhosphoserineCombined sources

Post-translational modificationi

Extensively phosphorylated on serine residues in the RS domain.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ16629.
MaxQBiQ16629.
PaxDbiQ16629.
PeptideAtlasiQ16629.
PRIDEiQ16629.
TopDownProteomicsiQ16629-1. [Q16629-1]
Q16629-2. [Q16629-2]
Q16629-3. [Q16629-3]
Q16629-4. [Q16629-4]

2D gel databases

SWISS-2DPAGEP99058.

PTM databases

iPTMnetiQ16629.
PhosphoSiteiQ16629.
SwissPalmiQ16629.

Expressioni

Tissue specificityi

Brain, liver, kidney and lung.

Gene expression databases

BgeeiQ16629.
CleanExiHS_SFRS7.
ExpressionAtlasiQ16629. baseline and differential.
GenevisibleiQ16629. HS.

Organism-specific databases

HPAiHPA043850.
HPA056926.

Interactioni

Subunit structurei

Found in large molecular weight complexes containing CCNL1 and the p110 isoforms of either CDC2L1 or CDC2L2. Interacts with CCNL2 and CPSF6. Interacts with NXF1.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LUC7L2Q9Y3833EBI-398885,EBI-352851
NXF1Q9UBU94EBI-398885,EBI-398874
RBBP6Q7Z6E93EBI-398885,EBI-2117026
SDCBPO005603EBI-398885,EBI-727004
Srek1Q9JKL73EBI-398885,EBI-6452221From a different organism.
SRPK1Q96SB42EBI-398885,EBI-539478
SRPK2P783622EBI-398885,EBI-593303

Protein-protein interaction databases

BioGridi112330. 108 interactions.
DIPiDIP-31790N.
IntActiQ16629. 33 interactions.
MINTiMINT-3032898.
STRINGi9606.ENSP00000325905.

Structurei

Secondary structure

1
238
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 165Combined sources
Helixi24 – 3411Combined sources
Beta strandi38 – 5316Combined sources
Helixi57 – 6913Combined sources
Beta strandi72 – 743Combined sources
Beta strandi78 – 847Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HVZNMR-A12-98[»]
ProteinModelPortaliQ16629.
SMRiQ16629. Positions 12-98.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16629.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 8474RRMPROSITE-ProRule annotationAdd
BLAST
Repeati153 – 16081
Repeati161 – 16882
Repeati169 – 17683
Repeati177 – 18484
Repeati211 – 21885; approximate
Repeati219 – 22686; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 9818Sufficient for interaction with NXF1Add
BLAST
Regioni153 – 226746 X 8 AA repeats of R-R-S-R-S-X-S-XAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi121 – 238118Arg/Ser-rich (RS domain)Add
BLAST

Sequence similaritiesi

Belongs to the splicing factor SR family.Curated
Contains 1 CCHC-type zinc finger.PROSITE-ProRule annotation
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri104 – 12017CCHC-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0107. Eukaryota.
ENOG4111N8Y. LUCA.
GeneTreeiENSGT00700000104103.
HOGENOMiHOG000276234.
HOVERGENiHBG107480.
InParanoidiQ16629.
KOiK12896.
OMAiASPERMG.
OrthoDBiEOG73NG5V.
PhylomeDBiQ16629.
TreeFamiTF351858.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Isoforms, often lacking the RS domain and differentially expressed in fetal tissues, may be involved in modulation of 9G8 function.

Isoform 1 (identifier: Q16629-1) [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
MSRYGRYGGE TKVYVGNLGT GAGKGELERA FSYYGPLRTV WIARNPPGFA
60 70 80 90 100
FVEFEDPRDA EDAVRGLDGK VICGSRVRVE LSTGMPRRSR FDRPPARRPF
110 120 130 140 150
DPNDRCYECG EKGHYAYDCH RYSRRRRSRS RSRSHSRSRG RRYSRSRSRS
160 170 180 190 200
RGRRSRSASP RRSRSISLRR SRSASLRRSR SGSIKGSRYF QSPSRSRSRS
210 220 230
RSISRPRSSR SKSRSPSPKR SRSPSGSPRR SASPERMD
Length:238
Mass (Da):27,367
Last modified:November 1, 1996 - v1
Checksum:i49136754D9630853
GO
Isoform 2 (identifier: Q16629-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     130-135: SRSRSH → AENLRR
     136-238: Missing.

Show »
Length:135
Mass (Da):15,573
Checksum:iD390DEB80ADEA752
GO
Isoform 3 (identifier: Q16629-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     130-132: SRS → YLF
     133-238: Missing.

Show »
Length:132
Mass (Da):15,257
Checksum:iF586F82752DEDCF0
GO
Isoform 4 (identifier: Q16629-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     209-220: Missing.

Note: No experimental confirmation available.
Show »
Length:226
Mass (Da):26,012
Checksum:iA2FAEE66A5E4DCE7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561D → G in BAG59658 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei130 – 1356SRSRSH → AENLRR in isoform 2. CuratedVSP_005872
Alternative sequencei130 – 1323SRS → YLF in isoform 3. CuratedVSP_005874
Alternative sequencei133 – 238106Missing in isoform 3. CuratedVSP_005875Add
BLAST
Alternative sequencei136 – 238103Missing in isoform 2. CuratedVSP_005873Add
BLAST
Alternative sequencei209 – 22012Missing in isoform 4. 1 PublicationVSP_045840Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22253 mRNA. Translation: AAA35495.1.
L41887 Genomic DNA. Translation: AAA88098.1.
AB445102 mRNA. Translation: BAI99737.1.
AY166860 mRNA. Translation: AAN87842.1.
BT006745 mRNA. Translation: AAP35391.1.
AY513287 mRNA. Translation: AAT08040.1.
AK297161 mRNA. Translation: BAG59658.1.
AC074366 Genomic DNA. Translation: AAX93102.1.
CH471053 Genomic DNA. Translation: EAX00365.1.
CH471053 Genomic DNA. Translation: EAX00366.1.
BC000997 mRNA. Translation: AAH00997.1.
BC017369 mRNA. Translation: AAH17369.1.
BC017908 mRNA. Translation: AAH17908.1.
BC022328 mRNA. Translation: AAH22328.1.
CCDSiCCDS33183.1. [Q16629-1]
CCDS56115.1. [Q16629-4]
PIRiA57198.
RefSeqiNP_001026854.1. NM_001031684.2. [Q16629-1]
NP_001182375.1. NM_001195446.1. [Q16629-4]
UniGeneiHs.309090.

Genome annotation databases

EnsembliENST00000313117; ENSP00000325905; ENSG00000115875. [Q16629-1]
ENST00000431066; ENSP00000398159; ENSG00000115875. [Q16629-3]
ENST00000443213; ENSP00000402544; ENSG00000115875. [Q16629-3]
ENST00000446327; ENSP00000402264; ENSG00000115875. [Q16629-4]
GeneIDi6432.
KEGGihsa:6432.
UCSCiuc002rqz.3. human. [Q16629-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L22253 mRNA. Translation: AAA35495.1.
L41887 Genomic DNA. Translation: AAA88098.1.
AB445102 mRNA. Translation: BAI99737.1.
AY166860 mRNA. Translation: AAN87842.1.
BT006745 mRNA. Translation: AAP35391.1.
AY513287 mRNA. Translation: AAT08040.1.
AK297161 mRNA. Translation: BAG59658.1.
AC074366 Genomic DNA. Translation: AAX93102.1.
CH471053 Genomic DNA. Translation: EAX00365.1.
CH471053 Genomic DNA. Translation: EAX00366.1.
BC000997 mRNA. Translation: AAH00997.1.
BC017369 mRNA. Translation: AAH17369.1.
BC017908 mRNA. Translation: AAH17908.1.
BC022328 mRNA. Translation: AAH22328.1.
CCDSiCCDS33183.1. [Q16629-1]
CCDS56115.1. [Q16629-4]
PIRiA57198.
RefSeqiNP_001026854.1. NM_001031684.2. [Q16629-1]
NP_001182375.1. NM_001195446.1. [Q16629-4]
UniGeneiHs.309090.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HVZNMR-A12-98[»]
ProteinModelPortaliQ16629.
SMRiQ16629. Positions 12-98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112330. 108 interactions.
DIPiDIP-31790N.
IntActiQ16629. 33 interactions.
MINTiMINT-3032898.
STRINGi9606.ENSP00000325905.

PTM databases

iPTMnetiQ16629.
PhosphoSiteiQ16629.
SwissPalmiQ16629.

Polymorphism and mutation databases

BioMutaiSRSF7.
DMDMi3929380.

2D gel databases

SWISS-2DPAGEP99058.

Proteomic databases

EPDiQ16629.
MaxQBiQ16629.
PaxDbiQ16629.
PeptideAtlasiQ16629.
PRIDEiQ16629.
TopDownProteomicsiQ16629-1. [Q16629-1]
Q16629-2. [Q16629-2]
Q16629-3. [Q16629-3]
Q16629-4. [Q16629-4]

Protocols and materials databases

DNASUi6432.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313117; ENSP00000325905; ENSG00000115875. [Q16629-1]
ENST00000431066; ENSP00000398159; ENSG00000115875. [Q16629-3]
ENST00000443213; ENSP00000402544; ENSG00000115875. [Q16629-3]
ENST00000446327; ENSP00000402264; ENSG00000115875. [Q16629-4]
GeneIDi6432.
KEGGihsa:6432.
UCSCiuc002rqz.3. human. [Q16629-1]

Organism-specific databases

CTDi6432.
GeneCardsiSRSF7.
HGNCiHGNC:10789. SRSF7.
HPAiHPA043850.
HPA056926.
MIMi600572. gene.
neXtProtiNX_Q16629.
PharmGKBiPA35705.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0107. Eukaryota.
ENOG4111N8Y. LUCA.
GeneTreeiENSGT00700000104103.
HOGENOMiHOG000276234.
HOVERGENiHBG107480.
InParanoidiQ16629.
KOiK12896.
OMAiASPERMG.
OrthoDBiEOG73NG5V.
PhylomeDBiQ16629.
TreeFamiTF351858.

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.
SIGNORiQ16629.

Miscellaneous databases

ChiTaRSiSRSF7. human.
EvolutionaryTraceiQ16629.
GeneWikiiSFRS7.
GenomeRNAii6432.
PROiQ16629.
SOURCEiSearch...

Gene expression databases

BgeeiQ16629.
CleanExiHS_SFRS7.
ExpressionAtlasiQ16629. baseline and differential.
GenevisibleiQ16629. HS.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
4.10.60.10. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
SSF57756. SSF57756. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and cloning of the human splicing factor 9G8: a novel 35 kDa factor of the serine/arginine protein family."
    Cavaloc Y., Popielarz M., Fuchs J.-P., Gattoni R., Stevenin J.
    EMBO J. 13:2639-2649(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-24; 30-58 AND 79-87.
    Tissue: Placenta.
  2. "The gene encoding human splicing factor 9G8. Structure, chromosomal localization, and expression of alternatively processed transcripts."
    Popielarz M., Cavaloc Y., Mattei M.-G., Gattoni R., Stevenin J.
    J. Biol. Chem. 270:17830-17835(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    Tissue: Placenta.
  3. "Novel cis-active structures in the coding region mediate CRM1-dependent nuclear export of IFN-alpha 1 mRNA."
    Kimura T., Hashimoto I., Nishizawa M., Ito S., Yamada H.
    Med. Mol. Morphol. 43:145-157(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Guo J.H., Yu L.
    Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Identification of human aging-associated gene."
    Kim J.W.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Brain.
  8. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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].
    Tissue: Brain, Cervix, Prostate and Skin.
  11. "Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA."
    Huang Y., Steitz J.A.
    Mol. Cell 7:899-905(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION.
  12. Cited for: INTERACTION WITH CCNL1; CDC2L1 AND CDC2L2.
  13. "SR splicing factors serve as adapter proteins for TAP-dependent mRNA export."
    Huang Y., Gattoni R., Stevenin J., Steitz J.A.
    Mol. Cell 11:837-843(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA EXPORT, INTERACTION WITH NXF1.
  14. "Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved in pre-mRNA splicing and induces apoptosis of human hepatocellular carcinoma cells."
    Yang L., Li N., Wang C., Yu Y., Yuan L., Zhang M., Cao X.
    J. Biol. Chem. 279:11639-11648(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCNL2.
  15. "Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization."
    Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M.
    J. Biol. Chem. 279:35788-35797(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CPSF6.
  16. "Tau exon 10, whose missplicing causes frontotemporal dementia, is regulated by an intricate interplay of cis elements and trans factors."
    Wang J., Gao Q.S., Wang Y., Lafyatis R., Stamm S., Andreadis A.
    J. Neurochem. 88:1078-1090(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "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-231 AND SER-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-194 AND SER-196, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Mutually exclusive interactions drive handover of mRNA from export adaptors to TAP."
    Hautbergue G.M., Hung M.L., Golovanov A.P., Lian L.Y., Wilson S.A.
    Proc. Natl. Acad. Sci. U.S.A. 105:5154-5159(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MRNA EXPORT.
  20. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-194; SER-231 AND SER-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-163; SER-165 AND SER-167, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Molecular basis of RNA recognition and TAP binding by the SR proteins SRp20 and 9G8."
    Hargous Y., Hautbergue G.M., Tintaru A.M., Skrisovska L., Golovanov A.P., Stevenin J., Lian L.Y., Wilson S.A., Allain F.H.
    EMBO J. 25:5126-5137(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 12-98, RNA-BINDING, INTERACTION WITH NXF1, MUTAGENESIS OF 87-ARG-ARG-88 AND 97-ARG-ARG-98.

Entry informationi

Entry nameiSRSF7_HUMAN
AccessioniPrimary (citable) accession number: Q16629
Secondary accession number(s): B4DLU6, G5E9M3, Q564D3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 186 of the entry and version 1 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.