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Protein
Submitted name:

Splicing factor arginine/serine-rich 3

Gene

SFRS3

Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Submitted name:
Splicing factor arginine/serine-rich 3Imported
Submitted name:
Splicing factor, arginine/serine-rich 3, isoform CRA_dImported
Submitted name:
cDNA, FLJ92926, Homo sapiens splicing factor, arginine/serine-rich 3 (SFRS3), mRNAImported
Gene namesi
Name:SFRS3Imported
ORF Names:hCG_14802Imported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35701.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000362820.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini10 – 8374RRM (RNA recognition motif)InterPro annotationAdd
BLAST

Phylogenomic databases

eggNOGiKOG0107. Eukaryota.
ENOG4111N8Y. LUCA.
HOGENOMiHOG000276234.
HOVERGENiHBG107480.
KOiK12892.
OMAiDSIMHRD.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

B2R6F3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHRDSCPLDC KVYVGNLGNN GNKTELERAF GYYGPLRSVW VARNPPGFAF
60 70 80 90 100
VEFEDPRDAA DAVRELDGRT LCGCRVRVEL SNGEKRSRNR GPPPSWGRRP
110 120 130 140 150
RDDYRRRSPP PRRRSPRRRS FSRSRSRSLS RDRRRERSLS RERNHKPSRS
160
FSRSRSRSRS NERK
Length:164
Mass (Da):19,330
Last modified:July 1, 2008 - v1
Checksum:i02F0A5EE33FF28A0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei164 – 1641Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK312553 mRNA. Translation: BAG35450.1.
AB451229 mRNA. Translation: BAG70043.1.
AB451352 mRNA. Translation: BAG70166.1.
CH471081 Genomic DNA. Translation: EAX03901.1.
CH471081 Genomic DNA. Translation: EAX03903.1.
RefSeqiNP_003008.1. NM_003017.4.
UniGeneiHs.405144.

Genome annotation databases

GeneIDi6428.
KEGGihsa:6428.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK312553 mRNA. Translation: BAG35450.1.
AB451229 mRNA. Translation: BAG70043.1.
AB451352 mRNA. Translation: BAG70166.1.
CH471081 Genomic DNA. Translation: EAX03901.1.
CH471081 Genomic DNA. Translation: EAX03903.1.
RefSeqiNP_003008.1. NM_003017.4.
UniGeneiHs.405144.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000362820.

Protocols and materials databases

DNASUi6428.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi6428.
KEGGihsa:6428.

Organism-specific databases

CTDi6428.
PharmGKBiPA35701.

Phylogenomic databases

eggNOGiKOG0107. Eukaryota.
ENOG4111N8Y. LUCA.
HOGENOMiHOG000276234.
HOVERGENiHBG107480.
KOiK12892.
OMAiDSIMHRD.

Miscellaneous databases

GenomeRNAii6428.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of the human genome."
    Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.
    , Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.
    Science 291:1304-1351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE.
  3. "NEDO functional analysis of protein and research application project."
    Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., Isogai T.
    Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: TongueImported.
  4. "Human Protein Factory: an infrastructure to convert the human transcriptome into the in vitro-expressed human proteome of versatile utility."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J.-I., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K.-I., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J.-I., Watanabe S., Nomura N.
    Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiB2R6F3_HUMAN
AccessioniPrimary (citable) accession number: B2R6F3
Entry historyi
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: June 8, 2016
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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.

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.