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Protein

Spliceosome-associated protein CWC15 homolog

Gene

Cwc15

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Spliceosome-associated protein CWC15 homolog
Alternative name(s):
Embryonic development factor 1
Short name:
mED1
Gene namesi
Name:Cwc15
Synonyms:Ed1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1913320. Cwc15.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 229228Spliceosome-associated protein CWC15 homologPRO_0000291544Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei18 – 181N6-acetyllysineCombined sources
Modified residuei110 – 1101PhosphothreonineCombined sources
Modified residuei121 – 1211PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9JHS9.
MaxQBiQ9JHS9.
PaxDbiQ9JHS9.
PRIDEiQ9JHS9.

PTM databases

iPTMnetiQ9JHS9.
PhosphoSiteiQ9JHS9.

Expressioni

Gene expression databases

BgeeiQ9JHS9.
CleanExiMM_CWC15.
GenevisibleiQ9JHS9. MM.

Interactioni

Subunit structurei

Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts directly with CTNNBL1 in the complex (By similarity).By similarity

Protein-protein interaction databases

IntActiQ9JHS9. 2 interactions.
MINTiMINT-4129699.
STRINGi10090.ENSMUSP00000004200.

Structurei

3D structure databases

ProteinModelPortaliQ9JHS9.
SMRiQ9JHS9. Positions 141-228.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili123 – 16543Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the CWC15 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG3228. Eukaryota.
ENOG410Z258. LUCA.
GeneTreeiENSGT00390000012084.
HOGENOMiHOG000214250.
HOVERGENiHBG107412.
InParanoidiQ9JHS9.
KOiK12863.
OMAiIKYRQPT.
OrthoDBiEOG7FFMTR.
PhylomeDBiQ9JHS9.
TreeFamiTF321323.

Family and domain databases

InterProiIPR006973. Cwf_Cwc_15.
[Graphical view]
PANTHERiPTHR12718. PTHR12718. 1 hit.
PfamiPF04889. Cwf_Cwc_15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9JHS9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTAARPTFE PARGGRGKGE GDLSQLSKQY SSRDLPSHTK IKYRQTTQDA
60 70 80 90 100
PEEVRNRDFR RELEERERAA ARDKNRDRPT REHTTSSSVS KKPRLDQIPA
110 120 130 140 150
ANLDADDPLT DEEDEDFEEE SDDDDTAALL AELEKIKKER AEEQARKEQE
160 170 180 190 200
QKAEEERIRM ENILSGNPLL NLTGPSQPQA NFKVKRRWDD DVVFKNCAKG
210 220
IDDQKKDKRF VNDTLRSEFH KKFMEKYIK
Length:229
Mass (Da):26,624
Last modified:October 1, 2000 - v1
Checksum:iA8AE6F44423EA7DC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti223 – 2231F → L in BAE40300 (PubMed:16141072).Curated
Sequence conflicti223 – 2231F → L in BAE39808 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250394 mRNA. Translation: CAB96547.1.
AY842452 mRNA. Translation: AAW32096.1.
AK002864 mRNA. Translation: BAB22414.1.
AK003202 mRNA. Translation: BAB22638.1.
AK003591 mRNA. Translation: BAB22880.1.
AK003834 mRNA. Translation: BAB23026.1.
AK145249 mRNA. Translation: BAE26327.1.
AK167776 mRNA. Translation: BAE39808.1.
AK168365 mRNA. Translation: BAE40300.1.
BC004726 mRNA. Translation: AAH04726.1.
CCDSiCCDS22823.1.
RefSeqiNP_075642.1. NM_023153.3.
XP_006510600.1. XM_006510537.2.
UniGeneiMm.245938.

Genome annotation databases

EnsembliENSMUST00000004200; ENSMUSP00000004200; ENSMUSG00000004096.
GeneIDi66070.
KEGGimmu:66070.
UCSCiuc009oeo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250394 mRNA. Translation: CAB96547.1.
AY842452 mRNA. Translation: AAW32096.1.
AK002864 mRNA. Translation: BAB22414.1.
AK003202 mRNA. Translation: BAB22638.1.
AK003591 mRNA. Translation: BAB22880.1.
AK003834 mRNA. Translation: BAB23026.1.
AK145249 mRNA. Translation: BAE26327.1.
AK167776 mRNA. Translation: BAE39808.1.
AK168365 mRNA. Translation: BAE40300.1.
BC004726 mRNA. Translation: AAH04726.1.
CCDSiCCDS22823.1.
RefSeqiNP_075642.1. NM_023153.3.
XP_006510600.1. XM_006510537.2.
UniGeneiMm.245938.

3D structure databases

ProteinModelPortaliQ9JHS9.
SMRiQ9JHS9. Positions 141-228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JHS9. 2 interactions.
MINTiMINT-4129699.
STRINGi10090.ENSMUSP00000004200.

PTM databases

iPTMnetiQ9JHS9.
PhosphoSiteiQ9JHS9.

Proteomic databases

EPDiQ9JHS9.
MaxQBiQ9JHS9.
PaxDbiQ9JHS9.
PRIDEiQ9JHS9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000004200; ENSMUSP00000004200; ENSMUSG00000004096.
GeneIDi66070.
KEGGimmu:66070.
UCSCiuc009oeo.1. mouse.

Organism-specific databases

CTDi51503.
MGIiMGI:1913320. Cwc15.

Phylogenomic databases

eggNOGiKOG3228. Eukaryota.
ENOG410Z258. LUCA.
GeneTreeiENSGT00390000012084.
HOGENOMiHOG000214250.
HOVERGENiHBG107412.
InParanoidiQ9JHS9.
KOiK12863.
OMAiIKYRQPT.
OrthoDBiEOG7FFMTR.
PhylomeDBiQ9JHS9.
TreeFamiTF321323.

Enzyme and pathway databases

ReactomeiR-MMU-72163. mRNA Splicing - Major Pathway.

Miscellaneous databases

PROiQ9JHS9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JHS9.
CleanExiMM_CWC15.
GenevisibleiQ9JHS9. MM.

Family and domain databases

InterProiIPR006973. Cwf_Cwc_15.
[Graphical view]
PANTHERiPTHR12718. PTHR12718. 1 hit.
PfamiPF04889. Cwf_Cwc_15. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "mED1 (mouse embryonic development factor 1)."
    Duan J.-Z., Zhang J.-P.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: KM.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ and C57BL/6J.
    Tissue: Kidney and Mammary gland.
  4. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiCWC15_MOUSE
AccessioniPrimary (citable) accession number: Q9JHS9
Secondary accession number(s): Q3TH98, Q9CTH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.