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Protein

Spliceosome-associated protein CWC15 homolog

Gene

CWC15

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

GO - Molecular functioni

  1. RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. mRNA splicing, via spliceosome Source: UniProtKB
  3. RNA splicing Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Spliceosome-associated protein CWC15 homolog
Gene namesi
Name:CWC15
Synonyms:C11orf5
ORF Names:AD-002, HSPC148
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:26939. CWC15.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. spliceosomal complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162383026.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 229228Spliceosome-associated protein CWC15 homologPRO_0000291543Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei18 – 181N6-acetyllysineBy similarity
Modified residuei110 – 1101Phosphothreonine3 Publications
Modified residuei121 – 1211Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9P013.
PaxDbiQ9P013.
PeptideAtlasiQ9P013.
PRIDEiQ9P013.

PTM databases

PhosphoSiteiQ9P013.

Expressioni

Gene expression databases

CleanExiHS_CWC15.
ExpressionAtlasiQ9P013. baseline and differential.
GenevestigatoriQ9P013.

Organism-specific databases

HPAiHPA039878.

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.1 Publication

Protein-protein interaction databases

BioGridi119575. 21 interactions.
IntActiQ9P013. 19 interactions.
MINTiMINT-3077614.
STRINGi9606.ENSP00000279839.

Structurei

3D structure databases

ProteinModelPortaliQ9P013.
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

eggNOGiNOG326120.
GeneTreeiENSGT00390000012084.
HOGENOMiHOG000214250.
HOVERGENiHBG107412.
InParanoidiQ9P013.
KOiK12863.
OMAiNCARSEP.
OrthoDBiEOG7FFMTR.
PhylomeDBiQ9P013.

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.

Q9P013-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTAARPTFE PARGGRGKGE GDLSQLSKQY SSRDLPSHTK IKYRQTTQDA
60 70 80 90 100
PEEVRNRDFR RELEERERAA AREKNRDRPT REHTTSSSVS KKPRLDQIPA
110 120 130 140 150
ANLDADDPLT DEEDEDFEEE SDDDDTAALL AELEKIKKER AEEQARKEQE
160 170 180 190 200
QKAEEERIRM ENILSGNPLL NLTGPSQPQA NFKVKRRWDD DVVFKNCAKG
210 220
VDDQKKDKRF VNDTLRSEFH KKFMEKYIK
Length:229
Mass (Da):26,624
Last modified:June 26, 2007 - v2
Checksum:iB21E6EEF46C4427C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti148 – 1481E → D in AAF29112 (PubMed:11042152).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250393 mRNA. Translation: CAB96541.1.
AF161497 mRNA. Translation: AAF29112.1.
AF110775 mRNA. Translation: AAF14858.1.
AK314900 mRNA. Translation: BAG37414.1.
BC006975 mRNA. Translation: AAH06975.1. Different termination.
BC032629 mRNA. Translation: AAH32629.1. Different termination.
BC040946 mRNA. Translation: AAH40946.1.
CCDSiCCDS73369.1.
RefSeqiNP_057487.2. NM_016403.3.
UniGeneiHs.503597.

Genome annotation databases

EnsembliENST00000279839; ENSP00000475615; ENSG00000150316.
GeneIDi51503.
KEGGihsa:51503.
UCSCiuc001pfd.4. human.

Polymorphism databases

DMDMi150438891.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ250393 mRNA. Translation: CAB96541.1.
AF161497 mRNA. Translation: AAF29112.1.
AF110775 mRNA. Translation: AAF14858.1.
AK314900 mRNA. Translation: BAG37414.1.
BC006975 mRNA. Translation: AAH06975.1. Different termination.
BC032629 mRNA. Translation: AAH32629.1. Different termination.
BC040946 mRNA. Translation: AAH40946.1.
CCDSiCCDS73369.1.
RefSeqiNP_057487.2. NM_016403.3.
UniGeneiHs.503597.

3D structure databases

ProteinModelPortaliQ9P013.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119575. 21 interactions.
IntActiQ9P013. 19 interactions.
MINTiMINT-3077614.
STRINGi9606.ENSP00000279839.

PTM databases

PhosphoSiteiQ9P013.

Polymorphism databases

DMDMi150438891.

Proteomic databases

MaxQBiQ9P013.
PaxDbiQ9P013.
PeptideAtlasiQ9P013.
PRIDEiQ9P013.

Protocols and materials databases

DNASUi51503.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000279839; ENSP00000475615; ENSG00000150316.
GeneIDi51503.
KEGGihsa:51503.
UCSCiuc001pfd.4. human.

Organism-specific databases

CTDi51503.
GeneCardsiGC11M094695.
H-InvDBHIX0010036.
HGNCiHGNC:26939. CWC15.
HPAiHPA039878.
neXtProtiNX_Q9P013.
PharmGKBiPA162383026.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG326120.
GeneTreeiENSGT00390000012084.
HOGENOMiHOG000214250.
HOVERGENiHBG107412.
InParanoidiQ9P013.
KOiK12863.
OMAiNCARSEP.
OrthoDBiEOG7FFMTR.
PhylomeDBiQ9P013.

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

GeneWikiiCWC15.
GenomeRNAii51503.
NextBioi55183.
PROiQ9P013.

Gene expression databases

CleanExiHS_CWC15.
ExpressionAtlasiQ9P013. baseline and differential.
GenevestigatoriQ9P013.

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. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Blood.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney, Liver and Testis.
  6. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
    Submitted (NOV-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 17-28; 45-55; 188-195 AND 210-216, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  7. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110 AND SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH CTNNBL1, FUNCTION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110 AND SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiCWC15_HUMAN
AccessioniPrimary (citable) accession number: Q9P013
Secondary accession number(s): B2RC17
, Q05BV9, Q05DM1, Q9UI29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: March 4, 2015
This is version 87 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

Caution

Has been termed C11orf5, but is not the official C11orf5 as defined by HGNC.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.