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Protein

Pre-mRNA-splicing factor CWC22 homolog

Gene

CWC22

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 and for exon-junction complex (EJC) assembly. Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay.3 Publications

GO - Molecular functioni

  • RNA binding Source: UniProtKB

GO - Biological processi

  • mRNA splicing, via spliceosome Source: UniProtKB
  • regulation of mRNA splicing, via spliceosome Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing factor CWC22 homolog
Alternative name(s):
Nucampholin homolog
fSAPb
Gene namesi
Name:CWC22
Synonyms:KIAA1604, NCM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:29322. CWC22.

Subcellular locationi

  • Nucleus
  • Nucleus speckle

  • Note: Concentrates around speckles, which are sites of pre-mRNA synthesis and processing, where it colocalizes with EJC core proteins.

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytoplasm Source: HPA
  • Golgi apparatus Source: HPA
  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: HPA
  • spliceosomal complex Source: UniProtKB
  • U2-type catalytic step 1 spliceosome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi168 – 1681G → Y: No effect on EIF4A3 incorporation into EJCs. 1 Publication
Mutagenesisi171 – 1744NKVN → AAVA: Loss of EIF4A3-binding.
Mutagenesisi171 – 1722NK → DE: Loss of EIF4A3-binding. 1 Publication
Mutagenesisi331 – 3311R → A: Decreased EIF4A3-binding; when associated with A-334. 1 Publication
Mutagenesisi334 – 3341Y → A: Decreased EIF4A3-binding; when associated with A-331. 1 Publication

Organism-specific databases

PharmGKBiPA164718415.

Polymorphism and mutation databases

BioMutaiCWC22.
DMDMi296439380.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 908908Pre-mRNA-splicing factor CWC22 homologPRO_0000302005Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391PhosphoserineCombined sources
Modified residuei61 – 611PhosphoserineCombined sources
Modified residuei107 – 1071PhosphoserineBy similarity
Modified residuei786 – 7861PhosphoserineCombined sources
Modified residuei829 – 8291PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9HCG8.
MaxQBiQ9HCG8.
PaxDbiQ9HCG8.
PeptideAtlasiQ9HCG8.
PRIDEiQ9HCG8.

PTM databases

iPTMnetiQ9HCG8.
PhosphoSiteiQ9HCG8.

Expressioni

Gene expression databases

BgeeiQ9HCG8.
ExpressionAtlasiQ9HCG8. baseline and differential.
GenevisibleiQ9HCG8. HS.

Organism-specific databases

HPAiHPA036748.
HPA036749.

Interactioni

Subunit structurei

Component of the spliceosome C complex. Interacts with EIF4A3 and PRPF19 in an RNA-independent manner. Direct interaction with EIF4A3 is mediated by the MIF4G domain. Full interaction with EIF4A3 occurs only when EIF4A3 is not part of the EJC and prevents EIF4A3 binding to RNA.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF4A3P389193EBI-373289,EBI-299104
FAM32AQ9Y4212EBI-373289,EBI-726146
FRG1Q143312EBI-373289,EBI-2515248

Protein-protein interaction databases

BioGridi121727. 33 interactions.
DIPiDIP-31268N.
IntActiQ9HCG8. 11 interactions.
MINTiMINT-3070547.
STRINGi9606.ENSP00000387006.

Structurei

Secondary structure

1
908
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi136 – 1405Combined sources
Helixi150 – 17223Combined sources
Turni175 – 1773Combined sources
Helixi178 – 1869Combined sources
Turni190 – 1934Combined sources
Helixi194 – 20714Combined sources
Helixi209 – 2113Combined sources
Helixi212 – 22514Combined sources
Helixi227 – 24721Combined sources
Helixi250 – 26516Combined sources
Helixi272 – 28312Combined sources
Helixi287 – 30721Combined sources
Helixi309 – 32416Combined sources
Helixi330 – 34415Combined sources
Helixi362 – 3643Combined sources
Beta strandi372 – 3743Combined sources
Helixi380 – 3834Combined sources
Helixi391 – 40515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C9BX-ray2.00B116-406[»]
ProteinModelPortaliQ9HCG8.
SMRiQ9HCG8. Positions 123-406.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini163 – 346184MIF4GPROSITE-ProRule annotationAdd
BLAST
Domaini454 – 570117MIPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi16 – 9782Arg-richAdd
BLAST
Compositional biasi116 – 1194Poly-Lys
Compositional biasi423 – 43816Poly-GluAdd
BLAST
Compositional biasi666 – 71348Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the CWC22 family.Curated
Contains 1 MI domain.PROSITE-ProRule annotation
Contains 1 MIF4G domain.Curated

Phylogenomic databases

eggNOGiKOG2140. Eukaryota.
ENOG410XNP2. LUCA.
GeneTreeiENSGT00650000093379.
InParanoidiQ9HCG8.
KOiK13100.
OMAiDVEPNKS.
OrthoDBiEOG7GFB4M.
PhylomeDBiQ9HCG8.
TreeFamiTF300510.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PfamiPF02847. MA3. 1 hit.
[Graphical view]
SMARTiSM00544. MA3. 1 hit.
SM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51366. MI. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9HCG8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSSVAQIKP SSGHDRRENL NSYQRNSSPE DRYEEQERSP RDRDYFDYSR
60 70 80 90 100
SDYEHSRRGR SYDSSMESRN RDREKRRERE RDTDRKRSRK SPSPGRRNPE
110 120 130 140 150
TSVTQSSSAQ DEPATKKKKD ELDPLLTRTG GAYIPPAKLR MMQEQITDKN
160 170 180 190 200
SLAYQRMSWE ALKKSINGLI NKVNISNISI IIQELLQENI VRGRGLLSRS
210 220 230 240 250
VLQAQSASPI FTHVYAALVA IINSKFPQIG ELILKRLILN FRKGYRRNDK
260 270 280 290 300
QLCLTASKFV AHLINQNVAH EVLCLEMLTL LLERPTDDSV EVAIGFLKEC
310 320 330 340 350
GLKLTQVSPR GINAIFERLR NILHESEIDK RVQYMIEVMF AVRKDGFKDH
360 370 380 390 400
PIILEGLDLV EEDDQFTHML PLEDDYNPED VLNVFKMDPN FMENEEKYKA
410 420 430 440 450
IKKEILDEGD TDSNTDQDAG SSEEDEEEEE EEGEEDEEGQ KVTIHDKTEI
460 470 480 490 500
NLVSFRRTIY LAIQSSLDFE ECAHKLLKME FPESQTKELC NMILDCCAQQ
510 520 530 540 550
RTYEKFFGLL AGRFCMLKKE YMESFEGIFK EQYDTIHRLE TNKLRNVAKM
560 570 580 590 600
FAHLLYTDSL PWSVLECIKL SEETTTSSSR IFVKIFFQEL CEYMGLPKLN
610 620 630 640 650
ARLKDETLQP FFEGLLPRDN PRNTRFAINF FTSIGLGGLT DELREHLKNT
660 670 680 690 700
PKVIVAQKPD VEQNKSSPSS SSSASSSSES DSSDSDSDSS DSSSESSSEE
710 720 730 740 750
SDSSSISSHS SASANDVRKK GHGKTRSKEV DKLIRNQQTN DRKQKERRQE
760 770 780 790 800
HGHQETRTER ERRSEKHRDQ NSSGSNWRDP ITKYTSDKDV PSERNNYSRV
810 820 830 840 850
ANDRDQEMHI DLENKHGDPK KKRGERRNSF SENEKHTHRI KDSENFRRKD
860 870 880 890 900
RSKSKEMNRK HSGSRSDEDR YQNGAERRWE KSSRYSEQSR ESKKNQDRRR

EKSPAKQK
Length:908
Mass (Da):105,466
Last modified:May 18, 2010 - v3
Checksum:i00EF9B361B5F55AB
GO

Sequence cautioni

The sequence AAH16651.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH31216.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAH57826.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAB13430.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAB15197.1 differs from that shown. Reason: Frameshift at position 555. Curated
The sequence BAB15612.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti270 – 2701H → Y in BAB15197 (PubMed:14702039).Curated
Sequence conflicti550 – 5501M → V in BAB15197 (PubMed:14702039).Curated
Sequence conflicti613 – 6131E → G in AAH31216 (PubMed:15489334).Curated
Sequence conflicti685 – 6851S → F in AAH16651 (PubMed:15489334).Curated
Sequence conflicti701 – 7011S → G in AAH31216 (PubMed:15489334).Curated
Sequence conflicti742 – 7421R → K in AAH31216 (PubMed:15489334).Curated
Sequence conflicti773 – 7731S → R in BAB15612 (PubMed:14702039).Curated
Sequence conflicti773 – 7731S → R in AAH53573 (PubMed:15489334).Curated
Sequence conflicti773 – 7731S → R in AAH93952 (PubMed:15489334).Curated
Sequence conflicti773 – 7731S → R in AAH93954 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti656 – 6561A → V.
Corresponds to variant rs17778270 [ dbSNP | Ensembl ].
VAR_057513
Natural varianti741 – 7411D → V.
Corresponds to variant rs11903115 [ dbSNP | Ensembl ].
VAR_057514
Natural varianti794 – 7941R → Q.
Corresponds to variant rs1046356 [ dbSNP | Ensembl ].
VAR_057515

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB046824 mRNA. Translation: BAB13430.1. Different initiation.
AK025635 mRNA. Translation: BAB15197.1. Frameshift.
AK026978 mRNA. Translation: BAB15612.1. Different initiation.
AC068194 Genomic DNA. No translation available.
AC096587 Genomic DNA. No translation available.
BC016651 mRNA. Translation: AAH16651.1. Sequence problems.
BC031216 mRNA. Translation: AAH31216.1. Sequence problems.
BC053573 mRNA. Translation: AAH53573.1.
BC057826 mRNA. Translation: AAH57826.1. Sequence problems.
BC093952 mRNA. Translation: AAH93952.1.
BC093954 mRNA. Translation: AAH93954.1.
CCDSiCCDS46465.1.
RefSeqiNP_065994.1. NM_020943.2.
XP_005246783.1. XM_005246726.1.
UniGeneiHs.311363.

Genome annotation databases

EnsembliENST00000410053; ENSP00000387006; ENSG00000163510.
GeneIDi57703.
KEGGihsa:57703.
UCSCiuc010frh.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB046824 mRNA. Translation: BAB13430.1. Different initiation.
AK025635 mRNA. Translation: BAB15197.1. Frameshift.
AK026978 mRNA. Translation: BAB15612.1. Different initiation.
AC068194 Genomic DNA. No translation available.
AC096587 Genomic DNA. No translation available.
BC016651 mRNA. Translation: AAH16651.1. Sequence problems.
BC031216 mRNA. Translation: AAH31216.1. Sequence problems.
BC053573 mRNA. Translation: AAH53573.1.
BC057826 mRNA. Translation: AAH57826.1. Sequence problems.
BC093952 mRNA. Translation: AAH93952.1.
BC093954 mRNA. Translation: AAH93954.1.
CCDSiCCDS46465.1.
RefSeqiNP_065994.1. NM_020943.2.
XP_005246783.1. XM_005246726.1.
UniGeneiHs.311363.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4C9BX-ray2.00B116-406[»]
ProteinModelPortaliQ9HCG8.
SMRiQ9HCG8. Positions 123-406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121727. 33 interactions.
DIPiDIP-31268N.
IntActiQ9HCG8. 11 interactions.
MINTiMINT-3070547.
STRINGi9606.ENSP00000387006.

PTM databases

iPTMnetiQ9HCG8.
PhosphoSiteiQ9HCG8.

Polymorphism and mutation databases

BioMutaiCWC22.
DMDMi296439380.

Proteomic databases

EPDiQ9HCG8.
MaxQBiQ9HCG8.
PaxDbiQ9HCG8.
PeptideAtlasiQ9HCG8.
PRIDEiQ9HCG8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000410053; ENSP00000387006; ENSG00000163510.
GeneIDi57703.
KEGGihsa:57703.
UCSCiuc010frh.2. human.

Organism-specific databases

CTDi57703.
GeneCardsiCWC22.
H-InvDBHIX0022794.
HGNCiHGNC:29322. CWC22.
HPAiHPA036748.
HPA036749.
MIMi615186. gene.
neXtProtiNX_Q9HCG8.
PharmGKBiPA164718415.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2140. Eukaryota.
ENOG410XNP2. LUCA.
GeneTreeiENSGT00650000093379.
InParanoidiQ9HCG8.
KOiK13100.
OMAiDVEPNKS.
OrthoDBiEOG7GFB4M.
PhylomeDBiQ9HCG8.
TreeFamiTF300510.

Miscellaneous databases

ChiTaRSiCWC22. human.
GenomeRNAii57703.
PROiQ9HCG8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HCG8.
ExpressionAtlasiQ9HCG8. baseline and differential.
GenevisibleiQ9HCG8. HS.

Family and domain databases

Gene3Di1.25.40.180. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR003891. Initiation_fac_eIF4g_MI.
IPR016021. MIF4-like.
IPR003890. MIF4G-like_typ-3.
[Graphical view]
PfamiPF02847. MA3. 1 hit.
[Graphical view]
SMARTiSM00544. MA3. 1 hit.
SM00543. MIF4G. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS51366. MI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
    DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  2. "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].
    Tissue: Hepatoma.
  3. "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].
  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].
    Tissue: Brain, Eye, Lymph, Placenta and Testis.
  5. "Comprehensive proteomic analysis of the human spliceosome."
    Zhou Z., Licklider L.J., Gygi S.P., Reed R.
    Nature 419:182-185(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN SPLICEOSOME C COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-829, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "CWC22 connects pre-mRNA splicing and exon junction complex assembly."
    Steckelberg A.L., Boehm V., Gromadzka A.M., Gehring N.H.
    Cell Rep. 2:454-461(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EIF4A3, MUTAGENESIS OF 171-ASN-LYS-172.
  13. "Human CWC22 escorts the helicase eIF4AIII to spliceosomes and promotes exon junction complex assembly."
    Barbosa I., Haque N., Fiorini F., Barrandon C., Tomasetto C., Blanchette M., Le Hir H.
    Nat. Struct. Mol. Biol. 19:983-990(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EIF4A3, IDENTIFICATION IN SPLICEOSOME C COMPLEX, SUBCELLULAR LOCATION.
  14. "Human spliceosomal protein CWC22 plays a role in coupling splicing to exon junction complex deposition and nonsense-mediated decay."
    Alexandrov A., Colognori D., Shu M.D., Steitz J.A.
    Proc. Natl. Acad. Sci. U.S.A. 109:21313-21318(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EIF4A3, MUTAGENESIS OF GLY-168; ARG-331 AND TYR-334.
  15. "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-39 AND SER-786, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.

Entry informationi

Entry nameiCWC22_HUMAN
AccessioniPrimary (citable) accession number: Q9HCG8
Secondary accession number(s): Q05DC2
, Q4G135, Q52LF0, Q6PEX2, Q7Z6I0, Q9H5L3, Q9H6Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 18, 2010
Last modified: July 6, 2016
This is version 110 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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.