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Q99459 (CDC5L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell division cycle 5-like protein

Short name=Cdc5-like protein
Alternative name(s):
Pombe cdc5-related protein
Gene names
Name:CDC5L
Synonyms:KIAA0432, PCDC5RP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length802 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA-binding protein involved in cell cycle control. May act as a transcription activator. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. Ref.1 Ref.3 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.20

Subunit structure

Homodimer. Interacts with DAPK3 By similarity. Binds DNA. Binds to adeno-pre-mRNA in an ATP-stimulated manner. Belongs to the spliceosome complex. Part of a spliceosomal 'core' complex consisting of CDC5L, PLRG1, SPF27, CCAP1, CCAP3 and CCAP6. Interacts with PLRG1, Lodestar/TTF2, and NIPP1/PPP1R8. Identified in the spliceosome C complex. 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 (via its C-terminus) directly in the complex with PRPF19 and BCAS2. Interacts (via its C-terminus) directly with PRGL1 (via its WD40 repeat domain); the interaction is required for mRNA splicing but not for spliceosome assembly. Also interacts with CTNNBL1. Ref.10 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20 Ref.22 Ref.26 Ref.29

Subcellular location

Nucleus. Nucleus speckle. Cytoplasm. Note: May shuttle between cytoplasm and nucleus. Ref.1 Ref.2 Ref.10 Ref.11 Ref.13 Ref.16 Ref.20 Ref.26

Tissue specificity

Ubiquitously expressed in both fetal and adult tissues. Ref.1 Ref.2 Ref.3

Post-translational modification

Phosphorylated on serine and threonine residues. Phosphorylation on Thr-411 and Thr-438 is required for CDC5L-mediated mRNA splicing. Has no effect on subcellular location nor on homodimerization. Phosphorylated in vitro by CDK2. Phosphorylation enhances interaction with PPP1R8. Ref.1 Ref.10 Ref.20

Involvement in disease

A chromosomal aberration involving CDC5L is found in multicystic renal dysplasia. Translocation t(6;19)(p21;q13.1) with USF2.

Sequence similarities

Belongs to the CEF1 family.

Contains 2 HTH myb-type DNA-binding domains.

Sequence caution

The sequence BAA24862.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCell cycle
mRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DomainCoiled coil
Repeat
   LigandDNA-binding
RNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

mRNA splicing, via spliceosome

Inferred by curator Ref.17. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPrp19 complex

Inferred from direct assay Ref.26. Source: UniProtKB

catalytic step 2 spliceosome

Inferred from direct assay Ref.17. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear speck

Inferred from direct assay PubMed 16332694. Source: BHF-UCL

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.26. Source: UniProtKB

   Molecular_functionDNA binding

Non-traceable author statement Ref.9. Source: UniProtKB

WD40-repeat domain binding

Inferred from direct assay Ref.26. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.22Ref.26. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 802802Cell division cycle 5-like protein
PRO_0000197091

Regions

Domain1 – 5656HTH myb-type 1
Domain57 – 10852HTH myb-type 2
DNA binding31 – 5424H-T-H motif By similarity
DNA binding82 – 10423H-T-H motif By similarity
Region165 – 271107Nuclear localization signal Potential
Region200 – 2067Required for interaction with CTNNBL1 By similarity
Region260 – 606347Interaction with PPP1R8
Region501 – 659159Interaction with DAPK3 By similarity
Region706 – 80095Interaction with PLRG1
Coiled coil142 – 245104 Potential
Coiled coil676 – 70126 Potential
Coiled coil764 – 80239 Potential

Sites

Site4141Breakpoint for translocation

Amino acid modifications

Modified residue2271Phosphothreonine Ref.20 Ref.23
Modified residue3031Phosphoserine Ref.19 Ref.20 Ref.27
Modified residue3581Phosphoserine Ref.20
Modified residue3771Phosphothreonine Ref.23 Ref.27 Ref.30
Modified residue3851Phosphothreonine Ref.20 Ref.21 Ref.23 Ref.25 Ref.30
Modified residue3961Phosphothreonine Ref.21 Ref.23 Ref.25 Ref.27 Ref.30
Modified residue4041Phosphothreonine Ref.20
Modified residue4111Phosphothreonine Ref.20
Modified residue4151Phosphothreonine Ref.23
Modified residue4171Phosphoserine Ref.20
Modified residue4241Phosphothreonine Ref.20 Ref.23
Modified residue4301Phosphothreonine Ref.23
Modified residue4371Phosphoserine Ref.23
Modified residue4381Phosphothreonine Ref.20 Ref.23
Modified residue4421Phosphothreonine Ref.23

Natural variations

Natural variant4591Y → C.
Corresponds to variant rs11572006 [ dbSNP | Ensembl ].
VAR_050181

Experimental info

Mutagenesis311W → G: Abolishes DNA-binding; when associated with G-53 and G-82. Ref.15
Mutagenesis531W → G: Abolishes DNA-binding; when associated with G-31 and G-82. Ref.15
Mutagenesis821W → G: Abolishes DNA-binding; when associated with G-31 and G-53. Ref.15
Mutagenesis2271T → A: Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-303; A-358; A-385; A-404; A-411; A-417; A-424 and A-438.
Mutagenesis3031S → A: Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-358; A-385; A-404; A-411; A-417; A-424 and A-438.
Mutagenesis3581S → A: Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-385; A-404; A-411; A-417; A-424 and A-438.
Mutagenesis4041T → A: Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-411; A-417; A-424 and A-438.
Mutagenesis4111T → A: Abolishes phosphorylation. Markedly diminished pre-mRNA splicing activity; when associated with A-438. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-404; A-417; A-424 and A-438. Ref.20
Mutagenesis4171S → A: Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-404; A-411; A-424 and A-438.
Mutagenesis4241T → A: Abolishes phosphorylation. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-404; A-411; A-417 and A-438.
Mutagenesis4381T → A: Abolishes phosphorylation. Markedly diminished pre-mRNA splicing activity; when associated with A-411. No effect on homodimerization nor on nuclear localization; when associated with A-227; A-303; A-358; A-385; A-404; A-411; A-417 and A-424. Ref.20
Sequence conflict121R → K in BAA20885. Ref.9

Secondary structure

............... 802
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q99459 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: 3390F91EE7E79DA6

FASTA80292,251
        10         20         30         40         50         60 
MPRIMIKGGV WRNTEDEILK AAVMKYGKNQ WSRIASLLHR KSAKQCKARW YEWLDPSIKK 

        70         80         90        100        110        120 
TEWSREEEEK LLHLAKLMPT QWRTIAPIIG RTAAQCLEHY EFLLDKAAQR DNEEETTDDP 

       130        140        150        160        170        180 
RKLKPGEIDP NPETKPARPD PIDMDEDELE MLSEARARLA NTQGKKAKRK AREKQLEEAR 

       190        200        210        220        230        240 
RLAALQKRRE LRAAGIEIQK KRKRKRGVDY NAEIPFEKKP ALGFYDTSEE NYQALDADFR 

       250        260        270        280        290        300 
KLRQQDLDGE LRSEKEGRDR KKDKQHLKRK KESDLPSAIL QTSGVSEFTK KRSKLVLPAP 

       310        320        330        340        350        360 
QISDAELQEV VKVGQASEIA RQTAEESGIT NSASSTLLSE YNVTNNSVAL RTPRTPASQD 

       370        380        390        400        410        420 
RILQEAQNLM ALTNVDTPLK GGLNTPLHES DFSGVTPQRQ VVQTPNTVLS TPFRTPSNGA 

       430        440        450        460        470        480 
EGLTPRSGTT PKPVINSTPG RTPLRDKLNI NPEDGMADYS DPSYVKQMER ESREHLRLGL 

       490        500        510        520        530        540 
LGLPAPKNDF EIVLPENAEK ELEEREIDDT YIEDAADVDA RKQAIRDAER VKEMKRMHKA 

       550        560        570        580        590        600 
VQKDLPRPSE VNETILRPLN VEPPLTDLQK SEELIKKEMI TMLHYDLLHH PYEPSGNKKG 

       610        620        630        640        650        660 
KTVGFGTNNS EHITYLEHNP YEKFSKEELK KAQDVLVQEM EVVKQGMSHG ELSSEAYNQV 

       670        680        690        700        710        720 
WEECYSQVLY LPGQSRYTRA NLASKKDRIE SLEKRLEINR GHMTTEAKRA AKMEKKMKIL 

       730        740        750        760        770        780 
LGGYQSRAMG LMKQLNDLWD QIEQAHLELR TFEELKKHED SAIPRRLECL KEDVQRQQER 

       790        800 
EKELQHRYAD LLLEKETLKS KF 

« Hide

References

« Hide 'large scale' references
[1]"Pombe Cdc5-related protein. A putative human transcription factor implicated in mitogen-activated signaling."
Bernstein H.S., Coughlin S.R.
J. Biol. Chem. 272:5833-5837(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION, FUNCTION.
Tissue: Epithelium.
[2]"Rearrangement of the human CDC5L gene by a t(6;19)(p21;q13.1) in a patient with multicystic renal dysplasia."
Groenen P.M.A., Vanderlinden G., Devriendt K., Fryns J.-P., Van de Ven W.J.M.
Genomics 49:218-229(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH USF2, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
Tissue: Fetal kidney.
[3]"Myb-related Schizosaccharomyces pombe cdc5p is structurally and functionally conserved in eukaryotes."
Ohi R., Feoktistova A., McCann S., Valentine V., Look A.T., Lipsick J.S., Gould K.L.
Mol. Cell. Biol. 18:4097-4108(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION.
Tissue: Vascular endothelial cell.
[4]"Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[6]NIEHS SNPs program
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: Placenta.
[9]"A cdc5+ homolog of a higher plant, Arabidopsis thaliana."
Hirayama T., Shinozaki K.
Proc. Natl. Acad. Sci. U.S.A. 93:13371-13376(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-162.
[10]"NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry."
Boudrez A., Beullens M., Groenen P.M.A., Van Eynde A., Vulsteke V., Jagiello I., Murray M., Krainer A.R., Stalmans W., Bollen M.
J. Biol. Chem. 275:25411-25417(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 259-614, INTERACTION WITH PPP1R8, SUBCELLULAR LOCATION, PHOSPHORYLATION.
Tissue: Epithelium.
[11]"A mammalian homolog of fission yeast Cdc5 regulates G2 progression and mitotic entry."
Bernstein H.S., Coughlin S.R.
J. Biol. Chem. 273:4666-4671(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]"Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex."
Neubauer G., King A., Rappsilber J., Calvio C., Watson M., Ajuh P., Sleeman J., Lamond A.I., Mann M.
Nat. Genet. 20:46-50(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY AS PART OF THE SPLICEOSOME.
[13]"Evidence that Myb-related CDC5 proteins are required for pre-mRNA splicing."
Burns C.G., Ohi R., Krainer A.R., Gould K.L.
Proc. Natl. Acad. Sci. U.S.A. 96:13789-13794(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[14]"Functional analysis of the human CDC5L complex and identification of its components by mass spectrometry."
Ajuh P., Kuster B., Panov K., Zomerdijk J.C.B.M., Mann M., Lamond A.I.
EMBO J. 19:6569-6581(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: RNA-BINDING, FUNCTION.
[15]"Human Cdc5, a regulator of mitotic entry, can act as a site-specific DNA binding protein."
Lei X.-H., Shen X., Xu X.-Q., Bernstein H.S.
J. Cell Sci. 113:4523-4531(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: DNA-BINDING, SUBUNIT, MUTAGENESIS OF TRP-31; TRP-53 AND TRP-82, FUNCTION.
[16]"A direct interaction between the carboxyl-terminal region of CDC5L and the WD40 domain of PLRG1 is essential for pre-mRNA splicing."
Ajuh P., Sleeman J., Chusainow J., Lamond A.I.
J. Biol. Chem. 276:42370-42381(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PLRG1, SUBCELLULAR LOCATION.
[17]"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 BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[18]"hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing."
Leonard D., Ajuh P., Lamond A.I., Legerski R.J.
Biochem. Biophys. Res. Commun. 308:793-801(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TTF2, IDENTIFICATION BY MASS SPECTROMETRY.
[19]"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-303, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Cell cycle-dependent phosphorylation of human CDC5 regulates RNA processing."
Graub R., Lancero H., Pedersen A., Chu M., Padmanabhan K., Xu X.Q., Spitz P., Chalkley R., Burlingame A.L., Stokoe D., Bernstein H.S.
Cell Cycle 7:1795-1803(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION, FUNCTION, PHOSPHORYLATION AT THR-227; SER-303; SER-358; THR-385; THR-404; THR-411; SER-417; THR-424 AND THR-438, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF THR-411 AND THR-438.
[21]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385 AND THR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Interaction between antibody-diversification enzyme AID and spliceosome-associated factor CTNNBL1."
Conticello S.G., Ganesh K., Xue K., Lu M., Rada C., Neuberger M.S.
Mol. Cell 31:474-484(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CTNNBL1.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227; THR-377; THR-385; THR-396; THR-415; THR-424; THR-430; SER-437; THR-438 AND THR-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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].
[25]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-385 AND THR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[26]"Molecular architecture of the human Prp19/CDC5L complex."
Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A., Fischle W., Urlaub H., Luhrmann R.
Mol. Cell. Biol. 30:2105-2119(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, INTERACTION WITH CTNNBL1; PRPF19 AND BCAS2.
[27]"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-303; THR-377 AND THR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"CTNNBL1 is a novel nuclear localization sequence-binding protein that recognizes RNA-splicing factors CDC5L and Prp31."
Ganesh K., Adam S., Taylor B., Simpson P., Rada C., Neuberger M.
J. Biol. Chem. 286:17091-17102(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CTNNBL1.
[30]"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 THR-377; THR-385 AND THR-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"Solution structure of the MYB DNA-binding domain of human cell division cycle 5-like protein."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 7-112.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U86753 mRNA. Translation: AAB61210.1.
AB007892 mRNA. Translation: BAA24862.2. Different initiation.
AY518540 Genomic DNA. Translation: AAR89913.1.
AL133262, AL353588 Genomic DNA. Translation: CAI20149.1.
AL353588, AL133262 Genomic DNA. Translation: CAI40750.1.
BC001568 mRNA. Translation: AAH01568.1.
D85423 mRNA. Translation: BAA20885.1.
CCDSCCDS4912.1.
RefSeqNP_001244.1. NM_001253.3.
UniGeneHs.485471.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIMNMR-A7-63[»]
2DINNMR-A59-111[»]
ProteinModelPortalQ99459.
SMRQ99459. Positions 10-118.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107424. 156 interactions.
DIPDIP-31731N.
IntActQ99459. 562 interactions.
MINTMINT-133723.
STRING9606.ENSP00000360532.

PTM databases

PhosphoSiteQ99459.

Polymorphism databases

DMDM73619933.

Proteomic databases

MaxQBQ99459.
PaxDbQ99459.
PeptideAtlasQ99459.
PRIDEQ99459.

Protocols and materials databases

DNASU988.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371477; ENSP00000360532; ENSG00000096401.
GeneID988.
KEGGhsa:988.
UCSCuc003oxl.3. human.

Organism-specific databases

CTD988.
GeneCardsGC06P044402.
HGNCHGNC:1743. CDC5L.
HPACAB012275.
HPA006302.
HPA011361.
MIM602868. gene.
neXtProtNX_Q99459.
PharmGKBPA26270.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5147.
HOGENOMHOG000182446.
HOVERGENHBG052766.
InParanoidQ99459.
KOK12860.
OMANMMALTH.
OrthoDBEOG7JDQWW.
PhylomeDBQ99459.
TreeFamTF101061.

Gene expression databases

BgeeQ99459.
CleanExHS_CDC5L.
GenevestigatorQ99459.

Family and domain databases

Gene3D1.10.10.60. 2 hits.
InterProIPR021786. DUF3351.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
[Graphical view]
PfamPF11831. Myb_Cef. 1 hit.
[Graphical view]
SMARTSM00717. SANT. 2 hits.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
PROSITEPS51294. HTH_MYB. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDC5L. human.
EvolutionaryTraceQ99459.
GeneWikiCDC5L.
GenomeRNAi988.
NextBio4146.
PMAP-CutDBQ99459.
PROQ99459.
SOURCESearch...

Entry information

Entry nameCDC5L_HUMAN
AccessionPrimary (citable) accession number: Q99459
Secondary accession number(s): Q76N46, Q99974
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: July 9, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM