Q99459 (CDC5L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	802 AA.
Sequence status	Complete.
Protein existence	Evidence 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.25 Ref.28
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.25
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 process	Cell cycle Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Domain	Coiled coil Repeat
Ligand	DNA-binding RNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW mRNA splicing, via spliceosome Inferred by curator Ref.17. Source: UniProtKB regulation of transcription, DNA-dependent Non-traceable author statement. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Prp19 complex Inferred from direct assay Ref.25. 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
Molecular_function	DNA binding Non-traceable author statement Ref.9. Source: UniProtKB RNA binding Inferred from electronic annotation. Source: UniProtKB-KW WD40-repeat domain binding Inferred from direct assay Ref.25. Source: UniProtKB chromatin binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 802

802

Cell division cycle 5-like protein

PRO_0000197091

Regions

Domain

1 – 56

56

HTH myb-type 1

Domain

57 – 108

52

HTH myb-type 2

DNA binding

31 – 54

24

H-T-H motif By similarity

DNA binding

82 – 104

23

H-T-H motif By similarity

Region

165 – 271

107

Nuclear localization signal Potential

Region

200 – 206

7

Required for interaction with CTNNBL1 By similarity

Region

260 – 606

347

Interaction with PPP1R8

Region

501 – 659

159

Interaction with DAPK3 By similarity

Region

706 – 800

95

Interaction with PLRG1

Coiled coil

142 – 245

104

Potential

Coiled coil

676 – 701

26

Potential

Coiled coil

764 – 802

39

Potential

Sites

Site

414

1

Breakpoint for translocation

Amino acid modifications

Modified residue

227

1

Phosphothreonine Ref.20 Ref.23

Modified residue

303

1

Phosphoserine Ref.19 Ref.20 Ref.26

Modified residue

358

1

Phosphoserine Ref.20

Modified residue

377

1

Phosphothreonine Ref.23 Ref.26 Ref.29

Modified residue

385

1

Phosphothreonine Ref.20 Ref.21 Ref.23 Ref.24 Ref.29

Modified residue

396

1

Phosphothreonine Ref.21 Ref.23 Ref.24 Ref.26 Ref.29

Modified residue

404

1

Phosphothreonine Ref.20

Modified residue

411

1

Phosphothreonine Ref.20

Modified residue

415

1

Phosphothreonine Ref.23

Modified residue

417

1

Phosphoserine Ref.20

Modified residue

424

1

Phosphothreonine Ref.20 Ref.23

Modified residue

430

1

Phosphothreonine Ref.23

Modified residue

437

1

Phosphoserine Ref.23

Modified residue

438

1

Phosphothreonine Ref.20 Ref.23

Modified residue

442

1

Phosphothreonine Ref.23

Natural variations

Natural variant

459

1

Y → C.
Corresponds to variant rs11572006 [ dbSNP | Ensembl ].

VAR_050181

Experimental info

Mutagenesis

31

1

W → G: Abolishes DNA-binding; when associated with G-53 and G-82. Ref.15

Mutagenesis

53

1

W → G: Abolishes DNA-binding; when associated with G-31 and G-82. Ref.15

Mutagenesis

82

1

W → G: Abolishes DNA-binding; when associated with G-31 and G-53. Ref.15

Mutagenesis

227

1

T → 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.

Mutagenesis

303

1

S → 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.

Mutagenesis

358

1

S → 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.

Mutagenesis

404

1

T → 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.

Mutagenesis

411

1

T → 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

Mutagenesis

417

1

S → 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.

Mutagenesis

424

1

T → 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.

Mutagenesis

438

1

T → 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 conflict

12

1

R → K in BAA20885. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

802

Helix Strand Turn

Details...

Helix

13 – 25

13

Helix

31 – 37

7

Helix

43 – 52

10

Beta strand

56 – 58

3

Helix

65 – 77

13

Helix

82 – 89

8

Helix

93 – 109

17

Sequences

	Sequence		Length	Mass (Da)
	Q99459 [UniParc]. Last modified August 16, 2005. Version 2. Checksum: 3390F91EE7E79DA6	FASTA	802	92,251
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[25]	"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.
[26]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"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].
[28]	"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.
[29]	"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, MASS SPECTROMETRY.
[30]	"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

NIEHS-SNPs

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.

IPI

IPI00465294.

RefSeq

NP_001244.1. NM_001253.3.

UniGene

Hs.485471.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DIM	NMR	-	A	7-63	[»]
2DIN	NMR	-	A	59-111	[»]

ProteinModelPortal

Q99459.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31731N.

IntAct

Q99459. 46 interactions.

MINT

MINT-133723.

STRING

9606.ENSP00000360532.

PTM databases

PhosphoSite

Q99459.

Polymorphism databases

DMDM

73619933.

Proteomic databases

PaxDb

Q99459.

PeptideAtlas

Q99459.

PRIDE

Q99459.

Protocols and materials databases

DNASU

988.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371477; ENSP00000360532; ENSG00000096401.

GeneID

988.

KEGG

hsa:988.

UCSC

uc003oxl.3. human.

Organism-specific databases

CTD

988.

GeneCards

GC06P044402.

HGNC

HGNC:1743. CDC5L.

HPA

CAB012275.
HPA006302.
HPA011361.

MIM

602868. gene.

neXtProt

NX_Q99459.

PharmGKB

PA26270.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5147.

HOGENOM

HOG000182446.

HOVERGEN

HBG052766.

InParanoid

Q99459.

KO

K12860.

OMA

HIAYLEH.

OrthoDB

EOG48GW2S.

PhylomeDB

Q99459.

Gene expression databases

Bgee

Q99459.

CleanEx

HS_CDC5L.

Genevestigator

Q99459.

GermOnline

ENSG00000096401. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.60. 2 hits.

InterPro

IPR021786. DUF3351.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
[Graphical view]

Pfam

PF11831. Myb_Cef. 1 hit.
[Graphical view]

SMART

SM00717. SANT. 2 hits.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 1 hit.

PROSITE

PS51294. HTH_MYB. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CDC5L. human.

EvolutionaryTrace

Q99459.

GenomeRNAi

988.

NextBio

4146.

PMAP-CutDB

Q99459.

SOURCE

Search...

Entry information

Entry name

CDC5L_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 127 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.