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Q99459

- CDC5L_HUMAN

UniProt

Q99459 - CDC5L_HUMAN

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Protein

Cell division cycle 5-like protein

Gene

CDC5L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR).10 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei414 – 4141Breakpoint for translocation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi31 – 5424H-T-H motifPROSITE-ProRule annotationAdd
BLAST
DNA bindingi82 – 10423H-T-H motifPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: InterPro
  2. DNA binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. WD40-repeat domain binding Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. mRNA splicing, via spliceosome Source: UniProtKB
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Cell cycle, DNA damage, DNA repair, mRNA processing, mRNA splicing, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiREACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell division cycle 5-like protein
Short name:
Cdc5-like protein
Alternative name(s):
Pombe cdc5-related protein
Gene namesi
Name:CDC5L
Synonyms:KIAA0432, PCDC5RP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:1743. CDC5L.

Subcellular locationi

Nucleus 5 Publications. Nucleus speckle 3 Publications. Cytoplasm 1 Publication
Note: May shuttle between cytoplasm and nucleus.1 Publication

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. membrane Source: UniProtKB
  4. nuclear speck Source: BHF-UCL
  5. nucleolus Source: HPA
  6. nucleus Source: UniProtKB
  7. Prp19 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Involvement in diseasei

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 311W → G: Abolishes DNA-binding; when associated with G-53 and G-82. 1 Publication
Mutagenesisi53 – 531W → G: Abolishes DNA-binding; when associated with G-31 and G-82. 1 Publication
Mutagenesisi82 – 821W → G: Abolishes DNA-binding; when associated with G-31 and G-53. 1 Publication
Mutagenesisi227 – 2271T → 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.
Mutagenesisi303 – 3031S → 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.
Mutagenesisi358 – 3581S → 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.
Mutagenesisi404 – 4041T → 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.
Mutagenesisi411 – 4111T → 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. 1 Publication
Mutagenesisi417 – 4171S → 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.
Mutagenesisi424 – 4241T → 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.
Mutagenesisi438 – 4381T → 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. 1 Publication

Organism-specific databases

PharmGKBiPA26270.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 802802Cell division cycle 5-like proteinPRO_0000197091Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei227 – 2271Phosphothreonine2 Publications
Modified residuei303 – 3031Phosphoserine3 Publications
Modified residuei358 – 3581Phosphoserine1 Publication
Modified residuei377 – 3771Phosphothreonine3 Publications
Modified residuei385 – 3851Phosphothreonine5 Publications
Modified residuei396 – 3961Phosphothreonine5 Publications
Modified residuei404 – 4041Phosphothreonine1 Publication
Modified residuei411 – 4111Phosphothreonine1 Publication
Modified residuei415 – 4151Phosphothreonine1 Publication
Modified residuei417 – 4171Phosphoserine1 Publication
Modified residuei424 – 4241Phosphothreonine2 Publications
Modified residuei430 – 4301Phosphothreonine1 Publication
Modified residuei437 – 4371Phosphoserine1 Publication
Modified residuei438 – 4381Phosphothreonine2 Publications
Modified residuei442 – 4421Phosphothreonine1 Publication

Post-translational modificationi

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 PPP1R8.9 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ99459.
PaxDbiQ99459.
PeptideAtlasiQ99459.
PRIDEiQ99459.

PTM databases

PhosphoSiteiQ99459.

Miscellaneous databases

PMAP-CutDBQ99459.

Expressioni

Tissue specificityi

Ubiquitously expressed in both fetal and adult tissues.3 Publications

Gene expression databases

BgeeiQ99459.
CleanExiHS_CDC5L.
GenevestigatoriQ99459.

Organism-specific databases

HPAiCAB012275.
HPA006302.
HPA011361.

Interactioni

Subunit structurei

Homodimer. Interacts with DAPK3 (By similarity). 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. Interacts with PRPF19 (via N-terminus) (By similarity).By similarity9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATRQ135353EBI-374880,EBI-968983
CTNNBL1Q8WYA62EBI-374880,EBI-748128
HNRNPMP522727EBI-374880,EBI-486809
ORC2Q134162EBI-374880,EBI-374957
PLRG1O436602EBI-374880,EBI-1051504
PRPF19Q9UMS42EBI-374880,EBI-395746
SF3A2Q154282EBI-374880,EBI-2462271

Protein-protein interaction databases

BioGridi107424. 166 interactions.
DIPiDIP-31731N.
IntActiQ99459. 562 interactions.
MINTiMINT-133723.
STRINGi9606.ENSP00000360532.

Structurei

Secondary structure

1
802
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 2513Combined sources
Helixi31 – 377Combined sources
Helixi43 – 5210Combined sources
Beta strandi56 – 583Combined sources
Helixi65 – 7713Combined sources
Helixi82 – 898Combined sources
Helixi93 – 10917Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DIMNMR-A7-63[»]
2DINNMR-A59-111[»]
ProteinModelPortaliQ99459.
SMRiQ99459. Positions 10-118.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99459.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 5656HTH myb-type 1PROSITE-ProRule annotationAdd
BLAST
Domaini57 – 10852HTH myb-type 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni165 – 271107Nuclear localization signalSequence AnalysisAdd
BLAST
Regioni200 – 2067Required for interaction with CTNNBL11 Publication
Regioni260 – 606347Interaction with PPP1R8Add
BLAST
Regioni501 – 659159Interaction with DAPK3By similarityAdd
BLAST
Regioni706 – 80095Interaction with PLRG1Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili142 – 245104Sequence AnalysisAdd
BLAST
Coiled coili676 – 70126Sequence AnalysisAdd
BLAST
Coiled coili764 – 80239Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the CEF1 family.Curated
Contains 2 HTH myb-type DNA-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG5147.
GeneTreeiENSGT00550000074922.
HOGENOMiHOG000182446.
HOVERGENiHBG052766.
InParanoidiQ99459.
KOiK12860.
OMAiNMMALTH.
OrthoDBiEOG7JDQWW.
PhylomeDBiQ99459.
TreeFamiTF101061.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
InterProiIPR021786. DUF3351.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
[Graphical view]
PfamiPF11831. Myb_Cef. 1 hit.
[Graphical view]
SMARTiSM00717. SANT. 2 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS51294. HTH_MYB. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99459-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRIMIKGGV WRNTEDEILK AAVMKYGKNQ WSRIASLLHR KSAKQCKARW
60 70 80 90 100
YEWLDPSIKK TEWSREEEEK LLHLAKLMPT QWRTIAPIIG RTAAQCLEHY
110 120 130 140 150
EFLLDKAAQR DNEEETTDDP RKLKPGEIDP NPETKPARPD PIDMDEDELE
160 170 180 190 200
MLSEARARLA NTQGKKAKRK AREKQLEEAR RLAALQKRRE LRAAGIEIQK
210 220 230 240 250
KRKRKRGVDY NAEIPFEKKP ALGFYDTSEE NYQALDADFR KLRQQDLDGE
260 270 280 290 300
LRSEKEGRDR KKDKQHLKRK KESDLPSAIL QTSGVSEFTK KRSKLVLPAP
310 320 330 340 350
QISDAELQEV VKVGQASEIA RQTAEESGIT NSASSTLLSE YNVTNNSVAL
360 370 380 390 400
RTPRTPASQD RILQEAQNLM ALTNVDTPLK GGLNTPLHES DFSGVTPQRQ
410 420 430 440 450
VVQTPNTVLS TPFRTPSNGA EGLTPRSGTT PKPVINSTPG RTPLRDKLNI
460 470 480 490 500
NPEDGMADYS DPSYVKQMER ESREHLRLGL LGLPAPKNDF EIVLPENAEK
510 520 530 540 550
ELEEREIDDT YIEDAADVDA RKQAIRDAER VKEMKRMHKA VQKDLPRPSE
560 570 580 590 600
VNETILRPLN VEPPLTDLQK SEELIKKEMI TMLHYDLLHH PYEPSGNKKG
610 620 630 640 650
KTVGFGTNNS EHITYLEHNP YEKFSKEELK KAQDVLVQEM EVVKQGMSHG
660 670 680 690 700
ELSSEAYNQV WEECYSQVLY LPGQSRYTRA NLASKKDRIE SLEKRLEINR
710 720 730 740 750
GHMTTEAKRA AKMEKKMKIL LGGYQSRAMG LMKQLNDLWD QIEQAHLELR
760 770 780 790 800
TFEELKKHED SAIPRRLECL KEDVQRQQER EKELQHRYAD LLLEKETLKS

KF
Length:802
Mass (Da):92,251
Last modified:August 16, 2005 - v2
Checksum:i3390F91EE7E79DA6
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121R → K in BAA20885. (PubMed:8917598)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti459 – 4591Y → C.
Corresponds to variant rs11572006 [ dbSNP | Ensembl ].
VAR_050181

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4912.1.
RefSeqiNP_001244.1. NM_001253.3.
UniGeneiHs.485471.

Genome annotation databases

EnsembliENST00000371477; ENSP00000360532; ENSG00000096401.
GeneIDi988.
KEGGihsa:988.
UCSCiuc003oxl.3. human.

Polymorphism databases

DMDMi73619933.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS4912.1.
RefSeqi NP_001244.1. NM_001253.3.
UniGenei Hs.485471.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DIM NMR - A 7-63 [» ]
2DIN NMR - A 59-111 [» ]
ProteinModelPortali Q99459.
SMRi Q99459. Positions 10-118.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107424. 166 interactions.
DIPi DIP-31731N.
IntActi Q99459. 562 interactions.
MINTi MINT-133723.
STRINGi 9606.ENSP00000360532.

PTM databases

PhosphoSitei Q99459.

Polymorphism databases

DMDMi 73619933.

Proteomic databases

MaxQBi Q99459.
PaxDbi Q99459.
PeptideAtlasi Q99459.
PRIDEi Q99459.

Protocols and materials databases

DNASUi 988.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371477 ; ENSP00000360532 ; ENSG00000096401 .
GeneIDi 988.
KEGGi hsa:988.
UCSCi uc003oxl.3. human.

Organism-specific databases

CTDi 988.
GeneCardsi GC06P044402.
HGNCi HGNC:1743. CDC5L.
HPAi CAB012275.
HPA006302.
HPA011361.
MIMi 602868. gene.
neXtProti NX_Q99459.
PharmGKBi PA26270.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5147.
GeneTreei ENSGT00550000074922.
HOGENOMi HOG000182446.
HOVERGENi HBG052766.
InParanoidi Q99459.
KOi K12860.
OMAi NMMALTH.
OrthoDBi EOG7JDQWW.
PhylomeDBi Q99459.
TreeFami TF101061.

Enzyme and pathway databases

Reactomei REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi CDC5L. human.
EvolutionaryTracei Q99459.
GeneWikii CDC5L.
GenomeRNAii 988.
NextBioi 4146.
PMAP-CutDB Q99459.
PROi Q99459.
SOURCEi Search...

Gene expression databases

Bgeei Q99459.
CleanExi HS_CDC5L.
Genevestigatori Q99459.

Family and domain databases

Gene3Di 1.10.10.60. 2 hits.
InterProi IPR021786. DUF3351.
IPR009057. Homeodomain-like.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
[Graphical view ]
Pfami PF11831. Myb_Cef. 1 hit.
[Graphical view ]
SMARTi SM00717. SANT. 2 hits.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 1 hit.
PROSITEi PS51294. HTH_MYB. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
  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. 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. 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. Cited for: IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L SPLICING COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, 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. 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. "PRP19 transforms into a sensor of RPA-ssDNA after DNA damage and drives ATR activation via a ubiquitin-mediated circuitry."
    Marechal A., Li J.M., Ji X.Y., Wu C.S., Yazinski S.A., Nguyen H.D., Liu S., Jimenez A.E., Jin J., Zou L.
    Mol. Cell 53:235-246(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  32. "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.

Entry informationi

Entry nameiCDC5L_HUMAN
AccessioniPrimary (citable) accession number: Q99459
Secondary accession number(s): Q76N46, Q99974
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: November 26, 2014
This is version 142 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

External Data

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