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Protein

Cell division cycle 5-like protein

Gene

CDC5L

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

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

GO - Biological processi

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

ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.
SIGNORiQ99459.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:1743. CDC5L.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: UniProtKB
  • cytoplasm Source: CACAO
  • membrane Source: UniProtKB
  • nuclear speck Source: BHF-UCL
  • nucleolus Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: Ensembl
  • protein-DNA complex Source: Ensembl
  • 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

Sites

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

Organism-specific databases

PharmGKBiPA26270.

Polymorphism and mutation databases

BioMutaiCDC5L.
DMDMi73619933.

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
Cross-linki219 – 219Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei227 – 2271PhosphothreonineCombined sources1 Publication
Modified residuei303 – 3031PhosphoserineCombined sources1 Publication
Modified residuei358 – 3581Phosphoserine1 Publication
Modified residuei377 – 3771PhosphothreonineCombined sources
Modified residuei385 – 3851PhosphothreonineCombined sources1 Publication
Modified residuei396 – 3961PhosphothreonineCombined sources
Modified residuei404 – 4041Phosphothreonine1 Publication
Modified residuei411 – 4111Phosphothreonine1 Publication
Modified residuei415 – 4151PhosphothreonineCombined sources
Modified residuei417 – 4171PhosphoserineCombined sources1 Publication
Modified residuei424 – 4241PhosphothreonineCombined sources1 Publication
Modified residuei430 – 4301PhosphothreonineCombined sources
Modified residuei437 – 4371PhosphoserineCombined sources
Modified residuei438 – 4381PhosphothreonineCombined sources1 Publication
Modified residuei442 – 4421PhosphothreonineCombined sources

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 PPP1R8.3 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ99459.
MaxQBiQ99459.
PaxDbiQ99459.
PeptideAtlasiQ99459.
PRIDEiQ99459.

PTM databases

iPTMnetiQ99459.
PhosphoSiteiQ99459.
SwissPalmiQ99459.

Miscellaneous databases

PMAP-CutDBQ99459.

Expressioni

Tissue specificityi

Ubiquitously expressed in both fetal and adult tissues.3 Publications

Gene expression databases

BgeeiENSG00000096401.
CleanExiHS_CDC5L.
GenevisibleiQ99459. HS.

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
GOLGA2Q083793EBI-374880,EBI-618309
GOLGA8DPQ0D2H93EBI-374880,EBI-10181276
GOLGA8GQ08AF83EBI-374880,EBI-10181260
HNRNPMP522727EBI-374880,EBI-486809
ORC2Q134162EBI-374880,EBI-374957
PLRG1O436602EBI-374880,EBI-1051504
PRPF19Q9UMS42EBI-374880,EBI-395746
SF3A2Q154282EBI-374880,EBI-2462271
TTF2Q9UNY45EBI-374880,EBI-2322921

GO - Molecular functioni

  • WD40-repeat domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107424. 597 interactions.
DIPiDIP-31731N.
IntActiQ99459. 576 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
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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi165 – 271107Nuclear localization signalSequence 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

eggNOGiKOG0050. Eukaryota.
COG5147. LUCA.
GeneTreeiENSGT00550000074922.
HOGENOMiHOG000182446.
HOVERGENiHBG052766.
InParanoidiQ99459.
KOiK12860.
OMAiKERMAHG.
OrthoDBiEOG091G0IYB.
PhylomeDBiQ99459.
TreeFamiTF101061.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
InterProiIPR021786. Cdc5p/Cef1.
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 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.4. human.

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.
CCDSiCCDS4912.1.
RefSeqiNP_001244.1. NM_001253.3.
UniGeneiHs.485471.

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...

Protein-protein interaction databases

BioGridi107424. 597 interactions.
DIPiDIP-31731N.
IntActiQ99459. 576 interactions.
MINTiMINT-133723.
STRINGi9606.ENSP00000360532.

PTM databases

iPTMnetiQ99459.
PhosphoSiteiQ99459.
SwissPalmiQ99459.

Polymorphism and mutation databases

BioMutaiCDC5L.
DMDMi73619933.

Proteomic databases

EPDiQ99459.
MaxQBiQ99459.
PaxDbiQ99459.
PeptideAtlasiQ99459.
PRIDEiQ99459.

Protocols and materials databases

DNASUi988.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371477; ENSP00000360532; ENSG00000096401.
GeneIDi988.
KEGGihsa:988.
UCSCiuc003oxl.4. human.

Organism-specific databases

CTDi988.
GeneCardsiCDC5L.
HGNCiHGNC:1743. CDC5L.
HPAiCAB012275.
HPA006302.
HPA011361.
MIMi602868. gene.
neXtProtiNX_Q99459.
PharmGKBiPA26270.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0050. Eukaryota.
COG5147. LUCA.
GeneTreeiENSGT00550000074922.
HOGENOMiHOG000182446.
HOVERGENiHBG052766.
InParanoidiQ99459.
KOiK12860.
OMAiKERMAHG.
OrthoDBiEOG091G0IYB.
PhylomeDBiQ99459.
TreeFamiTF101061.

Enzyme and pathway databases

ReactomeiR-HSA-72163. mRNA Splicing - Major Pathway.
SIGNORiQ99459.

Miscellaneous databases

ChiTaRSiCDC5L. human.
EvolutionaryTraceiQ99459.
GeneWikiiCDC5L.
GenomeRNAii988.
PMAP-CutDBQ99459.
PROiQ99459.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000096401.
CleanExiHS_CDC5L.
GenevisibleiQ99459. HS.

Family and domain databases

Gene3Di1.10.10.60. 2 hits.
InterProiIPR021786. Cdc5p/Cef1.
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]
ProtoNetiSearch...

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: September 7, 2016
This is version 161 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

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.