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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)DescriptionActionsGraphical viewLength
DNA bindingi31 – 54H-T-H motifPROSITE-ProRule annotationAdd BLAST24
DNA bindingi82 – 104H-T-H motifPROSITE-ProRule annotationAdd BLAST23

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding, RNA-binding
Biological processCell cycle, DNA damage, DNA repair, mRNA processing, mRNA splicing, Transcription, Transcription regulation

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

EuPathDBiHostDB:ENSG00000096401.7.
HGNCiHGNC:1743. CDC5L.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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)DescriptionActionsGraphical viewLength
Mutagenesisi31W → G: Abolishes DNA-binding; when associated with G-53 and G-82. 1 Publication1
Mutagenesisi53W → G: Abolishes DNA-binding; when associated with G-31 and G-82. 1 Publication1
Mutagenesisi82W → G: Abolishes DNA-binding; when associated with G-31 and G-53. 1 Publication1
Mutagenesisi227T → 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. 1
Mutagenesisi303S → 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. 1
Mutagenesisi358S → 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. 1
Mutagenesisi404T → 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. 1
Mutagenesisi411T → 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 Publication1
Mutagenesisi417S → 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. 1
Mutagenesisi424T → 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. 1
Mutagenesisi438T → 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 Publication1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei414Breakpoint for translocation1

Organism-specific databases

DisGeNETi988.
OpenTargetsiENSG00000096401.
PharmGKBiPA26270.

Polymorphism and mutation databases

BioMutaiCDC5L.
DMDMi73619933.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001970911 – 802Cell division cycle 5-like proteinAdd BLAST802

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki219Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei227PhosphothreonineCombined sources1 Publication1
Modified residuei303PhosphoserineCombined sources1 Publication1
Modified residuei358Phosphoserine1 Publication1
Modified residuei377PhosphothreonineCombined sources1
Modified residuei385PhosphothreonineCombined sources1 Publication1
Modified residuei396PhosphothreonineCombined sources1
Modified residuei404Phosphothreonine1 Publication1
Modified residuei411Phosphothreonine1 Publication1
Modified residuei415PhosphothreonineCombined sources1
Modified residuei417PhosphoserineCombined sources1 Publication1
Modified residuei424PhosphothreonineCombined sources1 Publication1
Modified residuei430PhosphothreonineCombined sources1
Modified residuei437PhosphoserineCombined sources1
Modified residuei438PhosphothreonineCombined sources1 Publication1
Modified residuei442PhosphothreonineCombined sources1
Cross-linki487Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined 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.
PhosphoSitePlusiQ99459.
SwissPalmiQ99459.

Miscellaneous databases

PMAP-CutDBiQ99459.

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

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi107424. 607 interactors.
CORUMiQ99459.
DIPiDIP-31731N.
IntActiQ99459. 585 interactors.
MINTiMINT-133723.
STRINGi9606.ENSP00000360532.

Structurei

Secondary structure

1802
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 25Combined sources13
Helixi31 – 37Combined sources7
Helixi43 – 52Combined sources10
Beta strandi56 – 58Combined sources3
Helixi65 – 77Combined sources13
Helixi82 – 89Combined sources8
Helixi93 – 109Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DIMNMR-A7-63[»]
2DINNMR-A59-111[»]
5MQFelectron microscopy5.90L1-802[»]
5XJCelectron microscopy3.60L1-802[»]
ProteinModelPortaliQ99459.
SMRiQ99459.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99459.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 56HTH myb-type 1PROSITE-ProRule annotationAdd BLAST56
Domaini57 – 108HTH myb-type 2PROSITE-ProRule annotationAdd BLAST52

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni200 – 206Required for interaction with CTNNBL11 Publication7
Regioni260 – 606Interaction with PPP1R81 PublicationAdd BLAST347
Regioni501 – 659Interaction with DAPK3By similarityAdd BLAST159
Regioni706 – 800Interaction with PLRG11 PublicationAdd BLAST95

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili142 – 245Sequence analysisAdd BLAST104
Coiled coili676 – 701Sequence analysisAdd BLAST26
Coiled coili764 – 802Sequence analysisAdd BLAST39

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi165 – 271Nuclear localization signalSequence analysisAdd BLAST107

Sequence similaritiesi

Belongs to the CEF1 family.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

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

Family and domain databases

CDDicd00167. SANT. 1 hit.
InterProiView protein in InterPro
IPR021786. Cdc5p/Cef1.
IPR009057. Homeobox-like_sf.
IPR017930. Myb_dom.
IPR001005. SANT/Myb.
PfamiView protein in Pfam
PF11831. Myb_Cef. 1 hit.
SMARTiView protein in SMART
SM00717. SANT. 2 hits.
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiView protein in PROSITE
PS51294. HTH_MYB. 2 hits.

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)DescriptionActionsGraphical viewLength
Sequence conflicti12R → K in BAA20885 (PubMed:8917598).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_050181459Y → C. Corresponds to variant dbSNP:rs11572006Ensembl.1

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 Genomic DNA. No translation available.
AL353588 Genomic DNA. No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiCDC5L_HUMAN
AccessioniPrimary (citable) accession number: Q99459
Secondary accession number(s): Q76N46, Q99974
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: November 22, 2017
This is version 173 of the entry and version 2 of the sequence. See 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