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Q9NZJ0

- DTL_HUMAN

UniProt

Q9NZJ0 - DTL_HUMAN

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Protein

Denticleless protein homolog

Gene

DTL

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

Functioni

Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1) and SETD8. CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication. CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing. SETD8 degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration. Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis.11 Publications

Pathwayi

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: UniProtKB
  2. DNA replication Source: UniProtKB-KW
  3. G2 DNA damage checkpoint Source: UniProtKB
  4. protein monoubiquitination Source: UniProtKB
  5. protein polyubiquitination Source: UniProtKB
  6. regulation of cell cycle Source: UniProtKB
  7. response to UV Source: UniProtKB
  8. translesion synthesis Source: UniProtKB
  9. ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA replication, Ubl conjugation pathway

Enzyme and pathway databases

SignaLinkiQ9NZJ0.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Denticleless protein homolog
Alternative name(s):
DDB1- and CUL4-associated factor 2
Lethal(2) denticleless protein homolog
Retinoic acid-regulated nuclear matrix-associated protein
Gene namesi
Name:DTL
Synonyms:CDT2, CDW1, DCAF2, L2DTL, RAMP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:30288. DTL.

Subcellular locationi

Nucleus. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Chromosome
Note: Nuclear matrix-associated protein. Translocates from the interphase nucleus to the metaphase cytoplasm during mitosis.

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. chromosome Source: UniProtKB-KW
  3. Cul4A-RING E3 ubiquitin ligase complex Source: UniProtKB
  4. Cul4B-RING E3 ubiquitin ligase complex Source: UniProtKB
  5. cytoplasm Source: HPA
  6. intracellular membrane-bounded organelle Source: HPA
  7. membrane Source: UniProtKB-KW
  8. nucleolus Source: HPA
  9. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi246 – 2461R → A: Blocks association with DDB1 and ubiquitination by DCX(DTL). No effect on ubiquitination by SCF(FBXO11). 2 Publications
Mutagenesisi457 – 4571D → A: Increases protein stability, but no effect on interaction with FBXO11 and polyubiquitination. Delays cell migration. 1 Publication
Mutagenesisi462 – 4621S → A: Blocks interaction with FBXO11 and ubiquitination, increasing protein stability. Delays cell migration. 1 Publication
Mutagenesisi463 – 4631N → A: No effect on interaction with FBXO11. Increases protein stability. 1 Publication
Mutagenesisi464 – 4641T → A: Blocks interaction with FBXO11 and increases protein stability. Not phosphorylated by CDK1 or CDK2. 1 Publication
Mutagenesisi464 – 4641T → D: Blocks interaction with FBXO11. 1 Publication
Mutagenesisi465 – 4651P → A: Inhibits phosphorylation on T-464. No effect on interaction with FBXO11. 1 Publication
Mutagenesisi466 – 4661T → A: No effect on interaction with FBXO11. 1 Publication
Mutagenesisi466 – 4661T → D: No effect on interaction with FBXO11. 1 Publication
Mutagenesisi467 – 4671F → A: No effect on interaction with FBXO11. 1 Publication
Mutagenesisi468 – 4681S → A: No effect on interaction with FBXO11. 1 Publication
Mutagenesisi468 – 4681S → D: No effect on interaction with FBXO11. 1 Publication
Mutagenesisi471 – 4711T → A: No effect on interaction with FBXO11. 1 Publication
Mutagenesisi471 – 4711T → D: No effect on interaction with FBXO11. 1 Publication
Mutagenesisi472 – 4721S → A: No effect on interaction with FBXO11. 1 Publication
Mutagenesisi472 – 4721S → D: No effect on interaction with FBXO11. 1 Publication

Organism-specific databases

PharmGKBiPA142671941.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 730730Denticleless protein homologPRO_0000274867Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei410 – 4101Phosphoserine1 Publication
Modified residuei464 – 4641Phosphothreonine; by CDK1 and CDK21 Publication
Modified residuei485 – 4851Phosphoserine1 Publication
Modified residuei490 – 4901Phosphoserine2 Publications
Modified residuei495 – 4951Phosphoserine1 Publication
Modified residuei512 – 5121Phosphoserine4 Publications
Modified residuei516 – 5161Phosphothreonine4 Publications
Modified residuei557 – 5571Phosphoserine1 Publication
Modified residuei676 – 6761Phosphoserine1 Publication
Modified residuei679 – 6791Phosphoserine1 Publication
Modified residuei684 – 6841Phosphothreonine1 Publication

Post-translational modificationi

Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C). Autoubiquitinated through 'Lys-48'-polyubiquitin chains in a PCNA-independent reaction, allowing proteasomal turnover. Polyubiquitinated by SCF(FBXO11) when not phosphorylated, leading to its degradation. A tight regulation of the polyubiquitination by SCF(FBXO11) is involved in the control of different processes such as TGF-beta signaling, cell cycle progression and exit.3 Publications
Phosphorylated at Thr-464 by CDK1/Cyclin-B and CDK2/Cyclin-A but not by CDK2/Cyclin-E, MAPK1 or PLK1. Phosphorylation at Thr-464 inhibits the interaction with FBXO11 and decreases upon cell cycle exit induced by TGF-beta or serum starvation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9NZJ0.
PaxDbiQ9NZJ0.
PRIDEiQ9NZJ0.

PTM databases

PhosphoSiteiQ9NZJ0.

Expressioni

Tissue specificityi

Expressed in placenta and testis, very low expression seen in skeletal muscle. Detected in all hematopoietic tissues examined, with highest expression in thymus and bone marrow. A low level detected in the spleen and lymph node, and barely detectable level in the peripheral leukocytes. RA treatment down-regulated the expression in NT2 cell.2 Publications

Developmental stagei

Expressed in all fetal tissues examined, included brain, lung, liver, and kidney. Protein levels peak at G1 and decrease through S-phase.2 Publications

Inductioni

Induced by TGF-beta, the up-regulation is immediate and transient.1 Publication

Gene expression databases

BgeeiQ9NZJ0.
CleanExiHS_DTL.
ExpressionAtlasiQ9NZJ0. baseline and differential.
GenevestigatoriQ9NZJ0.

Organism-specific databases

HPAiHPA028016.
HPA032023.
HPA032031.
HPA032032.

Interactioni

Subunit structurei

Component of the DCX(DTL) E3 ubiquitin ligase complex, at least composed of CUL4 (CUL4A or CUL4B), DDB1, DTL/CDT2 and RBX1. Interacts with CDKN1A and CDT1. Interacts with FBXO11; SCF(FBXWO11) controls DTL stability but DCX(DTL) does not control FBXO11 stability.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DDB1Q165313EBI-1176075,EBI-350322

Protein-protein interaction databases

BioGridi119582. 37 interactions.
IntActiQ9NZJ0. 8 interactions.
STRINGi9606.ENSP00000355958.

Structurei

3D structure databases

ProteinModelPortaliQ9NZJ0.
SMRiQ9NZJ0. Positions 9-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati47 – 8943WD 1Add
BLAST
Repeati96 – 13540WD 2Add
BLAST
Repeati138 – 17841WD 3Add
BLAST
Repeati214 – 25340WD 4Add
BLAST
Repeati267 – 30842WD 5Add
BLAST
Repeati313 – 35442WD 6Add
BLAST
Repeati358 – 39841WD 7Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi168 – 1714DDB1-binding motif
Motifi197 – 2037Nuclear localization signalSequence Analysis
Motifi243 – 2464DDB1-binding motif

Sequence similaritiesi

Belongs to the WD repeat cdt2 family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00530000064210.
HOVERGENiHBG057737.
InParanoidiQ9NZJ0.
KOiK11790.
OMAiICTYFHR.
OrthoDBiEOG7W153G.
PhylomeDBiQ9NZJ0.
TreeFamiTF324483.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 4 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 2 hits.
PROSITEiPS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NZJ0-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLFNSVLRQP QLGVLRNGWS SQYPLQSLLT GYQCSGNDEH TSYGETGVPV
60 70 80 90 100
PPFGCTFSSA PNMEHVLAVA NEEGFVRLYN TESQSFRKKC FKEWMAHWNA
110 120 130 140 150
VFDLAWVPGE LKLVTAAGDQ TAKFWDVKAG ELIGTCKGHQ CSLKSVAFSK
160 170 180 190 200
FEKAVFCTGG RDGNIMVWDT RCNKKDGFYR QVNQISGAHN TSDKQTPSKP
210 220 230 240 250
KKKQNSKGLA PSVDFQQSVT VVLFQDENTL VSAGAVDGII KVWDLRKNYT
260 270 280 290 300
AYRQEPIASK SFLYPGSSTR KLGYSSLILD STGSTLFANC TDDNIYMFNM
310 320 330 340 350
TGLKTSPVAI FNGHQNSTFY VKSSLSPDDQ FLVSGSSDEA AYIWKVSTPW
360 370 380 390 400
QPPTVLLGHS QEVTSVCWCP SDFTKIATCS DDNTLKIWRL NRGLEEKPGG
410 420 430 440 450
DKLSTVGWAS QKKKESRPGL VTVTSSQSTP AKAPRAKCNP SNSSPSSAAC
460 470 480 490 500
APSCAGDLPL PSNTPTFSIK TSPAKARSPI NRRGSVSSVS PKPPSSFKMS
510 520 530 540 550
IRNWVTRTPS SSPPITPPAS ETKIMSPRKA LIPVSQKSSQ AEACSESRNR
560 570 580 590 600
VKRRLDSSCL ESVKQKCVKS CNCVTELDGQ VENLHLDLCC LAGNQEDLSK
610 620 630 640 650
DSLGPTKSSK IEGAGTSISE PPSPISPYAS ESCGTLPLPL RPCGEGSEMV
660 670 680 690 700
GKENSSPENK NWLLAMAAKR KAENPSPRSP SSQTPNSRRQ SGKKLPSPVT
710 720 730
ITPSSMRKIC TYFHRKSQED FCGPEHSTEL
Length:730
Mass (Da):79,468
Last modified:August 10, 2010 - v3
Checksum:iCE8D54234D44F002
GO
Isoform 2 (identifier: Q9NZJ0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     18-59: Missing.
     240-253: IKVWDLRKNYTAYR → FKSDFGFHWLYFIC
     254-730: Missing.

Note: No experimental confirmation available.

Show »
Length:211
Mass (Da):23,682
Checksum:i23E4B52CFC514F80
GO

Sequence cautioni

The sequence BAA91552.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA91586.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti83 – 831S → P in BAA91355. (PubMed:14702039)Curated
Sequence conflicti356 – 3561L → F in BAF85032. (PubMed:14702039)Curated
Sequence conflicti532 – 5321I → T in BAA91552. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti425 – 4251S → N.
Corresponds to variant rs35137676 [ dbSNP | Ensembl ].
VAR_062095
Natural varianti436 – 4361A → V.6 Publications
Corresponds to variant rs3135474 [ dbSNP | Ensembl ].
VAR_030353
Natural varianti694 – 6941K → T.5 Publications
Corresponds to variant rs6540718 [ dbSNP | Ensembl ].
VAR_030354

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei18 – 5942Missing in isoform 2. 1 PublicationVSP_022879Add
BLAST
Alternative sequencei240 – 25314IKVWD…YTAYR → FKSDFGFHWLYFIC in isoform 2. 1 PublicationVSP_022880Add
BLAST
Alternative sequencei254 – 730477Missing in isoform 2. 1 PublicationVSP_022881Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF345896 mRNA. Translation: AAK54706.1.
DQ641253 mRNA. Translation: ABG23317.1.
AF195765 mRNA. Translation: AAF35182.1.
AK000742 mRNA. Translation: BAA91355.1.
AK001206 mRNA. Translation: BAA91552.1. Different initiation.
AK001261 mRNA. Translation: BAA91586.1. Different initiation.
AK027651 mRNA. Translation: BAB55267.1.
AK292343 mRNA. Translation: BAF85032.1.
AL606468, AC092814, AL592297 Genomic DNA. Translation: CAH70697.1.
AL592297, AC092814, AL606468 Genomic DNA. Translation: CAH73803.1.
CH471100 Genomic DNA. Translation: EAW93395.1.
CH471100 Genomic DNA. Translation: EAW93397.1.
BC033540 mRNA. Translation: AAH33540.1.
BC033297 mRNA. Translation: AAH33297.1.
CCDSiCCDS1502.1. [Q9NZJ0-1]
RefSeqiNP_001273158.1. NM_001286229.1.
NP_057532.3. NM_016448.3.
UniGeneiHs.656473.

Genome annotation databases

EnsembliENST00000366991; ENSP00000355958; ENSG00000143476. [Q9NZJ0-1]
GeneIDi51514.
KEGGihsa:51514.
UCSCiuc001hiz.4. human. [Q9NZJ0-1]

Polymorphism databases

DMDMi302393825.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF345896 mRNA. Translation: AAK54706.1 .
DQ641253 mRNA. Translation: ABG23317.1 .
AF195765 mRNA. Translation: AAF35182.1 .
AK000742 mRNA. Translation: BAA91355.1 .
AK001206 mRNA. Translation: BAA91552.1 . Different initiation.
AK001261 mRNA. Translation: BAA91586.1 . Different initiation.
AK027651 mRNA. Translation: BAB55267.1 .
AK292343 mRNA. Translation: BAF85032.1 .
AL606468 , AC092814 , AL592297 Genomic DNA. Translation: CAH70697.1 .
AL592297 , AC092814 , AL606468 Genomic DNA. Translation: CAH73803.1 .
CH471100 Genomic DNA. Translation: EAW93395.1 .
CH471100 Genomic DNA. Translation: EAW93397.1 .
BC033540 mRNA. Translation: AAH33540.1 .
BC033297 mRNA. Translation: AAH33297.1 .
CCDSi CCDS1502.1. [Q9NZJ0-1 ]
RefSeqi NP_001273158.1. NM_001286229.1.
NP_057532.3. NM_016448.3.
UniGenei Hs.656473.

3D structure databases

ProteinModelPortali Q9NZJ0.
SMRi Q9NZJ0. Positions 9-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119582. 37 interactions.
IntActi Q9NZJ0. 8 interactions.
STRINGi 9606.ENSP00000355958.

PTM databases

PhosphoSitei Q9NZJ0.

Polymorphism databases

DMDMi 302393825.

Proteomic databases

MaxQBi Q9NZJ0.
PaxDbi Q9NZJ0.
PRIDEi Q9NZJ0.

Protocols and materials databases

DNASUi 51514.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366991 ; ENSP00000355958 ; ENSG00000143476 . [Q9NZJ0-1 ]
GeneIDi 51514.
KEGGi hsa:51514.
UCSCi uc001hiz.4. human. [Q9NZJ0-1 ]

Organism-specific databases

CTDi 51514.
GeneCardsi GC01P212208.
H-InvDB HIX0020157.
HGNCi HGNC:30288. DTL.
HPAi HPA028016.
HPA032023.
HPA032031.
HPA032032.
MIMi 610617. gene.
neXtProti NX_Q9NZJ0.
PharmGKBi PA142671941.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00530000064210.
HOVERGENi HBG057737.
InParanoidi Q9NZJ0.
KOi K11790.
OMAi ICTYFHR.
OrthoDBi EOG7W153G.
PhylomeDBi Q9NZJ0.
TreeFami TF324483.

Enzyme and pathway databases

UniPathwayi UPA00143 .
SignaLinki Q9NZJ0.

Miscellaneous databases

GeneWikii DTL_(gene).
GenomeRNAii 51514.
NextBioi 55210.
PROi Q9NZJ0.
SOURCEi Search...

Gene expression databases

Bgeei Q9NZJ0.
CleanExi HS_DTL.
ExpressionAtlasi Q9NZJ0. baseline and differential.
Genevestigatori Q9NZJ0.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF00400. WD40. 4 hits.
[Graphical view ]
SMARTi SM00320. WD40. 6 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 2 hits.
PROSITEi PS00678. WD_REPEATS_1. 2 hits.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of a novel nuclear matrix-associated protein that is regulated during the retinoic acid-induced neuronal differentiation."
    Cheung W.M., Chu A.H., Chu P.W., Ip N.Y.
    J. Biol. Chem. 276:17083-17091(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, VARIANTS VAL-436 AND THR-694.
  2. "L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and regulates CDT1 proteolysis in response to DNA damage."
    Higa L.A., Banks D., Wu M., Kobayashi R., Sun H., Zhang H.
    Cell Cycle 5:1675-1680(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN A DCX (DDB1-CUL4-X-BOX) E3 UBIQUITIN-PROTEIN LIGASE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, VARIANTS VAL-436 AND THR-694.
  3. "Identification of L2DTL, a human WD-40 repeat gene homolog of the Drosophila lethal (2) denticleless heat shock gene [l(2)dtl]."
    Mueller R., Ziegler B.L.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS VAL-436 AND THR-694.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS VAL-436 AND THR-694.
    Tissue: Hepatoma, Teratocarcinoma and Testis.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-436.
  7. "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] (ISOFORM 1), VARIANTS VAL-436 AND THR-694.
    Tissue: Lymph and Testis.
  8. "Role of L2DTL, cell cycle-regulated nuclear and centrosome protein, in aggressive hepatocellular carcinoma."
    Pan H.W., Chou H.Y., Liu S.H., Peng S.Y., Liu C.L., Hsu H.C.
    Cell Cycle 5:2676-2687(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, UBIQUITINATION.
  9. "DTL/CDT2 is essential for both CDT1 regulation and the early G2/M checkpoint."
    Sansam C.L., Shepard J.L., Lai K., Ianari A., Danielian P.S., Amsterdam A., Hopkins N., Lees J.A.
    Genes Dev. 20:3117-3129(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A DCX (DDB1-CUL4-X-BOX) E3 UBIQUITIN-PROTEIN LIGASE COMPLEX.
  10. "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1."
    Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.
    Mol. Cell 23:709-721(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DDB1, IDENTIFICATION IN A DCX (DDB1-CUL4-X-BOX) E3 UBIQUITIN-PROTEIN LIGASE COMPLEX, MUTAGENESIS OF ARG-246.
  11. "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation."
    Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.
    Nat. Cell Biol. 8:1277-1283(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A DCX (DDB1-CUL4-X-BOX) E3 UBIQUITIN-PROTEIN LIGASE COMPLEX.
  12. "Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery."
    Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.
    Nature 443:590-593(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex."
    Abbas T., Sivaprasad U., Terai K., Amador V., Pagano M., Dutta A.
    Genes Dev. 22:2496-2506(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A DCX (DDB1-CUL4-X-BOX) E3 UBIQUITIN-PROTEIN LIGASE COMPLEX.
  14. "The CRL4Cdt2 ubiquitin ligase targets the degradation of p21Cip1 to control replication licensing."
    Kim Y., Starostina N.G., Kipreos E.T.
    Genes Dev. 22:2507-2519(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A DCX (DDB1-CUL4-X-BOX) E3 UBIQUITIN-PROTEIN LIGASE COMPLEX.
  15. "CDK inhibitor p21 is degraded by a proliferating cell nuclear antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV irradiation."
    Nishitani H., Shiomi Y., Iida H., Michishita M., Takami T., Tsurimoto T.
    J. Biol. Chem. 283:29045-29052(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485; SER-490; SER-495; SER-512; THR-516; SER-557; SER-676; SER-679 AND THR-684, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "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].
  18. "Ionizing radiation induces ATM-independent degradation of p21Cip1 in transformed cells."
    Stuart S.A., Wang J.Y.
    J. Biol. Chem. 284:15061-15070(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "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 SER-512 AND THR-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis."
    Terai K., Abbas T., Jazaeri A.A., Dutta A.
    Mol. Cell 37:143-149(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "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-410; SER-490; SER-512 AND THR-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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 SER-512 AND THR-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Regulation of TGF-beta signaling, exit from the cell cycle, and cellular migration through cullin cross-regulation: SCF-FBXO11 turns off CRL4-Cdt2."
    Abbas T., Keaton M., Dutta A.
    Cell Cycle 12:2175-2182(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  27. "CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration."
    Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.
    Mol. Cell 49:1147-1158(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DDB1 AND FBXO11, INDUCTION, UBIQUITINATION, MUTAGENESIS OF ARG-246; ASP-457 AND SER-462.
  28. "Regulation of the CRL4(Cdt2) ubiquitin ligase and cell-cycle exit by the SCF(Fbxo11) ubiquitin ligase."
    Rossi M., Duan S., Jeong Y.T., Horn M., Saraf A., Florens L., Washburn M.P., Antebi A., Pagano M.
    Mol. Cell 49:1159-1166(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FBXO11, IDENTIFICATION IN THE DCX(DTL) COMPLEX, UBIQUITINATION, PHOSPHORYLATION AT THR-464 BY CDK1 AND CDK2, MUTAGENESIS OF ASN-463; THR-464; PRO-465; THR-466; PHE-467; SER-468; THR-471 AND SER-472.

Entry informationi

Entry nameiDTL_HUMAN
AccessioniPrimary (citable) accession number: Q9NZJ0
Secondary accession number(s): A8K8H8
, D3DT98, Q5VT77, Q96SN0, Q9NW03, Q9NW34, Q9NWM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: August 10, 2010
Last modified: October 29, 2014
This is version 117 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3