Q9NZJ0 (DTL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DTL
Synonyms:	CDT2, CDW1, DCAF2, L2DTL, RAMP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	730 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 and CDKN1A/p21(CIP1). 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. 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. Ref.2 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18
Pathway	Protein modification; protein ubiquitination.
Subunit structure	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. Ref.2 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Nucleus. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Cytoplasm › cytoskeleton › centrosome. Note: Nuclear matrix-associated protein. Translocates from the interphase nucleus to the metaphase cytoplasm during mitosis. Ref.8
Tissue specificity	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. Ref.1 Ref.8
Developmental stage	Expressed in all fetal tissues examined, included brain, lung, liver, and kidney. Ref.1
Post-translational modification	Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C). Ref.8
Sequence similarities	Belongs to the WD repeat cdt2 family. Contains 7 WD repeats.
Sequence caution	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.

Ontologies

Keywords
Biological process	DNA damage DNA replication Ubl conjugation pathway
Cellular component	Cytoplasm Cytoskeleton Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat WD repeat
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW G2 DNA damage checkpoint Inferred from mutant phenotype Ref.9. Source: UniProtKB protein monoubiquitination Inferred from direct assay Ref.18. Source: UniProtKB protein polyubiquitination Inferred from direct assay Ref.12. Source: UniProtKB regulation of cell cycle Inferred from mutant phenotype Ref.9. Source: UniProtKB response to UV Inferred from direct assay Ref.12. Source: UniProtKB translesion synthesis Inferred from direct assay Ref.18. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from direct assay Ref.12. Source: UniProtKB
Cellular_component	Cul4A-RING ubiquitin ligase complex Inferred from direct assay Ref.9Ref.12Ref.18. Source: UniProtKB Cul4B-RING ubiquitin ligase complex Inferred from direct assay Ref.12. Source: UniProtKB centrosome Inferred from direct assay Ref.8. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.8. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DDB1	Q16531	3	EBI-1176075,EBI-350322

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NZJ0-1)

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.

Isoform 2 (identifier: Q9NZJ0-2)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 730	730	Denticleless protein homolog		PRO_0000274867
Regions
	Repeat	47 – 89	43	WD 1
	Repeat	96 – 135	40	WD 2
	Repeat	138 – 178	41	WD 3
	Repeat	214 – 253	40	WD 4
	Repeat	267 – 308	42	WD 5
	Repeat	313 – 354	42	WD 6
	Repeat	358 – 398	41	WD 7
	Motif	168 – 171	4	DDB1-binding motif
	Motif	197 – 203	7	Nuclear localization signal Potential
	Motif	243 – 246	4	DDB1-binding motif
Amino acid modifications
	Modified residue	410	1	Phosphoserine Ref.19
	Modified residue	485	1	Phosphoserine Ref.15
	Modified residue	490	1	Phosphoserine Ref.15 Ref.19
	Modified residue	495	1	Phosphoserine Ref.15
	Modified residue	512	1	Phosphoserine Ref.15 Ref.17 Ref.19 Ref.21
	Modified residue	516	1	Phosphothreonine Ref.15 Ref.17 Ref.19 Ref.21
	Modified residue	557	1	Phosphoserine Ref.15
	Modified residue	599	1	Phosphoserine By similarity
	Modified residue	676	1	Phosphoserine Ref.15
	Modified residue	679	1	Phosphoserine Ref.15
	Modified residue	684	1	Phosphothreonine Ref.15
Natural variations
	Alternative sequence	18 – 59	42	Missing in isoform 2.		VSP_022879
	Alternative sequence	240 – 253	14	IKVWD…YTAYR → FKSDFGFHWLYFIC in isoform 2.		VSP_022880
	Alternative sequence	254 – 730	477	Missing in isoform 2.		VSP_022881
	Natural variant	425	1	S → N. Corresponds to variant rs35137676 [ dbSNP | Ensembl ].		VAR_062095
	Natural variant	436	1	A → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.7 Corresponds to variant rs3135474 [ dbSNP | Ensembl ].		VAR_030353
	Natural variant	694	1	K → T. Ref.1 Ref.2 Ref.3 Ref.4 Ref.7 Corresponds to variant rs6540718 [ dbSNP | Ensembl ].		VAR_030354
Experimental info
	Mutagenesis	246	1	R → A: Blocks association with DDB1. Ref.10
	Sequence conflict	83	1	S → P in BAA91355. Ref.4
	Sequence conflict	356	1	L → F in BAF85032. Ref.4
	Sequence conflict	532	1	I → T in BAA91552. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 10, 2010. Version 3. Checksum: CE8D54234D44F002	FASTA	730	79,468
	10 20 30 40 50 60 MLFNSVLRQP QLGVLRNGWS SQYPLQSLLT GYQCSGNDEH TSYGETGVPV PPFGCTFSSA 70 80 90 100 110 120 PNMEHVLAVA NEEGFVRLYN TESQSFRKKC FKEWMAHWNA VFDLAWVPGE LKLVTAAGDQ 130 140 150 160 170 180 TAKFWDVKAG ELIGTCKGHQ CSLKSVAFSK FEKAVFCTGG RDGNIMVWDT RCNKKDGFYR 190 200 210 220 230 240 QVNQISGAHN TSDKQTPSKP KKKQNSKGLA PSVDFQQSVT VVLFQDENTL VSAGAVDGII 250 260 270 280 290 300 KVWDLRKNYT AYRQEPIASK SFLYPGSSTR KLGYSSLILD STGSTLFANC TDDNIYMFNM 310 320 330 340 350 360 TGLKTSPVAI FNGHQNSTFY VKSSLSPDDQ FLVSGSSDEA AYIWKVSTPW QPPTVLLGHS 370 380 390 400 410 420 QEVTSVCWCP SDFTKIATCS DDNTLKIWRL NRGLEEKPGG DKLSTVGWAS QKKKESRPGL 430 440 450 460 470 480 VTVTSSQSTP AKAPRAKCNP SNSSPSSAAC APSCAGDLPL PSNTPTFSIK TSPAKARSPI 490 500 510 520 530 540 NRRGSVSSVS PKPPSSFKMS IRNWVTRTPS SSPPITPPAS ETKIMSPRKA LIPVSQKSSQ 550 560 570 580 590 600 AEACSESRNR VKRRLDSSCL ESVKQKCVKS CNCVTELDGQ VENLHLDLCC LAGNQEDLSK 610 620 630 640 650 660 DSLGPTKSSK IEGAGTSISE PPSPISPYAS ESCGTLPLPL RPCGEGSEMV GKENSSPENK 670 680 690 700 710 720 NWLLAMAAKR KAENPSPRSP SSQTPNSRRQ SGKKLPSPVT ITPSSMRKIC TYFHRKSQED 730 FCGPEHSTEL
	Isoform 2 [UniParc]. Checksum: 23E4B52CFC514F80	FASTA	211	23,682
	10 20 30 40 50 60 MLFNSVLRQP QLGVLRNAPN MEHVLAVANE EGFVRLYNTE SQSFRKKCFK EWMAHWNAVF 70 80 90 100 110 120 DLAWVPGELK LVTAAGDQTA KFWDVKAGEL IGTCKGHQCS LKSVAFSKFE KAVFCTGGRD 130 140 150 160 170 180 GNIMVWDTRC NKKDGFYRQV NQISGAHNTS DKQTPSKPKK KQNSKGLAPS VDFQQSVTVV 190 200 210 LFQDENTLVS AGAVDGIFKS DFGFHWLYFI C

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"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.
[13]	"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.
[14]	"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.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485; SER-490; SER-495; SER-512; THR-516; SER-557; SER-676; SER-679 AND THR-684, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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.
[17]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"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.
[19]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00643808. IPI00827740.
RefSeq	NP_057532.2. NM_016448.2.
UniGene	Hs.656473.
3D structure databases
ProteinModelPortal	Q9NZJ0.
SMR	Q9NZJ0. Positions 9-393.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NZJ0. 8 interactions.
STRING	9606.ENSP00000355958.
PTM databases
PhosphoSite	Q9NZJ0.
Polymorphism databases
DMDM	302393825.
Proteomic databases
PaxDb	Q9NZJ0.
PRIDE	Q9NZJ0.
Protocols and materials databases
DNASU	51514.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000366991; ENSP00000355958; ENSG00000143476.
GeneID	51514.
KEGG	hsa:51514.
UCSC	uc001hiz.4. human.
Organism-specific databases
CTD	51514.
GeneCards	GC01P212208.
H-InvDB	HIX0020157.
HGNC	HGNC:30288. DTL.
HPA	HPA028016.
MIM	610617. gene.
neXtProt	NX_Q9NZJ0.
PharmGKB	PA142671941.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2319.
HOVERGEN	HBG057737.
InParanoid	Q9NZJ0.
KO	K11790.
OMA	ICTYFHR.
OrthoDB	EOG4N5VWH.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q9NZJ0.
Bgee	Q9NZJ0.
CleanEx	HS_DTL.
Genevestigator	Q9NZJ0.
Family and domain databases
Gene3D	2.130.10.10. 1 hit.
InterPro	IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR019775. WD40_repeat_CS. IPR017986. WD40_repeat_dom. [Graphical view]
Pfam	PF00400. WD40. 4 hits. [Graphical view]
SMART	SM00320. WD40. 6 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. 2 hits. PS50082. WD_REPEATS_2. 5 hits. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	51514.
NextBio	55210.
SOURCE	Search...

Entry information

Entry name

DTL_HUMAN

Accession

Primary (citable) accession number: Q9NZJ0
Secondary accession number(s): A8K8H8 , D3DT98, Q5VT77, Q96SN0, Q9NW03, Q9NW34, Q9NWM5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 6, 2007
Last sequence update:	August 10, 2010
Last modified:	May 1, 2013
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.