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Q16531

- DDB1_HUMAN

UniProt

Q16531 - DDB1_HUMAN

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Protein

DNA damage-binding protein 1

Gene

DDB1

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

Functioni

Required for DNA repair. Binds to DDB2 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). May also play a role in ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2.16 Publications

Pathwayi

GO - Molecular functioni

  1. damaged DNA binding Source: ProtInc
  2. DNA binding Source: ProtInc

GO - Biological processi

  1. DNA repair Source: Reactome
  2. histone H2A monoubiquitination Source: UniProt
  3. negative regulation of apoptotic process Source: Ensembl
  4. nucleotide-excision repair Source: Reactome
  5. nucleotide-excision repair, DNA damage removal Source: Reactome
  6. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  7. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  8. regulation of mitotic cell cycle phase transition Source: UniProtKB
  9. UV-damage excision repair Source: UniProt
  10. viral process Source: UniProtKB-KW
  11. Wnt signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Host-virus interaction, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_257. Formation of incision complex in GG-NER.
REACT_311. Dual incision reaction in GG-NER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA damage-binding protein 1
Alternative name(s):
DDB p127 subunit
DNA damage-binding protein a
Short name:
DDBa
Damage-specific DNA-binding protein 1
HBV X-associated protein 1
Short name:
XAP-1
UV-damaged DNA-binding factor
UV-damaged DNA-binding protein 1
Short name:
UV-DDB 1
XPE-binding factor
Short name:
XPE-BF
Xeroderma pigmentosum group E-complementing protein
Short name:
XPCe
Gene namesi
Name:DDB1
Synonyms:XAP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:2717. DDB1.

Subcellular locationi

Cytoplasm. Nucleus
Note: Primarily cytoplasmic. Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage.

GO - Cellular componenti

  1. Cul4A-RING E3 ubiquitin ligase complex Source: UniProtKB
  2. Cul4B-RING E3 ubiquitin ligase complex Source: UniProtKB
  3. Cul4-RING E3 ubiquitin ligase complex Source: UniProtKB
  4. cytoplasm Source: UniProtKB
  5. extracellular space Source: UniProt
  6. extracellular vesicular exosome Source: UniProt
  7. nucleoplasm Source: Reactome
  8. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi316 – 3194YLDN → ALAA: Impairs interaction with DDA1. 1 Publication
Mutagenesisi537 – 5371E → A: Slightly impairs interaction with CUL4A. 1 Publication
Mutagenesisi561 – 5611W → A: Strongly impairs interaction with CUL4A. 1 Publication
Mutagenesisi840 – 8423EAE → AAA: Impairs interaction with AMBRA1, DTL, DET1, VPRBP, DCAF5, DCAF11 and DCAF8. 1 Publication
Mutagenesisi910 – 9134MALY → AAAA: Impairs interaction with AMBRA1, DTL and DCAF5. 1 Publication
Mutagenesisi953 – 9531W → A: Impairs interaction with AMBRA1, ERCC8, DCAF5 and DCAF11. 1 Publication

Organism-specific databases

PharmGKBiPA27187.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11401139DNA damage-binding protein 1PRO_0000079840Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei1067 – 10671N6-acetyllysine1 Publication

Post-translational modificationi

Phosphorylated by ABL1.By similarity
Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ16531.
PaxDbiQ16531.
PRIDEiQ16531.

PTM databases

PhosphoSiteiQ16531.

Expressioni

Gene expression databases

BgeeiQ16531.
CleanExiHS_DDB1.
ExpressionAtlasiQ16531. baseline and differential.
GenevestigatoriQ16531.

Organism-specific databases

HPAiCAB032821.

Interactioni

Subunit structurei

Component of the UV-DDB complex which includes DDB1 and DDB2. The UV-DDB complex interacts with monoubiquitinated histone H2A and binds to XPC via the DDB2 subunit. Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1. DDB1 may recruit specific substrate targeting subunits to the DCX complex. These substrate targeting subunits are generally known as DCAF (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins. Interacts with AMBRA1, ATG16L1, BTRC, DCAF1, DCAF17, DCAF16, DCAF15, DDA1, DET1, DTL, ERCC8, FBXW5, FBXW8, GRWD1, DCAF6, KATNB1, NLE1, NUP43, PAFAH1B1, PHIP, PWP1, RBBP4, RBBP5, RBBP7, RFWD2, SNRNP40, VPRBP, WDR5, WDR5B, WDR12, DCAF4, DCAF5, DCAF11, WDR26, DCAF10, WDR39, DCAF12, WDR42, DCAF8, WDR53, WDR59, WDR61, DCAF7, WSB1, WSB2, LRWD1 and WDTC1. DCX complexes may associate with the COP9 signalosome, and this inhibits the E3 ubiquitin-protein ligase activity of the complex. Interacts with NF2, TSC1 and TSC2. Interacts with Simian virus 5 protein V and the HBV X protein. Interaction with SV5 protein V may prevent the recruitment of DCAF proteins to DCX complexes. Interacts with AGO1 and AGO2. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP proteins (EDVP complex). Interacts directly with DYRK2. DCX(DTL) complex interacts with FBXO11; does not ubiquitinate and degradate FBXO11.28 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTR5Q9H9F93EBI-350322,EBI-769418
CUL4AQ136194EBI-350322,EBI-456106
CUL4BQ1362015EBI-350322,EBI-456067
DDB2Q924663EBI-350322,EBI-1176171
DTLQ9NZJ03EBI-350322,EBI-1176075
EEDO755304EBI-350322,EBI-923794
INO80Q9ULG14EBI-350322,EBI-769345
P/VP112073EBI-350322,EBI-6148694From a different organism.
STAT1P422242EBI-350322,EBI-1057697
TLE2Q047252EBI-350322,EBI-1176061
VPRBPQ9Y4B63EBI-350322,EBI-1996353
vpxP180452EBI-350322,EBI-6558105From a different organism.

Protein-protein interaction databases

BioGridi108009. 205 interactions.
DIPiDIP-430N.
IntActiQ16531. 82 interactions.
MINTiMINT-1134697.
STRINGi9606.ENSP00000301764.

Structurei

Secondary structure

1
1140
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107
Beta strandi17 – 215
Beta strandi26 – 283
Beta strandi30 – 356
Beta strandi38 – 458
Beta strandi48 – 569
Beta strandi61 – 677
Beta strandi72 – 743
Beta strandi76 – 816
Turni82 – 843
Beta strandi85 – 928
Beta strandi95 – 973
Beta strandi99 – 1079
Beta strandi121 – 1244
Beta strandi128 – 1347
Beta strandi139 – 1446
Beta strandi146 – 1483
Beta strandi155 – 1584
Beta strandi164 – 1696
Beta strandi177 – 1848
Beta strandi187 – 19610
Turni197 – 2004
Beta strandi201 – 2044
Beta strandi210 – 2123
Beta strandi218 – 2214
Turni224 – 2263
Beta strandi229 – 2324
Beta strandi237 – 2415
Beta strandi244 – 2485
Helixi251 – 2555
Beta strandi258 – 2636
Beta strandi268 – 2758
Beta strandi279 – 28810
Beta strandi291 – 2933
Beta strandi296 – 30712
Beta strandi312 – 3165
Beta strandi321 – 3255
Beta strandi327 – 3293
Beta strandi331 – 3366
Helixi342 – 3443
Beta strandi347 – 3537
Beta strandi358 – 3658
Beta strandi369 – 3713
Beta strandi374 – 3796
Helixi382 – 3843
Beta strandi386 – 3949
Beta strandi396 – 4027
Beta strandi409 – 4135
Beta strandi417 – 4193
Beta strandi420 – 4223
Beta strandi424 – 4296
Beta strandi432 – 4398
Beta strandi442 – 4465
Beta strandi449 – 4513
Beta strandi453 – 4553
Beta strandi457 – 4637
Turni464 – 4663
Beta strandi467 – 4748
Beta strandi476 – 4838
Beta strandi486 – 4905
Beta strandi493 – 4953
Beta strandi500 – 5034
Beta strandi505 – 5128
Beta strandi515 – 5228
Beta strandi525 – 5339
Beta strandi535 – 5373
Beta strandi538 – 5425
Beta strandi547 – 5493
Beta strandi550 – 5523
Beta strandi554 – 5607
Turni561 – 5644
Beta strandi565 – 5706
Turni571 – 5733
Beta strandi576 – 5816
Beta strandi583 – 5853
Beta strandi588 – 5969
Beta strandi599 – 6068
Beta strandi609 – 6168
Turni618 – 6203
Beta strandi623 – 6308
Beta strandi637 – 6459
Beta strandi647 – 6559
Beta strandi657 – 67418
Beta strandi678 – 6825
Beta strandi685 – 6873
Beta strandi690 – 6945
Beta strandi696 – 6983
Beta strandi699 – 7046
Beta strandi707 – 71610
Beta strandi718 – 72710
Helixi728 – 7303
Beta strandi732 – 74312
Beta strandi745 – 7539
Helixi756 – 7594
Beta strandi761 – 7655
Beta strandi781 – 7833
Beta strandi785 – 79511
Turni796 – 7983
Beta strandi801 – 8066
Beta strandi811 – 8199
Beta strandi823 – 8264
Beta strandi828 – 8358
Beta strandi840 – 8423
Beta strandi846 – 8549
Beta strandi857 – 86812
Beta strandi870 – 8767
Beta strandi879 – 8846
Beta strandi887 – 8937
Beta strandi895 – 8973
Beta strandi899 – 9057
Beta strandi911 – 9177
Beta strandi920 – 9289
Beta strandi930 – 9367
Turni937 – 9404
Beta strandi941 – 9477
Beta strandi954 – 9618
Beta strandi964 – 9696
Beta strandi972 – 9798
Beta strandi982 – 9843
Turni985 – 9873
Helixi988 – 9903
Beta strandi991 – 9999
Beta strandi1004 – 10096
Beta strandi1017 – 10204
Beta strandi1024 – 10329
Beta strandi1037 – 10437
Helixi1045 – 106117
Helixi1065 – 10673
Helixi1070 – 10745
Beta strandi1075 – 10773
Beta strandi1081 – 10833
Beta strandi1086 – 10905
Helixi1091 – 10955
Helixi1096 – 10994
Helixi1102 – 11087
Turni1109 – 11113
Beta strandi1117 – 11204
Helixi1127 – 113610
Helixi1137 – 11393

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2B5LX-ray2.85A/B1-1140[»]
2B5MX-ray2.92A1-1140[»]
2B5NX-ray2.80A/B/C/D391-709[»]
2HYEX-ray3.10A1-1140[»]
3E0CX-ray2.41A1-1140[»]
3EI1X-ray2.80A1-1140[»]
3EI2X-ray2.60A1-1140[»]
3EI3X-ray2.30A1-1140[»]
3EI4X-ray3.30A/C/E1-1140[»]
3I7HX-ray2.90A1-1140[»]
3I7KX-ray2.80A1-1140[»]
3I7LX-ray2.80A1-1140[»]
3I7NX-ray2.80A1-1140[»]
3I7OX-ray2.80A1-1140[»]
3I7PX-ray3.00A1-1140[»]
3I89X-ray3.00A1-1140[»]
3I8CX-ray2.80A1-1140[»]
3I8EX-ray3.40A/B1-1140[»]
4A08X-ray3.00A1-1140[»]
4A09X-ray3.10A1-1140[»]
4A0AX-ray3.60A1-1140[»]
4A0BX-ray3.80A/C1-1140[»]
4A0KX-ray5.93C1-1140[»]
4A0LX-ray7.40A/C1-1140[»]
4A11X-ray3.31A1-1140[»]
4CI1X-ray2.98A1-1140[»]
4CI2X-ray2.95A1-1140[»]
4CI3X-ray3.50A1-1140[»]
4E54X-ray2.85A2-1140[»]
4E5ZX-ray3.22A2-1140[»]
4TZ4X-ray3.01A2-1140[»]
ProteinModelPortaliQ16531.
SMRiQ16531. Positions 2-1140.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16531.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 768767Interaction with CDT1Add
BLAST
Regioni13 – 356344WD repeat beta-propeller AAdd
BLAST
Regioni392 – 708317WD repeat beta-propeller B; Interaction with CUL4AAdd
BLAST
Regioni709 – 1043335WD repeat beta-propeller CAdd
BLAST
Regioni771 – 1140370Interaction with CDT1 and CUL4AAdd
BLAST

Domaini

The core of the protein consists of three WD40 beta-propeller domains.

Sequence similaritiesi

Belongs to the DDB1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG247734.
GeneTreeiENSGT00530000063396.
HOGENOMiHOG000007241.
HOVERGENiHBG005460.
InParanoidiQ16531.
KOiK10610.
OMAiMCPLNSE.
OrthoDBiEOG7X0VG9.
PhylomeDBiQ16531.
TreeFamiTF105840.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR004871. Cleavage/polyA-sp_fac_asu_C.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF03178. CPSF_A. 1 hit.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16531-1) [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
MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR
60 70 80 90 100
PVKEVGMYGK IAVMELFRPK GESKDLLFIL TAKYNACILE YKQSGESIDI
110 120 130 140 150
ITRAHGNVQD RIGRPSETGI IGIIDPECRM IGLRLYDGLF KVIPLDRDNK
160 170 180 190 200
ELKAFNIRLE ELHVIDVKFL YGCQAPTICF VYQDPQGRHV KTYEVSLREK
210 220 230 240 250
EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH NGDKYLAIAP
260 270 280 290 300
PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL
310 320 330 340 350
RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM
360 370 380 390 400
ETFTNLGPIV DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA
410 420 430 440 450
SIDLPGIKGL WPLRSDPNRE TDDTLVLSFV GQTRVLMLNG EEVEETELMG
460 470 480 490 500
FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS QEPKALVSEW KEPQAKNISV
510 520 530 540 550
ASCNSSQVVV AVGRALYYLQ IHPQELRQIS HTEMEHEVAC LDITPLGDSN
560 570 580 590 600
GLSPLCAIGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH
610 620 630 640 650
YLLCALGDGA LFYFGLNIET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF
660 670 680 690 700
ACSDRPTVIY SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT
710 720 730 740 750
IGTIDEIQKL HIRTVPLYES PRKICYQEVS QCFGVLSSRI EVQDTSGGTT
760 770 780 790 800
ALRPSASTQA LSSSVSSSKL FSSSTAPHET SFGEEVEVHN LLIIDQHTFE
810 820 830 840 850
VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE AEPKQGRIVV
860 870 880 890 900
FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTTEKELR
910 920 930 940 950
TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN
960 970 980 990 1000
PNWMSAVEIL DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLFHL
1010 1020 1030 1040 1050
GEFVNVFCHG SLVMQNLGET STPTQGSVLF GTVNGMIGLV TSLSESWYNL
1060 1070 1080 1090 1100
LLDMQNRLNK VIKSVGKIEH SFWRSFHTER KTEPATGFID GDLIESFLDI
1110 1120 1130 1140
SRPKMQEVVA NLQYDDGSGM KREATADDLI KVVEELTRIH
Length:1,140
Mass (Da):126,968
Last modified:November 1, 1996 - v1
Checksum:i74D082023E3D846D
GO
Isoform 2 (identifier: Q16531-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     71-759: Missing.

Note: No experimental confirmation available.

Show »
Length:451
Mass (Da):50,611
Checksum:i3288A0DB0A0FE535
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti422 – 4221D → Y in AAA88883. (PubMed:8538642)Curated
Sequence conflicti533 – 5331E → G in CAA05770. 1 PublicationCurated
Sequence conflicti869 – 8691A → D in CAA05770. 1 PublicationCurated
Sequence conflicti898 – 8992EL → DV in AAA88883. (PubMed:8538642)Curated
Sequence conflicti898 – 8992EL → DV in CAA05770. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti427 – 4271L → F.1 Publication
Corresponds to variant rs28720299 [ dbSNP | Ensembl ].
VAR_023074

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei71 – 759689Missing in isoform 2. 1 PublicationVSP_055540Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U18299 mRNA. Translation: AAC50349.1.
L40326 mRNA. Translation: AAA62838.1.
U32986 mRNA. Translation: AAA88883.1.
AJ002955 mRNA. Translation: CAA05770.1.
AK294341 mRNA. Translation: BAG57611.1.
AK312436 mRNA. Translation: BAG35345.1.
AY960579 Genomic DNA. Translation: AAX44048.1.
AP003037 Genomic DNA. No translation available.
AP003108 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73935.1.
BC011686 mRNA. Translation: AAH11686.1.
BC050530 mRNA. Translation: AAH50530.1.
BC051764 mRNA. Translation: AAH51764.1.
CCDSiCCDS31576.1. [Q16531-1]
PIRiI38908.
RefSeqiNP_001914.3. NM_001923.4. [Q16531-1]
UniGeneiHs.290758.

Genome annotation databases

EnsembliENST00000301764; ENSP00000301764; ENSG00000167986. [Q16531-1]
GeneIDi1642.
KEGGihsa:1642.
UCSCiuc001nrc.5. human. [Q16531-1]

Polymorphism databases

DMDMi12643730.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Allelic variations of the XP genes
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U18299 mRNA. Translation: AAC50349.1 .
L40326 mRNA. Translation: AAA62838.1 .
U32986 mRNA. Translation: AAA88883.1 .
AJ002955 mRNA. Translation: CAA05770.1 .
AK294341 mRNA. Translation: BAG57611.1 .
AK312436 mRNA. Translation: BAG35345.1 .
AY960579 Genomic DNA. Translation: AAX44048.1 .
AP003037 Genomic DNA. No translation available.
AP003108 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73935.1 .
BC011686 mRNA. Translation: AAH11686.1 .
BC050530 mRNA. Translation: AAH50530.1 .
BC051764 mRNA. Translation: AAH51764.1 .
CCDSi CCDS31576.1. [Q16531-1 ]
PIRi I38908.
RefSeqi NP_001914.3. NM_001923.4. [Q16531-1 ]
UniGenei Hs.290758.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2B5L X-ray 2.85 A/B 1-1140 [» ]
2B5M X-ray 2.92 A 1-1140 [» ]
2B5N X-ray 2.80 A/B/C/D 391-709 [» ]
2HYE X-ray 3.10 A 1-1140 [» ]
3E0C X-ray 2.41 A 1-1140 [» ]
3EI1 X-ray 2.80 A 1-1140 [» ]
3EI2 X-ray 2.60 A 1-1140 [» ]
3EI3 X-ray 2.30 A 1-1140 [» ]
3EI4 X-ray 3.30 A/C/E 1-1140 [» ]
3I7H X-ray 2.90 A 1-1140 [» ]
3I7K X-ray 2.80 A 1-1140 [» ]
3I7L X-ray 2.80 A 1-1140 [» ]
3I7N X-ray 2.80 A 1-1140 [» ]
3I7O X-ray 2.80 A 1-1140 [» ]
3I7P X-ray 3.00 A 1-1140 [» ]
3I89 X-ray 3.00 A 1-1140 [» ]
3I8C X-ray 2.80 A 1-1140 [» ]
3I8E X-ray 3.40 A/B 1-1140 [» ]
4A08 X-ray 3.00 A 1-1140 [» ]
4A09 X-ray 3.10 A 1-1140 [» ]
4A0A X-ray 3.60 A 1-1140 [» ]
4A0B X-ray 3.80 A/C 1-1140 [» ]
4A0K X-ray 5.93 C 1-1140 [» ]
4A0L X-ray 7.40 A/C 1-1140 [» ]
4A11 X-ray 3.31 A 1-1140 [» ]
4CI1 X-ray 2.98 A 1-1140 [» ]
4CI2 X-ray 2.95 A 1-1140 [» ]
4CI3 X-ray 3.50 A 1-1140 [» ]
4E54 X-ray 2.85 A 2-1140 [» ]
4E5Z X-ray 3.22 A 2-1140 [» ]
4TZ4 X-ray 3.01 A 2-1140 [» ]
ProteinModelPortali Q16531.
SMRi Q16531. Positions 2-1140.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108009. 205 interactions.
DIPi DIP-430N.
IntActi Q16531. 82 interactions.
MINTi MINT-1134697.
STRINGi 9606.ENSP00000301764.

PTM databases

PhosphoSitei Q16531.

Polymorphism databases

DMDMi 12643730.

Proteomic databases

MaxQBi Q16531.
PaxDbi Q16531.
PRIDEi Q16531.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301764 ; ENSP00000301764 ; ENSG00000167986 . [Q16531-1 ]
GeneIDi 1642.
KEGGi hsa:1642.
UCSCi uc001nrc.5. human. [Q16531-1 ]

Organism-specific databases

CTDi 1642.
GeneCardsi GC11M061066.
H-InvDB HIX0171380.
HGNCi HGNC:2717. DDB1.
HPAi CAB032821.
MIMi 600045. gene.
neXtProti NX_Q16531.
PharmGKBi PA27187.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG247734.
GeneTreei ENSGT00530000063396.
HOGENOMi HOG000007241.
HOVERGENi HBG005460.
InParanoidi Q16531.
KOi K10610.
OMAi MCPLNSE.
OrthoDBi EOG7X0VG9.
PhylomeDBi Q16531.
TreeFami TF105840.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_257. Formation of incision complex in GG-NER.
REACT_311. Dual incision reaction in GG-NER.

Miscellaneous databases

ChiTaRSi DDB1. human.
EvolutionaryTracei Q16531.
GeneWikii DDB1.
GenomeRNAii 1642.
NextBioi 35471627.
PROi Q16531.
SOURCEi Search...

Gene expression databases

Bgeei Q16531.
CleanExi HS_DDB1.
ExpressionAtlasi Q16531. baseline and differential.
Genevestigatori Q16531.

Family and domain databases

Gene3Di 2.130.10.10. 2 hits.
InterProi IPR004871. Cleavage/polyA-sp_fac_asu_C.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF03178. CPSF_A. 1 hit.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Chromosomal localization and cDNA cloning of the genes (DDB1 and DDB2) for the p127 and p48 subunits of a human damage-specific DNA binding protein."
    Dualan R., Brody T., Keeney S., Nichols A.F., Admon A., Linn S.
    Genomics 29:62-69(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Epidermis and Fetal lung.
  2. "Hepatitis B virus X protein interacts with a probable cellular DNA repair protein."
    Lee T.H., Elledge S.J., Butel J.S.
    J. Virol. 69:1107-1114(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Peripheral blood.
  3. "Isolation of a cDNA encoding a UV-damaged DNA binding factor defective in xeroderma pigmentosum group E cells."
    Hwang B.J., Liao J.C., Chu G.
    Mutat. Res. 362:105-117(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Molecular cloning and characterization of human XPE protein: a component of UV-damaged DNA recognition activity."
    Huang S.L., Lin-Chao S., Chao C.K.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta and Skin.
  5. "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).
    Tissue: Amygdala and Brain.
  6. NIEHS SNPs program
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-427.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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).
    Tissue: Placenta and Skin.
  10. "p48 Activates a UV-damaged-DNA binding factor and is defective in xeroderma pigmentosum group E cells that lack binding activity."
    Hwang B.J., Toering S., Francke U., Chu G.
    Mol. Cell. Biol. 18:4391-4399(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDB1, DNA-BINDING.
  11. "Nuclear transport of human DDB protein induced by ultraviolet light."
    Liu W., Nichols A.F., Graham J.A., Dualan R., Abbas A., Linn S.
    J. Biol. Chem. 275:21429-21434(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "UV-damaged DNA-binding proteins are targets of CUL-4A-mediated ubiquitination and degradation."
    Chen X., Zhang Y., Douglas L., Zhou P.
    J. Biol. Chem. 276:48175-48182(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CUL4A, SUBCELLULAR LOCATION, UBIQUITINATION.
  13. "Hepatitis B virus X protein interferes with cell viability through interaction with the p127-kDa UV-damaged DNA-binding protein."
    Lin-Marq N., Bontron S., Leupin O., Strubin M.
    Virology 287:266-274(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HBV X PROTEIN.
  14. "The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage."
    Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y.
    Cell 113:357-367(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH CUL4A; DDB2 AND RBX1, IDENTIFICATION IN THE CSA COMPLEX WITH CUL4A; ERCC8 AND RBX1, INTERACTION OF THE CSA COMPLEX WITH RNA POLYMERASE II, INTERACTION WITH THE COP9 SIGNALOSOME.
  15. "Hepatitis B virus X protein and simian virus 5 V protein exhibit similar UV-DDB1 binding properties to mediate distinct activities."
    Leupin O., Bontron S., Strubin M.
    J. Virol. 77:6274-6283(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HBV X PROTEIN AND SV5 PROTEIN V.
  16. "Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage."
    Hu J., McCall C.M., Ohta T., Xiong Y.
    Nat. Cell Biol. 6:1003-1009(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CDT1; CUL4A; RBX1 AND THE COP9 SIGNALOSOME.
  17. "Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase."
    Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D., Deshaies R.J., Dixit V.M.
    Science 303:1371-1374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CUL4A; DET1; RBX1 AND RFWD2.
  18. "UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex."
    Sugasawa K., Okuda Y., Saijo M., Nishi R., Matsuda N., Chu G., Mori T., Iwai S., Tanaka K., Tanaka K., Hanaoka F.
    Cell 121:387-400(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUL4A; DDB2 AND RBX1, DNA-BINDING.
  19. "DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound lesions in DNA."
    Wittschieben B.O., Iwai S., Wood R.D.
    J. Biol. Chem. 280:39982-39989(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDB2, DNA-BINDING.
  20. "Simian virus 5 V protein acts as an adaptor, linking DDB1 to STAT2, to facilitate the ubiquitination of STAT1."
    Precious B., Childs K., Fitzpatrick-Swallow V., Goodbourn S., Randall R.E.
    J. Virol. 79:13434-13441(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIMIAN VIRUS 5 PROTEIN V.
  21. "Xeroderma pigmentosum complementation group E protein (XPE/DDB2): purification of various complexes of XPE and analyses of their damaged DNA binding and putative DNA repair properties."
    Kulaksiz G., Reardon J.T., Sancar A.
    Mol. Cell. Biol. 25:9784-9792(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUL4A; DDB2; RBX1 AND THE COP9 SIGNALOSOME, DNA-BINDING.
  22. Cited for: FUNCTION.
  23. "DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-ROC1 ubiquitin ligases."
    He Y.J., McCall C.M., Hu J., Zeng Y., Xiong Y.
    Genes Dev. 20:2949-2954(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ATG16L1; BTRC; CUL4A; DDB2; ERCC8; FBXW5; FBXW8; GRWD1; KATNB1; NUP43; PWP1; RBBP4; RBBP7; RFWD2; VPRBP; DCAF11; WSB1 AND WSB2.
  24. "An evolutionarily conserved function of proliferating cell nuclear antigen for Cdt1 degradation by the Cul4-Ddb1 ubiquitin ligase in response to DNA damage."
    Hu J., Xiong Y.
    J. Biol. Chem. 281:3753-3756(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. "PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination."
    Senga T., Sivaprasad U., Zhu W., Park J.H., Arias E.E., Walter J.C., Dutta A.
    J. Biol. Chem. 281:6246-6252(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  26. "Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites regulates in vivo lesion recognition by XPC."
    El-Mahdy M.A., Zhu Q., Wang Q.-E., Wani G., Praetorius-Ibba M., Wani A.A.
    J. Biol. Chem. 281:13404-13411(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CUL4A AND DDB2.
  27. "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage."
    Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H., Tempst P., Xiong Y., Zhang Y.
    Mol. Cell 22:383-394(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH DDB2; CUL4A; CUL4B AND RBX1, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  28. "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: INTERACTION WITH AMBRA1; DCAF17; DCAF16; DCAF15; DDA1; DDB2; DET1; DTL; ERCC8; DCAF6; PHIP; VPRBP; DCAF4; DCAF5; DCAF11; DCAF10; DCAF12; DCAF8; DCAF7 AND WDTC1, MUTAGENESIS OF 316-TYR--ASN-319; 840-GLU--GLU-842; 910-MET--TYR-913 AND TRP-953.
  29. "DDB1 maintains genome integrity through regulation of Cdt1."
    Lovejoy C.A., Lock K., Yenamandra A., Cortez D.
    Mol. Cell. Biol. 26:7977-7990(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "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: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CUL4B; DTL; NLE1; PAFAH1B1; RBBP5; RFWD2; SNRNP40; WDR5; WDR5B; WDR12; WDR26; WDR39; WDR53; WDR59 AND WDR61.
  31. "The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites."
    Kapetanaki M.G., Guerrero-Santoro J., Bisi D.C., Hsieh C.L., Rapic-Otrin V., Levine A.S.
    Proc. Natl. Acad. Sci. U.S.A. 103:2588-2593(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUL4A; DDB2; HISTONE H2A AND RBX1, DNA-BINDING, SUBCELLULAR LOCATION.
  32. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
    Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
    EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AGO1 AND AGO2.
  33. "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A."
    Guerrero-Santoro J., Kapetanaki M.G., Hsieh C.L., Gorbachinsky I., Levine A.S., Rapic-Otrin V.
    Cancer Res. 68:5014-5022(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUL4A; CUL4B AND DDB2, SUBCELLULAR LOCATION.
  34. "WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by DDB1-CUL4-ROC1 ligase."
    Hu J., Zacharek S., He Y.J., Lee H., Shumway S., Duronio R.J., Xiong Y.
    Genes Dev. 22:866-871(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FBXW5; TSC1 AND TSC2.
  35. "Human immunodeficiency virus type 1 Vpr-binding protein VprBP, a WD40 protein associated with the DDB1-CUL4 E3 ubiquitin ligase, is essential for DNA replication and embryonic development."
    McCall C.M., Miliani de Marval P.L., Chastain P.D. II, Jackson S.C., He Y.J., Kotake Y., Cook J.G., Xiong Y.
    Mol. Cell. Biol. 28:5621-5633(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DCAF1/VPRBP.
  36. "VprBP targets Merlin to the Roc1-Cul4A-DDB1 E3 ligase complex for degradation."
    Huang J., Chen J.
    Oncogene 27:4056-4064(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NF2.
  37. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  38. "Protein kinase DYRK2 is a scaffold that facilitates assembly of an E3 ligase."
    Maddika S., Chen J.
    Nat. Cell Biol. 11:409-419(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EDVP COMPLEX.
  39. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1067, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  41. "Orc2 protects ORCA from ubiquitin-mediated degradation."
    Shen Z., Prasanth S.G.
    Cell Cycle 11:3578-3589(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRWD1.
  42. "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: INTERACTION WITH DTL.
  43. "Structure of DDB1 in complex with a paramyxovirus V protein: viral hijack of a propeller cluster in ubiquitin ligase."
    Li T., Chen X., Garbutt K.C., Zhou P., Zheng N.
    Cell 124:105-117(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 1-1140 IN COMPLEX WITH SIMIAN VIRUS 5 PROTEIN V, INTERACTION WITH CUL4A AND DET1, MUTAGENESIS OF GLU-537 AND TRP-561.
  44. "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: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 1-1140 IN COMPLEX WITH CUL4A; RBX1 AND SIMIAN VIRUS 5 PROTEIN V, INTERACTION WITH DDB2; DTL; DCAF11; DCAF8 AND WDTC1.
  45. Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH DDB2 AND DNA, WD BETA-PROPELLER DOMAINS, SUBUNIT.

Entry informationi

Entry nameiDDB1_HUMAN
AccessioniPrimary (citable) accession number: Q16531
Secondary accession number(s): A6NG77
, B2R648, B4DG00, O15176, Q13289, Q58F96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 146 of the entry and version 1 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 11
    Human chromosome 11: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3