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Q16531

- DDB1_HUMAN

UniProt

Q16531 - DDB1_HUMAN

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
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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
    3. nucleic acid binding Source: InterPro
    4. protein binding Source: UniProtKB

    GO - Biological processi

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

    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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi316 – 3194YLDN → ALAA: Impairs interaction with DDA1.
    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.
    Mutagenesisi910 – 9134MALY → AAAA: Impairs interaction with AMBRA1, DTL and DCAF5.
    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

    ArrayExpressiQ16531.
    BgeeiQ16531.
    CleanExiHS_DDB1.
    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. 194 interactions.
    DIPiDIP-430N.
    IntActiQ16531. 81 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[»]
    4E54X-ray2.85A2-1140[»]
    4E5ZX-ray3.22A2-1140[»]
    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.
    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

    MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR     50
    PVKEVGMYGK IAVMELFRPK GESKDLLFIL TAKYNACILE YKQSGESIDI 100
    ITRAHGNVQD RIGRPSETGI IGIIDPECRM IGLRLYDGLF KVIPLDRDNK 150
    ELKAFNIRLE ELHVIDVKFL YGCQAPTICF VYQDPQGRHV KTYEVSLREK 200
    EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH NGDKYLAIAP 250
    PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL 300
    RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM 350
    ETFTNLGPIV DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA 400
    SIDLPGIKGL WPLRSDPNRE TDDTLVLSFV GQTRVLMLNG EEVEETELMG 450
    FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS QEPKALVSEW KEPQAKNISV 500
    ASCNSSQVVV AVGRALYYLQ IHPQELRQIS HTEMEHEVAC LDITPLGDSN 550
    GLSPLCAIGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH 600
    YLLCALGDGA LFYFGLNIET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF 650
    ACSDRPTVIY SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT 700
    IGTIDEIQKL HIRTVPLYES PRKICYQEVS QCFGVLSSRI EVQDTSGGTT 750
    ALRPSASTQA LSSSVSSSKL FSSSTAPHET SFGEEVEVHN LLIIDQHTFE 800
    VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE AEPKQGRIVV 850
    FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTTEKELR 900
    TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN 950
    PNWMSAVEIL DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLFHL 1000
    GEFVNVFCHG SLVMQNLGET STPTQGSVLF GTVNGMIGLV TSLSESWYNL 1050
    LLDMQNRLNK VIKSVGKIEH SFWRSFHTER KTEPATGFID GDLIESFLDI 1100
    SRPKMQEVVA NLQYDDGSGM KREATADDLI KVVEELTRIH 1140
    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.
    PIRiI38908.
    RefSeqiNP_001914.3. NM_001923.4.
    UniGeneiHs.290758.

    Genome annotation databases

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

    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.
    PIRi I38908.
    RefSeqi NP_001914.3. NM_001923.4.
    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 [» ]
    4E54 X-ray 2.85 A 2-1140 [» ]
    4E5Z X-ray 3.22 A 2-1140 [» ]
    ProteinModelPortali Q16531.
    SMRi Q16531. Positions 2-1140.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108009. 194 interactions.
    DIPi DIP-430N.
    IntActi Q16531. 81 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.

    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.
    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 6750.
    PROi Q16531.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16531.
    Bgeei Q16531.
    CleanExi HS_DDB1.
    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

    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 1, 2014
    This is version 145 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