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Protein

DNA damage-binding protein 1

Gene

DDB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 SKP2.20 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: UniProtKB
  3. interaction with symbiont Source: AgBase
  4. negative regulation of apoptotic process Source: Ensembl
  5. nucleotide-excision repair Source: Reactome
  6. nucleotide-excision repair, DNA damage removal Source: Reactome
  7. positive regulation by virus of viral protein levels in host cell Source: AgBase
  8. positive regulation of viral genome replication Source: AgBase
  9. positive regulation of viral release from host cell Source: AgBase
  10. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  11. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  12. regulation of mitotic cell cycle phase transition Source: UniProtKB
  13. UV-damage excision repair Source: UniProtKB
  14. viral process Source: UniProtKB-KW
  15. 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

BRENDAi6.3.2.19. 2681.
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 Componenti: 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: UniProtKB
  6. extracellular vesicular exosome Source: UniProtKB
  7. nucleoplasm Source: HPA
  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.
HPA045174.

Interactioni

Subunit structurei

Component of the UV-DDB complex which includes DDB1 and DDB2; the heterodimer dimerizes to give rise to a heterotetramer when bound to damaged DNA (PubMed:22822215). 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, CRBN, DCAF1, DCAF4, DCAF5, DCAF6, DCAF7, DCAF8, DCAF9, DCAF10, DCAF11, DCAF12, DCAF15, DCAF16, DCAF17, DDA1, DET1, DTL, ERCC8, FBXW5, FBXW8, GRWD1, KATNB1, NLE1, NUP43, PAFAH1B1, PHIP, PWP1, RBBP4, RBBP5, RBBP7, RFWD2, SNRNP40, VPRBP, WDR5, WDR5B, WDR12, WDR26, WDR39, WDR42, WDR53, WDR59, WDR61, 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. Interacts with the hepatitis B virus protein HBX, the woodchuck hepatitis virus X protein WHX and the paramyxovirus protein SV5-V; these viral proteins contain a short helical motif that competes for the same binding site as the N-terminal helical motif found in endogenous DCAF proteins (PubMed:19966799). 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. Interacts with TRPC4AP (PubMed:19966799).33 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
VPRBPQ9Y4B6-32EBI-350322,EBI-9915372
vpxP180452EBI-350322,EBI-6558105From a different organism.

Protein-protein interaction databases

BioGridi108009. 219 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 – 107Combined sources
Beta strandi17 – 215Combined sources
Beta strandi26 – 283Combined sources
Beta strandi30 – 356Combined sources
Beta strandi38 – 458Combined sources
Beta strandi48 – 569Combined sources
Beta strandi61 – 677Combined sources
Beta strandi72 – 743Combined sources
Beta strandi76 – 816Combined sources
Turni82 – 843Combined sources
Beta strandi85 – 928Combined sources
Beta strandi95 – 973Combined sources
Beta strandi99 – 1079Combined sources
Beta strandi121 – 1244Combined sources
Beta strandi128 – 1347Combined sources
Beta strandi139 – 1446Combined sources
Beta strandi146 – 1483Combined sources
Beta strandi155 – 1584Combined sources
Beta strandi164 – 1696Combined sources
Beta strandi177 – 1848Combined sources
Beta strandi187 – 19610Combined sources
Turni197 – 2004Combined sources
Beta strandi201 – 2044Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi218 – 2214Combined sources
Turni224 – 2263Combined sources
Beta strandi229 – 2324Combined sources
Beta strandi237 – 2415Combined sources
Beta strandi244 – 2485Combined sources
Helixi251 – 2555Combined sources
Beta strandi258 – 2636Combined sources
Beta strandi268 – 2758Combined sources
Beta strandi279 – 28810Combined sources
Beta strandi291 – 2933Combined sources
Beta strandi296 – 30712Combined sources
Beta strandi312 – 3165Combined sources
Turni318 – 3203Combined sources
Beta strandi321 – 3255Combined sources
Beta strandi327 – 3293Combined sources
Beta strandi331 – 3366Combined sources
Helixi342 – 3443Combined sources
Beta strandi347 – 3537Combined sources
Beta strandi358 – 3658Combined sources
Beta strandi369 – 3713Combined sources
Beta strandi374 – 3796Combined sources
Helixi382 – 3843Combined sources
Beta strandi386 – 3949Combined sources
Beta strandi396 – 4027Combined sources
Beta strandi409 – 4135Combined sources
Beta strandi417 – 4193Combined sources
Beta strandi420 – 4223Combined sources
Beta strandi424 – 4296Combined sources
Beta strandi432 – 4398Combined sources
Beta strandi442 – 4465Combined sources
Beta strandi449 – 4513Combined sources
Beta strandi453 – 4553Combined sources
Beta strandi457 – 4637Combined sources
Turni464 – 4663Combined sources
Beta strandi467 – 4748Combined sources
Beta strandi476 – 4838Combined sources
Beta strandi486 – 4905Combined sources
Beta strandi493 – 4953Combined sources
Beta strandi500 – 5034Combined sources
Beta strandi505 – 5128Combined sources
Beta strandi515 – 5228Combined sources
Beta strandi525 – 5339Combined sources
Beta strandi535 – 5373Combined sources
Beta strandi538 – 5425Combined sources
Beta strandi547 – 5493Combined sources
Beta strandi550 – 5523Combined sources
Beta strandi554 – 5607Combined sources
Turni561 – 5644Combined sources
Beta strandi565 – 5706Combined sources
Turni571 – 5733Combined sources
Beta strandi576 – 5816Combined sources
Beta strandi583 – 5853Combined sources
Beta strandi588 – 5969Combined sources
Beta strandi599 – 6068Combined sources
Beta strandi609 – 6168Combined sources
Turni618 – 6203Combined sources
Beta strandi623 – 6308Combined sources
Beta strandi637 – 6459Combined sources
Beta strandi647 – 6559Combined sources
Beta strandi657 – 67418Combined sources
Beta strandi678 – 6825Combined sources
Beta strandi685 – 6873Combined sources
Beta strandi690 – 6945Combined sources
Beta strandi696 – 6983Combined sources
Beta strandi699 – 7046Combined sources
Beta strandi707 – 71610Combined sources
Beta strandi718 – 72710Combined sources
Helixi728 – 7303Combined sources
Beta strandi732 – 74312Combined sources
Beta strandi745 – 7539Combined sources
Helixi756 – 7594Combined sources
Beta strandi761 – 7655Combined sources
Beta strandi781 – 7833Combined sources
Beta strandi785 – 79511Combined sources
Turni796 – 7983Combined sources
Beta strandi801 – 8066Combined sources
Beta strandi811 – 8199Combined sources
Beta strandi823 – 8264Combined sources
Beta strandi828 – 8358Combined sources
Beta strandi840 – 8423Combined sources
Beta strandi846 – 8549Combined sources
Beta strandi857 – 86812Combined sources
Beta strandi870 – 8767Combined sources
Beta strandi879 – 8846Combined sources
Beta strandi887 – 8937Combined sources
Beta strandi895 – 8973Combined sources
Beta strandi899 – 9057Combined sources
Beta strandi911 – 9177Combined sources
Beta strandi920 – 9289Combined sources
Beta strandi930 – 9367Combined sources
Turni937 – 9404Combined sources
Beta strandi941 – 9477Combined sources
Beta strandi954 – 9618Combined sources
Beta strandi964 – 9696Combined sources
Beta strandi972 – 9798Combined sources
Beta strandi982 – 9843Combined sources
Turni985 – 9873Combined sources
Helixi988 – 9903Combined sources
Beta strandi991 – 9999Combined sources
Beta strandi1004 – 10096Combined sources
Beta strandi1017 – 10204Combined sources
Beta strandi1024 – 10329Combined sources
Beta strandi1037 – 10437Combined sources
Helixi1045 – 106117Combined sources
Helixi1065 – 10673Combined sources
Helixi1070 – 10745Combined sources
Beta strandi1075 – 10773Combined sources
Beta strandi1081 – 10833Combined sources
Beta strandi1086 – 10905Combined sources
Helixi1091 – 10955Combined sources
Helixi1096 – 10994Combined sources
Helixi1102 – 11087Combined sources
Turni1109 – 11113Combined sources
Beta strandi1117 – 11204Combined sources
Helixi1127 – 113610Combined sources
Helixi1137 – 11393Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.1 Publication

Sequence similaritiesi

Belongs to the DDB1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG247734.
GeneTreeiENSGT00530000063396.
HOGENOMiHOG000007241.
HOVERGENiHBG005460.
InParanoidiQ16531.
KOiK10610.
OMAiQVIDVKF.
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. AlignAdd to basket

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:October 31, 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 (Ref. 4) Curated
Sequence conflicti869 – 8691A → D in CAA05770 (Ref. 4) Curated
Sequence conflicti898 – 8992EL → DV in AAA88883 (PubMed:8538642).Curated
Sequence conflicti898 – 8992EL → DV in CAA05770 (Ref. 4) Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi108009. 219 interactions.
DIPiDIP-430N.
IntActiQ16531. 82 interactions.
MINTiMINT-1134697.
STRINGi9606.ENSP00000301764.

PTM databases

PhosphoSiteiQ16531.

Polymorphism databases

DMDMi12643730.

Proteomic databases

MaxQBiQ16531.
PaxDbiQ16531.
PRIDEiQ16531.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1642.
GeneCardsiGC11M061066.
H-InvDBHIX0171380.
HGNCiHGNC:2717. DDB1.
HPAiCAB032821.
HPA045174.
MIMi600045. gene.
neXtProtiNX_Q16531.
PharmGKBiPA27187.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi6.3.2.19. 2681.
ReactomeiREACT_257. Formation of incision complex in GG-NER.
REACT_311. Dual incision reaction in GG-NER.

Miscellaneous databases

ChiTaRSiDDB1. human.
EvolutionaryTraceiQ16531.
GeneWikiiDDB1.
GenomeRNAii1642.
NextBioi35471627.
PROiQ16531.
SOURCEiSearch...

Gene expression databases

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

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.
ProtoNetiSearch...

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(1994) [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(1994) [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(1995) [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 (OCT-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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Amygdala and Brain.
  6. NIEHS SNPs program
    Submitted (FEB-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(2003) [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(1997) [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(1999) [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(2000) [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(2000) [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(2002) [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(2002) [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(2003) [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(2003) [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(2004) [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(2004) [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(2004) [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(2004) [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(2005) [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(2005) [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(2005) [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(2005) [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(2005) [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(2005) [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(2005) [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(2005) [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(2005) [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(2006) [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(2007) [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(2007) [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(2007) [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(2007) [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(2008) [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(2008) [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(2008) [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(2011) [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(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DTL.
  43. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  44. "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(2005) [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.
  45. "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(2005) [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.
  46. Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) IN COMPLEX WITH DDB2 AND DNA, WD BETA-PROPELLER DOMAINS, SUBUNIT.
  47. "A promiscuous alpha-helical motif anchors viral hijackers and substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery."
    Li T., Robert E.I., van Breugel P.C., Strubin M., Zheng N.
    Nat. Struct. Mol. Biol. 17:105-111(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), FUNCTION AS UBIQUITIN LIGASE COMPONENT, SUBUNIT, INTERACTION WITH TRPC4AP; DCAF4; DCAF5; DCAF6; DCAF8; DCAF9; DCAF12; DDB2; HEPATITIS VIRUS PROTEIN HBX; WOODCHUCK HEPATITIS VIRUS PROTEIN WHX AND PARAMYXOVIRUS PROTEIN SV5-V.
  48. "The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation."
    Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M., Faty M., Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S., Gut H., Sugasawa K., Thoma N.H.
    Cell 147:1024-1039(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEXES WITH DDB2; ERCC8 AND CUL4B, FUNCTION, SUBUNIT.
  49. "Structure and function of WD40 domain proteins."
    Xu C., Min J.
    Protein Cell 2:202-214(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS), DOMAIN.
  50. "Damaged DNA induced UV-damaged DNA-binding protein (UV-DDB) dimerization and its roles in chromatinized DNA repair."
    Yeh J.I., Levine A.S., Du S., Chinte U., Ghodke H., Wang H., Shi H., Hsieh C.L., Conway J.F., Van Houten B., Rapic-Otrin V.
    Proc. Natl. Acad. Sci. U.S.A. 109:E2737-E2746(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS), SUBUNIT, INTERACTION WITH DDB2.
  51. Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH CRBN, INTERACTION WITH CRBN, FUNCTION IN PROTEIN UBIQUITINATION.
  52. Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) IN COMPLEX WITH CRBN, INTERACTION WITH CRBN, FUNCTION.

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 10, 2001
Last sequence update: October 31, 1996
Last modified: March 31, 2015
This is version 151 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.