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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: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.2 Publications
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

GO - Molecular functioni

  • damaged DNA binding Source: ProtInc
  • DNA binding Source: ProtInc

GO - Biological processi

  • DNA damage response, detection of DNA damage Source: Reactome
  • DNA repair Source: ProtInc
  • global genome nucleotide-excision repair Source: Reactome
  • histone H2A monoubiquitination Source: UniProtKB
  • interaction with symbiont Source: AgBase
  • negative regulation of apoptotic process Source: Ensembl
  • nucleotide-excision repair Source: ProtInc
  • nucleotide-excision repair, DNA damage recognition Source: Reactome
  • nucleotide-excision repair, DNA duplex unwinding Source: Reactome
  • nucleotide-excision repair, DNA incision Source: Reactome
  • nucleotide-excision repair, DNA incision, 3'-to lesion Source: Reactome
  • nucleotide-excision repair, DNA incision, 5'-to lesion Source: Reactome
  • nucleotide-excision repair, preincision complex assembly Source: Reactome
  • nucleotide-excision repair, preincision complex stabilization Source: Reactome
  • positive regulation by virus of viral protein levels in host cell Source: AgBase
  • positive regulation of viral genome replication Source: AgBase
  • positive regulation of viral release from host cell Source: AgBase
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB
  • regulation of mitotic cell cycle phase transition Source: UniProtKB
  • transcription-coupled nucleotide-excision repair Source: Reactome
  • UV-damage excision repair Source: UniProtKB
  • viral process Source: UniProtKB-KW
  • 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

BioCyciZFISH:ENSG00000167986-MONOMER.
BRENDAi6.3.2.19. 2681.
ReactomeiR-HSA-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
SIGNORiQ16531.
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
Proteomesi
  • UP000005640 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

  • Cul4A-RING E3 ubiquitin ligase complex Source: UniProtKB
  • Cul4B-RING E3 ubiquitin ligase complex Source: UniProtKB
  • Cul4-RING E3 ubiquitin ligase complex Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi316 – 319YLDN → ALAA: Impairs interaction with DDA1. 1 Publication4
Mutagenesisi537E → A: Slightly impairs interaction with CUL4A. 1 Publication1
Mutagenesisi561W → A: Strongly impairs interaction with CUL4A. 1 Publication1
Mutagenesisi840 – 842EAE → AAA: Impairs interaction with AMBRA1, DTL, DET1, VPRBP, DCAF5, DCAF11 and DCAF8. 1 Publication3
Mutagenesisi910 – 913MALY → AAAA: Impairs interaction with AMBRA1, DTL and DCAF5. 1 Publication4
Mutagenesisi953W → A: Impairs interaction with AMBRA1, ERCC8, DCAF5 and DCAF11. 1 Publication1

Organism-specific databases

DisGeNETi1642.
OpenTargetsiENSG00000167986.
PharmGKBiPA27187.

Polymorphism and mutation databases

BioMutaiDDB1.
DMDMi12643730.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000798402 – 1140DNA damage-binding protein 1Add BLAST1139

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei1067N6-acetyllysineCombined sources1
Modified residuei1125PhosphothreonineBy similarity1

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

EPDiQ16531.
MaxQBiQ16531.
PaxDbiQ16531.
PeptideAtlasiQ16531.
PRIDEiQ16531.

PTM databases

iPTMnetiQ16531.
PhosphoSitePlusiQ16531.
SwissPalmiQ16531.

Expressioni

Gene expression databases

BgeeiENSG00000167986.
CleanExiHS_DDB1.
ExpressionAtlasiQ16531. baseline and differential.
GenevisibleiQ16531. HS.

Organism-specific databases

HPAiCAB032821.
HPA045174.
HPA068456.

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. 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).32 Publications
(Microbial infection) 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).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTR5Q9H9F93EBI-350322,EBI-769418
CUL4AQ136194EBI-350322,EBI-456106
CUL4BQ1362016EBI-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. 266 interactors.
DIPiDIP-430N.
IntActiQ16531. 90 interactors.
MINTiMINT-1134697.
STRINGi9606.ENSP00000301764.

Structurei

Secondary structure

11140
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Beta strandi17 – 21Combined sources5
Beta strandi26 – 28Combined sources3
Beta strandi30 – 35Combined sources6
Beta strandi38 – 45Combined sources8
Beta strandi48 – 56Combined sources9
Beta strandi61 – 67Combined sources7
Beta strandi72 – 74Combined sources3
Beta strandi76 – 81Combined sources6
Turni82 – 84Combined sources3
Beta strandi85 – 92Combined sources8
Beta strandi95 – 97Combined sources3
Beta strandi99 – 107Combined sources9
Beta strandi121 – 124Combined sources4
Beta strandi128 – 134Combined sources7
Beta strandi139 – 144Combined sources6
Beta strandi146 – 148Combined sources3
Beta strandi155 – 158Combined sources4
Beta strandi164 – 169Combined sources6
Beta strandi177 – 184Combined sources8
Beta strandi187 – 196Combined sources10
Turni197 – 200Combined sources4
Beta strandi201 – 204Combined sources4
Beta strandi210 – 212Combined sources3
Beta strandi218 – 221Combined sources4
Turni224 – 226Combined sources3
Beta strandi229 – 232Combined sources4
Beta strandi237 – 241Combined sources5
Beta strandi244 – 248Combined sources5
Helixi251 – 255Combined sources5
Beta strandi258 – 263Combined sources6
Beta strandi268 – 275Combined sources8
Beta strandi279 – 288Combined sources10
Beta strandi291 – 293Combined sources3
Beta strandi296 – 307Combined sources12
Beta strandi312 – 316Combined sources5
Turni318 – 320Combined sources3
Beta strandi321 – 325Combined sources5
Beta strandi327 – 329Combined sources3
Beta strandi331 – 336Combined sources6
Helixi342 – 344Combined sources3
Beta strandi347 – 353Combined sources7
Beta strandi358 – 365Combined sources8
Beta strandi369 – 371Combined sources3
Beta strandi374 – 379Combined sources6
Helixi382 – 384Combined sources3
Beta strandi386 – 394Combined sources9
Beta strandi396 – 402Combined sources7
Beta strandi409 – 413Combined sources5
Beta strandi417 – 419Combined sources3
Beta strandi420 – 422Combined sources3
Beta strandi424 – 429Combined sources6
Beta strandi432 – 439Combined sources8
Beta strandi442 – 446Combined sources5
Beta strandi449 – 451Combined sources3
Beta strandi453 – 455Combined sources3
Beta strandi457 – 463Combined sources7
Turni464 – 466Combined sources3
Beta strandi467 – 474Combined sources8
Beta strandi476 – 483Combined sources8
Beta strandi486 – 490Combined sources5
Beta strandi493 – 495Combined sources3
Beta strandi500 – 503Combined sources4
Beta strandi505 – 512Combined sources8
Beta strandi515 – 522Combined sources8
Beta strandi525 – 533Combined sources9
Beta strandi535 – 537Combined sources3
Beta strandi538 – 542Combined sources5
Beta strandi547 – 549Combined sources3
Beta strandi550 – 552Combined sources3
Beta strandi554 – 560Combined sources7
Turni561 – 564Combined sources4
Beta strandi565 – 570Combined sources6
Turni571 – 573Combined sources3
Beta strandi576 – 581Combined sources6
Beta strandi583 – 585Combined sources3
Beta strandi588 – 596Combined sources9
Beta strandi599 – 606Combined sources8
Beta strandi609 – 616Combined sources8
Turni618 – 620Combined sources3
Beta strandi623 – 630Combined sources8
Beta strandi637 – 645Combined sources9
Beta strandi647 – 655Combined sources9
Beta strandi657 – 674Combined sources18
Beta strandi678 – 682Combined sources5
Beta strandi685 – 687Combined sources3
Beta strandi690 – 694Combined sources5
Beta strandi696 – 698Combined sources3
Beta strandi699 – 704Combined sources6
Beta strandi707 – 716Combined sources10
Beta strandi718 – 727Combined sources10
Helixi728 – 730Combined sources3
Beta strandi732 – 743Combined sources12
Beta strandi745 – 753Combined sources9
Helixi756 – 759Combined sources4
Beta strandi761 – 765Combined sources5
Beta strandi781 – 783Combined sources3
Beta strandi785 – 795Combined sources11
Turni796 – 798Combined sources3
Beta strandi801 – 806Combined sources6
Beta strandi811 – 819Combined sources9
Beta strandi823 – 826Combined sources4
Beta strandi828 – 835Combined sources8
Beta strandi840 – 842Combined sources3
Beta strandi846 – 854Combined sources9
Beta strandi857 – 868Combined sources12
Beta strandi870 – 876Combined sources7
Beta strandi879 – 884Combined sources6
Beta strandi887 – 893Combined sources7
Beta strandi895 – 897Combined sources3
Beta strandi899 – 905Combined sources7
Beta strandi911 – 917Combined sources7
Beta strandi920 – 928Combined sources9
Beta strandi930 – 936Combined sources7
Turni937 – 940Combined sources4
Beta strandi941 – 947Combined sources7
Beta strandi954 – 961Combined sources8
Beta strandi964 – 969Combined sources6
Beta strandi972 – 979Combined sources8
Beta strandi982 – 984Combined sources3
Turni985 – 987Combined sources3
Helixi988 – 990Combined sources3
Beta strandi991 – 999Combined sources9
Beta strandi1004 – 1009Combined sources6
Beta strandi1017 – 1020Combined sources4
Beta strandi1024 – 1032Combined sources9
Beta strandi1037 – 1043Combined sources7
Helixi1045 – 1061Combined sources17
Helixi1065 – 1067Combined sources3
Helixi1070 – 1074Combined sources5
Beta strandi1075 – 1077Combined sources3
Beta strandi1081 – 1083Combined sources3
Beta strandi1086 – 1090Combined sources5
Helixi1091 – 1095Combined sources5
Helixi1096 – 1099Combined sources4
Helixi1102 – 1108Combined sources7
Turni1109 – 1111Combined sources3
Beta strandi1117 – 1120Combined sources4
Helixi1127 – 1136Combined sources10
Helixi1137 – 1139Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5FQDX-ray2.45A/D1-395[»]
A/D709-1140[»]
5HXBX-ray3.60B/Y1-1140[»]
5JK7X-ray3.49A/B1-1140[»]
ProteinModelPortaliQ16531.
SMRiQ16531.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16531.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 768Interaction with CDT11 PublicationAdd BLAST767
Regioni13 – 356WD repeat beta-propeller AAdd BLAST344
Regioni392 – 708WD repeat beta-propeller B; Interaction with CUL4AAdd BLAST317
Regioni709 – 1043WD repeat beta-propeller CAdd BLAST335
Regioni771 – 1140Interaction with CDT1 and CUL4A1 PublicationAdd BLAST370

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

eggNOGiKOG1897. Eukaryota.
ENOG410XPF6. LUCA.
GeneTreeiENSGT00530000063396.
HOGENOMiHOG000007241.
HOVERGENiHBG005460.
InParanoidiQ16531.
KOiK10610.
OMAiHVKSHEI.
OrthoDBiEOG091G017I.
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: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)DescriptionActionsGraphical viewLength
Sequence conflicti422D → Y in AAA88883 (PubMed:8538642).Curated1
Sequence conflicti533E → G in CAA05770 (Ref. 4) Curated1
Sequence conflicti869A → D in CAA05770 (Ref. 4) Curated1
Sequence conflicti898 – 899EL → DV in AAA88883 (PubMed:8538642).Curated2
Sequence conflicti898 – 899EL → DV in CAA05770 (Ref. 4) Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023074427L → F.1 PublicationCorresponds to variant rs28720299dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05554071 – 759Missing in isoform 2. 1 PublicationAdd BLAST689

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.6. human. [Q16531-1]

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
PDB 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[»]
5FQDX-ray2.45A/D1-395[»]
A/D709-1140[»]
5HXBX-ray3.60B/Y1-1140[»]
5JK7X-ray3.49A/B1-1140[»]
ProteinModelPortaliQ16531.
SMRiQ16531.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108009. 266 interactors.
DIPiDIP-430N.
IntActiQ16531. 90 interactors.
MINTiMINT-1134697.
STRINGi9606.ENSP00000301764.

PTM databases

iPTMnetiQ16531.
PhosphoSitePlusiQ16531.
SwissPalmiQ16531.

Polymorphism and mutation databases

BioMutaiDDB1.
DMDMi12643730.

Proteomic databases

EPDiQ16531.
MaxQBiQ16531.
PaxDbiQ16531.
PeptideAtlasiQ16531.
PRIDEiQ16531.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301764; ENSP00000301764; ENSG00000167986. [Q16531-1]
GeneIDi1642.
KEGGihsa:1642.
UCSCiuc001nrc.6. human. [Q16531-1]

Organism-specific databases

CTDi1642.
DisGeNETi1642.
GeneCardsiDDB1.
H-InvDBHIX0171380.
HGNCiHGNC:2717. DDB1.
HPAiCAB032821.
HPA045174.
HPA068456.
MIMi600045. gene.
neXtProtiNX_Q16531.
OpenTargetsiENSG00000167986.
PharmGKBiPA27187.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1897. Eukaryota.
ENOG410XPF6. LUCA.
GeneTreeiENSGT00530000063396.
HOGENOMiHOG000007241.
HOVERGENiHBG005460.
InParanoidiQ16531.
KOiK10610.
OMAiHVKSHEI.
OrthoDBiEOG091G017I.
PhylomeDBiQ16531.
TreeFamiTF105840.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000167986-MONOMER.
BRENDAi6.3.2.19. 2681.
ReactomeiR-HSA-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
SIGNORiQ16531.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000167986.
CleanExiHS_DDB1.
ExpressionAtlasiQ16531. baseline and differential.
GenevisibleiQ16531. HS.

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...

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: November 30, 2016
This is version 170 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

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 one 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.