(data stored in ACNUC21049 zone)

HOGENOM: HS11_PE1549

ID   HS11_PE1549                          STANDARD;      PRT;   1140 AA.
AC   HS11_PE1549; Q16531; A6NG77; B2R648; O15176; Q13289; Q58F96;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=DNA damage-binding protein 1;AltName: Full=DDB p127
DE   subunit;AltName: Full=DNA damage-binding protein a; Short=DDBa;AltName:
DE   Full=Damage-specific DNA-binding protein 1;AltName: Full=HBV X-associated
DE   protein 1; Short=XAP-1;AltName: Full=UV-damaged DNA-binding
DE   factor;AltName: Full=UV-damaged DNA-binding protein 1; Short=UV-DDB
DE   1;AltName: Full=XPE-binding factor; Short=XPE-BF;AltName: Full=Xeroderma
DE   pigmentosum group E-complementing protein; Short=XPCe; (HS11.PE1549).
GN   Name=DDB1; Synonyms=XAP1;
OS   HOMO SAPIENS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Primates; Haplorrhini; Simiiformes; Catarrhini;
OC   Hominoidea; Hominidae; Homininae; Homo.
OX   NCBI_TaxID=9606;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HS11.PE1549.
CC       Homo sapiens chromosome 11 GRCh37  sequence 1..134946516 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:DDB1_HUMAN
CC   -!- FUNCTION: Required for DNA repair. Binds to DDB2 to form the UV-
CC       damaged DNA-binding protein complex (the UV-DDB complex). The UV-
CC       DDB complex may recognize UV-induced DNA damage and recruit
CC       proteins of the nucleotide excision repair pathway (the NER
CC       pathway) to initiate DNA repair. The UV-DDB complex preferentially
CC       binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts
CC       (6-4 PP), apurinic sites and short mismatches. Also appears to
CC       function as a component of numerous distinct DCX (DDB1-CUL4-X-box)
CC       E3 ubiquitin-protein ligase complexes which mediate the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins. The functional specificity of the DCX E3 ubiquitin-
CC       protein ligase complex is determined by the variable substrate
CC       recognition component recruited by DDB1. DCX(DDB2) (also known as
CC       DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate
CC       histone H2A, histone H3 and histone H4 at sites of UV-induced DNA
CC       damage. The ubiquitination of histones may facilitate their
CC       removal from the nucleosome and promote subsequent DNA repair.
CC       DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by
CC       XPC and promote NER. DCX(DTL) plays a role in PCNA-dependent
CC       polyubiquitination of CDT1 and MDM2-dependent ubiquitination of
CC       TP53 in response to radiation-induced DNA damage and during DNA
CC       replication. DCX(ERCC8) (the CSA complex) plays a role in
CC       transcription-coupled repair (TCR). May also play a role in
CC       ubiquitination of CDKN1B/p27kip when associated with CUL4 and
CC       SKP2.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the UV-DDB complex which includes DDB1 and
CC       DDB2. The UV-DDB complex interacts with monoubiquitinated histone
CC       H2A and binds to XPC via the DDB2 subunit. Component of numerous
CC       DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which
CC       consist of a core of DDB1, CUL4A or CUL4B and RBX1. DDB1 may
CC       recruit specific substrate targeting subunits to the DCX complex.
CC       These substrate targeting subunits are generally known as DCAF
CC       (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated
CC       WD40-repeat) proteins. Interacts with AMBRA1, ATG16L1, BTRC,
CC       DCAF1, DCAF17, DCAF16, DCAF15, DDA1, DET1, DTL, ERCC8, FBXW5,
CC       FBXW8, GRWD1, DCAF6, KATNB1, NLE1, NUP43, PAFAH1B1, PHIP, PWP1,
CC       RBBP4, RBBP5, RBBP7, RFWD2, SNRNP40, VPRBP, WDR5, WDR5B, WDR12,
CC       DCAF4, DCAF5, DCAF11, WDR26, DCAF10, WDR39, DCAF12, WDR42, DCAF8,
CC       WDR53, WDR59, WDR61, DCAF7, WSB1, WSB2 and WDTC1. DCX complexes
CC       may associate with the COP9 signalosome, and this inhibits the E3
CC       ubiquitin-protein ligase activity of the complex. Interacts with
CC       NF2, TSC1 and TSC2. Interacts with Simian virus 5 protein V and
CC       the HBV X protein. Interaction with SV5 protein V may prevent the
CC       recruitment of DCAF proteins to DCX complexes. Interacts with
CC       EIF2C1 and EIF2C2.
CC   -!- INTERACTION:
CC       Q92466:DDB2; NbExp=3; IntAct=EBI-350322, EBI-1176171;
CC       Q9NZJ0:DTL; NbExp=3; IntAct=EBI-350322, EBI-1176075;
CC       Q04725:TLE2; NbExp=2; IntAct=EBI-350322, EBI-1176061;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Primarily
CC       cytoplasmic. Translocates to the nucleus following UV irradiation
CC       and subsequently accumulates at sites of DNA damage.
CC   -!- PTM: Phosphorylated by ABL1 (By similarity).
CC   -!- PTM: Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-
CC       dependent proteolysis.
CC   -!- SIMILARITY: Belongs to the DDB1 family.
CC   -!- WEB RESOURCE: Name=Allelic variations of the XP genes;
CC       URL="http://www.xpmutations.org/";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/ddb1/";
CC   -!- GENE_FAMILY: HOG000007241 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Homo_sapiens;ENSG00000167986;ENST00000301764;ENSP00000301764.
DR   EMBL; AJ002955; - ;
DR   EMBL; AK294493; - ;
DR   EMBL; AK302924; - ;
DR   EMBL; AK312436; - ;
DR   EMBL; AP003108; - ;
DR   EMBL; AY960579; - ;
DR   EMBL; BC011686; - ;
DR   EMBL; BC050530; - ;
DR   EMBL; BC051764; - ;
DR   EMBL; CH471076; - ;
DR   EMBL; L40326; - ;
DR   EMBL; U18299; - ;
DR   EMBL; U32986; - ;
DR   UniProtKB/Swiss-Prot; Q16531; A6NG77; B2R648; O15176; Q13289; Q58F96; -.
DR   EMBL; U18299; AAC50349.1; -; mRNA.
DR   EMBL; L40326; AAA62838.1; -; mRNA.
DR   EMBL; U32986; AAA88883.1; -; mRNA.
DR   EMBL; AJ002955; CAA05770.1; -; mRNA.
DR   EMBL; AK312436; BAG35345.1; -; mRNA.
DR   EMBL; AY960579; AAX44048.1; -; Genomic_DNA.
DR   EMBL; AP003108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW73935.1; -; Genomic_DNA.
DR   EMBL; BC011686; AAH11686.1; -; mRNA.
DR   EMBL; BC050530; AAH50530.1; -; mRNA.
DR   EMBL; BC051764; AAH51764.1; -; mRNA.
DR   IPI; IPI00293464; -.
DR   PIR; I38908; I38908.
DR   RefSeq; NP_001914.3; NM_001923.3.
DR   RefSeq; XP_002347285.1; XM_002347244.2.
DR   RefSeq; XP_003120746.1; XM_003120698.1.
DR   RefSeq; XP_003120747.1; XM_003120699.1.
DR   UniGene; Hs.290758; -.
DR   PDB; 2B5L; X-ray; 2.85 A; A/B=1-1140.
DR   PDB; 2B5M; X-ray; 2.92 A; A=1-1140.
DR   PDB; 2B5N; X-ray; 2.80 A; A/B/C/D=391-709.
DR   PDB; 2HYE; X-ray; 3.10 A; A=1-1140.
DR   PDB; 3E0C; X-ray; 2.41 A; A=1-1140.
DR   PDB; 3EI1; X-ray; 2.80 A; A=1-1140.
DR   PDB; 3EI2; X-ray; 2.60 A; A=1-1140.
DR   PDB; 3EI3; X-ray; 2.30 A; A=1-1140.
DR   PDB; 3EI4; X-ray; 3.30 A; A/C/E=1-1140.
DR   PDB; 3I7H; X-ray; 2.90 A; A=1-1140.
DR   PDB; 3I7K; X-ray; 2.80 A; A=1-1140.
DR   PDB; 3I7L; X-ray; 2.80 A; A=1-1140.
DR   PDB; 3I7N; X-ray; 2.80 A; A=1-1140.
DR   PDB; 3I7O; X-ray; 2.80 A; A=1-1140.
DR   PDB; 3I7P; X-ray; 3.00 A; A=1-1140.
DR   PDB; 3I89; X-ray; 3.00 A; A=1-1140.
DR   PDB; 3I8C; X-ray; 2.80 A; A=1-1140.
DR   PDB; 3I8E; X-ray; 3.40 A; A/B=1-1140.
DR   PDBsum; 2B5L; -.
DR   PDBsum; 2B5M; -.
DR   PDBsum; 2B5N; -.
DR   PDBsum; 2HYE; -.
DR   PDBsum; 3E0C; -.
DR   PDBsum; 3EI1; -.
DR   PDBsum; 3EI2; -.
DR   PDBsum; 3EI3; -.
DR   PDBsum; 3EI4; -.
DR   PDBsum; 3I7H; -.
DR   PDBsum; 3I7K; -.
DR   PDBsum; 3I7L; -.
DR   PDBsum; 3I7N; -.
DR   PDBsum; 3I7O; -.
DR   PDBsum; 3I7P; -.
DR   PDBsum; 3I89; -.
DR   PDBsum; 3I8C; -.
DR   PDBsum; 3I8E; -.
DR   ProteinModelPortal; Q16531; -.
DR   SMR; Q16531; 390-707.
DR   DIP; DIP-430N; -.
DR   IntAct; Q16531; 35.
DR   MINT; MINT-1134697; -.
DR   STRING; Q16531; -.
DR   PhosphoSite; Q16531; -.
DR   PRIDE; Q16531; -.
DR   Ensembl; ENST00000301764; ENSP00000301764; ENSG00000167986.
DR   GeneID; 100290337; -.
DR   GeneID; 1642; -.
DR   KEGG; hsa:100290337; -.
DR   KEGG; hsa:1642; -.
DR   UCSC; uc001nrc.2; human.
DR   CTD; 1642; -.
DR   GeneCards; GC11M057394; -.
DR   H-InvDB; HIX0009685; -.
DR   HGNC; HGNC:2717; DDB1.
DR   HPA; CAB032821; -.
DR   MIM; 600045; gene.
DR   neXtProt; NX_Q16531; -.
DR   PharmGKB; PA27187; -.
DR   eggNOG; prNOG12562; -.
DR   GeneTree; ENSGT00530000063396; -.
DR   InParanoid; Q16531; -.
DR   OMA; CALGDGS; -.
DR   OrthoDB; EOG4KPT91; -.
DR   Reactome; REACT_216; DNA Repair.
DR   NextBio; 6750; -.
DR   ArrayExpress; Q16531; -.
DR   Bgee; Q16531; -.
DR   CleanEx; HS_DDB1; -.
DR   Genevestigator; Q16531; -.
DR   GermOnline; ENSG00000167986; Homo sapiens.
DR   GO; GO:0031464; C:Cul4A-RING ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0031465; C:Cul4B-RING ubiquitin ligase complex; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; EXP:Reactome.
DR   GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0000075; P:cell cycle checkpoint; IMP:UniProtKB.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW.
DR   GO; GO:0000718; P:nucleotide-excision repair, DNA damage removal; EXP:Reactome.
DR   GO; GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF03178; CPSF_A; 1.
DR   HOGENOMDNA; HS11.PE1549; -.
KW   ENSG000001679861755old_1320000031; ENSP000003017647901old_1320000031;
KW   B7Z2A1_HUMAN; B7Z859_HUMAN; AJ002955; AK294493; AK302924; AK312436;
KW   AY960579; BC011686; BC050530; BC051764; CH471076; L40326; U18299; U32986;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm; DNA damage;
KW   DNA repair; DNA-binding; Host-virus interaction; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation;
KW   Ubl conjugation pathway.
SQ   SEQUENCE   1140 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK
     IAVMELFRPK GESKDLLFIL TAKYNACILE YKQSGESIDI ITRAHGNVQD RIGRPSETGI
     IGIIDPECRM IGLRLYDGLF KVIPLDRDNK ELKAFNIRLE ELHVIDVKFL YGCQAPTICF
     VYQDPQGRHV KTYEVSLREK EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH
     NGDKYLAIAP PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL
     RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM ETFTNLGPIV
     DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA SIDLPGIKGL WPLRSDPNRE
     TDDTLVLSFV GQTRVLMLNG EEVEETELMG FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS
     QEPKALVSEW KEPQAKNISV ASCNSSQVVV AVGRALYYLQ IHPQELRQIS HTEMEHEVAC
     LDITPLGDSN GLSPLCAIGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH
     YLLCALGDGA LFYFGLNIET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF ACSDRPTVIY
     SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT IGTIDEIQKL HIRTVPLYES
     PRKICYQEVS QCFGVLSSRI EVQDTSGGTT ALRPSASTQA LSSSVSSSKL FSSSTAPHET
     SFGEEVEVHN LLIIDQHTFE VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE
     AEPKQGRIVV FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTTEKELR
     TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN PNWMSAVEIL
     DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLFHL GEFVNVFCHG SLVMQNLGET
     STPTQGSVLF GTVNGMIGLV TSLSESWYNL LLDMQNRLNK VIKSVGKIEH SFWRSFHTER
     KTEPATGFID GDLIESFLDI SRPKMQEVVA NLQYDDGSGM KREATADDLI KVVEELTRIH
//

If you have problems or comments...

PBIL Back to PBIL home page