(data stored in ACNUC16935 zone)

HOGENOM: MOUSE5_PE2507

ID   MOUSE5_PE2507                        STANDARD;      PRT;   734 AA.
AC   MOUSE5_PE2507;
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=Polyubiquitin-C;Contains: RecName: Full=Ubiquitin;Contains:
DE   RecName: Full=Ubiquitin-related 1;Contains: RecName:
DE   Full=Ubiquitin-related 2;Flags: Precursor; (MOUSE5.PE2507).
GN   Name=Ubc;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE5.PE2507.
CC       Mus musculus chromosome 5 NCBIM37  sequence 1..152537259 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:UBC_MOUSE
CC   -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC       protein, or free (unanchored). When covalently bound, it is
CC       conjugated to target proteins via an isopeptide bond either as a
CC       monomer (monoubiquitin), a polymer linked via different Lys
CC       residues of the ubiquitin (polyubiquitin chains) or a linear
CC       polymer linked via the initiator Met of the ubiquitin (linear
CC       polyubiquitin chains). Polyubiquitin chains, when attached to a
CC       target protein, have different functions depending on the Lys
CC       residue of the ubiquitin that is linked: Lys-6-linked may be
CC       involved in DNA repair; Lys-11-linked is involved in ERAD
CC       (endoplasmic reticulum-associated degradation) and in cell-cycle
CC       regulation; Lys-29-linked is involved in lysosomal degradation;
CC       Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC       involved in protein degradation via the proteasome; Lys-63-linked
CC       is involved in endocytosis, DNA-damage responses as well as in
CC       signaling processes leading to activation of the transcription
CC       factor NF-kappa-B. Linear polymer chains formed via attachment by
CC       the initiator Met lead to cell signaling. Ubiquitin is usually
CC       conjugated to Lys residues of target proteins, however, in rare
CC       cases, conjugation to Cys or Ser residues has been observed. When
CC       polyubiquitin is free (unanchored-polyubiquitin), it also has
CC       distinct roles, such as in activation of protein kinases, and in
CC       signaling.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. Uba52
CC       and Rps27a genes code for a single copy of ubiquitin fused to the
CC       ribosomal proteins L40 and S27a, respectively. UBB and UBC genes
CC       code for a polyubiquitin precursor with exact head to tail
CC       repeats, the number of repeats differ between species and strains.
CC   -!- MISCELLANEOUS: For a better understanding, features related to
CC       ubiquitin are only indicated for the first chain.
CC   -!- SIMILARITY: Belongs to the ubiquitin family.
CC   -!- SIMILARITY: Contains 9 ubiquitin-like domains.
CC   -!- GENE_FAMILY: HOG000233942 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000008348;ENSMUST00000156249;ENSMUSP00000115578.
DR   EMBL; AF285161; - ;
DR   EMBL; AF285162; - ;
DR   EMBL; AK010964; - ;
DR   EMBL; AK168448; - ;
DR   EMBL; AL596181; - ;
DR   EMBL; BC006680; - ;
DR   EMBL; BC008661; - ;
DR   EMBL; BC021837; - ;
DR   EMBL; BC025894; - ;
DR   EMBL; BC036303; - ;
DR   EMBL; BC094012; - ;
DR   EMBL; D50527; - ;
DR   EMBL; EF580991; - ;
DR   UniProtKB/Swiss-Prot; P0CG50; E9QKI0; P02248; P02249; P02250; P62991; Q29120; Q62317; -.
DR   UniProtKB/Swiss-Prot; Q64223; Q8VCH1; Q91887; Q91888; Q9CXY4; Q9CZM0; Q9D1R5; Q9D8D9; -.
DR   UniProtKB/Swiss-Prot; Q9ET23; Q9ET24; Q9Z0H9; -.
DR   EMBL; AF285161; AAG00512.1; -; Genomic_DNA.
DR   EMBL; AF285162; AAG00513.1; -; Genomic_DNA.
DR   EMBL; AC138613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; D50527; BAA09096.1; -; mRNA.
DR   IPI; IPI00969323; -.
DR   PIR; A49007; A49007.
DR   PIR; S11296; S11296.
DR   RefSeq; NP_062613.3; NM_019639.4.
DR   UniGene; Mm.331; -.
DR   UniGene; Mm.419997; -.
DR   PDB; 2ZNV; X-ray; 1.60 A; B/C/E/F=1-76.
DR   PDB; 3A1Q; X-ray; 2.20 A; A/B/D/E=1-76.
DR   PDB; 3A9J; X-ray; 1.18 A; A/B=1-76.
DR   PDB; 3A9K; X-ray; 1.40 A; A/B=1-76.
DR   PDBsum; 2ZNV; -.
DR   PDBsum; 3A1Q; -.
DR   PDBsum; 3A9J; -.
DR   PDBsum; 3A9K; -.
DR   ProteinModelPortal; P0CG50; -.
DR   PhosphoSite; P0CG50; -.
DR   REPRODUCTION-2DPAGE; P62991; -.
DR   PRIDE; P0CG50; -.
DR   Ensembl; ENSMUST00000136312; ENSMUSP00000114180; ENSMUSG00000008348.
DR   Ensembl; ENSMUST00000156249; ENSMUSP00000115578; ENSMUSG00000008348.
DR   GeneID; 22190; -.
DR   UCSC; uc008zro.2; mouse.
DR   CTD; 7316; -.
DR   MGI; MGI:98889; Ubc.
DR   InParanoid; P62991; -.
DR   PhylomeDB; P62991; -.
DR   Reactome; REACT_109335; Circadian Clock.
DR   Reactome; REACT_24972; Circadian Clock (mouse).
DR   Bgee; P0CG50; -.
DR   Genevestigator; P62991; -.
DR   GermOnline; ENSMUSG00000008348; Mus musculus.
DR   GermOnline; ENSMUSG00000019505; Mus musculus.
DR   GermOnline; ENSMUSG00000020460; Mus musculus.
DR   GermOnline; ENSMUSG00000044285; Mus musculus.
DR   GermOnline; ENSMUSG00000058838; Mus musculus.
DR   GermOnline; ENSMUSG00000061390; Mus musculus.
DR   GermOnline; ENSMUSG00000063789; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_subgr.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Pfam; PF00240; ubiquitin; 9.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 9.
DR   PROSITE; PS00299; UBIQUITIN_1; 8.
DR   PROSITE; PS50053; UBIQUITIN_2; 9.
DR   HOGENOMDNA; MOUSE5.PE2507; -.
KW   ENSMUSG000000083485old_1320000031; ENSMUSP000001155781old_1320000031;
KW   A5JUZ1_MOUSE; Q3TH47_MOUSE; Q5SX22_MOUSE; Q8R0Z9_MOUSE; Q8VC46_MOUSE;
KW   Q922Z8_MOUSE; AF285161; AF285162; AK010964; AK168448; AL596181; BC006680;
KW   BC021837; BC025894; BC036303; BC094012; D50527; EF580991;
KW   3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   Ubl conjugation.
SQ   SEQUENCE   734 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI
     FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE PSDTIENVKA
     KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
     ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
     LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL
     SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ
     QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE
     NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL
     TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH
     LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED
     GRTLSDYNIQ KESTLHLVLR LRGGMQIFVK TLTGKTITLD VEPSVTTKKV KQEDRRTFLT
     TVSKKSPPCA CSWV
//

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