(data stored in ACNUC16935 zone)

HOGENOM: RABIT19_5_PE5

ID   RABIT19_5_PE5                        STANDARD;      PRT;   229 AA.
AC   RABIT19_5_PE5;
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=Ubiquitin; (RABIT19_5.PE5).
OS   ORYCTOLAGUS CUNICULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RABIT19_5.PE5.
CC       Oryctolagus cuniculus chromosome 19 oryCun2 partial sequence
CC       3962384..4962383 annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:UBIQ_RABIT
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 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- MISCELLANEOUS: Ubiquitin is synthesized as a polyubiquitin
CC       precursor with exact head to tail repeats, the number of repeats
CC       differ between species. In some species there is a final amino-
CC       acid after the last repeat. Some ubiquitin genes contain a single
CC       copy of ubiquitin fused to a ribosomal protein (either L40 or
CC       S27a).
CC   -!- SIMILARITY: Belongs to the ubiquitin family.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC   -!- GENE_FAMILY: HOG000233942 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Oryctolagus_cuniculus;ENSOCUG00000001288;ENSOCUT00000001288;ENSOCUP00000001111.
DR   UniProtKB/Swiss-Prot; P62975; P02248; P02249; P02250; Q29120; Q91887; Q91888; -.
DR   PIR; S28203; S28203.
DR   ProteinModelPortal; P62975; -.
DR   SMR; P62975; 1-76.
DR   STRING; P62975; -.
DR   PRIDE; P62975; -.
DR   Ensembl; ENSOCUT00000001288; ENSOCUP00000001111; ENSOCUG00000001288.
DR   Ensembl; ENSOCUT00000003610; ENSOCUP00000003131; ENSOCUG00000003613.
DR   eggNOG; maNOG18772; -.
DR   GeneTree; ENSGT00550000074658; -.
DR   GeneTree; ENSGT00550000074763; -.
DR   OrthoDB; EOG4PZJ82; -.
DR   OrthoDB; EOG4WDDB6; -.
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; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   HOGENOMDNA; RABIT19_5.PE5; -.
KW   ENSOCUG00000001288820036002503210000011;
KW   UBIQ_RABIT;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW   Nucleus; Phosphoprotein; Ubl conjugation.
SQ   SEQUENCE   229 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 LVLRLRGGC
//

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