(data stored in ACNUC16935 zone)

HOGENOM: SCHPO_2_PE382

ID   SCHPO_2_PE382                        STANDARD;      PRT;   382 AA.
AC   SCHPO_2_PE382;
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-60S ribosomal protein L40;Contains: RecName:
DE   Full=Ubiquitin;Contains: RecName: Full=60S ribosomal protein L40;
DE   AltName: Full=CEP52;Flags: Precursor; (SCHPO_2.PE382).
GN   Name=ubi1; ORFNames=SPAC11G7.04;
OS   SCHIZOSACCHAROMYCES POMBE.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SCHPO_2.PE382.
CC       Schizosaccharomyces pombe chromosome II EF1 full sequence 1..4539804
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:RL401_SCHPO
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, and DNA-damage responses. Linear
CC       polymer chains formed via attachment by the initiator Met lead to
CC       cell signaling. Ubiquitin is usually conjugated to Lys residues of
CC       target proteins, however, in rare cases, conjugation to Cys or Ser
CC       residues has been observed. When polyubiquitin is free
CC       (unanchored-polyubiquitin), it also has distinct roles, such as in
CC       activation of protein kinases, and in signaling (By similarity).
CC   -!- FUNCTION: Ribosomal protein L40 is a component of the 60S subunit
CC       of the ribosome.
CC   -!- SUBUNIT: Ribosomal protein L40 is part of the 60S ribosomal
CC       subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm (By similarity).
CC       Nucleus (By similarity).
CC   -!- SUBCELLULAR LOCATION: 60S ribosomal protein L40: Cytoplasm (By
CC       similarity).
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 5 different genes. Ubi1 and
CC       ubi2 are synthesized as a polyprotein with one copy of ubiquitin
CC       fused to ribosomal protein L40. Ubi3 and ubi5 are polyproteins
CC       with one copy of ubiquitin fused to ribosomal proteins S27a and
CC       s27b respectively. Ubi4 is a polyprotein containing 5 exact head
CC       to tail repeats of ubiquitin.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin
CC       family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the ribosomal
CC       protein L40e family.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC   -!- GENE_FAMILY: HOG000233942 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Schizosaccharomyces_pombe;SPBC337.08C;SPBC337.08C-1;SPBC337.08C-1.
DR   UniProtKB/Swiss-Prot; P0CH06; O13697; O14257; P0C014; P0C015; Q76PD0; Q9HDZ4; -.
DR   EMBL; CU329670; CAB16209.1; -; Genomic_DNA.
DR   PIR; T37547; T37547.
DR   RefSeq; NP_593923.1; NM_001019352.1.
DR   RefSeq; NP_594398.1; NM_001019821.1.
DR   ProteinModelPortal; P0CH06; -.
DR   GeneID; 2541768; -.
DR   GeneID; 2542428; -.
DR   GenomeReviews; CU329670_GR; ubi1.
DR   KEGG; spo:SPAC11G7.04; -.
DR   KEGG; spo:SPAC1805.12c; -.
DR   GeneDB_Spombe; SPAC11G7.04; -.
DR   OrthoDB; EOG48WGBH; -.
DR   PhylomeDB; P0C014; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR001975; Ribosomal_L40e.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_subgr.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Pfam; PF01020; Ribosomal_L40e; 1.
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; SCHPO_2.PE382; -.
KW   SPBC337.08cccc7236820036002503210000011;
KW   P0C014;
KW   Complete proteome; Cytoplasm; DNA damage; DNA repair; Isopeptide bond;
KW   Nucleus; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   Ubl conjugation.
SQ   SEQUENCE   382 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVESSDTID NVKSKIQDKE GIPPDQQRLI
     FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE SSDTIDNVKS
     KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
     ITLEVESSDT IDNVKSKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
     LRGGMQIFVK TLTGKTITLE VESSDTIDNV KSKIQDKEGI PPDQQRLIFA GKQLEDGRTL
     SDYNIQKEST LHLVLRLRGG LF
//

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