(data stored in ACNUC16935 zone)

SWISSPROT: RL401_SCHPO

ID   RL401_SCHPO             Reviewed;         128 AA.
AC   P0CH06; O13697; O14257; P0C014; P0C015; Q76PD0; Q9HDZ4;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   05-JUL-2017, entry version 58.
DE   RecName: Full=Ubiquitin-60S ribosomal protein L40;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=60S ribosomal protein L40;
DE     AltName: Full=CEP52;
DE   Flags: Precursor;
GN   Name=ubi1; ORFNames=SPAC11G7.04;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
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       {ECO:0000250}.
CC   -!- FUNCTION: 60S ribosomal protein L40: component of the 60S subunit
CC       of the ribosome.
CC   -!- SUBUNIT: Ribosomal protein L40 is part of the 60S ribosomal
CC       subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: 60S ribosomal protein L40: Cytoplasm
CC       {ECO:0000250}.
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. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC       ribosomal protein eL40 family. {ECO:0000305}.
DR   EMBL; CU329670; CAB16209.1; -; Genomic_DNA.
DR   PIR; T37547; T37547.
DR   RefSeq; NP_593923.1; NM_001019352.2.
DR   RefSeq; NP_594398.1; NM_001019821.2.
DR   ProteinModelPortal; P0CH06; -.
DR   SMR; P0CH06; -.
DR   BioGrid; 278262; 5.
DR   BioGrid; 278890; 14.
DR   STRING; 4896.SPAC1805.12c.1; -.
DR   SwissPalm; P0CH06; -.
DR   MaxQB; P0CH06; -.
DR   PRIDE; P0CH06; -.
DR   EnsemblFungi; SPAC11G7.04.1; SPAC11G7.04.1:pep; SPAC11G7.04.
DR   EnsemblFungi; SPAC1805.12c.1; SPAC1805.12c.1:pep; SPAC1805.12c.
DR   GeneID; 2541768; -.
DR   GeneID; 2542428; -.
DR   KEGG; spo:SPAC11G7.04; -.
DR   KEGG; spo:SPAC1805.12c; -.
DR   PomBase; SPAC11G7.04; ubi1.
DR   InParanoid; P0CH06; -.
DR   KO; K02927; -.
DR   OMA; RKTKCGH; -.
DR   OrthoDB; EOG092C5P9Y; -.
DR   PhylomeDB; P0CH06; -.
DR   Reactome; R-SPO-110312; Translesion synthesis by REV1.
DR   Reactome; R-SPO-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-SPO-110320; Translesion Synthesis by POLH.
DR   Reactome; R-SPO-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR   Reactome; R-SPO-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-SPO-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR   Reactome; R-SPO-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   Reactome; R-SPO-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-SPO-5655862; Translesion synthesis by POLK.
DR   Reactome; R-SPO-5656121; Translesion synthesis by POLI.
DR   Reactome; R-SPO-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-SPO-5689603; UCH proteinases.
DR   Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR   Reactome; R-SPO-5689901; Metalloprotease DUBs.
DR   Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-SPO-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR   Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR   Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR   Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR   Reactome; R-SPO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-SPO-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-SPO-72689; Formation of a pool of free 40S subunits.
DR   Reactome; R-SPO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR   Reactome; R-SPO-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-SPO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-SPO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-SPO-901032; ER Quality Control Compartment (ERQC).
DR   Reactome; R-SPO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-SPO-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR   Reactome; R-SPO-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR   Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:P0CH06; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISO:PomBase.
DR   GO; GO:0002181; P:cytoplasmic translation; ISO:PomBase.
DR   GO; GO:0042254; P:ribosome biogenesis; ISO:PomBase.
DR   InterPro; IPR001975; Ribosomal_L40e.
DR   InterPro; IPR019956; Ubiquitin.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR000626; Ubiquitin_dom.
DR   Pfam; PF01020; Ribosomal_L40e; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM01377; Ribosomal_L40e; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P0CH06.
DR   SWISS-2DPAGE; P0CH06.
KW   Complete proteome; Cytoplasm; Isopeptide bond; Nucleus;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW   Ubl conjugation.
FT   CHAIN         1     76       Ubiquitin.
FT                                /FTId=PRO_0000114860.
FT   CHAIN        77    128       60S ribosomal protein L40.
FT                                /FTId=PRO_0000138774.
FT   DOMAIN        1     76       Ubiquitin-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   CROSSLNK      6      6       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK     11     11       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK     27     27       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK     29     29       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250}.
FT   CROSSLNK     33     33       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK     48     48       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250}.
FT   CROSSLNK     63     63       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250}.
FT   CROSSLNK     76     76       Glycyl lysine isopeptide (Gly-Lys)
FT                                (interchain with K-? in acceptor
FT                                proteins). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
SQ   SEQUENCE   128 AA;  14595 MW;  A35EA817EFD46D38 CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGIIEP SLKALASKYN CEKQICRKCY ARLPPRATNC RKKKCGHTNQ
     LRPKKKLK
//

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