UBI4P_SCHPO
ID UBI4P_SCHPO Reviewed; 382 AA.
AC P0CG72; O13697; O14257; P0C014; Q76PD0; Q9HDZ4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Polyubiquitin;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Flags: Precursor;
GN Name=ubi4; ORFNames=SPBC337.08c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC 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., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA 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 conjugated
CC to target proteins via an isopeptide bond either as a monomer
CC (monoubiquitin), a polymer linked via different Lys residues of the
CC ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC initiator Met of the ubiquitin (linear polyubiquitin chains).
CC Polyubiquitin chains, when attached to a target protein, have different
CC functions depending on the Lys residue of the ubiquitin that is linked:
CC Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved
CC in ERAD (endoplasmic reticulum-associated degradation) and in cell-
CC cycle 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 is
CC involved in endocytosis, and DNA-damage responses. Linear polymer
CC chains formed via attachment by the initiator Met lead to cell
CC signaling. Ubiquitin is usually conjugated to Lys residues of target
CC proteins, however, in rare cases, conjugation to Cys or Ser residues
CC has been observed. When polyubiquitin is free (unanchored-
CC polyubiquitin), it also has distinct roles, such as in activation of
CC protein kinases, and in signaling (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: For the sake of clarity sequence features are annotated
CC only for the first chain, and are not repeated for each of the
CC following chains.
CC -!- MISCELLANEOUS: Ubiquitin is encoded by 5 different genes. Ubi1 and ubi2
CC are synthesized as a polyprotein with one copy of ubiquitin fused to
CC ribosomal protein L40. Ubi3 and ubi5 are polyproteins with one copy of
CC ubiquitin fused to ribosomal proteins S27a and s27b respectively. Ubi4
CC is a polyprotein containing 5 exact head to tail repeats of ubiquitin.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; CU329671; CAA21278.1; -; Genomic_DNA.
DR RefSeq; NP_595409.1; NM_001021316.2.
DR AlphaFoldDB; P0CG72; -.
DR SMR; P0CG72; -.
DR BioGRID; 277545; 21.
DR STRING; 4896.SPBC337.08c.1; -.
DR iPTMnet; P0CG72; -.
DR MaxQB; P0CG72; -.
DR PaxDb; P0CG72; -.
DR EnsemblFungi; SPBC337.08c.1; SPBC337.08c.1:pep; SPBC337.08c.
DR GeneID; 2541030; -.
DR KEGG; spo:SPBC337.08c; -.
DR PomBase; SPBC337.08c; ubi4.
DR VEuPathDB; FungiDB:SPBC337.08c; -.
DR eggNOG; KOG0001; Eukaryota.
DR HOGENOM; CLU_010412_7_0_1; -.
DR InParanoid; P0CG72; -.
DR OMA; VHENTRR; -.
DR PhylomeDB; P0CG72; -.
DR PRO; PR:P0CG72; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004857; F:enzyme inhibitor activity; IPI:PomBase.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:PomBase.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0033621; P:nuclear-transcribed mRNA catabolic process, meiosis-specific transcripts; IGI:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; NAS:PomBase.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 5.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 5.
DR SUPFAM; SSF54236; SSF54236; 5.
DR PROSITE; PS00299; UBIQUITIN_1; 5.
DR PROSITE; PS50053; UBIQUITIN_2; 5.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396300"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396301"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396302"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396303"
FT CHAIN 305..380
FT /note="Ubiquitin"
FT /id="PRO_0000396304"
FT PROPEP 381..382
FT /id="PRO_0000396305"
FT DOMAIN 1..76
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 77..152
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 153..228
FT /note="Ubiquitin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 229..304
FT /note="Ubiquitin-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 305..380
FT /note="Ubiquitin-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ SEQUENCE 382 AA; 42972 MW; 8FEBA6235F9909A2 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
