UBIQP_SOYBN
ID UBIQP_SOYBN Reviewed; 305 AA.
AC P69325; O82079; P03993;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Polyubiquitin;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Flags: Precursor;
GN Name=SUBI-1;
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Miyagishirome; TISSUE=Seedling;
RX PubMed=8159798; DOI=10.1104/pp.104.2.805;
RA Bao-Sen X., Waterhouse R.N., Watanabe Y., Kajiwara H., Komatsu S.,
RA Hirano H.;
RT "Nucleotide sequence of a soybean (Glycine max L. Merr.) ubiquitin gene.";
RL Plant Physiol. 104:805-806(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 229-305.
RX PubMed=2849766; DOI=10.1093/nar/16.23.11377;
RA Fortin M.G., Purohit S.K., Verma D.P.S.;
RT "The primary structure of soybean (Glycine max) ubiquitin is identical to
RT other plant ubiquitins.";
RL Nucleic Acids Res. 16:11377-11377(1988).
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-48-linked is involved in protein degradation via the proteasome.
CC Linear polymer chains formed via attachment by the initiator Met lead
CC to 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 (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 -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; D16248; BAA03764.1; -; Genomic_DNA.
DR EMBL; X13251; CAA31627.1; -; mRNA.
DR RefSeq; NP_001235900.1; NM_001248971.1.
DR RefSeq; XP_006589609.1; XM_006589546.2.
DR RefSeq; XP_006606032.1; XM_006605969.2.
DR RefSeq; XP_014618863.1; XM_014763377.1.
DR AlphaFoldDB; P69325; -.
DR SMR; P69325; -.
DR STRING; 3847.GLYMA07G32020.1; -.
DR EnsemblPlants; KRG91230; KRG91230; GLYMA_20G141600.
DR EnsemblPlants; KRH19452; KRH19452; GLYMA_13G117700.
DR EnsemblPlants; KRH19454; KRH19454; GLYMA_13G117900.
DR EnsemblPlants; KRH19455; KRH19455; GLYMA_13G117900.
DR EnsemblPlants; KRH35591; KRH35591; GLYMA_10G251900.
DR EnsemblPlants; KRH35592; KRH35592; GLYMA_10G251900.
DR GeneID; 100799042; -.
DR Gramene; KRG91230; KRG91230; GLYMA_20G141600.
DR Gramene; KRH19452; KRH19452; GLYMA_13G117700.
DR Gramene; KRH19454; KRH19454; GLYMA_13G117900.
DR Gramene; KRH19455; KRH19455; GLYMA_13G117900.
DR Gramene; KRH35591; KRH35591; GLYMA_10G251900.
DR Gramene; KRH35592; KRH35592; GLYMA_10G251900.
DR KEGG; gmx:100799042; -.
DR eggNOG; KOG0001; Eukaryota.
DR HOGENOM; CLU_010412_7_0_1; -.
DR InParanoid; P69325; -.
DR OMA; MSQDQSK; -.
DR OrthoDB; 1536766at2759; -.
DR Proteomes; UP000008827; Chromosome 10.
DR Proteomes; UP000008827; Chromosome 13.
DR Proteomes; UP000008827; Chromosome 20.
DR Genevisible; P69325; GM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProt.
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:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
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; 4.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 4.
DR SUPFAM; SSF54236; SSF54236; 4.
DR PROSITE; PS00299; UBIQUITIN_1; 4.
DR PROSITE; PS50053; UBIQUITIN_2; 4.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000114852"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396425"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396426"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396427"
FT PROPEP 305
FT /id="PRO_0000396428"
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 CROSSLNK 48
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 305 AA; 34192 MW; 901C32F1D4F3BE8F CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVESSDTID NVKAKIQDKE GIPPDQQRLI
FAGKQLEDGR TLADYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE SSDTIDNVKA
KIQDKEGIPP DQQRLIFAGK QLEDGRTLAD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
ITLEVESSDT IDNVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLADYNIQ KESTLHLVLR
LRGGF
