UBI1P_NICSY
ID UBI1P_NICSY Reviewed; 457 AA.
AC P0CG85; O82079; P03993; P69320;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Polyubiquitin;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Flags: Precursor;
GN Name=UBI11;
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=1281439; DOI=10.1007/bf00027161;
RA Genschik P., Parmentier Y., Durr A., Marbach J., Criqui M.-C., Jamet E.,
RA Fleck J.;
RT "Ubiquitin genes are differentially regulated in protoplast-derived
RT cultures of Nicotiana sylvestris and in response to various stresses.";
RL Plant Mol. Biol. 20:897-910(1992).
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: Ubiquitin is generally synthesized as a polyubiquitin
CC precursor with tandem head to tail repeats. Often, there is one to
CC three additional amino acids after the last repeat, removed in the
CC mature protein. Alternatively, ubiquitin extension protein is
CC synthesized as a single copy of ubiquitin fused to a ribosomal protein
CC (either L40 or S27A) or to an ubiquitin-related protein (either RUB1 or
CC RUB2). Following translation, extension protein is cleaved from
CC ubiquitin.
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; M74101; AAA34123.1; -; mRNA.
DR RefSeq; XP_009792248.1; XM_009793946.1.
DR AlphaFoldDB; P0CG85; -.
DR SMR; P0CG85; -.
DR STRING; 4096.XP_009792248.1; -.
DR GeneID; 104239332; -.
DR KEGG; nsy:104239332; -.
DR eggNOG; KOG0001; Eukaryota.
DR Proteomes; UP000189701; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IEA:UniProt.
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; 6.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 6.
DR SUPFAM; SSF54236; SSF54236; 6.
DR PROSITE; PS00299; UBIQUITIN_1; 6.
DR PROSITE; PS50053; UBIQUITIN_2; 6.
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_0000396401"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396402"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396403"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396404"
FT CHAIN 305..380
FT /note="Ubiquitin"
FT /id="PRO_0000396405"
FT CHAIN 381..456
FT /note="Ubiquitin"
FT /id="PRO_0000396406"
FT PROPEP 457
FT /id="PRO_0000396407"
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 DOMAIN 381..456
FT /note="Ubiquitin-like 6"
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 457 AA; 51206 MW; A1BF346A29F15F43 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
LRGGMQIFVK TLTGKTITLE VESSDTIDNV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL
ADYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ
QRLIFAGKQL EDGRTLADYN IQKESTLHLV LRLRGGF
