UBIQP_XENLA
ID UBIQP_XENLA Reviewed; 167 AA.
AC P62972; P02248; P02249; P02250; Q29120; Q91887; Q91888;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Polyubiquitin;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Flags: Precursor; Fragment;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6209017; DOI=10.1016/0092-8674(84)90010-2;
RA Dworkin-Rastl E., Shrutkowski A., Dworkin M.B.;
RT "Multiple ubiquitin mRNAs during Xenopus laevis development contain tandem
RT repeats of the 76 amino acid coding sequence.";
RL Cell 39:321-325(1984).
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 proteotoxic stress
CC response and cell cycle; Lys-33-linked is involved in kinase
CC modification; Lys-48-linked is involved in protein degradation via the
CC proteasome; Lys-63-linked is involved in endocytosis, DNA-damage
CC responses as well as in signaling processes leading to activation of
CC the transcription factor NF-kappa-B. Linear polymer chains formed via
CC attachment by the initiator Met lead to cell signaling. Ubiquitin is
CC usually conjugated to Lys residues of target proteins, however, in rare
CC cases, conjugation to Cys or Ser residues has been observed. When
CC polyubiquitin is free (unanchored-polyubiquitin), it also has distinct
CC roles, such as in activation of protein kinases, and in signaling (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P62972; Q6P704: ufd1.S; NbExp=2; IntAct=EBI-412964, EBI-15677370;
CC P62972; Q9NPC3: CCNB1IP1; Xeno; NbExp=2; IntAct=EBI-412964, EBI-745269;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Ubiquitin is synthesized as a polyubiquitin precursor
CC with exact head to tail repeats, the number of repeats differ between
CC species (up to 12 in Xenopus). In some species there is a final amino-
CC acid after the last repeat. Some ubiquitin genes contain a single copy
CC of ubiquitin fused to a ribosomal protein (either L40 or S27a).
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; M11512; AAA49978.1; -; mRNA.
DR PDB; 2K39; NMR; -; A=92-167.
DR PDB; 2KDE; NMR; -; B/C=92-167.
DR PDBsum; 2K39; -.
DR PDBsum; 2KDE; -.
DR AlphaFoldDB; P62972; -.
DR SMR; P62972; -.
DR DIP; DIP-40040N; -.
DR IntAct; P62972; 4.
DR MINT; P62972; -.
DR EvolutionaryTrace; P62972; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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; 2.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 2.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS00299; UBIQUITIN_1; 2.
DR PROSITE; PS50053; UBIQUITIN_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Reference proteome;
KW Repeat; Ubl conjugation.
FT CHAIN <1..15
FT /note="Ubiquitin"
FT /id="PRO_0000114811"
FT CHAIN 16..91
FT /note="Ubiquitin"
FT /id="PRO_0000396250"
FT CHAIN 92..167
FT /note="Ubiquitin"
FT /id="PRO_0000396251"
FT DOMAIN <1..15
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 16..91
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 92..167
FT /note="Ubiquitin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT SITE 69
FT /note="Interacts with activating enzyme"
FT SITE 83
FT /note="Essential for function"
FT SITE 87
FT /note="Interacts with activating enzyme"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 26
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 44
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG47"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT NON_TER 1
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2K39"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:2K39"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:2K39"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:2K39"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2K39"
FT TURN 147..151
FT /evidence="ECO:0007829|PDB:2K39"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:2K39"
SQ SEQUENCE 167 AA; 18801 MW; 9C8F431544081131 CRC64;
QKESTLHLVL RLRGGMQIFV KTLTGKTITL EVEPSDTIEN VKAKIQDKEG IPPDQQRLIF
AGKQLEDGRT LSDYNIQKES TLHLVLRLRG GMQIFVKTLT GKTITLEVEP SDTIENVKAK
IQDKEGIPPD QQRLIFAGKQ LEDGRTLSDY NIQKESTLHL VLRLRGG
