UBIQP_ACEPE
ID UBIQP_ACEPE Reviewed; 423 AA.
AC P42739;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Polyubiquitin;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=Ubiquitin-related 1;
DE Contains:
DE RecName: Full=Ubiquitin-related 2;
DE Flags: Precursor; Fragment;
OS Acetabularia peniculus (Green alga) (Polyphysa peniculus).
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; TCBD clade;
OC Dasycladales; Polyphysaceae; Acetabularia.
OX NCBI_TaxID=35862;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Frank S., Menzel D.;
RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
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, DNA-damage responses as well as in signaling
CC processes leading to activation of the transcription factor NF-kappa-B.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z28649; CAA82268.1; -; Genomic_DNA.
DR AlphaFoldDB; P42739; -.
DR SMR; P42739; -.
DR PRIDE; P42739; -.
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; 5.
DR PROSITE; PS50053; UBIQUITIN_2; 6.
PE 3: Inferred from homology;
KW Cytoplasm; Isopeptide bond; Nucleus; Repeat; Ubl conjugation.
FT CHAIN <1..41
FT /note="Ubiquitin"
FT /id="PRO_0000114830"
FT CHAIN 42..117
FT /note="Ubiquitin-related 1"
FT /id="PRO_0000396377"
FT CHAIN 118..193
FT /note="Ubiquitin"
FT /id="PRO_0000396378"
FT CHAIN 194..269
FT /note="Ubiquitin"
FT /id="PRO_0000396379"
FT CHAIN 270..345
FT /note="Ubiquitin"
FT /id="PRO_0000396380"
FT CHAIN 346..421
FT /note="Ubiquitin-related 2"
FT /id="PRO_0000396381"
FT PROPEP 422..423
FT /id="PRO_0000396382"
FT DOMAIN <1..41
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 42..117
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 118..193
FT /note="Ubiquitin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 194..269
FT /note="Ubiquitin-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 270..345
FT /note="Ubiquitin-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 346..421
FT /note="Ubiquitin-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 89
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 117
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
SQ SEQUENCE 423 AA; 47449 MW; 068C4C2707E9AB22 CRC64;
IPPDQQRLIF AGKQLEDGRT LADYNIQKES TLHLVLRLRG GMQIFVKTLT GKTITLEVQS
SDTVENVKSK IQDKEGIPPD QQRLIFAGKQ LEDGLTLADY NIQKESTLHL VLRLRGGMQI
FVKTLTGKTI TLEVESSDTV ENVKSKIQDK EGIPPDQQRL IFAGKQLEDG RTLADYNIQK
ESTLHLVLRL RGGMQIFVKT LTGKTITLEV ESSDTVENVK SKIQDKEGIP PDQQRLIFAG
KQLEDGRTLA DYNIQKESTL HLVLRLRGGM QIFVKTLTGK TITLEVESSD TVENVKSKIQ
DKEGIPPDQQ RLIFAGKQLE DGRTLADYNI QKESTLHLVL RLRGGMQIFV KTLTGKTITL
EVESSDTVEN VKSKIQDKEG IPPDQQRIIF AGKQLEDGRT LADYNIQKES TLHLVLRLRG
GAF
