UBIQP_CRIGR
ID UBIQP_CRIGR Reviewed; 658 AA.
AC P62976; P02248; P02249; P02250; Q29120; Q60507; Q91887; Q91888;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 25-MAY-2022, entry version 81.
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;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lung fibroblast;
RX PubMed=8142469; DOI=10.1016/0167-4838(94)90018-3;
RA Nenoi M., Mita K., Ichimura S., Cartwright I.L.;
RT "Novel structure of a Chinese hamster polyubiquitin gene.";
RL Biochim. Biophys. Acta 1204:271-278(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-223.
RC TISSUE=Lung fibroblast;
RX PubMed=2537950; DOI=10.1093/nar/17.3.1215;
RA Fornace A.J. Jr., Alamo I. Jr., Hollander M.C., Lamoreaux E.;
RT "Ubiquitin mRNA is a major stress-induced transcript in mammalian cells.";
RL Nucleic Acids Res. 17:1215-1230(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-381.
RC TISSUE=Lung fibroblast;
RX PubMed=1314094; DOI=10.1016/0167-4781(92)90436-4;
RA Nenoi M., Mita K., Ichimura S.;
RT "Evolutionarily conserved structure of the 3' non-translated region of a
RT Chinese hamster polyubiquitin gene.";
RL Biochim. Biophys. Acta 1130:247-252(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-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 -!- 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; D63782; BAA09853.1; -; Genomic_DNA.
DR EMBL; X08013; CAA30815.1; -; mRNA.
DR EMBL; X60390; CAA42941.1; -; Genomic_DNA.
DR PIR; S42750; S42750.
DR RefSeq; NP_001231310.1; NM_001244381.1.
DR AlphaFoldDB; P62976; -.
DR SMR; P62976; -.
DR IntAct; P62976; 1.
DR STRING; 10029.NP_001231307.1; -.
DR GeneID; 100689268; -.
DR KEGG; cge:100689268; -.
DR CTD; 7314; -.
DR eggNOG; KOG0001; Eukaryota.
DR OrthoDB; 1536766at2759; -.
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; 8.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 8.
DR SUPFAM; SSF54236; SSF54236; 9.
DR PROSITE; PS00299; UBIQUITIN_1; 8.
DR PROSITE; PS50053; UBIQUITIN_2; 8.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; Repeat;
KW Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000114796"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396252"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396253"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396254"
FT CHAIN 305..380
FT /note="Ubiquitin"
FT /id="PRO_0000396255"
FT CHAIN 381..456
FT /note="Ubiquitin"
FT /id="PRO_0000396256"
FT CHAIN 457..532
FT /note="Ubiquitin"
FT /id="PRO_0000396257"
FT CHAIN 533..608
FT /note="Ubiquitin-related 1"
FT /id="PRO_0000396258"
FT CHAIN 609..658
FT /note="Ubiquitin-related 2"
FT /id="PRO_0000396259"
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 DOMAIN 457..532
FT /note="Ubiquitin-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 533..608
FT /note="Ubiquitin-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT SITE 54
FT /note="Interacts with activating enzyme"
FT SITE 68
FT /note="Essential for function"
FT SITE 72
FT /note="Interacts with activating enzyme"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CH28"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0CG48"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CONFLICT 381
FT /note="M -> Y (in Ref. 3; CAA42941)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 658 AA; 73950 MW; 4FBB4739B8803B53 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE PSDTIENVKA
KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
ITLEVEPSDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL
SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ
QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL
TGKTITLEVE PSDTIENVKA KIQDKQGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH
LVLRLRGGMQ IFVKTLTGKT ITLEVEPSNT IKKSKQEDGR TFLTTLSRKS TPCACSWA
