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Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]

 RS27A_BOVIN             Reviewed;         156 AA.
P62992; O97577; P02248; P02249; P02250; P0CG52; P62990; P80169;
Q01235; Q24K23; Q28169; Q28170; Q29120; Q3T0V5; Q3ZCE3; Q862C1;
Q862F4; Q862M4; Q862T5; Q862X8; Q91887; Q91888;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 2.
13-FEB-2019, entry version 105.
RecName: Full=Ubiquitin-40S ribosomal protein S27a;
AltName: Full=Ubiquitin carboxyl extension protein 80;
Contains:
RecName: Full=Ubiquitin;
Contains:
RecName: Full=40S ribosomal protein S27a;
Flags: Precursor;
Name=RPS27A; Synonyms=UBA80, UBCEP1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9765411;
Becher P., Orlich M., Thiel H.J.;
"Ribosomal S27a coding sequences upstream of ubiquitin coding
sequences in the genome of a pestivirus.";
J. Virol. 72:8697-8704(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12658628; DOI=10.1002/mrd.10292;
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H.,
Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y.,
Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
"Characterization of gene expression profiles in early bovine
pregnancy using a custom cDNA microarray.";
Mol. Reprod. Dev. 65:9-18(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Crossbred X Angus; TISSUE=Ileum, and Liver;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 1-74.
PubMed=1170880; DOI=10.1021/bi00681a026;
Schlesinger D.H., Goldstein G., Niall H.D.;
"The complete amino acid sequence of ubiquitin, an adenylate cyclase
stimulating polypeptide probably universal in living cells.";
Biochemistry 14:2214-2218(1975).
[5]
PROTEIN SEQUENCE OF 1-50.
PubMed=6254502; DOI=10.1016/0006-291X(80)91188-2;
Hamilton J.W., Rouse J.B.;
"The biosynthesis of ubiquitin by parathyroid gland.";
Biochem. Biophys. Res. Commun. 96:114-120(1980).
[6]
PROTEIN SEQUENCE OF 1-20.
TISSUE=Brain;
PubMed=1333954; DOI=10.1111/j.1432-1033.1992.tb17446.x;
Zdebska E., Antoniewicz J., Nilsson B., Sandhoff K., Fuerst W.,
Janik P., Koscielak J.;
"Ganglioside binding proteins of calf brain with ubiquitin-like N-
terminals.";
Eur. J. Biochem. 210:483-489(1992).
-!- FUNCTION: Ubiquitin: Exists either covalently attached to another
protein, or free (unanchored). When covalently bound, it is
conjugated to target proteins via an isopeptide bond either as a
monomer (monoubiquitin), a polymer linked via different Lys
residues of the ubiquitin (polyubiquitin chains) or a linear
polymer linked via the initiator Met of the ubiquitin (linear
polyubiquitin chains). Polyubiquitin chains, when attached to a
target protein, have different functions depending on the Lys
residue of the ubiquitin that is linked: Lys-6-linked may be
involved in DNA repair; Lys-11-linked is involved in ERAD
(endoplasmic reticulum-associated degradation) and in cell-cycle
regulation; Lys-29-linked is involved in lysosomal degradation;
Lys-33-linked is involved in kinase modification; Lys-48-linked is
involved in protein degradation via the proteasome; Lys-63-linked
is involved in endocytosis, DNA-damage responses as well as in
signaling processes leading to activation of the transcription
factor NF-kappa-B. Linear polymer chains formed via attachment by
the initiator Met lead to cell signaling. Ubiquitin is usually
conjugated to Lys residues of target proteins, however, in rare
cases, conjugation to Cys or Ser residues has been observed. When
polyubiquitin is free (unanchored-polyubiquitin), it also has
distinct roles, such as in activation of protein kinases, and in
signaling (By similarity). {ECO:0000250}.
-!- FUNCTION: 40S Ribosomal protein S27a: Component of the 40S subunit
of the ribosome.
-!- SUBUNIT: Ribosomal protein S27a is part of the 40S ribosomal
subunit. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- PTM: Ubiquitin: Phosphorylated at Ser-65 by PINK1 during
mitophagy. Phosphorylated ubiquitin specifically binds and
activates parkin (PRKN), triggering mitophagy. Phosphorylation
does not affect E1-mediated E2 charging of ubiquitin but affects
discharging of E2 enzymes to form polyubiquitin chains. It also
affects deubiquitination by deubiquitinase enzymes such as USP30.
{ECO:0000250|UniProtKB:P62979}.
-!- PTM: Ubiquitin: Mono-ADP-ribosylated at the C-terminus by PARP9, a
component of the PPAR9-DTX3L complex. ADP-ribosylation requires
processing by E1 and E2 enzymes and prevents ubiquitin conjugation
to substrates such as histones. {ECO:0000250|UniProtKB:P62979}.
-!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. Uba52
and Rps27a genes code for a single copy of ubiquitin fused to the
ribosomal proteins L40 and S27a, respectively. UBB and UBC genes
code for a polyubiquitin precursor with exact head to tail
repeats, the number of repeats differ between species and strains.
-!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin
family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
ribosomal protein eS31 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AF058700; AAC77907.1; -; mRNA.
EMBL; AB098891; BAC56381.1; -; mRNA.
EMBL; BC102491; AAI02492.2; -; mRNA.
PIR; A28144; A28144.
RefSeq; NP_777203.1; NM_174778.1.
RefSeq; XP_005212615.1; XM_005212558.2.
UniGene; Bt.4286; -.
PDB; 4M0W; X-ray; 1.40 A; B=1-76.
PDB; 4Y1H; X-ray; 1.40 A; A=1-76.
PDB; 4Z9S; X-ray; 2.30 A; A/B/C/D=1-76.
PDB; 5BZ0; X-ray; 2.10 A; B=1-76.
PDB; 5FER; X-ray; 2.34 A; C/F=1-76.
PDB; 5JQS; X-ray; 2.65 A; D=1-76.
PDB; 5MN9; X-ray; 2.05 A; A/B=1-76.
PDB; 5XU8; X-ray; 1.81 A; B=1-76.
PDB; 5XVE; X-ray; 1.24 A; B=1-76.
PDB; 6DJW; X-ray; 3.80 A; B=1-74.
PDB; 6DJX; X-ray; 4.80 A; B=1-76.
PDB; 6E2B; X-ray; 1.45 A; A/C/E/G/I/P=1-76.
PDBsum; 4M0W; -.
PDBsum; 4Y1H; -.
PDBsum; 4Z9S; -.
PDBsum; 5BZ0; -.
PDBsum; 5FER; -.
PDBsum; 5JQS; -.
PDBsum; 5MN9; -.
PDBsum; 5XU8; -.
PDBsum; 5XVE; -.
PDBsum; 6DJW; -.
PDBsum; 6DJX; -.
PDBsum; 6E2B; -.
ProteinModelPortal; P62992; -.
SMR; P62992; -.
BioGrid; 159949; 3.
STRING; 9913.ENSBTAP00000033015; -.
PaxDb; P62992; -.
PRIDE; P62992; -.
Ensembl; ENSBTAT00000033091; ENSBTAP00000033015; ENSBTAG00000015473.
GeneID; 286839; -.
KEGG; bta:286839; -.
CTD; 6233; -.
VGNC; VGNC:34135; RPS27A.
eggNOG; KOG0004; Eukaryota.
eggNOG; COG5272; LUCA.
GeneTree; ENSGT00910000144152; -.
HOVERGEN; HBG079148; -.
InParanoid; P62992; -.
KO; K02977; -.
OMA; MSILKYY; -.
OrthoDB; 1536766at2759; -.
TreeFam; TF300036; -.
Proteomes; UP000009136; Chromosome 11.
Bgee; ENSBTAG00000015473; Expressed in 9 organ(s), highest expression level in spleen.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031386; F:protein tag; IBA:GO_Central.
GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
GO; GO:0006412; P:translation; IEA:InterPro.
Gene3D; 2.20.25.660; -; 1.
InterPro; IPR002906; Ribosomal_S27a.
InterPro; IPR011332; Ribosomal_zn-bd.
InterPro; IPR038582; S27a-like_sf.
InterPro; IPR019956; Ubiquitin.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR019954; Ubiquitin_CS.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF01599; Ribosomal_S27; 1.
Pfam; PF00240; ubiquitin; 1.
PRINTS; PR00348; UBIQUITIN.
SMART; SM01402; Ribosomal_S27; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF57829; SSF57829; 1.
PROSITE; PS00299; UBIQUITIN_1; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Complete proteome;
Cytoplasm; Direct protein sequencing; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Repeat;
Ribonucleoprotein; Ribosomal protein; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 76 Ubiquitin.
/FTId=PRO_0000396474.
CHAIN 77 156 40S ribosomal protein S27a.
/FTId=PRO_0000137660.
DOMAIN 1 76 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
ZN_FING 121 144 C4-type.
COMPBIAS 77 99 Lys-rich (highly basic).
COMPBIAS 78 107 Lys-rich.
BINDING 54 54 Activating enzyme.
BINDING 72 72 Activating enzyme.
SITE 68 68 Essential for function.
MOD_RES 65 65 Phosphoserine; by PINK1.
{ECO:0000250|UniProtKB:P62979}.
MOD_RES 76 76 ADP-ribosylglycine.
{ECO:0000250|UniProtKB:P62979}.
MOD_RES 104 104 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62979}.
MOD_RES 113 113 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62979}.
MOD_RES 152 152 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62983}.
CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P62979}.
CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P62979}.
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P62979}.
CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P62979}.
CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P62979}.
CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P62979}.
CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys)
(interchain with K-? in acceptor
proteins).
CONFLICT 141 156 CGKCCLTYCFNKPEDK -> VANVV (in Ref. 2;
BAC56381). {ECO:0000305}.
STRAND 2 6 {ECO:0000244|PDB:5XVE}.
STRAND 8 10 {ECO:0000244|PDB:5XVE}.
STRAND 12 16 {ECO:0000244|PDB:5XVE}.
HELIX 23 34 {ECO:0000244|PDB:5XVE}.
HELIX 38 40 {ECO:0000244|PDB:5XVE}.
STRAND 42 45 {ECO:0000244|PDB:5XVE}.
HELIX 56 59 {ECO:0000244|PDB:5XVE}.
STRAND 66 70 {ECO:0000244|PDB:5XVE}.
STRAND 73 75 {ECO:0000244|PDB:5JQS}.
SEQUENCE 156 AA; 17965 MW; 617BC63DF3A904F7 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL AVLKYYKVDE NGKISRLRRE
CPSDECGAGV FMASHFDRHY CGKCCLTYCF NKPEDK


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Pathways :
WP211: BMP signaling pathway
WP2199: Seed Development
WP2292: Chemokine signaling pathway
WP210: Cytoplasmic Ribosomal Proteins
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair

Related Genes :
[Rps27a Uba80 Ubcep1] Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[RPS27A UBA80 UBCEP1] Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; 40S ribosomal protein S27a (Small ribosomal subunit protein eS31)]
[RPS27A UBA80 UBCEP1] Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[Rps27a Uba80 Ubcep1] Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[RPS27A UBA80] Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[RpS27A UB3-D UBI-F80 Ubi-m CG5271] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[RPS27A UBA80 UBCEP1 UBIZ] Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[RPS27AA UBQ16 At1g23410 F26F24.28 F28C11.5] Ubiquitin-40S ribosomal protein S27a-1 [Cleaved into: Ubiquitin; 40S ribosomal protein S27a-1]
[rps27a uba80] Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[ubi3 SPAC6G10.11c] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[RPS27AB UBQ6 At2g47110 F14M4.6] Ubiquitin-40S ribosomal protein S27a-2 [Cleaved into: Ubiquitin; 40S ribosomal protein S27a-2]
[RPS27AC UBQ5 At3g62250 T17J13.210] Ubiquitin-40S ribosomal protein S27a-3 [Cleaved into: Ubiquitin; 40S ribosomal protein S27a-3]
[ubi::crp-6 ubi-3 NCU04553] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a (Cytoplasmic ribosomal protein 6) (CRP6) (S37)]
[UBI3 RPS27A] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[ubi3 KLLA0D18304g] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[UBF9 RPS27A] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[ubqC DDB_G0276765] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[RPS27AB UBQ6 Os05g0160200 LOC_Os05g06770 OsJ_17209 OSJNBa0017J22.14 OSJNBa0034O12.6] Ubiquitin-40S ribosomal protein S27a-2 [Cleaved into: Ubiquitin; 40S ribosomal protein S27a-2]
[RPS31 RPS37 UBI3 YLR167W L9470.14] Ubiquitin-40S ribosomal protein S31 [Cleaved into: Ubiquitin; 40S ribosomal protein S31 (CEP76) (S37) (Small ribosomal subunit protein eS31) (YS24)]
[RPS27AA Os01g0328400 LOC_Os01g22490 OsJ_01558 P0537A05.41] Ubiquitin-40S ribosomal protein S27a-1 [Cleaved into: Ubiquitin; 40S ribosomal protein S27a-1]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[UBI3 RPS27A] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[MUB1 RPS27A1] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[MUB2 RPS27A2] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]
[] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a] (Fragment)
[] Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a] (Fragment)

Bibliography :
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