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P62983

- RS27A_MOUSE

UniProt

P62983 - RS27A_MOUSE

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Protein

Ubiquitin-40S ribosomal protein S27a

Gene
Rps27a, Uba80, Ubcep1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.
40S Ribosomal protein S27a: Component of the 40S subunit of the ribosome.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541Activating enzyme
Sitei68 – 681Essential for function
Binding sitei72 – 721Activating enzyme

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri121 – 14424C4-typeAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. structural constituent of ribosome Source: Ensembl

GO - Biological processi

  1. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_188191. Signaling by ERBB2.
REACT_188939. Glycogen synthesis.
REACT_188970. Oxidative Stress Induced Senescence.
REACT_188971. Oncogene Induced Senescence.
REACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196519. Regulation of innate immune responses to cytosolic DNA.
REACT_196549. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_196640. Stimuli-sensing channels.
REACT_196643. Constitutive Signaling by NOTCH1 HD Domain Mutants.
REACT_198518. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198525. Negative regulation of FGFR signaling.
REACT_198526. Spry regulation of FGF signaling.
REACT_198527. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_198536. IRAK2 mediated activation of TAK1 complex.
REACT_198539. TRAF6 mediated induction of TAK1 complex.
REACT_198543. IRAK1 recruits IKK complex.
REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_198634. Regulation of signaling by CBL.
REACT_198690. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199061. Downregulation of ERBB2:ERBB3 signaling.
REACT_199100. Downregulation of ERBB4 signaling.
REACT_199105. ER-Phagosome pathway.
REACT_199108. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_199123. Signaling by constitutively active EGFR.
REACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_199411. NOTCH2 Activation and Transmission of Signal to the Nucleus.
REACT_202271. NRIF signals cell death from the nucleus.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203841. Myoclonic epilepsy of Lafora.
REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_203917. EGFR downregulation.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_204812. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
REACT_205561. FCERI mediated NF-kB activation.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_207044. TCF dependent signaling in response to WNT.
REACT_207679. Separation of Sister Chromatids.
REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_211125. NOD1/2 Signaling Pathway.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_213035. regulation of FZD by ubiquitination.
REACT_214670. p75NTR recruits signalling complexes.
REACT_215733. Downregulation of TGF-beta receptor signaling.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_218887. NF-kB is activated and signals survival.
REACT_219118. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
REACT_219129. degradation of AXIN.
REACT_219771. deactivation of the beta-catenin transactivating complex.
REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_224208. Interleukin-1 signaling.
REACT_225145. Downstream TCR signaling.
REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_226192. IKK complex recruitment mediated by RIP1.
REACT_227429. degradation of DVL.
REACT_24972. Circadian Clock.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-40S ribosomal protein S27a
Alternative name(s):
Ubiquitin carboxyl extension protein 80
Cleaved into the following 2 chains:
Gene namesi
Name:Rps27a
Synonyms:Uba80, Ubcep1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1925544. Rps27a.

Subcellular locationi

Chain Ubiquitin : Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic small ribosomal subunit Source: Ensembl
  3. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676UbiquitinPRO_0000396479Add
BLAST
Chaini77 – 1568040S ribosomal protein S27aPRO_0000137663Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki6 – 6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki27 – 27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki29 – 29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki33 – 33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki48 – 48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-linki63 – 63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Modified residuei65 – 651Phosphoserine; by PINK1 By similarity
Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity
Modified residuei104 – 1041N6-acetyllysine By similarity
Modified residuei113 – 1131N6-acetyllysine By similarity
Modified residuei152 – 1521N6-acetyllysine1 Publication

Post-translational modificationi

Ubiquitin: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PARK2), triggering mitophagy By similarity.

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP62983.
PaxDbiP62983.
PRIDEiP62983.

2D gel databases

REPRODUCTION-2DPAGEP62991.

PTM databases

PhosphoSiteiP62983.

Expressioni

Gene expression databases

BgeeiP62983.
CleanExiMM_RPS27A.
GenevestigatoriP62991.

Interactioni

Subunit structurei

Ribosomal protein S27a is part of the 40S ribosomal subunit By similarity.

Protein-protein interaction databases

BioGridi219309. 14 interactions.
IntActiP62983. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP62983.
SMRiP62983. Positions 1-76, 82-152.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Ubiquitin-likeAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi77 – 9923Lys-rich (highly basic)Add
BLAST
Compositional biasi78 – 10730Lys-richAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the ubiquitin family.
In the C-terminal section; belongs to the ribosomal protein S27Ae family.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5272.
HOVERGENiHBG079153.
InParanoidiP62983.
KOiK02977.
OMAiMSILKYY.
OrthoDBiEOG7JDR1W.
PhylomeDBiP62983.
TreeFamiTF300036.

Family and domain databases

InterProiIPR002906. Ribosomal_S27a.
IPR011332. Ribosomal_zn-bd.
IPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamiPF01599. Ribosomal_S27. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF57829. SSF57829. 1 hit.
PROSITEiPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62983-1 [UniParc]FASTAAdd to Basket

« Hide

MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL    50
EDGRTLSDYN IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL 100
AVLKYYKVDE NGKISRLRRE CPSDECGAGV FMGSHFDRHY CGKCCLTYCF 150
NKPEDK 156
Length:156
Mass (Da):17,951
Last modified:August 10, 2010 - v2
Checksum:iC11DC63DF3A904F3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK018706 mRNA. Translation: BAB31357.1.
BC002108 mRNA. Translation: AAH02108.1.
CCDSiCCDS24497.1.
RefSeqiNP_001029037.1. NM_001033865.1.
NP_077239.1. NM_024277.2.
UniGeneiMm.180003.
Mm.458088.

Genome annotation databases

EnsembliENSMUST00000102844; ENSMUSP00000099908; ENSMUSG00000020460.
ENSMUST00000102845; ENSMUSP00000099909; ENSMUSG00000020460.
GeneIDi78294.
KEGGimmu:78294.
UCSCiuc007ihg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK018706 mRNA. Translation: BAB31357.1 .
BC002108 mRNA. Translation: AAH02108.1 .
CCDSi CCDS24497.1.
RefSeqi NP_001029037.1. NM_001033865.1.
NP_077239.1. NM_024277.2.
UniGenei Mm.180003.
Mm.458088.

3D structure databases

ProteinModelPortali P62983.
SMRi P62983. Positions 1-76, 82-152.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 219309. 14 interactions.
IntActi P62983. 2 interactions.

PTM databases

PhosphoSitei P62983.

2D gel databases

REPRODUCTION-2DPAGE P62991.

Proteomic databases

MaxQBi P62983.
PaxDbi P62983.
PRIDEi P62983.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102844 ; ENSMUSP00000099908 ; ENSMUSG00000020460 .
ENSMUST00000102845 ; ENSMUSP00000099909 ; ENSMUSG00000020460 .
GeneIDi 78294.
KEGGi mmu:78294.
UCSCi uc007ihg.1. mouse.

Organism-specific databases

CTDi 6233.
MGIi MGI:1925544. Rps27a.

Phylogenomic databases

eggNOGi COG5272.
HOVERGENi HBG079153.
InParanoidi P62983.
KOi K02977.
OMAi MSILKYY.
OrthoDBi EOG7JDR1W.
PhylomeDBi P62983.
TreeFami TF300036.

Enzyme and pathway databases

Reactomei REACT_188191. Signaling by ERBB2.
REACT_188939. Glycogen synthesis.
REACT_188970. Oxidative Stress Induced Senescence.
REACT_188971. Oncogene Induced Senescence.
REACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_196464. NOTCH1 Intracellular Domain Regulates Transcription.
REACT_196519. Regulation of innate immune responses to cytosolic DNA.
REACT_196549. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_196589. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
REACT_196591. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_196640. Stimuli-sensing channels.
REACT_196643. Constitutive Signaling by NOTCH1 HD Domain Mutants.
REACT_198518. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198525. Negative regulation of FGFR signaling.
REACT_198526. Spry regulation of FGF signaling.
REACT_198527. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_198532. Negative regulators of RIG-I/MDA5 signaling.
REACT_198536. IRAK2 mediated activation of TAK1 complex.
REACT_198539. TRAF6 mediated induction of TAK1 complex.
REACT_198543. IRAK1 recruits IKK complex.
REACT_198546. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
REACT_198634. Regulation of signaling by CBL.
REACT_198690. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199061. Downregulation of ERBB2:ERBB3 signaling.
REACT_199100. Downregulation of ERBB4 signaling.
REACT_199105. ER-Phagosome pathway.
REACT_199108. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_199123. Signaling by constitutively active EGFR.
REACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_199411. NOTCH2 Activation and Transmission of Signal to the Nucleus.
REACT_202271. NRIF signals cell death from the nucleus.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203841. Myoclonic epilepsy of Lafora.
REACT_203903. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
REACT_203917. EGFR downregulation.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_204812. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
REACT_205561. FCERI mediated NF-kB activation.
REACT_206033. Senescence-Associated Secretory Phenotype (SASP).
REACT_207044. TCF dependent signaling in response to WNT.
REACT_207679. Separation of Sister Chromatids.
REACT_210462. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_211125. NOD1/2 Signaling Pathway.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_213035. regulation of FZD by ubiquitination.
REACT_214670. p75NTR recruits signalling complexes.
REACT_215733. Downregulation of TGF-beta receptor signaling.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_218887. NF-kB is activated and signals survival.
REACT_219118. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
REACT_219129. degradation of AXIN.
REACT_219771. deactivation of the beta-catenin transactivating complex.
REACT_219800. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220566. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_224208. Interleukin-1 signaling.
REACT_225145. Downstream TCR signaling.
REACT_225463. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_226192. IKK complex recruitment mediated by RIP1.
REACT_227429. degradation of DVL.
REACT_24972. Circadian Clock.

Miscellaneous databases

NextBioi 348635.
PROi P62983.
SOURCEi Search...

Gene expression databases

Bgeei P62983.
CleanExi MM_RPS27A.
Genevestigatori P62991.

Family and domain databases

InterProi IPR002906. Ribosomal_S27a.
IPR011332. Ribosomal_zn-bd.
IPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view ]
Pfami PF01599. Ribosomal_S27. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view ]
PRINTSi PR00348. UBIQUITIN.
SMARTi SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
SSF57829. SSF57829. 1 hit.
PROSITEi PS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head and Kidney.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Liver and Mammary tumor.
  3. "The emerging complexity of protein ubiquitination."
    Komander D.
    Biochem. Soc. Trans. 37:937-953(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, FUNCTION.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRS27A_MOUSE
AccessioniPrimary (citable) accession number: P62983
Secondary accession number(s): P02248
, P02249, P02250, P49664, P62991, Q29120, Q62317, Q64223, Q8VCH1, Q91887, Q91888, Q9CXY4, Q9CZM0, Q9D1R5, Q9D2W3, Q9D8D9, Q9ET23, Q9ET24, Q9Z0H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 10, 2010
Last modified: September 3, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi