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P0CG49

- UBB_MOUSE

UniProt

P0CG49 - UBB_MOUSE

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Protein

Polyubiquitin-B

Gene

Ubb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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.1 Publication

Sites

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

GO - Biological processi

  1. adipose tissue development Source: MGI
  2. energy homeostasis Source: MGI
  3. fat pad development Source: MGI
  4. female gonad development Source: MGI
  5. female meiosis I Source: MGI
  6. hypothalamus gonadotrophin-releasing hormone neuron development Source: MGI
  7. male gonad development Source: MGI
  8. male meiosis I Source: MGI
  9. mitochondrion transport along microtubule Source: MGI
  10. neuron projection morphogenesis Source: MGI
  11. positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
  12. regulation of mitochondrial membrane potential Source: MGI
  13. regulation of neuron death Source: MGI
  14. regulation of proteasomal protein catabolic process Source: MGI
  15. seminiferous tubule development Source: MGI
  16. ubiquitin homeostasis Source: MGI
Complete GO annotation...

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_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_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_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_203336. Degradation of beta-catenin by the destruction complex.
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_232069. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_232469. Hh ligand biogenesis disease.
REACT_232842. Fanconi Anemia pathway.
REACT_233316. Hedgehog ligand biogenesis.
REACT_237946. activated TAK1 mediates p38 MAPK activation.
REACT_241925. Circadian Clock.
REACT_244558. CDT1 association with the CDC6:ORC:origin complex.
REACT_245230. Orc1 removal from chromatin.
REACT_24972. Circadian Clock.
REACT_249922. CDK-mediated phosphorylation and removal of Cdc6.
REACT_258573. Cyclin D associated events in G1.
REACT_260435. Regulation of the Fanconi anemia pathway.
REACT_262002. Association of licensing factors with the pre-replicative complex.
REACT_263467. Ubiquitin-dependent degradation of Cyclin D1.
REACT_268522. GLI3 is processed to GLI3R by the proteasome.
REACT_268705. Degradation of GLI1 by the proteasome.
REACT_270923. Degradation of GLI2 by the proteasome.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyubiquitin-B
Cleaved into the following chain:
Gene namesi
Name:Ubb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:98888. Ubb.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: MGI
  3. neuronal cell body Source: MGI
  4. neuron projection Source: MGI
  5. nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676UbiquitinPRO_0000114801Add
BLAST
Chaini77 – 15276UbiquitinPRO_0000396188Add
BLAST
Chaini153 – 22876UbiquitinPRO_0000396189Add
BLAST
Chaini229 – 30476UbiquitinPRO_0000396190Add
BLAST
Propeptidei305 – 3051PRO_0000396191

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 PINK1By similarity
Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

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

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP0CG49.
PRIDEiP0CG49.

2D gel databases

REPRODUCTION-2DPAGEP62991.

PTM databases

PhosphoSiteiP0CG49.

Expressioni

Gene expression databases

BgeeiP0CG49.
ExpressionAtlasiP0CG49. baseline.
GenevestigatoriP62991.

Interactioni

Protein-protein interaction databases

BioGridi204402. 13 interactions.
IntActiP0CG49. 2 interactions.
MINTiMINT-8372791.

Structurei

3D structure databases

ProteinModelPortaliP0CG49.
SMRiP0CG49. Positions 1-303.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Ubiquitin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini77 – 15276Ubiquitin-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini153 – 22876Ubiquitin-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini229 – 30476Ubiquitin-like 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family.Curated
Contains 4 ubiquitin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

InParanoidiP0CG49.
KOiK04551.
OMAiVHENTRR.
OrthoDBiEOG7JDR1W.
PhylomeDBiP0CG49.
TreeFamiTF300820.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamiPF00240. ubiquitin. 4 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 4 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 4 hits.
PROSITEiPS00299. UBIQUITIN_1. 4 hits.
PS50053. UBIQUITIN_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0CG49-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE
110 120 130 140 150
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR
160 170 180 190 200
GGMQIFVKTL TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK
210 220 230 240 250
QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT
260 270 280 290 300
IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR

LRGGY
Length:305
Mass (Da):34,369
Last modified:August 10, 2010 - v1
Checksum:i0B8C7878AE958E68
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311Q → R in BAB29028. (PubMed:16141072)Curated
Sequence conflicti54 – 541R → S in BAB29028. (PubMed:16141072)Curated
Sequence conflicti61 – 611I → N in BAB29028. (PubMed:16141072)Curated
Sequence conflicti92 – 921E → G in BAB29028. (PubMed:16141072)Curated
Sequence conflicti117 – 1171Q → H in AAH19850. (PubMed:15489334)Curated
Sequence conflicti147 – 1471L → F in BAB28242. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51703 mRNA. Translation: CAA35999.1.
AK012443 mRNA. Translation: BAB28242.1.
AK003190 mRNA. Translation: BAB22630.1.
AK013873 mRNA. Translation: BAB29028.1.
BC019850 mRNA. Translation: AAH19850.1.
CCDSiCCDS24826.1.
PIRiS12583.
RefSeqiNP_035794.1. NM_011664.3.
XP_006533222.1. XM_006533159.1.
UniGeneiMm.282093.
Mm.371592.

Genome annotation databases

EnsembliENSMUST00000019649; ENSMUSP00000019649; ENSMUSG00000019505.
GeneIDi22187.
KEGGimmu:22187.
UCSCiuc007jjg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51703 mRNA. Translation: CAA35999.1 .
AK012443 mRNA. Translation: BAB28242.1 .
AK003190 mRNA. Translation: BAB22630.1 .
AK013873 mRNA. Translation: BAB29028.1 .
BC019850 mRNA. Translation: AAH19850.1 .
CCDSi CCDS24826.1.
PIRi S12583.
RefSeqi NP_035794.1. NM_011664.3.
XP_006533222.1. XM_006533159.1.
UniGenei Mm.282093.
Mm.371592.

3D structure databases

ProteinModelPortali P0CG49.
SMRi P0CG49. Positions 1-303.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204402. 13 interactions.
IntActi P0CG49. 2 interactions.
MINTi MINT-8372791.

PTM databases

PhosphoSitei P0CG49.

2D gel databases

REPRODUCTION-2DPAGE P62991.

Proteomic databases

MaxQBi P0CG49.
PRIDEi P0CG49.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000019649 ; ENSMUSP00000019649 ; ENSMUSG00000019505 .
GeneIDi 22187.
KEGGi mmu:22187.
UCSCi uc007jjg.1. mouse.

Organism-specific databases

CTDi 7314.
MGIi MGI:98888. Ubb.

Phylogenomic databases

InParanoidi P0CG49.
KOi K04551.
OMAi VHENTRR.
OrthoDBi EOG7JDR1W.
PhylomeDBi P0CG49.
TreeFami TF300820.

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_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_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_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_203336. Degradation of beta-catenin by the destruction complex.
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_232069. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_232469. Hh ligand biogenesis disease.
REACT_232842. Fanconi Anemia pathway.
REACT_233316. Hedgehog ligand biogenesis.
REACT_237946. activated TAK1 mediates p38 MAPK activation.
REACT_241925. Circadian Clock.
REACT_244558. CDT1 association with the CDC6:ORC:origin complex.
REACT_245230. Orc1 removal from chromatin.
REACT_24972. Circadian Clock.
REACT_249922. CDK-mediated phosphorylation and removal of Cdc6.
REACT_258573. Cyclin D associated events in G1.
REACT_260435. Regulation of the Fanconi anemia pathway.
REACT_262002. Association of licensing factors with the pre-replicative complex.
REACT_263467. Ubiquitin-dependent degradation of Cyclin D1.
REACT_268522. GLI3 is processed to GLI3R by the proteasome.
REACT_268705. Degradation of GLI1 by the proteasome.
REACT_270923. Degradation of GLI2 by the proteasome.

Miscellaneous databases

NextBioi 302157.
PROi P0CG49.
SOURCEi Search...

Gene expression databases

Bgeei P0CG49.
ExpressionAtlasi P0CG49. baseline.
Genevestigatori P62991.

Family and domain databases

InterProi IPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view ]
Pfami PF00240. ubiquitin. 4 hits.
[Graphical view ]
PRINTSi PR00348. UBIQUITIN.
SMARTi SM00213. UBQ. 4 hits.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 4 hits.
PROSITEi PS00299. UBIQUITIN_1. 4 hits.
PS50053. UBIQUITIN_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  2. "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.
  3. "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.
  4. "The emerging complexity of protein ubiquitination."
    Komander D.
    Biochem. Soc. Trans. 37:937-953(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, FUNCTION.

Entry informationi

Entry nameiUBB_MOUSE
AccessioniPrimary (citable) accession number: P0CG49
Secondary accession number(s): P02248
, P02249, P02250, P62991, Q29120, Q62317, Q64223, Q8VCH1, Q91887, Q91888, Q9CXY4, Q9CZM0, Q9D1R5, Q9D8D9, Q9ET23, Q9ET24, Q9Z0H9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: November 26, 2014
This is version 43 of the entry and version 1 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.
For the sake of clarity sequence features are annotated only for the first chain, and are not repeated for each of the following chains.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3