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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.

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. seminiferous tubule development Source: MGI
  10. ubiquitin homeostasis Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_24972. Circadian Clock.

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. 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 PINK1 By similarity
Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity

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

PRIDEiP0CG49.

2D gel databases

REPRODUCTION-2DPAGEP62991.

PTM databases

PhosphoSiteiP0CG49.

Expressioni

Gene expression databases

BgeeiP0CG49.
GenevestigatoriP62991.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP0CG49.
SMRiP0CG49. Positions 1-303.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Belongs to the ubiquitin family.

Keywords - Domaini

Repeat

Phylogenomic databases

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

MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL    50
EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE 100
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR 150
GGMQIFVKTL TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK 200
QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT 250
IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR 300
LRGGY 305
Length:305
Mass (Da):34,369
Last modified:August 10, 2010 - v1
Checksum:i0B8C7878AE958E68
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti31 – 311Q → R in BAB29028. 1 Publication
Sequence conflicti54 – 541R → S in BAB29028. 1 Publication
Sequence conflicti61 – 611I → N in BAB29028. 1 Publication
Sequence conflicti92 – 921E → G in BAB29028. 1 Publication
Sequence conflicti117 – 1171Q → H in AAH19850. 1 Publication
Sequence conflicti147 – 1471L → F in BAB28242. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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

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

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

Enzyme and pathway databases

Reactomei REACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
REACT_24972. Circadian Clock.

Miscellaneous databases

ChiTaRSi UBB. mouse.
NextBioi 302157.
PROi P0CG49.
SOURCEi Search...

Gene expression databases

Bgeei P0CG49.
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: September 3, 2014
This is version 40 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

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