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Reviewed, UniProtKB/Swiss-Prot Q8K2Z8 (UB2Q2_MOUSE)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ubiquitin-conjugating enzyme E2 Q2
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase Q2
    Ubiquitin carrier protein Q2
Gene names
Name: Ube2q2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length378 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin to other proteins By similarity.

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathway

Protein modification; protein ubiquitination.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8K2Z8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8K2Z8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-123: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 378378Ubiquitin-conjugating enzyme E2 Q2
PRO_0000223880

Regions

Compositional bias41 – 5616Pro-rich
Compositional bias138 – 18144Glu-rich

Sites

Active site3071Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue3721Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 123123Missing in isoform 2.
VSP_017300
Natural variant2351I → T in strain: FVB/N. Ref.2

Experimental info

Sequence conflict2461L → Q in BAC38813. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 21, 2006. Version 2.
Checksum: 4A81D0AC4BD302E3

FASTA37842,935
        10         20         30         40         50         60 
MSVSGLKAEL KFLASIFDKN HERFRIVSWK LDELHCQFLV PPPPPPPGSS LSPPPPLTLH 

        70         80         90        100        110        120 
CNITESYPSS SPIWFVDSDD PNLTSVLERL EDTKNNSSLR QQLKWLICDL CRLYNLPKHL 

       130        140        150        160        170        180 
DVEMLDQPLP TGQNGTTEEV TSEEEEEEEM AEDIEDLDHY EMKEEEPING KKSEDEGIEK 

       190        200        210        220        230        240 
ENLAILEKIR KTQRQDHLNG AVSGSVQASD RLMKELRDVY RSQSYKAGIY SVELINDSLY 

       250        260        270        280        290        300 
DWHVKLHKVD SDSPLHSDLQ ILKEKEGIEY ILLNFSFKDN FPFDPPFVRV VLPVLSGGYV 

       310        320        330        340        350        360 
LGGGALCMEL LTKQGWSSAY SIESVIMQIN ATLVKGKARV QFGANKNQYN LARAQQSYNS 

       370 
IVQIHEKNGW YTPPKEDG 

« Hide

Isoform 2.

Checksum: 2F5077B3FAC2D6DF
Show »

FASTA25528,916

References

[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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Bone marrow, Fetal head, Hippocampus and Thymus.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-235.
Strain: FVB/N.
Tissue: Mammary tumor.

Cross-references

Sequence databases

AK083216 mRNA. Translation: BAC38813.1.
AK076148 mRNA. Translation: BAC36218.1.
AK042515 mRNA. Translation: BAE20633.1.
AK150776 mRNA. Translation: BAE29841.1.
BC029111 mRNA. Translation: AAH29111.1.
IPIIPI00345026.
IPI00719933.
RefSeqNP_850931.1.
UniGeneMm.207894

3D structure databases

SMRQ8K2Z8. Positions 204-365.
ModBaseSearch...

PTM databases

PhosphoSiteQ8K2Z8.

Genome annotation databases

EnsemblENSMUSG00000032307. Mus musculus. [Contig view]
GeneID109161.
KEGGmmu:109161.

Organism-specific databases

MGIMGI:2388672. Ube2q2.

Phylogenomic databases

HOGENOMQ8K2Z8.
HOVERGENQ8K2Z8.
OMAQ8K2Z8. YKAGIYS.

Enzyme and pathway databases

BRENDA6.3.2.19. 244.

Gene expression databases

ArrayExpressQ8K2Z8.
BgeeQ8K2Z8.
CleanExMM_UBE2Q2.
GermOnlineENSMUSG00000032307. Mus musculus.

Family and domain databases

InterProIPR006575. RWD.
IPR016135. UBQ-conjugat/RWD-like.
IPR000608. UBQ-conjugat_E2.
[Graphical view]
Gene3DG3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
PfamPF05773. RWD. 1 hit.
PF00179. UQ_con. 1 hit.
[Graphical view]
ProDomPD000461. UBQ_conjugat. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00591. RWD. 1 hit.
SM00212. UBCc. 1 hit.
[Graphical view]
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. False negative.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio361712.
SOURCESearch...

Entry information

Entry nameUB2Q2_MOUSE
AccessionPrimary (citable) accession number: Q8K2Z8
Secondary accession number(s): Q3UBX3 expand/collapse secondary AC list , Q3V3A5, Q8BUN2, Q8BVX5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: February 21, 2006
Last modified: June 16, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents