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Q3UE37 (UBE2Z_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 Z

EC=6.3.2.19
Alternative name(s):
Uba6-specific E2 conjugating enzyme 1
Short name=Use1
Ubiquitin carrier protein Z
Ubiquitin-protein ligase Z
Gene names
Name:Ube2z
Synonyms:D11Moh35
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin to other proteins. Specific substrate for UBA6, not charged with ubiquitin by UBE1. May be involved in apoptosis regulation By similarity.

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence caution

The sequence AAH54412.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAB24097.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAC37014.1 differs from that shown. Reason: Frameshift at position 115.

Ontologies

Keywords
   Biological processApoptosis
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Ubiquitin-conjugating enzyme E2 Z
PRO_0000280516

Sites

Active site1901Glycyl thioester intermediate By similarity

Experimental info

Sequence conflict71E → D in BAC37014. Ref.1
Sequence conflict101A → S in BAC37014. Ref.1
Sequence conflict16 – 172AG → SW in BAC37014. Ref.1
Sequence conflict2001P → H in BAC37014. Ref.1
Sequence conflict2231P → R in BAC37014. Ref.1
Sequence conflict2381D → E in BAC37014. Ref.1
Sequence conflict3361E → G in BAE29074. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3UE37 [UniParc].

Last modified March 20, 2007. Version 2.
Checksum: 15FB00E9988B0A6D

FASTA35638,368
        10         20         30         40         50         60 
MAESPTEEAA TATAGAGAAG PGSSGVAGVV GVSGSGGGFG PPFLPDVWAA AAAAGGAGGP 

        70         80         90        100        110        120 
GSGLAPLPGL PPSAAAHGAA LLSHWDPTLS SDWDGERTAP QCLLRIKRDI MSIYKEPPPG 

       130        140        150        160        170        180 
MFVVPDTVDM TKIHALITGP FDTPYEGGFF LFVFRCPPDY PIHPPRVKLM TTGNNTVRFN 

       190        200        210        220        230        240 
PNFYRNGKVC LSILGTWTGP AWSPAQSISS VLISIQSLMT ENPYHNEPGF EQERHPGDSK 

       250        260        270        280        290        300 
NYNECIRHET IRVAVCDMME GKCPCPEPLR GVMEKSFLEY YDFYEVACKD RLHLQGQTMQ 

       310        320        330        340        350 
DPFGEKRGHF DYQSLLMRLG LIRQKVLERL HNENAEMDSD SSSSGTETDL HGSLRV 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Amnion, Bone marrow, Placenta and Thymus.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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] OF 70-356.
Strain: Czech II.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK005524 mRNA. Translation: BAB24097.1. Different initiation.
AK077793 mRNA. Translation: BAC37014.1. Frameshift.
AK149770 mRNA. Translation: BAE29074.1.
AK153328 mRNA. Translation: BAE31907.1.
AK168942 mRNA. Translation: BAE40750.1.
AL603682 Genomic DNA. Translation: CAM18270.1.
BC054412 mRNA. Translation: AAH54412.1. Different initiation.
RefSeqNP_758504.3. NM_172300.3.
UniGeneMm.38802.

3D structure databases

ProteinModelPortalQ3UE37.
SMRQ3UE37. Positions 96-334.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ3UE37. 1 interaction.
MINTMINT-8178502.

PTM databases

PhosphoSiteQ3UE37.

Proteomic databases

PaxDbQ3UE37.
PRIDEQ3UE37.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000100528; ENSMUSP00000098097; ENSMUSG00000014349.
GeneID268470.
KEGGmmu:268470.
UCSCuc007lbd.2. mouse.

Organism-specific databases

CTD65264.
MGIMGI:1343160. Ube2z.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00730000110680.
HOVERGENHBG083204.
InParanoidA2A6M3.
KOK10585.
OMAAVMANMS.
OrthoDBEOG7MSMP5.
PhylomeDBQ3UE37.
TreeFamTF354204.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeQ3UE37.
CleanExMM_UBE2Z.
GenevestigatorQ3UE37.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2Z. mouse.
NextBio392311.
PROQ3UE37.
SOURCESearch...

Entry information

Entry nameUBE2Z_MOUSE
AccessionPrimary (citable) accession number: Q3UE37
Secondary accession number(s): A2A6M3 expand/collapse secondary AC list , Q3TFZ8, Q3U618, Q7TMY6, Q8BVL2, Q9DAU4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: April 16, 2014
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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