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Protein

Ubiquitin-conjugating enzyme E2 Z

Gene

Ube2z

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).PROSITE-ProRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei190 – 1901Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. ubiquitin conjugating enzyme activity Source: MGI
  4. ubiquitin-like protein transferase activity Source: GO_Central
  5. ubiquitin protein ligase activity Source: GO_Central
  6. ubiquitin protein ligase binding Source: GO_Central

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. protein polyubiquitination Source: GO_Central
  3. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ube2z
Synonyms:D11Moh35
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1343160. Ube2z.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Ubiquitin-conjugating enzyme E2 ZPRO_0000280516Add
BLAST

Proteomic databases

MaxQBiQ3UE37.
PaxDbiQ3UE37.
PRIDEiQ3UE37.

PTM databases

PhosphoSiteiQ3UE37.

Expressioni

Gene expression databases

BgeeiQ3UE37.
CleanExiMM_UBE2Z.
GenevestigatoriQ3UE37.

Interactioni

Protein-protein interaction databases

BioGridi234504. 1 interaction.
IntActiQ3UE37. 1 interaction.
MINTiMINT-8178502.

Structurei

3D structure databases

ProteinModelPortaliQ3UE37.
SMRiQ3UE37. Positions 121-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00540000070023.
HOVERGENiHBG083204.
InParanoidiQ3UE37.
KOiK10585.
OMAiAVMANMS.
OrthoDBiEOG7MSMP5.
PhylomeDBiQ3UE37.
TreeFamiTF354204.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3UE37-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAESPTEEAA TATAGAGAAG PGSSGVAGVV GVSGSGGGFG PPFLPDVWAA
60 70 80 90 100
AAAAGGAGGP GSGLAPLPGL PPSAAAHGAA LLSHWDPTLS SDWDGERTAP
110 120 130 140 150
QCLLRIKRDI MSIYKEPPPG MFVVPDTVDM TKIHALITGP FDTPYEGGFF
160 170 180 190 200
LFVFRCPPDY PIHPPRVKLM TTGNNTVRFN PNFYRNGKVC LSILGTWTGP
210 220 230 240 250
AWSPAQSISS VLISIQSLMT ENPYHNEPGF EQERHPGDSK NYNECIRHET
260 270 280 290 300
IRVAVCDMME GKCPCPEPLR GVMEKSFLEY YDFYEVACKD RLHLQGQTMQ
310 320 330 340 350
DPFGEKRGHF DYQSLLMRLG LIRQKVLERL HNENAEMDSD SSSSGTETDL

HGSLRV
Length:356
Mass (Da):38,368
Last modified:March 19, 2007 - v2
Checksum:i15FB00E9988B0A6D
GO

Sequence cautioni

The sequence AAH54412.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB24097.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC37014.1 differs from that shown. Reason: Frameshift at position 115. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71E → D in BAC37014 (PubMed:16141072).Curated
Sequence conflicti10 – 101A → S in BAC37014 (PubMed:16141072).Curated
Sequence conflicti16 – 172AG → SW in BAC37014 (PubMed:16141072).Curated
Sequence conflicti200 – 2001P → H in BAC37014 (PubMed:16141072).Curated
Sequence conflicti223 – 2231P → R in BAC37014 (PubMed:16141072).Curated
Sequence conflicti238 – 2381D → E in BAC37014 (PubMed:16141072).Curated
Sequence conflicti336 – 3361E → G in BAE29074 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS36289.1.
RefSeqiNP_758504.3. NM_172300.3.
UniGeneiMm.38802.

Genome annotation databases

EnsembliENSMUST00000100528; ENSMUSP00000098097; ENSMUSG00000014349.
GeneIDi268470.
KEGGimmu:268470.
UCSCiuc007lbd.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS36289.1.
RefSeqiNP_758504.3. NM_172300.3.
UniGeneiMm.38802.

3D structure databases

ProteinModelPortaliQ3UE37.
SMRiQ3UE37. Positions 121-277.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234504. 1 interaction.
IntActiQ3UE37. 1 interaction.
MINTiMINT-8178502.

PTM databases

PhosphoSiteiQ3UE37.

Proteomic databases

MaxQBiQ3UE37.
PaxDbiQ3UE37.
PRIDEiQ3UE37.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000100528; ENSMUSP00000098097; ENSMUSG00000014349.
GeneIDi268470.
KEGGimmu:268470.
UCSCiuc007lbd.2. mouse.

Organism-specific databases

CTDi65264.
MGIiMGI:1343160. Ube2z.

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00540000070023.
HOVERGENiHBG083204.
InParanoidiQ3UE37.
KOiK10585.
OMAiAVMANMS.
OrthoDBiEOG7MSMP5.
PhylomeDBiQ3UE37.
TreeFamiTF354204.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

ChiTaRSiUbe2z. mouse.
NextBioi392311.
PROiQ3UE37.
SOURCEiSearch...

Gene expression databases

BgeeiQ3UE37.
CleanExiMM_UBE2Z.
GenevestigatoriQ3UE37.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Amnion, Bone marrow, Placenta and Thymus.
  2. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-356.
    Strain: Czech II.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiUBE2Z_MOUSE
AccessioniPrimary (citable) accession number: Q3UE37
Secondary accession number(s): A2A6M3
, Q3TFZ8, Q3U618, Q7TMY6, Q8BVL2, Q9DAU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 2007
Last sequence update: March 19, 2007
Last modified: March 31, 2015
This is version 88 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.