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P51965

- UB2E1_HUMAN

UniProt

P51965 - UB2E1_HUMAN

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Protein

Ubiquitin-conjugating enzyme E2 E1

Gene

UBE2E1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes the covalent attachment of ISG15 to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. In vitro also catalyzes 'Lys-48'-linked polyubiquitination.2 Publications

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei131 – 1311Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ISG15 ligase activity Source: HGNC
  3. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. cytokine-mediated signaling pathway Source: Reactome
  3. histone H2B ubiquitination Source: UniProtKB
  4. histone monoubiquitination Source: UniProtKB
  5. ISG15-protein conjugation Source: HGNC
  6. mitotic cell cycle Source: Reactome
  7. mitotic spindle assembly checkpoint Source: Reactome
  8. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  9. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  10. protein K48-linked ubiquitination Source: UniProtKB
  11. protein polyubiquitination Source: UniProtKB
  12. protein ubiquitination Source: BHF-UCL
  13. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  14. ubiquitin-dependent protein catabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_115831. ISG15 antiviral mechanism.
REACT_150471. Separation of Sister Chromatids.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6904. Phosphorylation of the APC/C.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP51965.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 E1 (EC:6.3.2.19)
Alternative name(s):
UbcH6
Ubiquitin carrier protein E1
Ubiquitin-protein ligase E1
Gene namesi
Name:UBE2E1
Synonyms:UBCH6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:12477. UBE2E1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37127.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 193192Ubiquitin-conjugating enzyme E2 E1PRO_0000082470Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Cross-linki136 – 136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15)

Post-translational modificationi

ISGylation suppresses ubiquitin E2 enzyme activity.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP51965.
PaxDbiP51965.
PRIDEiP51965.

PTM databases

PhosphoSiteiP51965.

Expressioni

Gene expression databases

BgeeiP51965.
CleanExiHS_UBE2E1.
ExpressionAtlasiP51965. baseline and differential.
GenevestigatoriP51965.

Organism-specific databases

HPAiHPA030445.

Interactioni

Subunit structurei

Interacts with RNF14.

Binary interactionsi

WithEntry#Exp.IntActNotes
ospGQ99PZ63EBI-348546,EBI-9316527From a different organism.
PAF1Q8N7H52EBI-348546,EBI-2607770
RNF11Q9Y3C52EBI-348546,EBI-396669
RNF20Q5VTR22EBI-348546,EBI-2372238
ZNRF1Q8ND253EBI-348546,EBI-2129250

Protein-protein interaction databases

BioGridi113172. 110 interactions.
IntActiP51965. 63 interactions.
MINTiMINT-109083.
STRINGi9606.ENSP00000303709.

Structurei

Secondary structure

1
193
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi22 – 243Combined sources
Helixi42 – 6120Combined sources
Beta strandi67 – 748Combined sources
Beta strandi78 – 847Combined sources
Turni90 – 934Combined sources
Beta strandi95 – 1017Combined sources
Turni104 – 1085Combined sources
Beta strandi112 – 1176Combined sources
Helixi133 – 1353Combined sources
Turni136 – 1383Combined sources
Helixi145 – 15713Combined sources
Helixi167 – 1759Combined sources
Helixi177 – 19115Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XR9X-ray1.79C83-91[»]
3BZHX-ray1.60A1-193[»]
4JJQX-ray1.95B5-14[»]
ProteinModelPortaliP51965.
SMRiP51965. Positions 21-193.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51965.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi9 – 1810Poly-Ser

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00760000119012.
HOGENOMiHOG000233455.
HOVERGENiHBG063308.
InParanoidiP51965.
KOiK06689.
OMAiLSHRRIP.
OrthoDBiEOG7PCJGX.
PhylomeDBiP51965.
TreeFamiTF101117.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P51965) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSDDDSRAST SSSSSSSSNQ QTEKETNTPK KKESKVSMSK NSKLLSTSAK
60 70 80 90 100
RIQKELADIT LDPPPNCSAG PKGDNIYEWR STILGPPGSV YEGGVFFLDI
110 120 130 140 150
TFTPEYPFKP PKVTFRTRIY HCNINSQGVI CLDILKDNWS PALTISKVLL
160 170 180 190
SICSLLTDCN PADPLVGSIA TQYMTNRAEH DRMARQWTKR YAT
Length:193
Mass (Da):21,404
Last modified:October 1, 1996 - v1
Checksum:i2FBC50BE2A6A0008
GO
Isoform 2 (identifier: P51965-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: MSDDDSRASTSSSSSSSSNQQTEKETNTPKKKESKVSMSKNSKLLSTSAK → MKEVGRPREVRGRPGKS

Note: No experimental confirmation available.

Show »
Length:160
Mass (Da):18,000
Checksum:i412FAB80EBA7A2A7
GO
Isoform 3 (identifier: P51965-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     51-67: Missing.

Note: No experimental confirmation available.

Show »
Length:176
Mass (Da):19,499
Checksum:i4CFBF51A6FB61C8C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311C → R in BI223271. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251E → D.
Corresponds to variant rs36060625 [ dbSNP | Ensembl ].
VAR_061868

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5050MSDDD…STSAK → MKEVGRPREVRGRPGKS in isoform 2. 1 PublicationVSP_045884Add
BLAST
Alternative sequencei51 – 6717Missing in isoform 3. 1 PublicationVSP_047200Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X92963 mRNA. Translation: CAA63539.1.
AK314854 mRNA. Translation: BAG37371.1.
AC020626 Genomic DNA. No translation available.
AC124914 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64329.1.
CH471055 Genomic DNA. Translation: EAW64331.1.
CH471055 Genomic DNA. Translation: EAW64332.1.
BC009139 mRNA. Translation: AAH09139.1.
BI223271 mRNA. No translation available.
BI666638 mRNA. No translation available.
CCDSiCCDS2638.1. [P51965-1]
CCDS2639.1. [P51965-3]
CCDS56244.1. [P51965-2]
RefSeqiNP_001189405.1. NM_001202476.1. [P51965-2]
NP_003332.1. NM_003341.4. [P51965-1]
NP_872607.1. NM_182666.2. [P51965-3]
UniGeneiHs.164853.

Genome annotation databases

EnsembliENST00000306627; ENSP00000303709; ENSG00000170142. [P51965-1]
ENST00000346855; ENSP00000329113; ENSG00000170142. [P51965-3]
ENST00000424381; ENSP00000411351; ENSG00000170142. [P51965-2]
GeneIDi7324.
KEGGihsa:7324.
UCSCiuc003cch.3. human. [P51965-1]
uc003cci.3. human.
uc021wua.1. human.

Polymorphism databases

DMDMi1717857.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X92963 mRNA. Translation: CAA63539.1 .
AK314854 mRNA. Translation: BAG37371.1 .
AC020626 Genomic DNA. No translation available.
AC124914 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64329.1 .
CH471055 Genomic DNA. Translation: EAW64331.1 .
CH471055 Genomic DNA. Translation: EAW64332.1 .
BC009139 mRNA. Translation: AAH09139.1 .
BI223271 mRNA. No translation available.
BI666638 mRNA. No translation available.
CCDSi CCDS2638.1. [P51965-1 ]
CCDS2639.1. [P51965-3 ]
CCDS56244.1. [P51965-2 ]
RefSeqi NP_001189405.1. NM_001202476.1. [P51965-2 ]
NP_003332.1. NM_003341.4. [P51965-1 ]
NP_872607.1. NM_182666.2. [P51965-3 ]
UniGenei Hs.164853.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XR9 X-ray 1.79 C 83-91 [» ]
3BZH X-ray 1.60 A 1-193 [» ]
4JJQ X-ray 1.95 B 5-14 [» ]
ProteinModelPortali P51965.
SMRi P51965. Positions 21-193.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113172. 110 interactions.
IntActi P51965. 63 interactions.
MINTi MINT-109083.
STRINGi 9606.ENSP00000303709.

PTM databases

PhosphoSitei P51965.

Polymorphism databases

DMDMi 1717857.

Proteomic databases

MaxQBi P51965.
PaxDbi P51965.
PRIDEi P51965.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000306627 ; ENSP00000303709 ; ENSG00000170142 . [P51965-1 ]
ENST00000346855 ; ENSP00000329113 ; ENSG00000170142 . [P51965-3 ]
ENST00000424381 ; ENSP00000411351 ; ENSG00000170142 . [P51965-2 ]
GeneIDi 7324.
KEGGi hsa:7324.
UCSCi uc003cch.3. human. [P51965-1 ]
uc003cci.3. human.
uc021wua.1. human.

Organism-specific databases

CTDi 7324.
GeneCardsi GC03P023847.
HGNCi HGNC:12477. UBE2E1.
HPAi HPA030445.
MIMi 602916. gene.
neXtProti NX_P51965.
PharmGKBi PA37127.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00760000119012.
HOGENOMi HOG000233455.
HOVERGENi HBG063308.
InParanoidi P51965.
KOi K06689.
OMAi LSHRRIP.
OrthoDBi EOG7PCJGX.
PhylomeDBi P51965.
TreeFami TF101117.

Enzyme and pathway databases

UniPathwayi UPA00143 .
Reactomei REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
REACT_115831. ISG15 antiviral mechanism.
REACT_150471. Separation of Sister Chromatids.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_6904. Phosphorylation of the APC/C.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki P51965.

Miscellaneous databases

EvolutionaryTracei P51965.
GeneWikii UBE2E1.
GenomeRNAii 7324.
NextBioi 28656.
PROi P51965.
SOURCEi Search...

Gene expression databases

Bgeei P51965.
CleanExi HS_UBE2E1.
ExpressionAtlasi P51965. baseline and differential.
Genevestigatori P51965.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5."
    Nuber U., Schwarz S., Kaiser P., Schneider R., Scheffner M.
    J. Biol. Chem. 271:2795-2800(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Amygdala.
  3. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 1; 2 AND 3).
    Tissue: Cervix carcinoma, Colon and Hypothalamus.
  6. "Link between the ubiquitin conjugation system and the ISG15 conjugation system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme."
    Takeuchi T., Iwahara S., Saeki Y., Sasajima H., Yokosawa H.
    J. Biochem. 138:711-719(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ISGYLATION AT LYS-136.
  7. "The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but enters the nucleus upon cellular exposure to nitric oxide."
    Espinosa A., Oke V., Elfving A., Nyberg F., Covacu R., Wahren-Herlenius M.
    Exp. Cell Res. 314:3605-3613(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  9. "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
    David Y., Ziv T., Admon A., Navon A.
    J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUB2E1_HUMAN
AccessioniPrimary (citable) accession number: P51965
Secondary accession number(s): B2RBX4, C9J8K2, K4DI90
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3