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Q969M7 - UBE2F_HUMAN

UniProt

Q969M7 - UBE2F_HUMAN

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Protein

NEDD8-conjugating enzyme UBE2F

Gene

UBE2F

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

Functioni

Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1, suggests that the RBX2-UBE2F complex neddylates specific target proteins, such as CUL5.1 Publication

Catalytic activityi

ATP + NEDD8 + protein lysine = AMP + diphosphate + protein N-NEDD8yllysine.

Pathwayi

Protein modification; protein neddylation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei116 – 1161Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. NEDD8 transferase activity Source: UniProtKB

GO - Biological processi

  1. protein neddylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiC9J212.
Q969M7.
UniPathwayiUPA00885.

Names & Taxonomyi

Protein namesi
Recommended name:
NEDD8-conjugating enzyme UBE2F (EC:6.3.2.-)
Alternative name(s):
NEDD8 carrier protein UBE2F
NEDD8 protein ligase UBE2F
NEDD8-conjugating enzyme 2
Ubiquitin-conjugating enzyme E2 F
Gene namesi
Name:UBE2F
Synonyms:NCE2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:12480. UBE2F.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37130.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185NEDD8-conjugating enzyme UBE2FPRO_0000263077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Post-translational modificationi

The acetylation of Met-1 increases affinity for DCUN1D3 by about 2 orders of magnitude and is crucial for NEDD8 transfer to cullins.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ969M7.
PaxDbiQ969M7.
PeptideAtlasiQ969M7.
PRIDEiQ969M7.

PTM databases

PhosphoSiteiQ969M7.

Expressioni

Tissue specificityi

Widely expressed (at protein level).1 Publication

Gene expression databases

BgeeiQ969M7.
CleanExiHS_UBE2F.
ExpressionAtlasiQ969M7. baseline and differential.
GenevestigatoriQ969M7.

Organism-specific databases

HPAiHPA037444.

Interactioni

Subunit structurei

Interacts with UBA3 and RBX2.2 Publications

Protein-protein interaction databases

BioGridi126682. 12 interactions.
IntActiQ969M7. 6 interactions.
STRINGi9606.ENSP00000272930.

Structurei

Secondary structure

1
185
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 85Combined sources
Helixi32 – 4413Combined sources
Helixi45 – 473Combined sources
Beta strandi52 – 554Combined sources
Beta strandi57 – 604Combined sources
Beta strandi64 – 696Combined sources
Beta strandi72 – 743Combined sources
Turni75 – 784Combined sources
Beta strandi81 – 866Combined sources
Beta strandi97 – 1004Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi111 – 1133Combined sources
Helixi118 – 1203Combined sources
Beta strandi124 – 1263Combined sources
Helixi136 – 14510Combined sources
Turni146 – 1505Combined sources
Beta strandi153 – 1553Combined sources
Helixi159 – 1679Combined sources
Helixi169 – 18315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EDINMR-A26-185[»]
3FN1X-ray2.50B21-185[»]
4GBAX-ray2.40F/G1-25[»]
ProteinModelPortaliQ969M7.
SMRiQ969M7. Positions 26-185.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ969M7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2929Interaction with UBA3Add
BLAST

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family. UBE2F subfamily.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00630000089859.
HOGENOMiHOG000233456.
HOVERGENiHBG098591.
InParanoidiQ969M7.
KOiK10687.
OMAiWHPNISE.
PhylomeDBiQ969M7.
TreeFamiTF101125.

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 (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q969M7-1) [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
MLTLASKLKR DDGLKGSRTA ATASDSTRRV SVRDKLLVKE VAELEANLPC 
        60         70         80         90        100
TCKVHFPDPN KLHCFQLTVT PDEGYYQGGK FQFETEVPDA YNMVPPKVKC 
       110        120        130        140        150
LTKIWHPNIT ETGEICLSLL REHSIDGTGW APTRTLKDVV WGLNSLFTDL 
       160        170        180 
LNFDDPLNIE AAEHHLRDKE DFRNKVDDYI KRYAR
Length:185
Mass (Da):21,077
Last modified:December 1, 2001 - v1
Checksum:iB22C86238D13216E
GO
Isoform 2 (identifier: Q969M7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     170-185: EDFRNKVDDYIKRYAR → SPMLLLHRRTSGIKWMTTSNVMPDNKRGRLQAHGLCYSLSLT

Note: No experimental confirmation available.

Show »
Length:211
Mass (Da):23,760
Checksum:i26D6D083CACA07ED
GO
Isoform 3 (identifier: Q969M7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     40-71: Missing.

Note: No experimental confirmation available.

Show »
Length:153
Mass (Da):17,500
Checksum:i738B62CEF923150C
GO
Isoform 4 (identifier: Q969M7-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     118-120: SLL → RIF
     121-185: Missing.

Note: No experimental confirmation available.

Show »
Length:120
Mass (Da):13,513
Checksum:iB7A58924FDDB46AF
GO
Isoform 5 (identifier: Q969M7-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     72-185: DEGYYQGGKF...VDDYIKRYAR → ASQSEMPDQDLAPQHHRDRGNMSEFIERTFN

Note: No experimental confirmation available.

Show »
Length:102
Mass (Da):11,450
Checksum:i676F8ABBE02435AE
GO
Isoform 6 (identifier: Q969M7-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     149-169: Missing.

Note: Gene prediction based on EST data.

Show »
Length:164
Mass (Da):18,619
Checksum:iF8EDC983E452DE4D
GO
Isoform 7 (identifier: Q969M7-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MLTLASKLKRDDGLKGSRTAATASDSTRRVSVRDKLLVK → MVLGAGPASPVSGSP

Note: Gene prediction based on EST data.

Show »
Length:161
Mass (Da):18,158
Checksum:i44700812DFACB9CE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811K → E in BAF82752. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3939MLTLA…KLLVK → MVLGAGPASPVSGSP in isoform 7. CuratedVSP_055749Add
BLAST
Alternative sequencei40 – 7132Missing in isoform 3. 1 PublicationVSP_037270Add
BLAST
Alternative sequencei72 – 185114DEGYY…KRYAR → ASQSEMPDQDLAPQHHRDRG NMSEFIERTFN in isoform 5. 1 PublicationVSP_037271Add
BLAST
Alternative sequencei118 – 1203SLL → RIF in isoform 4. 1 PublicationVSP_037272
Alternative sequencei121 – 18565Missing in isoform 4. 1 PublicationVSP_037273Add
BLAST
Alternative sequencei149 – 16921Missing in isoform 6. CuratedVSP_055750Add
BLAST
Alternative sequencei170 – 18516EDFRN…KRYAR → SPMLLLHRRTSGIKWMTTSN VMPDNKRGRLQAHGLCYSLS LT in isoform 2. 1 PublicationVSP_037274Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF310723 mRNA. Translation: AAL26792.1.
AK290063 mRNA. Translation: BAF82752.1.
AK293334 mRNA. Translation: BAG56850.1.
AK294107 mRNA. Translation: BAG57442.1.
AK297502 mRNA. Translation: BAG59915.1.
AK303094 mRNA. Translation: BAG64204.1.
AC016776 Genomic DNA. Translation: AAY24220.1.
CH471063 Genomic DNA. Translation: EAW71129.1.
CH471063 Genomic DNA. Translation: EAW71132.1.
BC010549 mRNA. Translation: AAH10549.1.
CCDSiCCDS2523.1. [Q969M7-1]
CCDS63175.1. [Q969M7-7]
CCDS63176.1. [Q969M7-6]
CCDS63177.1. [Q969M7-3]
RefSeqiNP_001265234.1. NM_001278305.1. [Q969M7-1]
NP_001265235.1. NM_001278306.1. [Q969M7-7]
NP_001265236.1. NM_001278307.1. [Q969M7-3]
NP_001265237.1. NM_001278308.1. [Q969M7-6]
NP_542409.1. NM_080678.2. [Q969M7-1]
UniGeneiHs.471785.

Genome annotation databases

EnsembliENST00000272930; ENSP00000272930; ENSG00000184182. [Q969M7-1]
ENST00000409633; ENSP00000387299; ENSG00000184182. [Q969M7-6]
ENST00000409953; ENSP00000386680; ENSG00000184182. [Q969M7-7]
ENST00000414443; ENSP00000399183; ENSG00000184182. [Q969M7-3]
ENST00000433241; ENSP00000393515; ENSG00000184182. [Q969M7-4]
ENST00000441728; ENSP00000409749; ENSG00000184182. [Q969M7-5]
ENST00000612130; ENSP00000478474; ENSG00000184182. [Q969M7-1]
GeneIDi140739.
KEGGihsa:140739.
UCSCiuc002vxk.3. human. [Q969M7-1]
uc010znn.2. human. [Q969M7-3]
uc010znp.2. human. [Q969M7-4]

Polymorphism databases

DMDMi74751725.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF310723 mRNA. Translation: AAL26792.1.
AK290063 mRNA. Translation: BAF82752.1.
AK293334 mRNA. Translation: BAG56850.1.
AK294107 mRNA. Translation: BAG57442.1.
AK297502 mRNA. Translation: BAG59915.1.
AK303094 mRNA. Translation: BAG64204.1.
AC016776 Genomic DNA. Translation: AAY24220.1.
CH471063 Genomic DNA. Translation: EAW71129.1.
CH471063 Genomic DNA. Translation: EAW71132.1.
BC010549 mRNA. Translation: AAH10549.1.
CCDSiCCDS2523.1. [Q969M7-1]
CCDS63175.1. [Q969M7-7]
CCDS63176.1. [Q969M7-6]
CCDS63177.1. [Q969M7-3]
RefSeqiNP_001265234.1. NM_001278305.1. [Q969M7-1]
NP_001265235.1. NM_001278306.1. [Q969M7-7]
NP_001265236.1. NM_001278307.1. [Q969M7-3]
NP_001265237.1. NM_001278308.1. [Q969M7-6]
NP_542409.1. NM_080678.2. [Q969M7-1]
UniGeneiHs.471785.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EDINMR-A26-185[»]
3FN1X-ray2.50B21-185[»]
4GBAX-ray2.40F/G1-25[»]
ProteinModelPortaliQ969M7.
SMRiQ969M7. Positions 26-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126682. 12 interactions.
IntActiQ969M7. 6 interactions.
STRINGi9606.ENSP00000272930.

PTM databases

PhosphoSiteiQ969M7.

Polymorphism databases

DMDMi74751725.

Proteomic databases

MaxQBiQ969M7.
PaxDbiQ969M7.
PeptideAtlasiQ969M7.
PRIDEiQ969M7.

Protocols and materials databases

DNASUi140739.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272930; ENSP00000272930; ENSG00000184182. [Q969M7-1]
ENST00000409633; ENSP00000387299; ENSG00000184182. [Q969M7-6]
ENST00000409953; ENSP00000386680; ENSG00000184182. [Q969M7-7]
ENST00000414443; ENSP00000399183; ENSG00000184182. [Q969M7-3]
ENST00000433241; ENSP00000393515; ENSG00000184182. [Q969M7-4]
ENST00000441728; ENSP00000409749; ENSG00000184182. [Q969M7-5]
ENST00000612130; ENSP00000478474; ENSG00000184182. [Q969M7-1]
GeneIDi140739.
KEGGihsa:140739.
UCSCiuc002vxk.3. human. [Q969M7-1]
uc010znn.2. human. [Q969M7-3]
uc010znp.2. human. [Q969M7-4]

Organism-specific databases

CTDi140739.
GeneCardsiGC02P238875.
HGNCiHGNC:12480. UBE2F.
HPAiHPA037444.
neXtProtiNX_Q969M7.
PharmGKBiPA37130.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00630000089859.
HOGENOMiHOG000233456.
HOVERGENiHBG098591.
InParanoidiQ969M7.
KOiK10687.
OMAiWHPNISE.
PhylomeDBiQ969M7.
TreeFamiTF101125.

Enzyme and pathway databases

UniPathwayiUPA00885.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiC9J212.
Q969M7.

Miscellaneous databases

ChiTaRSiUBE2F. human.
EvolutionaryTraceiQ969M7.
GenomeRNAii140739.
NextBioi35484635.
PROiQ969M7.

Gene expression databases

BgeeiQ969M7.
CleanExiHS_UBE2F.
ExpressionAtlasiQ969M7. baseline and differential.
GenevestigatoriQ969M7.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "NEDD8-conjugating enzyme."
    Gladysheva T., Chau V.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    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] (ISOFORMS 1; 2; 3; 4 AND 5).
    Tissue: Brain, Brain cortex, Glial tumor, Substantia nigra and Thymus.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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] (ISOFORM 1).
    Tissue: Brain.
  6. "E2-RING expansion of the NEDD8 cascade confers specificity to cullin modification."
    Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M., Scott D.C., Borg L.A., Neale G., Murray P.J., Roussel M.F., Schulman B.A.
    Mol. Cell 33:483-495(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 22-185 IN COMPLEX WITH UBA3, FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH UBA3; NAE1 AND RBX2.
  7. "Solution structure of the UQ_CON domain from human NEDD8-conjugating enzyme NCE2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 23-185.
  8. "Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes."
    Monda J.K., Scott D.C., Miller D.J., Lydeard J., King D., Harper J.W., Bennett E.J., Schulman B.A.
    Structure 21:42-53(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-25 IN COMPLEX WITH DCUN1D3, ACETYLATION AT MET-1.

Entry informationi

Entry nameiUBE2F_HUMAN
AccessioniPrimary (citable) accession number: Q969M7
Secondary accession number(s): A8K1Z8
, B4DDT9, B4DFI1, B4DMK3, B4DZU2, B8ZZG2, C9J212, H9KVB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 1, 2001
Last modified: February 4, 2015
This is version 109 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.