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Q969M7 (UBE2F_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:UBE2F
Synonyms:NCE2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Catalytic activity

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

Pathway

Protein modification; protein neddylation.

Subunit structure

Interacts with UBA3 and RBX2. Ref.6

Tissue specificity

Widely expressed (at protein level). Ref.6

Post-translational modification

The acetylation of Met-1 increases affinity for DCUN1D3 by about 2 orders of magnitude and is crucial for NEDD8 transfer to cullins. Ref.8

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family. UBE2F subfamily.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein neddylation

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

NEDD8 ligase activity

Inferred from direct assay Ref.6. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q969M7-1)

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: Q969M7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     170-185: EDFRNKVDDYIKRYAR → SPMLLLHRRTSGIKWMTTSNVMPDNKRGRLQAHGLCYSLSLT
Note: No experimental confirmation available.
Isoform 3 (identifier: Q969M7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     40-71: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q969M7-4)

The sequence of this isoform differs from the canonical sequence as follows:
     118-120: SLL → RIF
     121-185: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q969M7-5)

The sequence of this isoform differs from the canonical sequence as follows:
     72-185: DEGYYQGGKF...VDDYIKRYAR → ASQSEMPDQDLAPQHHRDRGNMSEFIERTFN
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185NEDD8-conjugating enzyme UBE2F
PRO_0000263077

Regions

Region1 – 2929Interaction with UBA3

Sites

Active site1161Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8

Natural variations

Alternative sequence40 – 7132Missing in isoform 3.
VSP_037270
Alternative sequence72 – 185114DEGYY…KRYAR → ASQSEMPDQDLAPQHHRDRG NMSEFIERTFN in isoform 5.
VSP_037271
Alternative sequence118 – 1203SLL → RIF in isoform 4.
VSP_037272
Alternative sequence121 – 18565Missing in isoform 4.
VSP_037273
Alternative sequence170 – 18516EDFRN…KRYAR → SPMLLLHRRTSGIKWMTTSN VMPDNKRGRLQAHGLCYSLS LT in isoform 2.
VSP_037274

Experimental info

Sequence conflict1811K → E in BAF82752. Ref.2

Secondary structure

.................................... 185
Helix Strand Turn

Details...

Sequences

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

Last modified December 1, 2001. Version 1.
Checksum: B22C86238D13216E

FASTA18521,077
        10         20         30         40         50         60 
MLTLASKLKR DDGLKGSRTA ATASDSTRRV SVRDKLLVKE VAELEANLPC TCKVHFPDPN 

        70         80         90        100        110        120 
KLHCFQLTVT PDEGYYQGGK FQFETEVPDA YNMVPPKVKC LTKIWHPNIT ETGEICLSLL 

       130        140        150        160        170        180 
REHSIDGTGW APTRTLKDVV WGLNSLFTDL LNFDDPLNIE AAEHHLRDKE DFRNKVDDYI 


KRYAR 

« Hide

Isoform 2 [UniParc].

Checksum: 26D6D083CACA07ED
Show »

FASTA21123,760
Isoform 3 [UniParc].

Checksum: 738B62CEF923150C
Show »

FASTA15317,500
Isoform 4 [UniParc].

Checksum: B7A58924FDDB46AF
Show »

FASTA12013,513
Isoform 5 [UniParc].

Checksum: 676F8ABBE02435AE
Show »

FASTA10211,450

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2523.1. [Q969M7-1]
CCDS63177.1. [Q969M7-3]
RefSeqNP_001265234.1. NM_001278305.1. [Q969M7-1]
NP_001265235.1. NM_001278306.1.
NP_001265236.1. NM_001278307.1. [Q969M7-3]
NP_001265237.1. NM_001278308.1.
NP_542409.1. NM_080678.2. [Q969M7-1]
UniGeneHs.471785.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EDINMR-A26-185[»]
3FN1X-ray2.50B21-185[»]
4GBAX-ray2.40F/G1-25[»]
ProteinModelPortalQ969M7.
SMRQ969M7. Positions 26-185.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126682. 11 interactions.
IntActQ969M7. 6 interactions.
STRING9606.ENSP00000272930.

PTM databases

PhosphoSiteQ969M7.

Polymorphism databases

DMDM74751725.

Proteomic databases

MaxQBQ969M7.
PaxDbQ969M7.
PeptideAtlasQ969M7.
PRIDEQ969M7.

Protocols and materials databases

DNASU140739.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000272930; ENSP00000272930; ENSG00000184182. [Q969M7-1]
ENST00000414443; ENSP00000399183; ENSG00000184182. [Q969M7-3]
ENST00000433241; ENSP00000393515; ENSG00000184182. [Q969M7-4]
ENST00000441728; ENSP00000409749; ENSG00000184182. [Q969M7-5]
GeneID140739.
KEGGhsa:140739.
UCSCuc002vxk.3. human. [Q969M7-1]
uc010znn.2. human. [Q969M7-3]
uc010znp.2. human. [Q969M7-4]

Organism-specific databases

CTD140739.
GeneCardsGC02P238875.
HGNCHGNC:12480. UBE2F.
HPAHPA037444.
neXtProtNX_Q969M7.
PharmGKBPA37130.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOVERGENHBG098591.
InParanoidQ969M7.
KOK10687.
OMAWHPNISE.
PhylomeDBQ969M7.
TreeFamTF101125.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ969M7.
UniPathwayUPA00885.

Gene expression databases

ArrayExpressQ969M7.
BgeeQ969M7.
CleanExHS_UBE2F.
GenevestigatorQ969M7.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ969M7.
GenomeRNAi140739.
NextBio84333.
PROQ969M7.

Entry information

Entry nameUBE2F_HUMAN
AccessionPrimary (citable) accession number: Q969M7
Secondary accession number(s): A8K1Z8 expand/collapse secondary AC list , B4DDT9, B4DFI1, B4DMK3, B4DZU2, B8ZZG2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM