UB2FA_MOUSE
ID UB2FA_MOUSE Reviewed; 185 AA.
AC Q9CY34; Q99JK3; Q9D8K0; Q9D8K7;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=NEDD8-conjugating enzyme UBE2F;
DE EC=2.3.2.34;
DE AltName: Full=NEDD8 carrier protein UBE2F;
DE AltName: Full=NEDD8 protein ligase UBE2F;
DE AltName: Full=NEDD8-conjugating enzyme 2;
DE AltName: Full=RING-type E3 NEDD8 transferase UBE2F;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 F;
GN Name=Ube2f; Synonyms=Ube2fa;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Liver, Pancreas, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=19250909; DOI=10.1016/j.molcel.2009.01.011;
RA Huang D.T., Ayrault O., Hunt H.W., Taherbhoy A.M., Duda D.M., Scott D.C.,
RA Borg L.A., Neale G., Murray P.J., Roussel M.F., Schulman B.A.;
RT "E2-RING expansion of the NEDD8 cascade confers specificity to cullin
RT modification.";
RL Mol. Cell 33:483-495(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1
CC E1 complex and catalyzes its covalent attachment to other proteins. The
CC specific interaction with the E3 ubiquitin ligase RBX2, but not RBX1,
CC suggests that the RBX2-UBE2F complex neddylates specific target
CC proteins, such as CUL5. {ECO:0000269|PubMed:19250909}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine +
CC [E2 NEDD8-conjugating enzyme]-L-cysteine = [E1 NEDD8-activating
CC enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-
CC yl-L-cysteine.; EC=2.3.2.34;
CC -!- PATHWAY: Protein modification; protein neddylation.
CC -!- SUBUNIT: Interacts with UBA3 and RBX2. Interacts (N-terminally
CC acetylated form) with (via DCUN1 domain) DCUN1D1, DCUN1D2, DCUN1D3,
CC DCUN1D4 and DCUN1D5 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q969M7}.
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC {ECO:0000269|PubMed:19250909}.
CC -!- PTM: The acetylation of Met-1 increases affinity for DCUN1D3 by about 2
CC orders of magnitude and is crucial for NEDD8 transfer to cullins.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UBE2F
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AK007937; BAB25362.1; -; mRNA.
DR EMBL; AK007960; BAB25372.1; -; mRNA.
DR EMBL; AK010957; BAB27290.1; -; mRNA.
DR EMBL; AK030594; BAC27036.1; -; mRNA.
DR EMBL; AK153481; BAE32030.1; -; mRNA.
DR EMBL; BC006057; AAH06057.1; -; mRNA.
DR EMBL; BC016117; AAH16117.1; -; mRNA.
DR CCDS; CCDS48322.1; -.
DR RefSeq; NP_080730.1; NM_026454.3.
DR RefSeq; XP_006529899.1; XM_006529836.3.
DR RefSeq; XP_006529900.1; XM_006529837.3.
DR RefSeq; XP_006529901.1; XM_006529838.3.
DR RefSeq; XP_006529902.1; XM_006529839.3.
DR RefSeq; XP_006529903.1; XM_006529840.3.
DR RefSeq; XP_011246369.1; XM_011248067.2.
DR AlphaFoldDB; Q9CY34; -.
DR SMR; Q9CY34; -.
DR BioGRID; 212535; 6.
DR STRING; 10090.ENSMUSP00000126173; -.
DR iPTMnet; Q9CY34; -.
DR PhosphoSitePlus; Q9CY34; -.
DR SwissPalm; Q9CY34; -.
DR EPD; Q9CY34; -.
DR MaxQB; Q9CY34; -.
DR PaxDb; Q9CY34; -.
DR PeptideAtlas; Q9CY34; -.
DR PRIDE; Q9CY34; -.
DR ProteomicsDB; 297773; -.
DR DNASU; 67921; -.
DR Ensembl; ENSMUST00000059743; ENSMUSP00000054303; ENSMUSG00000034343.
DR Ensembl; ENSMUST00000171112; ENSMUSP00000131330; ENSMUSG00000034343.
DR Ensembl; ENSMUST00000171165; ENSMUSP00000126173; ENSMUSG00000034343.
DR Ensembl; ENSMUST00000178627; ENSMUSP00000136915; ENSMUSG00000034343.
DR Ensembl; ENSMUST00000191368; ENSMUSP00000140743; ENSMUSG00000034343.
DR GeneID; 67921; -.
DR KEGG; mmu:67921; -.
DR UCSC; uc007bzy.1; mouse.
DR CTD; 140739; -.
DR MGI; MGI:1915171; Ube2f.
DR VEuPathDB; HostDB:ENSMUSG00000034343; -.
DR eggNOG; KOG0420; Eukaryota.
DR GeneTree; ENSGT00940000154349; -.
DR HOGENOM; CLU_030988_6_4_1; -.
DR InParanoid; Q9CY34; -.
DR OMA; YNMAPPK; -.
DR OrthoDB; 1302735at2759; -.
DR PhylomeDB; Q9CY34; -.
DR TreeFam; TF101125; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00885; -.
DR BioGRID-ORCS; 67921; 11 hits in 107 CRISPR screens.
DR ChiTaRS; Ube2f; mouse.
DR PRO; PR:Q9CY34; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CY34; protein.
DR Bgee; ENSMUSG00000034343; Expressed in blood and 248 other tissues.
DR ExpressionAtlas; Q9CY34; baseline and differential.
DR Genevisible; Q9CY34; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061654; F:NEDD8 conjugating enzyme activity; ISO:MGI.
DR GO; GO:0019788; F:NEDD8 transferase activity; IMP:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; IMP:UniProtKB.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..185
FT /note="NEDD8-conjugating enzyme UBE2F"
FT /id="PRO_0000263078"
FT DOMAIN 32..185
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..29
FT /note="Interaction with UBA3"
FT /evidence="ECO:0000250"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 116
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q969M7"
FT CONFLICT 30
FT /note="V -> C (in Ref. 1; BAB25362)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="S -> A (in Ref. 1; BAB25372)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 185 AA; 21110 MW; DE16464086DBFB06 CRC64;
MLTLASKLKR DDGLKGSRTS ASTSDSTRRV SVRDKLLVKE VAELEANLPC TCKVHFPDPN
KLHCFQLTVS PDEGYYQGGK FQFETEVPDA YNMVPPKVKC LTKIWHPNIT ETGEICLSLL
REHSIDGTGW APTRTLKDVV WGLNSLFTDL LNFDDPLNIE AAEHHLRDKE DFRDKVDEYI
KRYAR
