UB2FB_MOUSE
ID UB2FB_MOUSE Reviewed; 185 AA.
AC Q3UWQ3;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=NEDD8-conjugating enzyme UBE2F-B;
DE EC=2.3.2.34;
DE AltName: Full=NEDD8 carrier protein UBE2F-B;
DE AltName: Full=NEDD8 protein ligase UBE2F-B;
DE AltName: Full=RING-type E3 NEDD8 transferase UBE2F-B;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 F-B;
GN Name=Ube2fb; Synonyms=Gm5434;
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=Egg;
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).
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:0000250}.
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 -!- 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; AK136183; BAE22861.1; -; mRNA.
DR AlphaFoldDB; Q3UWQ3; -.
DR SMR; Q3UWQ3; -.
DR STRING; 10090.ENSMUSP00000071728; -.
DR MaxQB; Q3UWQ3; -.
DR PaxDb; Q3UWQ3; -.
DR PeptideAtlas; Q3UWQ3; -.
DR PRIDE; Q3UWQ3; -.
DR ProteomicsDB; 298348; -.
DR UCSC; uc007njo.1; mouse.
DR MGI; MGI:3646221; Gm5434.
DR eggNOG; KOG0420; Eukaryota.
DR HOGENOM; CLU_030988_6_4_1; -.
DR InParanoid; Q3UWQ3; -.
DR PhylomeDB; Q3UWQ3; -.
DR TreeFam; TF101125; -.
DR UniPathway; UPA00885; -.
DR PRO; PR:Q3UWQ3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UWQ3; protein.
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; ISS:UniProtKB.
DR GO; GO:0019788; F:NEDD8 transferase activity; IBA:GO_Central.
DR GO; GO:0045116; P:protein neddylation; ISS: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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..185
FT /note="NEDD8-conjugating enzyme UBE2F-B"
FT /id="PRO_0000374071"
FT DOMAIN 32..185
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 116
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 185 AA; 21352 MW; D24B42C8BA2B55CC CRC64;
MLTLASKLKW DEDLKGSQTS VSTSDSTRRF SMRDKLLVTE VAELEANLPW TCKVHFPDPN
KLHCFQLTVS PDEGYYQGGN FQFEIEVPDA YNMVPPKVKC LTKIWHPNIT ETGEICLSLL
REHSADGTGW APTRTLKDVV WGLNSLFTDL LNFYDPLNIE AAEHHLQDKE DFRDKVDEYI
RRYAR
