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ULA1_MOUSE
ID   ULA1_MOUSE              Reviewed;         534 AA.
AC   Q8VBW6; Q8CFL6;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=NEDD8-activating enzyme E1 regulatory subunit;
DE   AltName: Full=Amyloid beta precursor protein-binding protein 1, 59 kDa;
DE            Short=APP-BP1;
DE   AltName: Full=Amyloid protein-binding protein 1;
GN   Name=Nae1; Synonyms=Appbp1;
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=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   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and 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).
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-341, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1
CC       activates NEDD8 by first adenylating its C-terminal glycine residue
CC       with ATP, thereafter linking this residue to the side chain of the
CC       catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1
CC       finally transfers NEDD8 to the catalytic cysteine of UBE2M. Necessary
CC       for cell cycle progression through the S-M checkpoint. Overexpression
CC       of NAE1 causes apoptosis through deregulation of NEDD8 conjugation (By
CC       similarity). {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: Binding of TP53BP2 to the regulatory subunit NAE1
CC       decreases neddylation activity. {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC   -!- SUBUNIT: Heterodimer of UBA3 and NAE1. The complex binds NEDD8 and
CC       UBE2M. Binds APP and TP53BP2 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Note=Colocalizes
CC       with APP in lipid rafts. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated by TRIP12, leading to its degradation by the
CC       proteasome. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. ULA1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BC019163; AAH19163.1; -; mRNA.
DR   EMBL; BC021510; AAH21510.1; -; mRNA.
DR   EMBL; BC023680; AAH23680.1; -; mRNA.
DR   EMBL; BC023897; AAH23897.1; -; mRNA.
DR   EMBL; BC027124; AAH27124.1; -; mRNA.
DR   CCDS; CCDS40452.1; -.
DR   RefSeq; NP_659180.1; NM_144931.3.
DR   AlphaFoldDB; Q8VBW6; -.
DR   SMR; Q8VBW6; -.
DR   BioGRID; 231552; 19.
DR   STRING; 10090.ENSMUSP00000034349; -.
DR   iPTMnet; Q8VBW6; -.
DR   PhosphoSitePlus; Q8VBW6; -.
DR   EPD; Q8VBW6; -.
DR   MaxQB; Q8VBW6; -.
DR   PaxDb; Q8VBW6; -.
DR   PRIDE; Q8VBW6; -.
DR   ProteomicsDB; 298478; -.
DR   Antibodypedia; 29312; 424 antibodies from 33 providers.
DR   DNASU; 234664; -.
DR   Ensembl; ENSMUST00000034349; ENSMUSP00000034349; ENSMUSG00000031878.
DR   GeneID; 234664; -.
DR   KEGG; mmu:234664; -.
DR   UCSC; uc009nas.2; mouse.
DR   CTD; 8883; -.
DR   MGI; MGI:2384561; Nae1.
DR   VEuPathDB; HostDB:ENSMUSG00000031878; -.
DR   eggNOG; KOG2016; Eukaryota.
DR   GeneTree; ENSGT00550000074901; -.
DR   HOGENOM; CLU_019618_2_1_1; -.
DR   InParanoid; Q8VBW6; -.
DR   OMA; LHEICRY; -.
DR   OrthoDB; 454386at2759; -.
DR   PhylomeDB; Q8VBW6; -.
DR   TreeFam; TF313972; -.
DR   Reactome; R-MMU-8951664; Neddylation.
DR   UniPathway; UPA00885; -.
DR   BioGRID-ORCS; 234664; 25 hits in 72 CRISPR screens.
DR   ChiTaRS; Nae1; mouse.
DR   PRO; PR:Q8VBW6; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8VBW6; protein.
DR   Bgee; ENSMUSG00000031878; Expressed in primitive streak and 260 other tissues.
DR   ExpressionAtlas; Q8VBW6; baseline and differential.
DR   Genevisible; Q8VBW6; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005769; C:early endosome; ISO:MGI.
DR   GO; GO:0045121; C:membrane raft; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0019781; F:NEDD8 activating enzyme activity; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; ISO:MGI.
DR   GO; GO:0051402; P:neuron apoptotic process; ISO:MGI.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IBA:GO_Central.
DR   GO; GO:0045116; P:protein neddylation; ISO:MGI.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:MGI.
DR   InterPro; IPR030667; APP-BP1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR10953; PTHR10953; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   PIRSF; PIRSF039099; APP-BP1; 1.
DR   SUPFAM; SSF69572; SSF69572; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Cell cycle; Cell membrane; Membrane;
KW   Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q13564"
FT   CHAIN           2..534
FT                   /note="NEDD8-activating enzyme E1 regulatory subunit"
FT                   /id="PRO_0000194953"
FT   REGION          331..344
FT                   /note="Interaction with UBA3"
FT                   /evidence="ECO:0000250"
FT   SITE            211
FT                   /note="Interaction with UBA3"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13564"
FT   MOD_RES         6
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13564"
FT   MOD_RES         341
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CONFLICT        127
FT                   /note="V -> F (in Ref. 1; AAH23680)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   534 AA;  60274 MW;  5CFCABFE5FA7AC62 CRC64;
     MAQPGKILKE QKYDRQLRLW GDHGQEALES AHVCLINATA TGTEILKNLV LPGIGSFTII
     DGNLVSGEDA GNNFFLQKSS IGKNRAQAAM EFLQELNSDV SGSFVEESPE NLLDNDPSFF
     CRFTIVVATQ LLESTLLRLA DVLWNSQIPL LICRTYGLVG YMRIIIKEHP VIESHPDNAL
     EDLRLDKPFP ELREHLQSYD LDHMEKKDHS HTPWIVIIAK YLAQWYNETN GRIPKSYKEK
     EDFRDLIRQG ILKNENGAPE DEENFEEAIK NVNTALNTTQ IPSSIEDIFN DDRCINITKQ
     TPTFWILARA LKEFVAKEGQ GNLPVRGTIP DMIADSNKYI KLQNVYREKA KKDAAAVGNH
     VAKLLQSVGQ APESISEKEL KLLCSNSAFL RVVRCRSLAE EYGLDTVNKD EIISSMDNPD
     NEIVLYLMLR AVDRFHKQHG RYPGVSNYQV EEDIGKLKSC LTGFLQEYGL SVMVKDDYVH
     EFCRYGAAEP HTIAAFLGGA AAQEVIKIIT KQFVIFNNTY IYSGMSQTSA TFQL
 
 
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