ID   ULA1_MACFA              Reviewed;         510 AA.
AC   Q4R3L6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 82.
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; ORFNames=QtsA-16060;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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; AB179250; BAE02301.1; -; mRNA.
DR   RefSeq; XP_005592228.1; XM_005592171.2.
DR   AlphaFoldDB; Q4R3L6; -.
DR   SMR; Q4R3L6; -.
DR   STRING; 9541.XP_005592226.1; -.
DR   GeneID; 102146039; -.
DR   KEGG; mcf:102146039; -.
DR   CTD; 8883; -.
DR   eggNOG; KOG2016; Eukaryota.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019781; F:NEDD8 activating enzyme activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0045116; P:protein neddylation; IEA:UniProtKB-UniPathway.
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   2: Evidence at transcript 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..510
FT                   /note="NEDD8-activating enzyme E1 regulatory subunit"
FT                   /id="PRO_0000194952"
FT   REGION          307..320
FT                   /note="Interaction with UBA3"
FT                   /evidence="ECO:0000250"
FT   SITE            187
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         317
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VBW6"
SQ   SEQUENCE   510 AA;  57611 MW;  C6B572CF8C9E1611 CRC64;
     MAQPGKLLKE QKYDRQLRLW GDHGQEALES AHVCLINATA TGTEILKNLV LPGIGSFTII
     DGNQVSGEDA GNNFFLQRSS IGKSPENLLD NDPSFFCRFT VVVATQLPES TLLRLADVLW
     NSQIPLLICR TYGLVGYMRI IIKEHPVIES HPDNALEDLR LDKPFPELRE HFQSYDLDHM
     EKKDHSHTPW IVIIAKYLAQ WYSETNGRIP KTYKEKEDFR DLIRQGILKN ENGAPEDEEN
     FEEAIKNVNT ALNTTQIPSS IEDIFNDDRC INITKQTPSF WILARALKEF VAKEGQGNLP
     VRGTIPDMIA DSGKYIKLQN VYREKAKKDA AAVGNHVAKL LQSIGQAPES ISEKELKLLC
     SNSAFLRVVR CRSLAEEYGL DTINKDEIIS SMDNPDNEIV LYLMLRAVDR FHKQHGRYPG
     VSNYQVEEDI GKLKSCLTGF LQEYGLSVMV KDDYVHEFCR YGAAEPHTIA AFLGGAAAQE
     VIKIITKQFV IFNNTYIYSG MSQTSATFQL