NACA2_HUMAN
ID NACA2_HUMAN Reviewed; 215 AA.
AC Q9H009; Q2VIR9;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Nascent polypeptide-associated complex subunit alpha-2;
DE AltName: Full=Alpha-NAC-like;
DE AltName: Full=Hom s 2.01;
DE AltName: Full=Nascent polypeptide-associated complex subunit alpha-like;
DE Short=NAC-alpha-like;
GN Name=NACA2; Synonyms=NACAL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Epithelium;
RX PubMed=12406326; DOI=10.1046/j.1523-1747.2002.00518.x;
RA Mossabeb R., Seiberler S., Mittermann I., Reininger R., Spitzauer S.,
RA Natter S., Verdino P., Keller W., Kraft D., Valenta R.;
RT "Characterization of a novel isoform of alpha-nascent polypeptide-
RT associated complex as IgE-defined autoantigen.";
RL J. Invest. Dermatol. 119:820-829(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-210, AND TISSUE SPECIFICITY.
RX PubMed=16201836; DOI=10.1371/journal.pbio.0030357;
RA Marques A.C., Dupanloup I., Vinckenbosch N., Reymond A., Kaessmann H.;
RT "Emergence of young human genes after a burst of retroposition in
RT primates.";
RL PLoS Biol. 3:E357-E357(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-214, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Prevents inappropriate targeting of non-secretory
CC polypeptides to the endoplasmic reticulum (ER). Binds to nascent
CC polypeptide chains as they emerge from the ribosome and blocks their
CC interaction with the signal recognition particle (SRP), which normally
CC targets nascent secretory peptides to the ER. Also reduces the inherent
CC affinity of ribosomes for protein translocation sites in the ER
CC membrane (M sites) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the nascent polypeptide-associated complex (NAC),
CC consisting of NACA and BTF3. NAC associates with ribosomes through the
CC BTF3 subunit. Both subunits can contact nascent polypeptide chains (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed specifically in testis and skeletal
CC muscle. {ECO:0000269|PubMed:16201836}.
CC -!- MISCELLANEOUS: NACAL arose from a recent (40-63 million-year-old),
CC anthropoid primate-specific retroduplication of NACA.
CC -!- SIMILARITY: Belongs to the NAC-alpha family. {ECO:0000305}.
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DR EMBL; AJ278883; CAC06614.1; -; Genomic_DNA.
DR EMBL; BC062710; AAH62710.1; -; mRNA.
DR EMBL; DQ120612; ABB92399.1; -; Genomic_DNA.
DR CCDS; CCDS11630.1; -.
DR RefSeq; NP_954984.1; NM_199290.3.
DR AlphaFoldDB; Q9H009; -.
DR SMR; Q9H009; -.
DR BioGRID; 131183; 21.
DR IntAct; Q9H009; 1.
DR STRING; 9606.ENSP00000427802; -.
DR Allergome; 412; Hom s 2.
DR iPTMnet; Q9H009; -.
DR PhosphoSitePlus; Q9H009; -.
DR BioMuta; NACA2; -.
DR DMDM; 74733511; -.
DR EPD; Q9H009; -.
DR jPOST; Q9H009; -.
DR MassIVE; Q9H009; -.
DR MaxQB; Q9H009; -.
DR PaxDb; Q9H009; -.
DR PeptideAtlas; Q9H009; -.
DR PRIDE; Q9H009; -.
DR ProteomicsDB; 80194; -.
DR Antibodypedia; 57003; 55 antibodies from 12 providers.
DR DNASU; 342538; -.
DR Ensembl; ENST00000521764.3; ENSP00000427802.1; ENSG00000253506.3.
DR GeneID; 342538; -.
DR KEGG; hsa:342538; -.
DR MANE-Select; ENST00000521764.3; ENSP00000427802.1; NM_199290.4; NP_954984.1.
DR UCSC; uc002izj.3; human.
DR CTD; 342538; -.
DR DisGeNET; 342538; -.
DR GeneCards; NACA2; -.
DR HGNC; HGNC:23290; NACA2.
DR HPA; ENSG00000253506; Tissue enriched (testis).
DR MIM; 609274; gene.
DR neXtProt; NX_Q9H009; -.
DR OpenTargets; ENSG00000253506; -.
DR PharmGKB; PA162396699; -.
DR VEuPathDB; HostDB:ENSG00000253506; -.
DR eggNOG; KOG2239; Eukaryota.
DR GeneTree; ENSGT00940000166484; -.
DR HOGENOM; CLU_057806_1_2_1; -.
DR InParanoid; Q9H009; -.
DR OMA; SDAYIVF; -.
DR OrthoDB; 1331328at2759; -.
DR PhylomeDB; Q9H009; -.
DR TreeFam; TF313348; -.
DR PathwayCommons; Q9H009; -.
DR BioGRID-ORCS; 342538; 21 hits in 1036 CRISPR screens.
DR ChiTaRS; NACA2; human.
DR GenomeRNAi; 342538; -.
DR Pharos; Q9H009; Tdark.
DR PRO; PR:Q9H009; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9H009; protein.
DR Bgee; ENSG00000253506; Expressed in left testis and 100 other tissues.
DR Genevisible; Q9H009; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR Gene3D; 2.20.70.30; -; 1.
DR InterPro; IPR016641; EGD2/NACA.
DR InterPro; IPR044034; NAC-like_UBA.
DR InterPro; IPR038187; NAC_A/B_dom_sf.
DR InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR PANTHER; PTHR21713; PTHR21713; 1.
DR Pfam; PF19026; HYPK_UBA; 1.
DR Pfam; PF01849; NAC; 1.
DR PIRSF; PIRSF015901; NAC_alpha; 1.
DR SMART; SM01407; NAC; 1.
DR PROSITE; PS51151; NAC_AB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..215
FT /note="Nascent polypeptide-associated complex subunit
FT alpha-2"
FT /id="PRO_0000280746"
FT DOMAIN 70..135
FT /note="NAC-A/B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT DOMAIN 176..213
FT /note="UBA"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 142
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 161
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CROSSLNK 142
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13765"
FT VARIANT 64
FT /note="V -> I (in dbSNP:rs17531723)"
FT /id="VAR_050218"
SQ SEQUENCE 215 AA; 23223 MW; C6B96A8370E9B24E CRC64;
MPGEATETVP ATEQELPQSQ AETGSGTASD SGESVPGIEE QDSTQTTTQK AWLVAAAEID
EEPVGKAKQS RSEKRARKAM SKLGLLQVTG VTRVTIWKSK NILFVITKLD VYKSPASDAY
IVFGEAKIQD LSQQAQLAAA EKFRVQGEAV GNIQENTQTP TVQEESEEEE VDETGVEVKD
VKLVMSQANV SRAKAVRALK NNSNDIVNAI MELTV
