N4BP3_HUMAN
ID N4BP3_HUMAN Reviewed; 544 AA.
AC O15049; B4DIL3; D3DWP3; Q6ZSQ6; Q7Z6I3;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=NEDD4-binding protein 3;
DE Short=N4BP3;
GN Name=N4BP3; Synonyms=KIAA0341;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 285-544.
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NEDD4.
RX PubMed=11717310; DOI=10.1074/jbc.m110047200;
RA Murillas R., Simms K.S., Hatakeyama S., Weissman A.M., Kuehn M.R.;
RT "Identification of developmentally expressed proteins that functionally
RT interact with Nedd4 ubiquitin ligase.";
RL J. Biol. Chem. 277:2897-2907(2002).
RN [6]
RP INTERACTION WITH 14-3-3 PROTEINS.
RX PubMed=15324660; DOI=10.1016/j.cub.2004.07.051;
RA Jin J., Smith F.D., Stark C., Wells C.D., Fawcett J.P., Kulkarni S.,
RA Metalnikov P., O'Donnell P., Taylor P., Taylor L., Zougman A.,
RA Woodgett J.R., Langeberg L.K., Scott J.D., Pawson T.;
RT "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding
RT proteins involved in cytoskeletal regulation and cellular organization.";
RL Curr. Biol. 14:1436-1450(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP FUNCTION, AND INTERACTION WITH MAVS.
RX PubMed=34880843; DOI=10.3389/fmicb.2021.770600;
RA Wang C., Ling T., Zhong N., Xu L.G.;
RT "N4BP3 Regulates RIG-I-Like Receptor Antiviral Signaling Positively by
RT Targeting Mitochondrial Antiviral Signaling Protein.";
RL Front. Microbiol. 12:770600-770600(2021).
CC -!- FUNCTION: Plays a positive role in the antiviral innate immune
CC signaling pathway. Mechanistically, interacts with MAVS and functions
CC as a positive regulator to promote 'Lys-63'-linked polyubiquitination
CC of MAVS and thus strengthens the interaction between MAVS and TRAF2
CC (PubMed:34880843). Also plays a role in axon and dendrite arborization
CC during cranial nerve development. May also be important for neural
CC crest migration and early development of other anterior structures
CC including eye, brain and cranial cartilage (By similarity).
CC {ECO:0000250|UniProtKB:A0A1L8GXY6, ECO:0000269|PubMed:34880843}.
CC -!- SUBUNIT: Binds NEDD4 (PubMed:11717310). Interacts with 14-3-3 proteins
CC (PubMed:15324660). Interacts with MAVS (PubMed:34880843).
CC {ECO:0000269|PubMed:11717310, ECO:0000269|PubMed:15324660,
CC ECO:0000269|PubMed:34880843}.
CC -!- INTERACTION:
CC O15049; Q8IYE0: CCDC146; NbExp=5; IntAct=EBI-2512055, EBI-10749669;
CC O15049; Q96LX7-5: CCDC17; NbExp=3; IntAct=EBI-2512055, EBI-12165781;
CC O15049; Q6P9H4: CNKSR3; NbExp=3; IntAct=EBI-2512055, EBI-10253274;
CC O15049; O14595: CTDSP2; NbExp=3; IntAct=EBI-2512055, EBI-2802973;
CC O15049; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-2512055, EBI-744099;
CC O15049; P61968: LMO4; NbExp=3; IntAct=EBI-2512055, EBI-2798728;
CC O15049; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2512055, EBI-741158;
CC O15049; P0CG20: PRR35; NbExp=3; IntAct=EBI-2512055, EBI-11986293;
CC O15049; P40937: RFC5; NbExp=5; IntAct=EBI-2512055, EBI-712376;
CC O15049; Q9H4P4: RNF41; NbExp=6; IntAct=EBI-2512055, EBI-2130266;
CC O15049; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-2512055, EBI-6257312;
CC O15049; O00560: SDCBP; NbExp=3; IntAct=EBI-2512055, EBI-727004;
CC O15049; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-2512055, EBI-742688;
CC O15049; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-2512055, EBI-7353612;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:11717310}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q3LUD3}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q3LUD3}. Note=In developing neurons, accumulates
CC in early growth cones and at branching points of axons and dendrites.
CC {ECO:0000250|UniProtKB:Q3LUD3}.
CC -!- SIMILARITY: Belongs to the N4BP3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20799.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC86891.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC86891.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=BAG58525.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB002339; BAA20799.1; ALT_INIT; mRNA.
DR EMBL; CH471165; EAW53851.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53852.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53853.1; -; Genomic_DNA.
DR EMBL; CH471165; EAW53854.1; -; Genomic_DNA.
DR EMBL; BC053323; AAH53323.2; -; mRNA.
DR EMBL; AK127224; BAC86891.1; ALT_SEQ; mRNA.
DR EMBL; AK295663; BAG58525.1; ALT_INIT; mRNA.
DR CCDS; CCDS34307.1; -.
DR RefSeq; NP_055926.1; NM_015111.1.
DR RefSeq; XP_006714897.1; XM_006714834.3.
DR RefSeq; XP_011532775.1; XM_011534473.1.
DR RefSeq; XP_011532776.1; XM_011534474.1.
DR AlphaFoldDB; O15049; -.
DR SMR; O15049; -.
DR BioGRID; 116755; 47.
DR IntAct; O15049; 37.
DR MINT; O15049; -.
DR STRING; 9606.ENSP00000274605; -.
DR iPTMnet; O15049; -.
DR PhosphoSitePlus; O15049; -.
DR BioMuta; N4BP3; -.
DR EPD; O15049; -.
DR MassIVE; O15049; -.
DR MaxQB; O15049; -.
DR PaxDb; O15049; -.
DR PeptideAtlas; O15049; -.
DR PRIDE; O15049; -.
DR ProteomicsDB; 48401; -.
DR Antibodypedia; 29410; 87 antibodies from 20 providers.
DR DNASU; 23138; -.
DR Ensembl; ENST00000274605.6; ENSP00000274605.4; ENSG00000145911.6.
DR GeneID; 23138; -.
DR KEGG; hsa:23138; -.
DR MANE-Select; ENST00000274605.6; ENSP00000274605.4; NM_015111.2; NP_055926.1.
DR UCSC; uc003mik.2; human.
DR CTD; 23138; -.
DR GeneCards; N4BP3; -.
DR HGNC; HGNC:29852; N4BP3.
DR HPA; ENSG00000145911; Tissue enhanced (esophagus).
DR MIM; 619140; gene.
DR neXtProt; NX_O15049; -.
DR OpenTargets; ENSG00000145911; -.
DR VEuPathDB; HostDB:ENSG00000145911; -.
DR eggNOG; ENOG502QVNK; Eukaryota.
DR GeneTree; ENSGT00940000158603; -.
DR HOGENOM; CLU_026379_3_1_1; -.
DR InParanoid; O15049; -.
DR OMA; EFSCPTT; -.
DR OrthoDB; 697945at2759; -.
DR PhylomeDB; O15049; -.
DR TreeFam; TF331420; -.
DR PathwayCommons; O15049; -.
DR SignaLink; O15049; -.
DR BioGRID-ORCS; 23138; 10 hits in 1074 CRISPR screens.
DR GenomeRNAi; 23138; -.
DR Pharos; O15049; Tdark.
DR PRO; PR:O15049; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O15049; protein.
DR Bgee; ENSG00000145911; Expressed in lower esophagus mucosa and 117 other tissues.
DR Genevisible; O15049; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR InterPro; IPR033571; N4BP3.
DR PANTHER; PTHR32274; PTHR32274; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasmic vesicle; Developmental protein;
KW Immunity; Innate immunity; Neurogenesis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..544
FT /note="NEDD4-binding protein 3"
FT /id="PRO_0000096682"
FT REGION 61..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 294..530
FT /evidence="ECO:0000255"
FT COMPBIAS 61..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CONFLICT 29
FT /note="L -> P (in Ref. 1; BAA20799)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="R -> Q (in Ref. 3; AAH53323)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="R -> H (in Ref. 4; BAC86891)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 544 AA; 60470 MW; 40F2652D0848C27C CRC64;
MATAPGPAGI AMGSVGSLLE RQDFSPEELR AALAGSRGSR QPDGLLRKGL GQREFLSYLH
LPKKDSKSTK NTKRAPRNEP ADYATLYYRE HSRAGDFSKT SLPERGRFDK CRIRPSVFKP
TAGNGKGFLS MQSLASHKGQ KLWRSNGSLH TLACHPPLSP GPRASQARAQ LLHALSLDEG
GPEPEPSLSD SSSGGSFGRS PGTGPSPFSS SLGHLNHLGG SLDRASQGPK EAGPPAVLSC
LPEPPPPYEF SCSSAEEMGA VLPETCEELK RGLGDEDGSN PFTQVLEERQ RLWLAELKRL
YVERLHEVTQ KAERSERNLQ LQLFMAQQEQ RRLRKELRAQ QGLAPEPRAP GTLPEADPSA
RPEEEARWEV CQKTAEISLL KQQLREAQAE LAQKLAEIFS LKTQLRGSRA QAQAQDAELV
RLREAVRSLQ EQAPREEAPG SCETDDCKSR GLLGEAGGSE ARDSAEQLRA ELLQERLRGQ
EQALRFEQER RTWQEEKERV LRYQREIQGG YMDMYRRNQA LEQELRALRE PPTPWSPRLE
SSKI
