NAB2_HUMAN
ID NAB2_HUMAN Reviewed; 525 AA.
AC Q15742; B2RAK3; O76006; Q14797;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=NGFI-A-binding protein 2;
DE AltName: Full=EGR-1-binding protein 2;
DE AltName: Full=Melanoma-associated delayed early response protein;
DE Short=Protein MADER;
GN Name=NAB2; Synonyms=MADER;
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 [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
RX PubMed=8668170; DOI=10.1128/mcb.16.7.3545;
RA Svaren J., Sevetson B.R., Apel E.D., Zimonjic D.B., Popescu N.C.,
RA Milbrandt J.;
RT "NAB2, a corepressor of NGFI-A (Egr-1) and Krox20, is induced by
RT proliferative and differentiative stimuli.";
RL Mol. Cell. Biol. 16:3545-3553(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORM 1).
RA Gerlinger M., Johnson J.P.;
RT "Genomic organization of the Mader/NAB2 gene.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 50-525 (ISOFORM 1).
RX PubMed=8649813;
RA Kirsch K.H., Korradi Y., Johnson J.P.;
RT "Mader: a novel nuclear protein over expressed in human melanomas.";
RL Oncogene 12:963-971(1996).
RN [7]
RP PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 3).
RA Johnson J.P.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=9126479; DOI=10.1006/geno.1997.4609;
RA Svaren J., Apel E.D., Simburger K.S., Jenkins N.A., Gilbert D.J.,
RA Copeland N.G., Milbrandt J.;
RT "The Nab2 and Stat6 genes share a common transcription termination
RT region.";
RL Genomics 41:33-39(1997).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP 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).
RN [12]
RP SUMOYLATION AT LYS-379 AND LYS-517 BY EGR2.
RX PubMed=21836637; DOI=10.1038/embor.2011.152;
RA Garcia-Gutierrez P., Juarez-Vicente F., Gallardo-Chamizo F., Charnay P.,
RA Garcia-Dominguez M.;
RT "The transcription factor Krox20 is an E3 ligase that sumoylates its Nab
RT coregulators.";
RL EMBO Rep. 12:1018-1023(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-162, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-159; SER-162 AND
RP SER-171, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-171, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-517, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Acts as a transcriptional repressor for zinc finger
CC transcription factors EGR1 and EGR2. Isoform 2 lacks repression ability
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homomultimers may associate with EGR1 bound to DNA.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q15742; Q12955-5: ANK3; NbExp=3; IntAct=EBI-8641936, EBI-12154305;
CC Q15742; X5D778: ANKRD11; NbExp=3; IntAct=EBI-8641936, EBI-17183751;
CC Q15742; Q9HC52: CBX8; NbExp=3; IntAct=EBI-8641936, EBI-712912;
CC Q15742; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-8641936, EBI-10961624;
CC Q15742; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-8641936, EBI-10175300;
CC Q15742; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-8641936, EBI-396137;
CC Q15742; P78358: CTAG1B; NbExp=3; IntAct=EBI-8641936, EBI-1188472;
CC Q15742; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-8641936, EBI-11962928;
CC Q15742; Q2TBE0: CWF19L2; NbExp=6; IntAct=EBI-8641936, EBI-5453285;
CC Q15742; P26196: DDX6; NbExp=3; IntAct=EBI-8641936, EBI-351257;
CC Q15742; Q9BY27: DGCR6L; NbExp=3; IntAct=EBI-8641936, EBI-742953;
CC Q15742; P55039: DRG2; NbExp=3; IntAct=EBI-8641936, EBI-750565;
CC Q15742; Q14241: ELOA; NbExp=3; IntAct=EBI-8641936, EBI-742350;
CC Q15742; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-8641936, EBI-744099;
CC Q15742; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-8641936, EBI-742102;
CC Q15742; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-8641936, EBI-8468186;
CC Q15742; Q96CN9: GCC1; NbExp=3; IntAct=EBI-8641936, EBI-746252;
CC Q15742; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-8641936, EBI-5916454;
CC Q15742; O75031: HSF2BP; NbExp=3; IntAct=EBI-8641936, EBI-7116203;
CC Q15742; Q96AA8: JAKMIP2; NbExp=3; IntAct=EBI-8641936, EBI-752007;
CC Q15742; Q9HAQ2: KIF9; NbExp=3; IntAct=EBI-8641936, EBI-8472129;
CC Q15742; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-8641936, EBI-14069005;
CC Q15742; O76011: KRT34; NbExp=3; IntAct=EBI-8641936, EBI-1047093;
CC Q15742; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-8641936, EBI-10171774;
CC Q15742; Q96BZ8: LENG1; NbExp=6; IntAct=EBI-8641936, EBI-726510;
CC Q15742; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-8641936, EBI-739832;
CC Q15742; P33993: MCM7; NbExp=3; IntAct=EBI-8641936, EBI-355924;
CC Q15742; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-8641936, EBI-348259;
CC Q15742; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-8641936, EBI-14086479;
CC Q15742; Q9UBU8: MORF4L1; NbExp=3; IntAct=EBI-8641936, EBI-399246;
CC Q15742; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-8641936, EBI-10288852;
CC Q15742; Q15014: MORF4L2; NbExp=3; IntAct=EBI-8641936, EBI-399257;
CC Q15742; Q15742: NAB2; NbExp=4; IntAct=EBI-8641936, EBI-8641936;
CC Q15742; Q9UHB4: NDOR1; NbExp=3; IntAct=EBI-8641936, EBI-10249760;
CC Q15742; Q14511: NEDD9; NbExp=4; IntAct=EBI-8641936, EBI-2108053;
CC Q15742; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-8641936, EBI-11746523;
CC Q15742; Q9Y5B8: NME7; NbExp=6; IntAct=EBI-8641936, EBI-744782;
CC Q15742; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-8641936, EBI-945833;
CC Q15742; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-8641936, EBI-741158;
CC Q15742; O43189: PHF1; NbExp=7; IntAct=EBI-8641936, EBI-530034;
CC Q15742; Q8TCD6: PHOSPHO2; NbExp=6; IntAct=EBI-8641936, EBI-2861380;
CC Q15742; Q92569: PIK3R3; NbExp=3; IntAct=EBI-8641936, EBI-79893;
CC Q15742; Q13526: PIN1; NbExp=6; IntAct=EBI-8641936, EBI-714158;
CC Q15742; O60568: PLOD3; NbExp=3; IntAct=EBI-8641936, EBI-741582;
CC Q15742; P54646: PRKAA2; NbExp=3; IntAct=EBI-8641936, EBI-1383852;
CC Q15742; O43741: PRKAB2; NbExp=3; IntAct=EBI-8641936, EBI-1053424;
CC Q15742; P25786: PSMA1; NbExp=3; IntAct=EBI-8641936, EBI-359352;
CC Q15742; P47897: QARS1; NbExp=3; IntAct=EBI-8641936, EBI-347462;
CC Q15742; P40937: RFC5; NbExp=8; IntAct=EBI-8641936, EBI-712376;
CC Q15742; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-8641936, EBI-726876;
CC Q15742; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-8641936, EBI-748391;
CC Q15742; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-8641936, EBI-358489;
CC Q15742; O60504: SORBS3; NbExp=3; IntAct=EBI-8641936, EBI-741237;
CC Q15742; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-8641936, EBI-742688;
CC Q15742; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-8641936, EBI-10175576;
CC Q15742; Q15560: TCEA2; NbExp=3; IntAct=EBI-8641936, EBI-710310;
CC Q15742; Q8N8B7: TCEANC; NbExp=3; IntAct=EBI-8641936, EBI-954696;
CC Q15742; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-8641936, EBI-11955057;
CC Q15742; Q9BT92: TCHP; NbExp=7; IntAct=EBI-8641936, EBI-740781;
CC Q15742; Q8IUE0: TGIF2LY; NbExp=6; IntAct=EBI-8641936, EBI-8063723;
CC Q15742; Q08117: TLE5; NbExp=3; IntAct=EBI-8641936, EBI-717810;
CC Q15742; Q08117-2: TLE5; NbExp=3; IntAct=EBI-8641936, EBI-11741437;
CC Q15742; Q12933: TRAF2; NbExp=3; IntAct=EBI-8641936, EBI-355744;
CC Q15742; P36406: TRIM23; NbExp=3; IntAct=EBI-8641936, EBI-740098;
CC Q15742; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-8641936, EBI-744794;
CC Q15742; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-8641936, EBI-10241197;
CC Q15742; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-8641936, EBI-948354;
CC Q15742; O75604: USP2; NbExp=3; IntAct=EBI-8641936, EBI-743272;
CC Q15742; Q5TAP6: UTP14C; NbExp=3; IntAct=EBI-8641936, EBI-11737646;
CC Q15742; Q8IZ13: ZBED8; NbExp=7; IntAct=EBI-8641936, EBI-7186123;
CC Q15742; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-8641936, EBI-2682299;
CC Q15742; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-8641936, EBI-12030590;
CC Q15742; Q96E35: ZMYND19; NbExp=7; IntAct=EBI-8641936, EBI-746595;
CC Q15742; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-8641936, EBI-740727;
CC Q15742-2; P55212: CASP6; NbExp=3; IntAct=EBI-25834665, EBI-718729;
CC Q15742-2; O00291: HIP1; NbExp=3; IntAct=EBI-25834665, EBI-473886;
CC Q15742-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-25834665, EBI-21591415;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Isoform 2 is not
CC localized to the nucleus. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15742-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15742-2; Sequence=VSP_003385, VSP_003386;
CC Name=3;
CC IsoId=Q15742-3; Sequence=VSP_003387;
CC -!- TISSUE SPECIFICITY: Widely expressed at low levels. Highly expressed in
CC melanoma cell lines.
CC -!- INDUCTION: By serum and phorbol myristate acetate (PMA) stimulation.
CC -!- DOMAIN: The NAB conserved domain 1 (NCD1) interacts with EGR1
CC inhibitory domain and mediates multimerization.
CC -!- DOMAIN: The NAB conserved domain 2 (NCD2) is necessary for
CC transcriptional repression.
CC -!- PTM: Sumoylation by EGR2 represses EGR2 transcriptional activity in
CC hindbrain. {ECO:0000269|PubMed:21836637}.
CC -!- SIMILARITY: Belongs to the NAB family. {ECO:0000305}.
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DR EMBL; U48361; AAC50589.1; -; mRNA.
DR EMBL; AF268380; AAF72545.1; -; Genomic_DNA.
DR EMBL; AK314229; BAG36900.1; -; mRNA.
DR EMBL; CH471054; EAW96989.1; -; Genomic_DNA.
DR EMBL; BC065931; AAH65931.1; -; mRNA.
DR EMBL; X70991; CAA50318.1; -; mRNA.
DR EMBL; AJ011081; CAA09472.1; -; Genomic_DNA.
DR CCDS; CCDS81701.1; -. [Q15742-3]
DR CCDS; CCDS8930.1; -. [Q15742-1]
DR RefSeq; NP_001317234.1; NM_001330305.1. [Q15742-3]
DR RefSeq; NP_005958.1; NM_005967.3. [Q15742-1]
DR AlphaFoldDB; Q15742; -.
DR SMR; Q15742; -.
DR BioGRID; 110747; 150.
DR IntAct; Q15742; 82.
DR MINT; Q15742; -.
DR STRING; 9606.ENSP00000300131; -.
DR GlyGen; Q15742; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15742; -.
DR PhosphoSitePlus; Q15742; -.
DR BioMuta; NAB2; -.
DR DMDM; 12643729; -.
DR EPD; Q15742; -.
DR jPOST; Q15742; -.
DR MassIVE; Q15742; -.
DR MaxQB; Q15742; -.
DR PaxDb; Q15742; -.
DR PeptideAtlas; Q15742; -.
DR PRIDE; Q15742; -.
DR ProteomicsDB; 60728; -. [Q15742-1]
DR ProteomicsDB; 60729; -. [Q15742-2]
DR ProteomicsDB; 60730; -. [Q15742-3]
DR Antibodypedia; 3858; 413 antibodies from 36 providers.
DR DNASU; 4665; -.
DR Ensembl; ENST00000300131.8; ENSP00000300131.3; ENSG00000166886.13. [Q15742-1]
DR Ensembl; ENST00000342556.6; ENSP00000341491.6; ENSG00000166886.13. [Q15742-3]
DR GeneID; 4665; -.
DR KEGG; hsa:4665; -.
DR MANE-Select; ENST00000300131.8; ENSP00000300131.3; NM_005967.4; NP_005958.1.
DR UCSC; uc001smz.3; human. [Q15742-1]
DR CTD; 4665; -.
DR DisGeNET; 4665; -.
DR GeneCards; NAB2; -.
DR HGNC; HGNC:7627; NAB2.
DR HPA; ENSG00000166886; Low tissue specificity.
DR MalaCards; NAB2; -.
DR MIM; 602381; gene.
DR neXtProt; NX_Q15742; -.
DR OpenTargets; ENSG00000166886; -.
DR Orphanet; 2126; Solitary fibrous tumor/hemangiopericytoma.
DR PharmGKB; PA31432; -.
DR VEuPathDB; HostDB:ENSG00000166886; -.
DR eggNOG; KOG3835; Eukaryota.
DR GeneTree; ENSGT00390000006330; -.
DR HOGENOM; CLU_029394_2_0_1; -.
DR InParanoid; Q15742; -.
DR OMA; HARTNAD; -.
DR OrthoDB; 1002244at2759; -.
DR PhylomeDB; Q15742; -.
DR TreeFam; TF315501; -.
DR PathwayCommons; Q15742; -.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; Q15742; -.
DR SIGNOR; Q15742; -.
DR BioGRID-ORCS; 4665; 11 hits in 1083 CRISPR screens.
DR ChiTaRS; NAB2; human.
DR GeneWiki; NAB2; -.
DR GenomeRNAi; 4665; -.
DR Pharos; Q15742; Tbio.
DR PRO; PR:Q15742; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q15742; protein.
DR Bgee; ENSG00000166886; Expressed in right hemisphere of cerebellum and 176 other tissues.
DR Genevisible; Q15742; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; IDA:MGI.
DR GO; GO:1902949; P:positive regulation of tau-protein kinase activity; ISS:ARUK-UCL.
DR GO; GO:0045682; P:regulation of epidermis development; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0014037; P:Schwann cell differentiation; IEA:Ensembl.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.20.120.2010; -; 1.
DR InterPro; IPR006989; NAB_co-repressor_dom.
DR InterPro; IPR039040; NAB_fam.
DR InterPro; IPR006988; Nab_N.
DR InterPro; IPR038398; NCD2_sf.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12623; PTHR12623; 1.
DR Pfam; PF04904; NCD1; 1.
DR Pfam; PF04905; NCD2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..525
FT /note="NGFI-A-binding protein 2"
FT /id="PRO_0000077042"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..113
FT /note="NCD1"
FT REGION 135..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..356
FT /note="NCD2"
FT REGION 353..384
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 380..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61127"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61127"
FT CROSSLNK 379
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:21836637"
FT CROSSLNK 517
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:21836637"
FT CROSSLNK 517
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 320..322
FT /note="LTI -> ASP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8668170"
FT /id="VSP_003385"
FT VAR_SEQ 323..525
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8668170"
FT /id="VSP_003386"
FT VAR_SEQ 426..489
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_003387"
FT CONFLICT 257..258
FT /note="PR -> Q (in Ref. 6 and 7)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 56594 MW; 38CF6CFEFE3756F9 CRC64;
MHRAPSPTAE QPPGGGDSAR RTLQPRLKPS ARAMALPRTL GELQLYRVLQ RANLLSYYET
FIQQGGDDVQ QLCEAGEEEF LEIMALVGMA TKPLHVRRLQ KALREWATNP GLFSQPVPAV
PVSSIPLFKI SETAGTRKGS MSNGHGSPGE KAGSARSFSP KSPLELGEKL SPLPGGPGAG
DPRIWPGRST PESDVGAGGE EEAGSPPFSP PAGGGVPEGT GAGGLAAGGT GGGPDRLEPE
MVRMVVESVE RIFRSFPRGD AGEVTSLLKL NKKLARSVGH IFEMDDNDSQ KEEEIRKYSI
IYGRFDSKRR EGKQLSLHEL TINEAAAQFC MRDNTLLLRR VELFSLSRQV ARESTYLSSL
KGSRLHPEEL GGPPLKKLKQ EVGEQSHPEI QQPPPGPESY VPPYRPSLEE DSASLSGESL
DGHLQAVGSC PRLTPPPADL PLALPAHGLW SRHILQQTLM DEGLRLARLV SHDRVGRLSP
CVPAKPPLAE FEEGLLDRCP APGPHPALVE GRRSSVKVEA EASRQ
