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 27-MAR-2024, entry version 186. 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; Q8IZ13: FAM200C; NbExp=7; IntAct=EBI-8641936, EBI-7186123; 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; 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}. 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; 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; 158. DR IntAct; Q15742; 81. DR MINT; Q15742; -. DR STRING; 9606.ENSP00000300131; -. DR GlyCosmos; Q15742; 1 site, 1 glycan. 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; 9606-ENSP00000300131; -. DR PeptideAtlas; Q15742; -. DR ProteomicsDB; 60728; -. [Q15742-1] DR ProteomicsDB; 60729; -. [Q15742-2] DR ProteomicsDB; 60730; -. [Q15742-3] DR Pumba; Q15742; -. DR Antibodypedia; 3858; 478 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 AGR; HGNC:7627; -. 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. 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; IFKMGSQ; -. DR OrthoDB; 4181992at2759; -. 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; 28 hits in 1161 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 178 other cell types or tissues. 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:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0045682; P:regulation of epidermis development; IEA:Ensembl. DR GO; GO:0014037; P:Schwann cell differentiation; IEA:Ensembl. DR Gene3D; 1.20.120.2010; NAB conserved domain 2; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 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; NGFI-A BINDING PROTEIN; 1. DR PANTHER; PTHR12623:SF6; NGFI-A-BINDING PROTEIN 2; 1. DR Pfam; PF04904; NCD1; 1. DR Pfam; PF04905; NCD2; 1. DR Genevisible; Q15742; HS. 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 //