NAB1_HUMAN
ID NAB1_HUMAN Reviewed; 487 AA.
AC Q13506; O75383; O75384; Q6GTU1; Q9UEV1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=NGFI-A-binding protein 1;
DE AltName: Full=EGR-1-binding protein 1;
DE AltName: Full=Transcriptional regulatory protein p54;
GN Name=NAB1;
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] (ISOFORM LONG).
RC TISSUE=Brain;
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 [MRNA] (ISOFORMS LONG AND SHORT).
RA Fan W.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103.
RA Cao J., Fan W.;
RT "Cloning and characterization of the 5' promoter region of human p54, a
RT transcriptional repressor.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP SUMOYLATION AT LYS-333 AND LYS-480 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 [8]
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 [9]
RP 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 [10]
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 [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-333; LYS-355 AND LYS-480, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-129; LYS-333 AND LYS-480, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-333, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-126; LYS-129; LYS-143; LYS-212;
RP LYS-333; LYS-355; LYS-369; LYS-373; LYS-454; LYS-465; LYS-477 AND LYS-480,
RP AND IDENTIFICATION BY MASS 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).
RN [15]
RP STRUCTURE BY NMR OF 183-317.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the NCD2 domain in human transcriptional repressor
RT NAB1 protein.";
RL Submitted (APR-2008) to the PDB data bank.
CC -!- FUNCTION: Acts as a transcriptional repressor for zinc finger
CC transcription factors EGR1 and EGR2. {ECO:0000250}.
CC -!- SUBUNIT: Homomultimers may associate with EGR1 bound to DNA.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q13506-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q13506-2; Sequence=VSP_003384;
CC -!- TISSUE SPECIFICITY: Isoform Short is found in myeloid leukemia cell
CC line KG-1.
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 -!- SIMILARITY: Belongs to the NAB family. {ECO:0000305}.
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DR EMBL; U47007; AAC50588.1; -; mRNA.
DR EMBL; AF045451; AAC25085.1; -; mRNA.
DR EMBL; AF045452; AAC25086.1; -; mRNA.
DR EMBL; AC006460; AAX93076.1; -; Genomic_DNA.
DR EMBL; BC035724; AAH35724.1; -; mRNA.
DR EMBL; AF052744; AAC28325.1; -; Genomic_DNA.
DR CCDS; CCDS2307.1; -. [Q13506-1]
DR RefSeq; NP_001308241.1; NM_001321312.1. [Q13506-1]
DR RefSeq; NP_001308242.1; NM_001321313.1. [Q13506-1]
DR RefSeq; NP_001308243.1; NM_001321314.1.
DR RefSeq; NP_001308244.1; NM_001321315.1.
DR RefSeq; NP_005957.2; NM_005966.3. [Q13506-1]
DR RefSeq; XP_005246639.1; XM_005246582.1. [Q13506-1]
DR RefSeq; XP_005246640.1; XM_005246583.1. [Q13506-1]
DR RefSeq; XP_011509521.1; XM_011511219.2. [Q13506-1]
DR RefSeq; XP_016859659.1; XM_017004170.1. [Q13506-1]
DR RefSeq; XP_016859665.1; XM_017004176.1. [Q13506-1]
DR PDB; 2YUF; NMR; -; A=189-317.
DR PDBsum; 2YUF; -.
DR AlphaFoldDB; Q13506; -.
DR SMR; Q13506; -.
DR BioGRID; 110746; 23.
DR IntAct; Q13506; 10.
DR STRING; 9606.ENSP00000336894; -.
DR iPTMnet; Q13506; -.
DR PhosphoSitePlus; Q13506; -.
DR BioMuta; NAB1; -.
DR DMDM; 90109928; -.
DR EPD; Q13506; -.
DR jPOST; Q13506; -.
DR MassIVE; Q13506; -.
DR MaxQB; Q13506; -.
DR PaxDb; Q13506; -.
DR PeptideAtlas; Q13506; -.
DR PRIDE; Q13506; -.
DR ProteomicsDB; 59502; -. [Q13506-1]
DR ProteomicsDB; 59503; -. [Q13506-2]
DR Antibodypedia; 1209; 327 antibodies from 26 providers.
DR DNASU; 4664; -.
DR Ensembl; ENST00000337386.10; ENSP00000336894.5; ENSG00000138386.17. [Q13506-1]
DR Ensembl; ENST00000409581.5; ENSP00000387089.1; ENSG00000138386.17. [Q13506-1]
DR GeneID; 4664; -.
DR KEGG; hsa:4664; -.
DR MANE-Select; ENST00000337386.10; ENSP00000336894.5; NM_005966.4; NP_005957.2.
DR UCSC; uc002usb.4; human. [Q13506-1]
DR CTD; 4664; -.
DR DisGeNET; 4664; -.
DR GeneCards; NAB1; -.
DR HGNC; HGNC:7626; NAB1.
DR HPA; ENSG00000138386; Low tissue specificity.
DR MIM; 600800; gene.
DR neXtProt; NX_Q13506; -.
DR OpenTargets; ENSG00000138386; -.
DR PharmGKB; PA31431; -.
DR VEuPathDB; HostDB:ENSG00000138386; -.
DR eggNOG; KOG3835; Eukaryota.
DR GeneTree; ENSGT00390000006330; -.
DR HOGENOM; CLU_561344_0_0_1; -.
DR InParanoid; Q13506; -.
DR OMA; DGYPDFQ; -.
DR OrthoDB; 1002244at2759; -.
DR PhylomeDB; Q13506; -.
DR TreeFam; TF315501; -.
DR PathwayCommons; Q13506; -.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; Q13506; -.
DR BioGRID-ORCS; 4664; 9 hits in 1080 CRISPR screens.
DR ChiTaRS; NAB1; human.
DR EvolutionaryTrace; Q13506; -.
DR GeneWiki; NAB1; -.
DR GenomeRNAi; 4664; -.
DR Pharos; Q13506; Tbio.
DR PRO; PR:Q13506; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q13506; protein.
DR Bgee; ENSG00000138386; Expressed in ganglionic eminence and 207 other tissues.
DR ExpressionAtlas; Q13506; baseline and differential.
DR Genevisible; Q13506; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0042552; P:myelination; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
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; 1.20.120.2010; -; 1.
DR InterPro; IPR006986; Nab1_C.
DR InterPro; IPR006989; NAB_co-repressor_dom.
DR InterPro; IPR039040; NAB_fam.
DR InterPro; IPR006988; Nab_N.
DR InterPro; IPR038398; NCD2_sf.
DR PANTHER; PTHR12623; PTHR12623; 1.
DR Pfam; PF04902; Nab1; 1.
DR Pfam; PF04904; NCD1; 1.
DR Pfam; PF04905; NCD2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..486
FT /note="NGFI-A-binding protein 1"
FT /id="PRO_0000077038"
FT REGION 4..82
FT /note="NCD1"
FT REGION 162..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..310
FT /note="NCD2"
FT REGION 307..338
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 399..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61122"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61122"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61122"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 143
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 333
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:21836637"
FT CROSSLNK 333
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 355
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 369
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 373
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 454
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 465
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 477
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:21836637"
FT CROSSLNK 480
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 336..364
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_003384"
FT CONFLICT 129
FT /note="K -> N (in Ref. 1; AAC50588)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="Missing (in Ref. 1; AAC50588)"
FT /evidence="ECO:0000305"
FT HELIX 193..209
FT /evidence="ECO:0007829|PDB:2YUF"
FT HELIX 215..224
FT /evidence="ECO:0007829|PDB:2YUF"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:2YUF"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:2YUF"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:2YUF"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2YUF"
FT HELIX 272..286
FT /evidence="ECO:0007829|PDB:2YUF"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:2YUF"
FT HELIX 294..310
FT /evidence="ECO:0007829|PDB:2YUF"
SQ SEQUENCE 487 AA; 54401 MW; 385B16391D670059 CRC64;
MAAALPRTLG ELQLYRILQK ANLLSYFDAF IQQGGDDVQQ LCEAGEEEFL EIMALVGMAS
KPLHVRRLQK ALRDWVTNPG LFNQPLTSLP VSSIPIYKLP EGSPTWLGIS CSSYERSSNA
REPHLKIPKC AATTCVQSLG QGKSDVVGSL ALQSVGESRL WQGHHATESE HSLSPADLGS
PASPKESSEA LDAAAALSVA ECVERMAPTL PKSDLNEVKE LLKTNKKLAK MIGHIFEMND
DDPHKEEEIR KYSAIYGRFD SKRKDGKHLT LHELTVNEAA AQLCVKDNAL LTRRDELFAL
ARQISREVTY KYTYRTTKSK CGERDELSPK RIKVEDGFPD FQDSVQTLFQ QARAKSEELA
ALSSQQPEKV MAKQMEFLCN QAGYERLQHA ERRLSAGLYR QSSEEHSPNG LTSDNSDGQG
ERPLNLRMPN LQNRQPHHFV VDGELSRLYP SEAKSHSSES LGILKDYPHS AFTLEKKVIK
TEPEDSR
