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Q15742

- NAB2_HUMAN

UniProt

Q15742 - NAB2_HUMAN

Protein

NGFI-A-binding protein 2

Gene

NAB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Acts as a transcriptional repressor for zinc finger transcription factors EGR1 and EGR2. Isoform 2 lacks repression ability By similarity.By similarity

    GO - Molecular functioni

    1. transcription corepressor activity Source: ProtInc

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. endochondral ossification Source: Ensembl
    3. myelination Source: Ensembl
    4. negative regulation of transcription from RNA polymerase III promoter Source: MGI
    5. nervous system development Source: ProtInc
    6. regulation of epidermis development Source: Ensembl
    7. Schwann cell differentiation Source: Ensembl
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NGFI-A-binding protein 2
    Alternative name(s):
    EGR-1-binding protein 2
    Melanoma-associated delayed early response protein
    Short name:
    Protein MADER
    Gene namesi
    Name:NAB2
    Synonyms:MADER
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:7627. NAB2.

    Subcellular locationi

    Nucleus By similarity
    Note: Isoform 2 is not localized to the nucleus.By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti2126. Solitary fibrous tumor.
    PharmGKBiPA31432.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 525525NGFI-A-binding protein 2PRO_0000077042Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei6 – 61Phosphoserine2 Publications
    Modified residuei159 – 1591Phosphoserine1 Publication
    Modified residuei162 – 1621Phosphoserine1 Publication
    Modified residuei171 – 1711PhosphoserineBy similarity
    Cross-linki379 – 379Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Curated
    Cross-linki517 – 517Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Curated

    Post-translational modificationi

    Sumoylation by EGR2 represses EGR2 transcriptional activity in hindbrain.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ15742.
    PaxDbiQ15742.
    PRIDEiQ15742.

    PTM databases

    PhosphoSiteiQ15742.

    Expressioni

    Tissue specificityi

    Widely expressed at low levels. Highly expressed in melanoma cell lines.

    Inductioni

    By serum and phorbol myristate acetate (PMA) stimulation.

    Gene expression databases

    BgeeiQ15742.
    CleanExiHS_NAB2.
    GenevestigatoriQ15742.

    Organism-specific databases

    HPAiCAB004510.
    HPA027464.

    Interactioni

    Subunit structurei

    Homomultimers may associate with EGR1 bound to DNA.By similarity

    Protein-protein interaction databases

    BioGridi110747. 7 interactions.
    IntActiQ15742. 2 interactions.
    STRINGi9606.ENSP00000300131.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15742.
    SMRiQ15742. Positions 228-356.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 11379NCD1Add
    BLAST
    Regioni267 – 35690NCD2Add
    BLAST
    Regioni353 – 38432Necessary for nuclear localizationBy similarityAdd
    BLAST

    Domaini

    The NAB conserved domain 1 (NCD1) interacts with EGR1 inhibitory domain and mediates multimerization.
    The NAB conserved domain 2 (NCD2) is necessary for transcriptional repression.

    Sequence similaritiesi

    Belongs to the NAB family.Curated

    Phylogenomic databases

    eggNOGiNOG307377.
    HOGENOMiHOG000026777.
    HOVERGENiHBG003127.
    InParanoidiQ15742.
    OMAiPGPESYA.
    OrthoDBiEOG776SPQ.
    PhylomeDBiQ15742.
    TreeFamiTF315501.

    Family and domain databases

    InterProiIPR006989. NAB_co-repressor_dom.
    IPR006988. Nab_N.
    [Graphical view]
    PfamiPF04904. NCD1. 1 hit.
    PF04905. NCD2. 1 hit.
    [Graphical view]
    ProDomiPD342192. Nab_N. 1 hit.
    [Graphical view] [Entries sharing at least one domain]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q15742-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MHRAPSPTAE QPPGGGDSAR RTLQPRLKPS ARAMALPRTL GELQLYRVLQ    50
    RANLLSYYET FIQQGGDDVQ QLCEAGEEEF LEIMALVGMA TKPLHVRRLQ 100
    KALREWATNP GLFSQPVPAV PVSSIPLFKI SETAGTRKGS MSNGHGSPGE 150
    KAGSARSFSP KSPLELGEKL SPLPGGPGAG DPRIWPGRST PESDVGAGGE 200
    EEAGSPPFSP PAGGGVPEGT GAGGLAAGGT GGGPDRLEPE MVRMVVESVE 250
    RIFRSFPRGD AGEVTSLLKL NKKLARSVGH IFEMDDNDSQ KEEEIRKYSI 300
    IYGRFDSKRR EGKQLSLHEL TINEAAAQFC MRDNTLLLRR VELFSLSRQV 350
    ARESTYLSSL KGSRLHPEEL GGPPLKKLKQ EVGEQSHPEI QQPPPGPESY 400
    VPPYRPSLEE DSASLSGESL DGHLQAVGSC PRLTPPPADL PLALPAHGLW 450
    SRHILQQTLM DEGLRLARLV SHDRVGRLSP CVPAKPPLAE FEEGLLDRCP 500
    APGPHPALVE GRRSSVKVEA EASRQ 525
    Length:525
    Mass (Da):56,594
    Last modified:November 1, 1996 - v1
    Checksum:i38CF6CFEFE3756F9
    GO
    Isoform 2 (identifier: Q15742-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         320-322: LTI → ASP
         323-525: Missing.

    Show »
    Length:322
    Mass (Da):34,356
    Checksum:i6C7ACFBFEAD113E0
    GO
    Isoform 3 (identifier: Q15742-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         426-489: Missing.

    Show »
    Length:461
    Mass (Da):49,748
    Checksum:iF7C955EEFDAFBA94
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti257 – 2582PR → Q(PubMed:8649813)Curated
    Sequence conflicti257 – 2582PR → Q1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei320 – 3223LTI → ASP in isoform 2. 1 PublicationVSP_003385
    Alternative sequencei323 – 525203Missing in isoform 2. 1 PublicationVSP_003386Add
    BLAST
    Alternative sequencei426 – 48964Missing in isoform 3. CuratedVSP_003387Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U48361 mRNA. Translation: AAC50589.1.
    AF268380 Genomic DNA. Translation: AAF72545.1.
    AK314229 mRNA. Translation: BAG36900.1.
    CH471054 Genomic DNA. Translation: EAW96989.1.
    BC065931 mRNA. Translation: AAH65931.1.
    X70991 mRNA. Translation: CAA50318.1.
    AJ011081 Genomic DNA. Translation: CAA09472.1.
    CCDSiCCDS8930.1. [Q15742-1]
    RefSeqiNP_005958.1. NM_005967.3. [Q15742-1]
    XP_005268951.1. XM_005268894.2. [Q15742-3]
    UniGeneiHs.159223.

    Genome annotation databases

    EnsembliENST00000300131; ENSP00000300131; ENSG00000166886. [Q15742-1]
    ENST00000342556; ENSP00000341491; ENSG00000166886. [Q15742-3]
    GeneIDi4665.
    KEGGihsa:4665.
    UCSCiuc001smz.3. human. [Q15742-1]

    Polymorphism databases

    DMDMi12643729.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U48361 mRNA. Translation: AAC50589.1 .
    AF268380 Genomic DNA. Translation: AAF72545.1 .
    AK314229 mRNA. Translation: BAG36900.1 .
    CH471054 Genomic DNA. Translation: EAW96989.1 .
    BC065931 mRNA. Translation: AAH65931.1 .
    X70991 mRNA. Translation: CAA50318.1 .
    AJ011081 Genomic DNA. Translation: CAA09472.1 .
    CCDSi CCDS8930.1. [Q15742-1 ]
    RefSeqi NP_005958.1. NM_005967.3. [Q15742-1 ]
    XP_005268951.1. XM_005268894.2. [Q15742-3 ]
    UniGenei Hs.159223.

    3D structure databases

    ProteinModelPortali Q15742.
    SMRi Q15742. Positions 228-356.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110747. 7 interactions.
    IntActi Q15742. 2 interactions.
    STRINGi 9606.ENSP00000300131.

    PTM databases

    PhosphoSitei Q15742.

    Polymorphism databases

    DMDMi 12643729.

    Proteomic databases

    MaxQBi Q15742.
    PaxDbi Q15742.
    PRIDEi Q15742.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300131 ; ENSP00000300131 ; ENSG00000166886 . [Q15742-1 ]
    ENST00000342556 ; ENSP00000341491 ; ENSG00000166886 . [Q15742-3 ]
    GeneIDi 4665.
    KEGGi hsa:4665.
    UCSCi uc001smz.3. human. [Q15742-1 ]

    Organism-specific databases

    CTDi 4665.
    GeneCardsi GC12P057457.
    HGNCi HGNC:7627. NAB2.
    HPAi CAB004510.
    HPA027464.
    MIMi 602381. gene.
    neXtProti NX_Q15742.
    Orphaneti 2126. Solitary fibrous tumor.
    PharmGKBi PA31432.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307377.
    HOGENOMi HOG000026777.
    HOVERGENi HBG003127.
    InParanoidi Q15742.
    OMAi PGPESYA.
    OrthoDBi EOG776SPQ.
    PhylomeDBi Q15742.
    TreeFami TF315501.

    Miscellaneous databases

    GeneWikii NAB2.
    GenomeRNAii 4665.
    NextBioi 17978.
    PROi Q15742.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q15742.
    CleanExi HS_NAB2.
    Genevestigatori Q15742.

    Family and domain databases

    InterProi IPR006989. NAB_co-repressor_dom.
    IPR006988. Nab_N.
    [Graphical view ]
    Pfami PF04904. NCD1. 1 hit.
    PF04905. NCD2. 1 hit.
    [Graphical view ]
    ProDomi PD342192. Nab_N. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    ProtoNeti Search...

    Publicationsi

    1. "NAB2, a corepressor of NGFI-A (Egr-1) and Krox20, is induced by proliferative and differentiative stimuli."
      Svaren J., Sevetson B.R., Apel E.D., Zimonjic D.B., Popescu N.C., Milbrandt J.
      Mol. Cell. Biol. 16:3545-3553(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Placenta.
    2. "Genomic organization of the Mader/NAB2 gene."
      Gerlinger M., Johnson J.P.
      Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Skin.
    6. "Mader: a novel nuclear protein over expressed in human melanomas."
      Kirsch K.H., Korradi Y., Johnson J.P.
      Oncogene 12:963-971(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 50-525 (ISOFORM 1).
    7. Johnson J.P.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 3).
    8. "The Nab2 and Stat6 genes share a common transcription termination region."
      Svaren J., Apel E.D., Simburger K.S., Jenkins N.A., Gilbert D.J., Copeland N.G., Milbrandt J.
      Genomics 41:33-39(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators."
      Garcia-Gutierrez P., Juarez-Vicente F., Gallardo-Chamizo F., Charnay P., Garcia-Dominguez M.
      EMBO Rep. 12:1018-1023(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-379 AND LYS-517 BY EGR2.
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNAB2_HUMAN
    AccessioniPrimary (citable) accession number: Q15742
    Secondary accession number(s): B2RAK3, O76006, Q14797
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3