Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

NGFI-A-binding protein 2

Gene

NAB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 – 61Phosphoserine3 Publications
Modified residuei159 – 1591Phosphoserine1 Publication
Modified residuei162 – 1621Phosphoserine1 Publication
Modified residuei171 – 1711Phosphoserine1 Publication
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. 40 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.
GeneTreeiENSGT00390000006330.
HOGENOMiHOG000026777.
HOVERGENiHBG003127.
InParanoidiQ15742.
OMAiHSELQQP.
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. AlignAdd to basket

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

        10         20         30         40         50
MHRAPSPTAE QPPGGGDSAR RTLQPRLKPS ARAMALPRTL GELQLYRVLQ
60 70 80 90 100
RANLLSYYET FIQQGGDDVQ QLCEAGEEEF LEIMALVGMA TKPLHVRRLQ
110 120 130 140 150
KALREWATNP GLFSQPVPAV PVSSIPLFKI SETAGTRKGS MSNGHGSPGE
160 170 180 190 200
KAGSARSFSP KSPLELGEKL SPLPGGPGAG DPRIWPGRST PESDVGAGGE
210 220 230 240 250
EEAGSPPFSP PAGGGVPEGT GAGGLAAGGT GGGPDRLEPE MVRMVVESVE
260 270 280 290 300
RIFRSFPRGD AGEVTSLLKL NKKLARSVGH IFEMDDNDSQ KEEEIRKYSI
310 320 330 340 350
IYGRFDSKRR EGKQLSLHEL TINEAAAQFC MRDNTLLLRR VELFSLSRQV
360 370 380 390 400
ARESTYLSSL KGSRLHPEEL GGPPLKKLKQ EVGEQSHPEI QQPPPGPESY
410 420 430 440 450
VPPYRPSLEE DSASLSGESL DGHLQAVGSC PRLTPPPADL PLALPAHGLW
460 470 480 490 500
SRHILQQTLM DEGLRLARLV SHDRVGRLSP CVPAKPPLAE FEEGLLDRCP
510 520
APGPHPALVE GRRSSVKVEA EASRQ
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 → Q (Ref. 7) Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi110747. 40 interactions.
IntActiQ15742. 2 interactions.
STRINGi9606.ENSP00000300131.

PTM databases

PhosphoSiteiQ15742.

Polymorphism databases

DMDMi12643729.

Proteomic databases

MaxQBiQ15742.
PaxDbiQ15742.
PRIDEiQ15742.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4665.
GeneCardsiGC12P057457.
HGNCiHGNC:7627. NAB2.
HPAiCAB004510.
HPA027464.
MIMi602381. gene.
neXtProtiNX_Q15742.
Orphaneti2126. Solitary fibrous tumor.
PharmGKBiPA31432.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG307377.
GeneTreeiENSGT00390000006330.
HOGENOMiHOG000026777.
HOVERGENiHBG003127.
InParanoidiQ15742.
OMAiHSELQQP.
OrthoDBiEOG776SPQ.
PhylomeDBiQ15742.
TreeFamiTF315501.

Miscellaneous databases

GeneWikiiNAB2.
GenomeRNAii4665.
NextBioi17978.
PROiQ15742.
SOURCEiSearch...

Gene expression databases

BgeeiQ15742.
CleanExiHS_NAB2.
GenevestigatoriQ15742.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-171, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: March 4, 2015
This is version 123 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.