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Protein

Nucleus accumbens-associated protein 1

Gene

NACC1

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

Functioni

Functions as a transcriptional repressor. Seems to function as a transcriptional corepressor in neuronal cells through recruitment of HDAC3 and HDAC4. Contributes to tumor progression, and tumor cell proliferation and survival. This may be mediated at least in part through repressing transcriptional activity of GADD45GIP1. Required for recruiting the proteasome from the nucleus to the cytoplasm and dendritic spines.2 Publications

GO - Biological processi

  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • 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:
Nucleus accumbens-associated protein 1
Short name:
NAC-1
Alternative name(s):
BTB/POZ domain-containing protein 14B
Gene namesi
Name:NACC1
Synonyms:BTBD14B, NAC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:20967. NACC1.

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Distribution in the cytoplasm is dependent on phosphorylation.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nuclear body Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164723404.

Polymorphism and mutation databases

BioMutaiNACC1.
DMDMi74732694.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 527527Nucleus accumbens-associated protein 1PRO_0000274041Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki167 – 167Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei188 – 1881PhosphoserineCombined sources
Modified residuei259 – 2591Phosphoserine; by PKCBy similarity
Cross-linki483 – 483Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ96RE7.
MaxQBiQ96RE7.
PaxDbiQ96RE7.
PeptideAtlasiQ96RE7.
PRIDEiQ96RE7.

PTM databases

iPTMnetiQ96RE7.
PhosphoSiteiQ96RE7.

Expressioni

Tissue specificityi

Overexpressed in several types of carcinomas including ovarian serous carcinomas. Expression levels positively correlate with tumor recurrence in ovarian serous carcinomas, and intense immunoreactivity in primary ovarian tumors predicts early recurrence. Up-regulated in ovarian carcinomas after chemotherapy, suggesting a role in development of chemotherapy resistance in ovarian cancer.2 Publications

Gene expression databases

BgeeiQ96RE7.
CleanExiHS_NACC1.
ExpressionAtlasiQ96RE7. baseline and differential.
GenevisibleiQ96RE7. HS.

Organism-specific databases

HPAiHPA021238.
HPA062245.

Interactioni

Subunit structurei

Homooligomer; mediated by the BTB domain. Interacts with HDAC3 and HDAC4. Interacts (via BTB domain) with CUL3, PSMD7 AND RCOR1.

Protein-protein interaction databases

BioGridi125217. 26 interactions.
IntActiQ96RE7. 10 interactions.
STRINGi9606.ENSP00000292431.

Structurei

Secondary structure

1
527
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi12 – 2514Combined sources
Turni26 – 294Combined sources
Beta strandi32 – 365Combined sources
Beta strandi39 – 435Combined sources
Helixi45 – 517Combined sources
Helixi53 – 619Combined sources
Beta strandi65 – 684Combined sources
Helixi75 – 8713Combined sources
Beta strandi88 – 914Combined sources
Turni94 – 963Combined sources
Helixi97 – 10610Combined sources
Helixi110 – 1134Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GA1X-ray2.10A/B2-125[»]
4U2NX-ray2.30A/B2-125[»]
ProteinModelPortaliQ96RE7.
SMRiQ96RE7. Positions 2-123.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96RE7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 9465BTBPROSITE-ProRule annotationAdd
BLAST
Domaini374 – 47198BENPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi194 – 1996Poly-Gly

Sequence similaritiesi

Contains 1 BEN domain.PROSITE-ProRule annotation
Contains 1 BTB (POZ) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000119063.
HOGENOMiHOG000231834.
HOVERGENiHBG052875.
InParanoidiQ96RE7.
KOiK10486.
OMAiNMGDQFL.
PhylomeDBiQ96RE7.
TreeFamiTF331184.

Family and domain databases

InterProiIPR018379. BEN_domain.
IPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
[Graphical view]
PfamiPF10523. BEN. 1 hit.
PF00651. BTB. 1 hit.
[Graphical view]
SMARTiSM01025. BEN. 1 hit.
SM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS51457. BEN. 1 hit.
PS50097. BTB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q96RE7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQTLQMEIP NFGNSILECL NEQRLQGLYC DVSVVVKGHA FKAHRAVLAA
60 70 80 90 100
SSSYFRDLFN NSRSAVVELP AAVQPQSFQQ ILSFCYTGRL SMNVGDQFLL
110 120 130 140 150
MYTAGFLQIQ EIMEKGTEFF LKVSSPSCDS QGLHAEEAPS SEPQSPVAQT
160 170 180 190 200
SGWPACSTPL PLVSRVKTEQ QESDSVQCMP VAKRLWDSGQ KEAGGGGNGS
210 220 230 240 250
RKMAKFSTPD LAANRPHQPP PPQQAPVVAA AQPAVAAGAG QPAGGVAAAG
260 270 280 290 300
GVVSGPSTSE RTSPGTSSAY TSDSPGSYHN EEDEEEDGGE EGMDEQYRQI
310 320 330 340 350
CNMYTMYSMM NVGQTAEKVE ALPEQVAPES RNRIRVRQDL ASLPAELINQ
360 370 380 390 400
IGNRCHPKLY DEGDPSEKLE LVTGTNVYIT RAQLMNCHVS AGTRHKVLLR
410 420 430 440 450
RLLASFFDRN TLANSCGTGI RSSTNDPRRK PLDSRVLHAV KYYCQNFAPN
460 470 480 490 500
FKESEMNAIA ADMCTNARRV VRKSWMPKVK VLKAEDDAYT TFISETGKIE
510 520
PDMMGVEHGF ETASHEGEAG PSAEALQ
Length:527
Mass (Da):57,258
Last modified:December 1, 2001 - v1
Checksum:i00BEA89D2DC3DAD2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF395817 mRNA. Translation: AAK83885.1.
BC055396 mRNA. Translation: AAH55396.1.
CCDSiCCDS12294.1.
RefSeqiNP_443108.1. NM_052876.3.
XP_005259778.1. XM_005259721.2.
UniGeneiHs.531614.

Genome annotation databases

EnsembliENST00000292431; ENSP00000292431; ENSG00000160877.
GeneIDi112939.
KEGGihsa:112939.
UCSCiuc002mwm.5. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF395817 mRNA. Translation: AAK83885.1.
BC055396 mRNA. Translation: AAH55396.1.
CCDSiCCDS12294.1.
RefSeqiNP_443108.1. NM_052876.3.
XP_005259778.1. XM_005259721.2.
UniGeneiHs.531614.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GA1X-ray2.10A/B2-125[»]
4U2NX-ray2.30A/B2-125[»]
ProteinModelPortaliQ96RE7.
SMRiQ96RE7. Positions 2-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125217. 26 interactions.
IntActiQ96RE7. 10 interactions.
STRINGi9606.ENSP00000292431.

PTM databases

iPTMnetiQ96RE7.
PhosphoSiteiQ96RE7.

Polymorphism and mutation databases

BioMutaiNACC1.
DMDMi74732694.

Proteomic databases

EPDiQ96RE7.
MaxQBiQ96RE7.
PaxDbiQ96RE7.
PeptideAtlasiQ96RE7.
PRIDEiQ96RE7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000292431; ENSP00000292431; ENSG00000160877.
GeneIDi112939.
KEGGihsa:112939.
UCSCiuc002mwm.5. human.

Organism-specific databases

CTDi112939.
GeneCardsiNACC1.
HGNCiHGNC:20967. NACC1.
HPAiHPA021238.
HPA062245.
MIMi610672. gene.
neXtProtiNX_Q96RE7.
PharmGKBiPA164723404.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1721. Eukaryota.
COG5048. LUCA.
GeneTreeiENSGT00760000119063.
HOGENOMiHOG000231834.
HOVERGENiHBG052875.
InParanoidiQ96RE7.
KOiK10486.
OMAiNMGDQFL.
PhylomeDBiQ96RE7.
TreeFamiTF331184.

Miscellaneous databases

ChiTaRSiNACC1. human.
EvolutionaryTraceiQ96RE7.
GeneWikiiBTBD14B.
GenomeRNAii112939.
NextBioi78713.
PROiQ96RE7.
SOURCEiSearch...

Gene expression databases

BgeeiQ96RE7.
CleanExiHS_NACC1.
ExpressionAtlasiQ96RE7. baseline and differential.
GenevisibleiQ96RE7. HS.

Family and domain databases

InterProiIPR018379. BEN_domain.
IPR000210. BTB/POZ_dom.
IPR011333. SKP1/BTB/POZ.
[Graphical view]
PfamiPF10523. BEN. 1 hit.
PF00651. BTB. 1 hit.
[Graphical view]
SMARTiSM01025. BEN. 1 hit.
SM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
PROSITEiPS51457. BEN. 1 hit.
PS50097. BTB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human NAC1 protein, a gene transcriptional repressor."
    Cha X.Y., Fakharzadeh S.S.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Keratinocyte.
  2. "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].
    Tissue: Eye.
  3. "A BTB/POZ protein, NAC-1, is related to tumor recurrence and is essential for tumor growth and survival."
    Nakayama K., Nakayama N., Davidson B., Sheu J.-J.C., Jinawath N., Santillan A., Salani R., Bristow R.E., Morin P.J., Kurman R.J., Wang T.-L., Shih I.-M.
    Proc. Natl. Acad. Sci. U.S.A. 103:18739-18744(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMOOLIGOMERIZATION, TISSUE SPECIFICITY.
  4. "NAC-1 controls cell growth and survival by repressing transcription of Gadd45GIP1, a candidate tumor suppressor."
    Nakayama K., Nakayama N., Wang T.-L., Shih I.-M.
    Cancer Res. 67:8058-8064(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Expression and clinical role of the bric-a-brac tramtrack broad complex/poxvirus and zinc protein NAC-1 in ovarian carcinoma effusions."
    Davidson B., Berner A., Trope' C.G., Wang T.-L., Shih I.-M.
    Hum. Pathol. 38:1030-1036(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167 AND LYS-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167 AND LYS-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-167 AND LYS-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-125.

Entry informationi

Entry nameiNACC1_HUMAN
AccessioniPrimary (citable) accession number: Q96RE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: December 1, 2001
Last modified: May 11, 2016
This is version 117 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.