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Protein

Helix-loop-helix protein 2

Gene

NHLH2

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

Functioni

May serve as DNA-binding protein and may be involved in the control of cell-type determination, possibly within the developing nervous system.

GO - Molecular functioni

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • central nervous system development Source: ProtInc
  • mating behavior Source: Ensembl
  • ovulation cycle Source: Ensembl
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Helix-loop-helix protein 2
Short name:
HEN-2
Alternative name(s):
Class A basic helix-loop-helix protein 34
Short name:
bHLHa34
Nescient helix loop helix 2
Short name:
NSCL-2
Gene namesi
Name:NHLH2
Synonyms:BHLHA34, HEN2, KIAA0490
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:7818. NHLH2.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • nucleus Source: GO_Central
  • transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31620.

Polymorphism and mutation databases

BioMutaiNHLH2.
DMDMi399887.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 135135Helix-loop-helix protein 2PRO_0000127199Add
BLAST

Proteomic databases

PaxDbiQ02577.
PRIDEiQ02577.

PTM databases

PhosphoSiteiQ02577.

Expressioni

Gene expression databases

BgeeiQ02577.
CleanExiHS_NHLH2.
ExpressionAtlasiQ02577. baseline and differential.
GenevisibleiQ02577. HS.

Organism-specific databases

HPAiHPA055238.

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein.

Binary interactionsi

WithEntry#Exp.IntActNotes
SIRT1Q96EB62EBI-5378683,EBI-1802965

GO - Molecular functioni

  • RNA polymerase II activating transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi110873. 1 interaction.
IntActiQ02577. 1 interaction.
STRINGi9606.ENSP00000322087.

Structurei

3D structure databases

ProteinModelPortaliQ02577.
SMRiQ02577. Positions 84-134.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini77 – 12953bHLHPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi69 – 735Poly-Arg

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4029. Eukaryota.
ENOG411227D. LUCA.
GeneTreeiENSGT00760000119097.
HOGENOMiHOG000016617.
HOVERGENiHBG016345.
InParanoidiQ02577.
KOiK09075.
OMAiATLYPHP.
OrthoDBiEOG7G1V82.
PhylomeDBiQ02577.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q02577-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMLSPDQAAD SDHPSSAHSD PESLGGTDTK VLGSVSDLEP VEEAEGDGKG
60 70 80 90 100
GSRAALYPHP QQLSREEKRR RRRATAKYRS AHATRERIRV EAFNLAFAEL
110 120 130
RKLLPTLPPD KKLSKIEILR LAICYISYLN HVLDV
Length:135
Mass (Da):15,018
Last modified:July 1, 1993 - v1
Checksum:i083730499F610AAE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97508 Genomic DNA. Translation: AAA58635.1.
AB007959 mRNA. No translation available.
AL449264 Genomic DNA. Translation: CAI14533.1.
BC096359 mRNA. Translation: AAH96359.1.
BC096360 mRNA. Translation: AAH96360.1.
CCDSiCCDS885.1.
PIRiB45075.
RefSeqiNP_001104531.1. NM_001111061.1.
NP_005590.1. NM_005599.3.
XP_006710729.1. XM_006710666.2.
UniGeneiHs.46296.

Genome annotation databases

EnsembliENST00000320238; ENSP00000322087; ENSG00000177551.
ENST00000369506; ENSP00000358519; ENSG00000177551.
GeneIDi4808.
KEGGihsa:4808.
UCSCiuc001efy.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97508 Genomic DNA. Translation: AAA58635.1.
AB007959 mRNA. No translation available.
AL449264 Genomic DNA. Translation: CAI14533.1.
BC096359 mRNA. Translation: AAH96359.1.
BC096360 mRNA. Translation: AAH96360.1.
CCDSiCCDS885.1.
PIRiB45075.
RefSeqiNP_001104531.1. NM_001111061.1.
NP_005590.1. NM_005599.3.
XP_006710729.1. XM_006710666.2.
UniGeneiHs.46296.

3D structure databases

ProteinModelPortaliQ02577.
SMRiQ02577. Positions 84-134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110873. 1 interaction.
IntActiQ02577. 1 interaction.
STRINGi9606.ENSP00000322087.

PTM databases

PhosphoSiteiQ02577.

Polymorphism and mutation databases

BioMutaiNHLH2.
DMDMi399887.

Proteomic databases

PaxDbiQ02577.
PRIDEiQ02577.

Protocols and materials databases

DNASUi4808.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000320238; ENSP00000322087; ENSG00000177551.
ENST00000369506; ENSP00000358519; ENSG00000177551.
GeneIDi4808.
KEGGihsa:4808.
UCSCiuc001efy.4. human.

Organism-specific databases

CTDi4808.
GeneCardsiNHLH2.
HGNCiHGNC:7818. NHLH2.
HPAiHPA055238.
MIMi162361. gene.
neXtProtiNX_Q02577.
PharmGKBiPA31620.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4029. Eukaryota.
ENOG411227D. LUCA.
GeneTreeiENSGT00760000119097.
HOGENOMiHOG000016617.
HOVERGENiHBG016345.
InParanoidiQ02577.
KOiK09075.
OMAiATLYPHP.
OrthoDBiEOG7G1V82.
PhylomeDBiQ02577.

Miscellaneous databases

GenomeRNAii4808.
NextBioi18528.
PROiQ02577.
SOURCEiSearch...

Gene expression databases

BgeeiQ02577.
CleanExiHS_NHLH2.
ExpressionAtlasiQ02577. baseline and differential.
GenevisibleiQ02577. HS.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "HEN1 and HEN2: a subgroup of basic helix-loop-helix genes that are coexpressed in a human neuroblastoma."
    Brown L., Espinosa R. III, le Beau M.M., Siciliano M.J., Baer R.
    Proc. Natl. Acad. Sci. U.S.A. 89:8492-8496(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Brain.
  2. "A comparative structural characterization of the human NSCL-1 and NSCL-2 genes. Two basic helix-loop-helix genes expressed in the developing nervous system."
    Lipkowitz S., Gobel V., Varterasian M.L., Nakahara K., Tchorz K., Kirsch I.R.
    J. Biol. Chem. 267:21065-21071(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Brain.
  3. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
    Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
    DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    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].

Entry informationi

Entry nameiHEN2_HUMAN
AccessioniPrimary (citable) accession number: Q02577
Secondary accession number(s): Q5T1P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 11, 2016
This is version 142 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 1
    Human chromosome 1: 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

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.