Q9NPG2 (NGB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Neuroglobin

Gene names

Name:

NGB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in oxygen transport in the brain. Hexacoordinate globin, displaying competitive binding of oxygen or the distal His residue to the iron atom. Not capable of penetrating cell membranes. The deoxygenated form exhibits nitrite reductase activity inhibiting cellular respiration via NO-binding to cytochrome c oxidase. Involved in neuroprotection during oxidative stress. May exert its anti-apoptotic activity by acting to reset the trigger level of mitochondrial cytochrome c release necessary to commit the cells to apoptosis. Ref.1 Ref.5 Ref.7 Ref.8 Ref.9
Subunit structure	Monomer. Homodimer and homotetramer; disulfide-linked By similarity. Interacts with 14-3-3. Ref.6 Ref.9 Ref.10
Subcellular location	Perikaryon By similarity. Cytoplasm. Mitochondrion.
Tissue specificity	Predominantly expressed in brain, the strongest expression is seen in the frontal lobe, the subthalamic nucleus and the thalamus. Ref.1
Post-translational modification	A redox disulfide bond regulates the heme pocket coordination and the rate of nitrite reduction to NO. Phosphorylated in vitro by ERK1, ERK2 and PKA, and in vivo during hypoxia. Phosphorylation increases nitrite reductase activity. Ref.10
Sequence similarities	Belongs to the globin family.

Ontologies

Keywords
Biological process	Apoptosis Oxygen transport Transport
Cellular component	Cytoplasm Mitochondrion
Ligand	Heme Iron Metal-binding
PTM	Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	hemoglobin complex Non-traceable author statement. Source: UniProtKB mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell perikaryon Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 151

151

Neuroglobin

PRO_0000053390

Regions

Region

1 – 149

149

Globin

Sites

Metal binding

64

1

Iron (heme distal ligand)

Metal binding

96

1

Iron (heme proximal ligand)

Amino acid modifications

Disulfide bond

46 ↔ 55

Redox-active Ref.6 Ref.9

Secondary structure

1

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151

Helix Strand Turn

Details...

Helix

6 – 17

12

Helix

20 – 34

15

Helix

36 – 41

6

Helix

52 – 55

4

Helix

59 – 77

19

Turn

78 – 80

3

Helix

82 – 85

4

Helix

86 – 98

13

Helix

105 – 121

17

Helix

122 – 124

3

Helix

127 – 144

18

Helix

145 – 147

3

Sequences

	Sequence		Length	Mass (Da)
	Q9NPG2 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 45A292A7D77B9CE3	FASTA	151	16,933
	10 20 30 40 50 60 MERPEPELIR QSWRAVSRSP LEHGTVLFAR LFALEPDLLP LFQYNCRQFS SPEDCLSSPE 70 80 90 100 110 120 FLDHIRKVML VIDAAVTNVE DLSSLEEYLA SLGRKHRAVG VKLSSFSTVG ESLLYMLEKC 130 140 150 LGPAFTPATR AAWSQLYGAV VQAMSRGWDG E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A vertebrate globin expressed in the brain." Burmester T., Weich B., Reinhardt S., Hankeln T. Nature 407:520-522(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Brain.
[2]	"Full-length cDNA cloning of human neuroglobin and tissue expression of rat neuroglobin." Zhang C.G., Wang C.L., Deng M.Y., Li L., Wang H.Y., Fan M., Xu W.L., Meng F.W., Qian L., He F.C. Biochem. Biophys. Res. Commun. 290:1411-1419(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: Brain.
[5]	"Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family." Dewilde S., Kiger L., Burmester T., Hankeln T., Baudin-Creuza V., Aerts T., Marden M.C., Caubergs R., Moens L. J. Biol. Chem. 276:38949-38955(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Coupling of the heme and an internal disulfide bond in human neuroglobin." Hamdane D., Kiger L., Dewilde S., Green B.N., Pesce A., Uzan J., Burmester T., Hankeln T., Bolognesi M., Moens L., Marden M.C. Micron 35:59-62(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BOND.
[7]	"Zebrafish neuroglobin is a cell-membrane-penetrating globin." Watanabe S., Wakasugi K. Biochemistry 47:5266-5270(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"A role for human neuroglobin in apoptosis." Brittain T., Skommer J., Henty K., Birch N., Raychaudhuri S. IUBMB Life 62:878-885(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN APOPTOSIS.
[9]	"Human neuroglobin functions as a redox-regulated nitrite reductase." Tiso M., Tejero J., Basu S., Azarov I., Wang X., Simplaceanu V., Frizzell S., Jayaraman T., Geary L., Shapiro C., Ho C., Shiva S., Kim-Shapiro D.B., Gladwin M.T. J. Biol. Chem. 286:18277-18289(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISULFIDE BOND.
[10]	"14-3-3 binding and phosphorylation of neuroglobin during hypoxia modulate six-to-five heme pocket coordination and rate of nitrite reduction to nitric oxide." Jayaraman T., Tejero J., Chen B.B., Blood A.B., Frizzell S., Shapiro C., Tiso M., Hood B.L., Wang X., Zhao X., Conrads T.P., Mallampalli R.K., Gladwin M.T. J. Biol. Chem. 286:42679-42689(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION DURING HYPOXIA, INTERACTION WITH 14-3-3.
[11]	"Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity." Pesce A., Dewilde S., Nardini M., Moens L., Ascenzi P., Hankeln T., Burmester T., Bolognesi M. Structure 11:1087-1095(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN A HEXACOORDINATED FE(3+)-BOUND FORM.
+	Additional computationally mapped references.

Web resources

Wikipedia

Neuroglobin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ245944 Genomic DNA. Translation: CAC12994.1.
AJ245946 mRNA. Translation: CAC11133.1.
AF422796 Genomic DNA. Translation: AAL98923.1.
AF422797 mRNA. Translation: AAL98924.1.
AC007375 Genomic DNA. Translation: AAF63183.1.
AC007954 Genomic DNA. Translation: AAF62557.1.
BC032509 mRNA. Translation: AAH32509.1.

IPI

IPI00009758.

RefSeq

NP_067080.1. NM_021257.3.

UniGene

Hs.274363.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1OJ6	X-ray	1.95	A/B/C/D	1-151	[»]

ProteinModelPortal

Q9NPG2.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000298352.

Polymorphism databases

DMDM

32171399.

Proteomic databases

PaxDb

Q9NPG2.

PRIDE

Q9NPG2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000298352; ENSP00000298352; ENSG00000165553.

GeneID

58157.

KEGG

hsa:58157.

UCSC

uc001xtg.1. human.

Organism-specific databases

CTD

58157.

GeneCards

GC14M077731.

HGNC

HGNC:14077. NGB.

HPA

CAB037319.

MIM

605304. gene.

neXtProt

NX_Q9NPG2.

PharmGKB

PA31612.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG317570.

HOGENOM

HOG000036573.

HOVERGEN

HBG039321.

InParanoid

Q9NPG2.

OMA

GRKHQAV.

OrthoDB

EOG4V9TRV.

PhylomeDB

Q9NPG2.

Gene expression databases

ArrayExpress

Q9NPG2.

Bgee

Q9NPG2.

CleanEx

HS_NGB.

Genevestigator

Q9NPG2.

GermOnline

ENSG00000165553. Homo sapiens.

Family and domain databases

Gene3D

1.10.490.10. 1 hit.

InterPro

IPR000971. Globin.
IPR009050. Globin-like.
IPR012292. Globin_dom.
[Graphical view]

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9NPG2.

GenomeRNAi

58157.

NextBio

64865.

SOURCE

Search...

Entry information

Entry name

NGB_HUMAN

Accession

Primary (citable) accession number: Q9NPG2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.