Hemoglobin subunit epsilon - Homo sapiens (Human)

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P02100 (HBE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Hemoglobin subunit epsilon

Alternative name(s):
Epsilon-globin
Hemoglobin epsilon chain

Gene names

Name:	HBE1
Synonyms:	HBE

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin.
Subunit structure	Heterotetramer of two alpha chains and two epsilon chains in early embryonic hemoglobin Gower-2; two zeta chains and two epsilon chains in early embryonic hemoglobin Gower-1.
Tissue specificity	Red blood cells.
Sequence similarities	Belongs to the globin family.

Ontologies

Keywords
Biological process	Oxygen transport Transport
Ligand	Heme Iron Metal-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: Reactome
Cellular component	hemoglobin complex Traceable author statement. Source: ProtInc
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro oxygen binding Inferred from electronic annotation. Source: InterPro oxygen transporter activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5

Chain

2 – 147

146

Hemoglobin subunit epsilon

PRO_0000053212

Sites

Metal binding

Iron (heme distal ligand)

Metal binding

Iron (heme proximal ligand)

Amino acid modifications

Modified residue

Phosphotyrosine Ref.6

Experimental info

Sequence conflict

143

A → G AA sequence Ref.5

Secondary structure

147

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P02100 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 223388816EDDE8D5
Show »

FASTA

147

16,203

        10         20         30         40         50         60 
MVHFTAEEKA AVTSLWSKMN VEEAGGEALG RLLVVYPWTQ RFFDSFGNLS SPSAILGNPK 

        70         80         90        100        110        120 
VKAHGKKVLT SFGDAIKNMD NLKPAFAKLS ELHCDKLHVD PENFKLLGNV MVIILATHFG 

       130        140 
KEFTPEVQAA WQKLVSAVAI ALAHKYH

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of the human epsilon-globin gene." Baralle F.E., Shoulders C.C., Proudfoot N.J. Cell 21:621-626(1980) [PubMed: 6254663] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[5]	"Embryonic hemoglobin: sequence of the epsilon and zeta chains." Clegg J.B. Tex. Rep. Biol. Med. 40:23-28(1980) [PubMed: 6172865] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-147.
[6]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"Crystal structure of a human embryonic haemoglobin: the carbonmonoxy form of Gower II (alpha2 epsilon2) haemoglobin at 2.9-A resolution." Sutherland-Smith A.J., Baker H.M., Hofmann O.M., Brittain T., Baker E.N. J. Mol. Biol. 280:475-484(1998) [PubMed: 9665850] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF HB GOWER-2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U01317 Genomic DNA. Translation: AAA16330.1.
V00508 Genomic DNA. Translation: CAA23766.1.
CR541912 mRNA. Translation: CAG46710.1.
CH471064 Genomic DNA. Translation: EAW68802.1.
BC015537 mRNA. Translation: AAH15537.1.

IPI

IPI00217471.

PIR

HEHU. A90802.

RefSeq

NP_005321.1. NM_005330.3.

UniGene

Hs.655195.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A9W	X-ray	2.90	E/F	2-147	[»]

ProteinModelPortal

P02100.

SMR

P02100. Positions 2-146.

ModBase

Search...

Protein-protein interaction databases

STRING

P02100.

PTM databases

PhosphoSite

P02100.

Polymorphism databases

DMDM

122726.

Proteomic databases

PeptideAtlas

P02100.

PRIDE

P02100.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000292896; ENSP00000292896; ENSG00000213931.
ENST00000380237; ENSP00000369586; ENSG00000213931.

GeneID

3046.

KEGG

hsa:3046.

UCSC

uc001mal.1. human.

Organism-specific databases

CTD

3046.

GeneCards

GC11M005289.

HGNC

HGNC:4830. HBE1.

MIM

142100. gene.

neXtProt

NX_P02100.

PharmGKB

PA29205.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG715197.

HOVERGEN

HBG009709.

InParanoid

P02100.

OMA

MDNLKTT.

OrthoDB

EOG4THVVF.

PhylomeDB

P02100.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P02100.

Bgee

P02100.

CleanEx

HS_HBE1.

Genevestigator

P02100.

GermOnline

ENSG00000196565. Homo sapiens.

Family and domain databases

InterPro

IPR009050. Globin-like.
IPR012292. Globin_dom.
IPR000971. Globin_subset.
IPR002337. Haemoglobin_b.
[Graphical view]

Gene3D

G3DSA:1.10.490.10. Globin_related. 1 hit.

K13825.

PANTHER

PTHR11442:SF7. Beta_haem. 1 hit.

Pfam

PF00042. Globin. 1 hit.
[Graphical view]

PRINTS

PR00814. BETAHAEM.

SUPFAM

SSF46458. Globin_like. 1 hit.

PROSITE

PS01033. GLOBIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

12059.

SOURCE

Search...

Entry information

Entry name

HBE_HUMAN

Accession

Primary (citable) accession number: P02100
Secondary accession number(s): Q6FH44

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 123 of the entry and version 2 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.

Relevant documents

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents