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Protein

Alpha-hemoglobin-stabilizing protein

Gene

AHSP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a chaperone to prevent the harmful aggregation of alpha-hemoglobin during normal erythroid cell development. Specifically protects free alpha-hemoglobin from precipitation. It is predicted to modulate pathological states of alpha-hemoglobin excess such as beta-thalassemia.1 Publication

GO - Molecular functioni

  • hemoglobin binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

  • hemoglobin metabolic process Source: UniProtKB
  • hemopoiesis Source: UniProtKB
  • protein folding Source: InterPro
  • protein stabilization Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-hemoglobin-stabilizing protein
Alternative name(s):
Erythroid differentiation-related factor
Erythroid-associated factor
Gene namesi
Name:AHSP
Synonyms:EDRF, ERAF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:18075. AHSP.

Subcellular locationi

GO - Cellular componenti

  • hemoglobin complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27842.

Polymorphism and mutation databases

BioMutaiAHSP.
DMDMi23813669.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 102102Alpha-hemoglobin-stabilizing proteinPRO_0000064509Add
BLAST

Proteomic databases

PaxDbiQ9NZD4.
PeptideAtlasiQ9NZD4.
PRIDEiQ9NZD4.

Expressioni

Tissue specificityi

Expressed in blood and bone marrow.2 Publications

Inductioni

By GATA1 during erythroid maturation.

Gene expression databases

BgeeiQ9NZD4.
CleanExiHS_ERAF.
ExpressionAtlasiQ9NZD4. baseline and differential.
GenevisibleiQ9NZD4. HS.

Organism-specific databases

HPAiHPA040940.

Interactioni

Subunit structurei

Monomer. Forms a heterodimer with free alpha-hemoglobin. Does not bind beta-hemoglobin nor alpha2beta2 hemoglobin A.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FKBP1AP629423EBI-720250,EBI-1027571
UBE3AQ05086-23EBI-720250,EBI-10175863
ZC3H12AQ5D1E84EBI-720250,EBI-747793

GO - Molecular functioni

  • hemoglobin binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119476. 6 interactions.
DIPiDIP-35198N.
IntActiQ9NZD4. 6 interactions.
MINTiMINT-1427628.
STRINGi9606.ENSP00000307199.

Structurei

Secondary structure

1
102
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2319Combined sources
Helixi27 – 293Combined sources
Helixi34 – 5219Combined sources
Turni53 – 553Combined sources
Helixi60 – 8627Combined sources
Beta strandi97 – 993Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W09NMR-A3-94[»]
1W0ANMR-A3-94[»]
1W0BNMR-A2-102[»]
1XZYNMR-A1-90[»]
1Y01X-ray2.80A1-102[»]
1Z8UX-ray2.40A/C1-102[»]
3IA3X-ray3.20A/C1-91[»]
3OVUX-ray2.83A2-102[»]
ProteinModelPortaliQ9NZD4.
SMRiQ9NZD4. Positions 2-91.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZD4.

Family & Domainsi

Sequence similaritiesi

Belongs to the AHSP family.Curated

Phylogenomic databases

eggNOGiENOG410J29P. Eukaryota.
ENOG411196Z. LUCA.
GeneTreeiENSGT00390000003648.
HOGENOMiHOG000030915.
HOVERGENiHBG023495.
InParanoidiQ9NZD4.
OMAiGMKEFNV.
OrthoDBiEOG7TF7CW.
PhylomeDBiQ9NZD4.
TreeFamiTF337056.

Family and domain databases

Gene3Di1.20.58.420. 1 hit.
InterProiIPR015317. A_Hb_stabilising_prot.
[Graphical view]
PANTHERiPTHR15914. PTHR15914. 1 hit.
PfamiPF09236. AHSP. 1 hit.
[Graphical view]
ProDomiPD285427. A_Hb_stabilising_prot. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF109751. SSF109751. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9NZD4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLKANKDL ISAGLKEFSV LLNQQVFNDP LVSEEDMVTV VEDWMNFYIN
60 70 80 90 100
YYRQQVTGEP QERDKALQEL RQELNTLANP FLAKYRDFLK SHELPSHPPP

SS
Length:102
Mass (Da):11,840
Last modified:October 1, 2000 - v1
Checksum:i275DDF8BC670EF20
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321V → A in AAL82894 (Ref. 3) Curated
Sequence conflicti87 – 871D → N in AAL82894 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti100 – 1001P → T.
Corresponds to variant rs36018996 [ dbSNP | Ensembl ].
VAR_050650

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF364517 mRNA. Translation: AAK50856.1.
AF208865 mRNA. Translation: AAF64279.1.
AY072612 Genomic DNA. Translation: AAL82894.1.
AF485325 Genomic DNA. Translation: AAO49381.1.
BC035842 mRNA. Translation: AAH35842.1.
CCDSiCCDS10716.1.
RefSeqiNP_001305150.1. NM_001318221.1.
NP_001305151.1. NM_001318222.1.
NP_057717.1. NM_016633.3.
UniGeneiHs.274309.

Genome annotation databases

EnsembliENST00000302312; ENSP00000307199; ENSG00000169877.
GeneIDi51327.
KEGGihsa:51327.
UCSCiuc002ecj.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF364517 mRNA. Translation: AAK50856.1.
AF208865 mRNA. Translation: AAF64279.1.
AY072612 Genomic DNA. Translation: AAL82894.1.
AF485325 Genomic DNA. Translation: AAO49381.1.
BC035842 mRNA. Translation: AAH35842.1.
CCDSiCCDS10716.1.
RefSeqiNP_001305150.1. NM_001318221.1.
NP_001305151.1. NM_001318222.1.
NP_057717.1. NM_016633.3.
UniGeneiHs.274309.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W09NMR-A3-94[»]
1W0ANMR-A3-94[»]
1W0BNMR-A2-102[»]
1XZYNMR-A1-90[»]
1Y01X-ray2.80A1-102[»]
1Z8UX-ray2.40A/C1-102[»]
3IA3X-ray3.20A/C1-91[»]
3OVUX-ray2.83A2-102[»]
ProteinModelPortaliQ9NZD4.
SMRiQ9NZD4. Positions 2-91.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119476. 6 interactions.
DIPiDIP-35198N.
IntActiQ9NZD4. 6 interactions.
MINTiMINT-1427628.
STRINGi9606.ENSP00000307199.

Polymorphism and mutation databases

BioMutaiAHSP.
DMDMi23813669.

Proteomic databases

PaxDbiQ9NZD4.
PeptideAtlasiQ9NZD4.
PRIDEiQ9NZD4.

Protocols and materials databases

DNASUi51327.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302312; ENSP00000307199; ENSG00000169877.
GeneIDi51327.
KEGGihsa:51327.
UCSCiuc002ecj.4. human.

Organism-specific databases

CTDi51327.
GeneCardsiAHSP.
HGNCiHGNC:18075. AHSP.
HPAiHPA040940.
MIMi605821. gene.
neXtProtiNX_Q9NZD4.
PharmGKBiPA27842.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410J29P. Eukaryota.
ENOG411196Z. LUCA.
GeneTreeiENSGT00390000003648.
HOGENOMiHOG000030915.
HOVERGENiHBG023495.
InParanoidiQ9NZD4.
OMAiGMKEFNV.
OrthoDBiEOG7TF7CW.
PhylomeDBiQ9NZD4.
TreeFamiTF337056.

Miscellaneous databases

ChiTaRSiAHSP. human.
EvolutionaryTraceiQ9NZD4.
GeneWikiiERAF.
GenomeRNAii51327.
PROiQ9NZD4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NZD4.
CleanExiHS_ERAF.
ExpressionAtlasiQ9NZD4. baseline and differential.
GenevisibleiQ9NZD4. HS.

Family and domain databases

Gene3Di1.20.58.420. 1 hit.
InterProiIPR015317. A_Hb_stabilising_prot.
[Graphical view]
PANTHERiPTHR15914. PTHR15914. 1 hit.
PfamiPF09236. AHSP. 1 hit.
[Graphical view]
ProDomiPD285427. A_Hb_stabilising_prot. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF109751. SSF109751. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel erythroid-specific marker of transmissible spongiform encephalopathies."
    Miele G., Manson J., Clinton M.
    Nat. Med. 7:361-364(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  3. Michel U., Schulz-Schaeffer W.
    Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Finning K., Anstee D.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [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].
  6. "An abundant erythroid protein that stabilizes free alpha-haemoglobin."
    Kihm A.J., Kong Y., Hong W., Russell J.E., Rouda S., Adachi K., Simon M.C., Blobel G.A., Weiss M.J.
    Nature 417:758-763(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "Biophysical characterization of the alpha-globin binding protein alpha-hemoglobin stabilizing protein."
    Gell D., Kong Y., Eaton S.A., Weiss M.J., Mackay J.P.
    J. Biol. Chem. 277:40602-40609(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  8. Cited for: STRUCTURE BY NMR OF 1-90, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH HBA.
  9. "NMR structure of the alpha-hemoglobin stabilizing protein: insights into conformational heterogeneity and binding."
    Santiveri C.M., Perez-Canadillas J.M., Vadivelu M.K., Allen M.D., Rutherford T.J., Watkins N.A., Bycroft M.
    J. Biol. Chem. 279:34963-34970(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-102 OF WILD TYPE AND MUTANT ALA-30.
  10. "Structure of oxidized alpha-haemoglobin bound to AHSP reveals a protective mechanism for haem."
    Feng L., Zhou S., Gu L., Gell D.A., Mackay J.P., Weiss M.J., Gow A.J., Shi Y.
    Nature 435:697-701(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH HBA.

Entry informationi

Entry nameiAHSP_HUMAN
AccessioniPrimary (citable) accession number: Q9NZD4
Secondary accession number(s): Q8TD01
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 121 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 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.