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Alpha-hemoglobin-stabilizing protein (Erythroid differentiation-related factor) (Erythroid-associated factor)

 AHSP_HUMAN              Reviewed;         102 AA.
Q9NZD4; Q8TD01;
10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
28-FEB-2018, entry version 133.
RecName: Full=Alpha-hemoglobin-stabilizing protein;
AltName: Full=Erythroid differentiation-related factor;
AltName: Full=Erythroid-associated factor;
Name=AHSP; Synonyms=EDRF, ERAF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=11231637; DOI=10.1038/85515;
Miele G., Manson J., Clinton M.;
"A novel erythroid-specific marker of transmissible spongiform
encephalopathies.";
Nat. Med. 7:361-364(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
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.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Michel U., Schulz-Schaeffer W.;
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Finning K., Anstee D.;
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12066189; DOI=10.1038/nature00803;
Kihm A.J., Kong Y., Hong W., Russell J.E., Rouda S., Adachi K.,
Simon M.C., Blobel G.A., Weiss M.J.;
"An abundant erythroid protein that stabilizes free alpha-
haemoglobin.";
Nature 417:758-763(2002).
[7]
CHARACTERIZATION.
PubMed=12192002; DOI=10.1074/jbc.M206084200;
Gell D., Kong Y., Eaton S.A., Weiss M.J., Mackay J.P.;
"Biophysical characterization of the alpha-globin binding protein
alpha-hemoglobin stabilizing protein.";
J. Biol. Chem. 277:40602-40609(2002).
[8]
STRUCTURE BY NMR OF 1-90, AND X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN
COMPLEX WITH HBA.
PubMed=15550245; DOI=10.1016/j.cell.2004.11.025;
Feng L., Gell D.A., Zhou S., Gu L., Kong Y., Li J., Hu M., Yan N.,
Lee C., Rich A.M., Armstrong R.S., Lay P.A., Gow A.J., Weiss M.J.,
Mackay J.P., Shi Y.;
"Molecular mechanism of AHSP-mediated stabilization of alpha-
hemoglobin.";
Cell 119:629-640(2004).
[9]
STRUCTURE BY NMR OF 2-102 OF WILD TYPE AND MUTANT ALA-30.
PubMed=15178680; DOI=10.1074/jbc.M405016200;
Santiveri C.M., Perez-Canadillas J.M., Vadivelu M.K., Allen M.D.,
Rutherford T.J., Watkins N.A., Bycroft M.;
"NMR structure of the alpha-hemoglobin stabilizing protein: insights
into conformational heterogeneity and binding.";
J. Biol. Chem. 279:34963-34970(2004).
[10]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH HBA.
PubMed=15931225; DOI=10.1038/nature03609;
Feng L., Zhou S., Gu L., Gell D.A., Mackay J.P., Weiss M.J., Gow A.J.,
Shi Y.;
"Structure of oxidized alpha-haemoglobin bound to AHSP reveals a
protective mechanism for haem.";
Nature 435:697-701(2005).
-!- FUNCTION: 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. {ECO:0000269|PubMed:12066189}.
-!- SUBUNIT: Monomer. Forms a heterodimer with free alpha-hemoglobin.
Does not bind beta-hemoglobin nor alpha(2)beta(2) hemoglobin A.
{ECO:0000269|PubMed:15550245, ECO:0000269|PubMed:15931225}.
-!- INTERACTION:
P62942:FKBP1A; NbExp=3; IntAct=EBI-720250, EBI-1027571;
P69905:HBA2; NbExp=2; IntAct=EBI-720250, EBI-714680;
Q05086-2:UBE3A; NbExp=3; IntAct=EBI-720250, EBI-10175863;
Q9Y2B5:VPS9D1; NbExp=4; IntAct=EBI-720250, EBI-9031083;
Q5D1E8:ZC3H12A; NbExp=4; IntAct=EBI-720250, EBI-747793;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12066189}.
-!- TISSUE SPECIFICITY: Expressed in blood and bone marrow.
{ECO:0000269|PubMed:11231637, ECO:0000269|PubMed:12066189}.
-!- INDUCTION: By GATA1 during erythroid maturation.
-!- SIMILARITY: Belongs to the AHSP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF364517; AAK50856.1; -; mRNA.
EMBL; AF208865; AAF64279.1; -; mRNA.
EMBL; AY072612; AAL82894.1; -; Genomic_DNA.
EMBL; AF485325; AAO49381.1; -; Genomic_DNA.
EMBL; BC035842; AAH35842.1; -; mRNA.
CCDS; CCDS10716.1; -.
RefSeq; NP_001305150.1; NM_001318221.1.
RefSeq; NP_001305151.1; NM_001318222.1.
RefSeq; NP_057717.1; NM_016633.3.
UniGene; Hs.274309; -.
PDB; 1W09; NMR; -; A=3-94.
PDB; 1W0A; NMR; -; A=3-94.
PDB; 1W0B; NMR; -; A=2-102.
PDB; 1XZY; NMR; -; A=1-90.
PDB; 1Y01; X-ray; 2.80 A; A=1-102.
PDB; 1Z8U; X-ray; 2.40 A; A/C=1-102.
PDB; 3IA3; X-ray; 3.20 A; A/C=1-91.
PDB; 3OVU; X-ray; 2.83 A; A=2-102.
PDBsum; 1W09; -.
PDBsum; 1W0A; -.
PDBsum; 1W0B; -.
PDBsum; 1XZY; -.
PDBsum; 1Y01; -.
PDBsum; 1Z8U; -.
PDBsum; 3IA3; -.
PDBsum; 3OVU; -.
ProteinModelPortal; Q9NZD4; -.
SMR; Q9NZD4; -.
BioGrid; 119476; 9.
DIP; DIP-35198N; -.
IntAct; Q9NZD4; 9.
STRING; 9606.ENSP00000307199; -.
BioMuta; AHSP; -.
DMDM; 23813669; -.
PaxDb; Q9NZD4; -.
PeptideAtlas; Q9NZD4; -.
PRIDE; Q9NZD4; -.
TopDownProteomics; Q9NZD4; -.
DNASU; 51327; -.
Ensembl; ENST00000302312; ENSP00000307199; ENSG00000169877.
GeneID; 51327; -.
KEGG; hsa:51327; -.
UCSC; uc002ecj.4; human.
CTD; 51327; -.
DisGeNET; 51327; -.
EuPathDB; HostDB:ENSG00000169877.9; -.
GeneCards; AHSP; -.
HGNC; HGNC:18075; AHSP.
HPA; HPA040940; -.
MIM; 605821; gene.
neXtProt; NX_Q9NZD4; -.
OpenTargets; ENSG00000169877; -.
PharmGKB; PA27842; -.
eggNOG; ENOG410J29P; Eukaryota.
eggNOG; ENOG411196Z; LUCA.
GeneTree; ENSGT00390000003648; -.
HOGENOM; HOG000030915; -.
HOVERGEN; HBG023495; -.
InParanoid; Q9NZD4; -.
OMA; GMKEFNV; -.
OrthoDB; EOG091G14TI; -.
PhylomeDB; Q9NZD4; -.
TreeFam; TF337056; -.
SIGNOR; Q9NZD4; -.
ChiTaRS; AHSP; human.
EvolutionaryTrace; Q9NZD4; -.
GeneWiki; ERAF; -.
GenomeRNAi; 51327; -.
PRO; PR:Q9NZD4; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000169877; -.
CleanEx; HS_ERAF; -.
ExpressionAtlas; Q9NZD4; baseline and differential.
Genevisible; Q9NZD4; HS.
GO; GO:0005833; C:hemoglobin complex; NAS:UniProtKB.
GO; GO:0030492; F:hemoglobin binding; NAS:UniProtKB.
GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
GO; GO:0030218; P:erythrocyte differentiation; IEA:InterPro.
GO; GO:0020027; P:hemoglobin metabolic process; NAS:UniProtKB.
GO; GO:0030097; P:hemopoiesis; NAS:UniProtKB.
GO; GO:0006457; P:protein folding; IEA:InterPro.
GO; GO:0050821; P:protein stabilization; IEA:InterPro.
InterPro; IPR015317; A_Hb_stabilising_prot.
InterPro; IPR036468; AHSP_sf.
PANTHER; PTHR15914; PTHR15914; 1.
Pfam; PF09236; AHSP; 1.
ProDom; PD285427; A_Hb_stabilising_prot; 1.
SUPFAM; SSF109751; SSF109751; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Complete proteome; Cytoplasm; Polymorphism;
Reference proteome.
CHAIN 1 102 Alpha-hemoglobin-stabilizing protein.
/FTId=PRO_0000064509.
VARIANT 100 100 P -> T (in dbSNP:rs36018996).
/FTId=VAR_050650.
CONFLICT 32 32 V -> A (in Ref. 3; AAL82894).
{ECO:0000305}.
CONFLICT 87 87 D -> N (in Ref. 3; AAL82894).
{ECO:0000305}.
HELIX 5 23 {ECO:0000244|PDB:1Z8U}.
HELIX 27 29 {ECO:0000244|PDB:1Z8U}.
HELIX 34 52 {ECO:0000244|PDB:1Z8U}.
TURN 53 55 {ECO:0000244|PDB:1Z8U}.
HELIX 60 86 {ECO:0000244|PDB:1Z8U}.
STRAND 97 99 {ECO:0000244|PDB:1W0B}.
SEQUENCE 102 AA; 11840 MW; 275DDF8BC670EF20 CRC64;
MALLKANKDL ISAGLKEFSV LLNQQVFNDP LVSEEDMVTV VEDWMNFYIN YYRQQVTGEP
QERDKALQEL RQELNTLANP FLAKYRDFLK SHELPSHPPP SS


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